{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T23:14:45Z","timestamp":1792624485126,"version":"4.5.0"},"reference-count":317,"publisher":"Pleiades Publishing Ltd","issue":"S1","license":[{"start":{"date-parts":[[2019,1,1]],"date-time":"2019-01-01T00:00:00Z","timestamp":1546300800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2019,1,1]],"date-time":"2019-01-01T00:00:00Z","timestamp":1546300800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Biochemistry Moscow"],"published-print":{"date-parts":[[2019,1]]},"DOI":"10.1134\/s0006297919140104","type":"journal-article","created":{"date-parts":[[2019,4,19]],"date-time":"2019-04-19T04:03:54Z","timestamp":1555646634000},"page":"159-192","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Proteasome: a Nanomachinery of Creative Destruction"],"prefix":"10.1134","volume":"84","author":[{"given":"A. A.","family":"Kudriaeva","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A. A.","family":"Belogurov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"137","published-online":{"date-parts":[[2019,4,19]]},"reference":[{"key":"762_CR1","doi-asserted-by":"publisher","first-page":"770","DOI":"10.1038\/35008096","volume":"404","author":"U. Schubert","year":"2000","unstructured":"Schubert, U., Anton, L. C., Gibbs, J., Norbury, C. C., Yewdell, J. W., and Bennink, J. R. (2000) Rapid degrada\u2013tion of a large fraction of newly synthesized proteins by pro\u2013teasomes, Nature, 404, 770\u2013774.","journal-title":"Nature"},{"key":"762_CR2","doi-asserted-by":"publisher","first-page":"343","DOI":"10.1146\/annurev-cellbio-111315-125249","volume":"33","author":"C. A. P. Joazeiro","year":"2017","unstructured":"Joazeiro, C. A. P. (2017) Ribosomal stalling during trans\u2013lation: providing substrates for ribosome\u2013associated pro\u2013tein quality control, Annu. Rev. Cell Dev. Biol., 33, 343\u2013368.","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"762_CR3","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1038\/nsmb.3147","volume":"23","author":"O. Brandman","year":"2016","unstructured":"Brandman, O., and Hegde, R. S. (2016) Ribosome\u2013associ\u2013ated protein quality control, Nat. Struct. Mol. Biol., 23, 7\u201315.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"762_CR4","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1146\/annurev-biochem-061516-045115","volume":"86","author":"F. Chiti","year":"2017","unstructured":"Chiti, F., and Dobson, C. M. (2017) Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade, Annu. Rev. Biochem., 86, 1\u201342.","journal-title":"Annu. Rev. Biochem."},{"key":"762_CR5","doi-asserted-by":"publisher","first-page":"609","DOI":"10.1042\/EBC20170035","volume":"61","author":"T. Lamark","year":"2017","unstructured":"Lamark, T., Svenning, S., and Johansen, T. (2017) Regulation of selective autophagy: the p62\/SQSTM1 para\u2013digm, Essays Biochem., 61, 609\u2013624.","journal-title":"Essays Biochem."},{"key":"762_CR6","doi-asserted-by":"publisher","first-page":"1088","DOI":"10.1038\/nature07195","volume":"454","author":"D. Kaganovich","year":"2008","unstructured":"Kaganovich, D., Kopito, R., and Frydman, J. (2008) Misfolded proteins partition between two distinct quality control compartments, Nature, 454, 1088\u20131095.","journal-title":"Nature"},{"key":"762_CR7","doi-asserted-by":"publisher","DOI":"10.1126\/science.aac4354","volume-title":"In vivo aspects of protein folding and quality control","author":"D. Balchin","year":"2016","unstructured":"Balchin, D., Hayer\u2013Hartl, M., and Hartl, F. U. (2016) In vivo aspects of protein folding and quality control, Science, 353, aac4354."},{"key":"762_CR8","doi-asserted-by":"publisher","first-page":"736","DOI":"10.1038\/ncb0805-736","volume":"7","author":"A. J. McClellan","year":"2005","unstructured":"McClellan, A. J., Tam, S., Kaganovich, D., and Frydman, J. (2005) Protein quality control: chaperones culling cor\u2013rupt conformations, Nat. Cell Biol., 7, 736\u2013741.","journal-title":"Nat. Cell Biol."},{"key":"762_CR9","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1146\/annurev-biochem-060614-033955","volume":"84","author":"J. Labbadia","year":"2015","unstructured":"Labbadia, J., and Morimoto, R. I. (2015) The biology of proteostasis in aging and disease, Annu. Rev. Biochem., 84, 1\u201330.","journal-title":"Annu. Rev. Biochem."},{"key":"762_CR10","doi-asserted-by":"publisher","first-page":"697","DOI":"10.1146\/annurev-biochem-062917-011931","volume":"87","author":"J. A. M. Bard","year":"2018","unstructured":"Bard, J. A. M., Goodall, E. A., Greene, E. R., Jonsson, E., Dong, K. C., and Martin, A. (2018) Structure and function of the 26S proteasome, Annu. Rev. Biochem., 87, 697\u2013724.","journal-title":"Annu. Rev. Biochem."},{"key":"762_CR11","doi-asserted-by":"publisher","first-page":"759","DOI":"10.1038\/nrm3696","volume":"14","author":"C. A. Lamb","year":"2013","unstructured":"Lamb, C. A., Yoshimori, T., and Tooze, S. A. (2013) The autophagosome: origins unknown, biogenesis complex, Nat. Rev. Mol. Cell Biol., 14, 759\u2013774.","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"762_CR12","doi-asserted-by":"publisher","first-page":"425","DOI":"10.1146\/annurev.biochem.67.1.425","volume":"67","author":"A. Hershko","year":"1998","unstructured":"Hershko, A., and Ciechanover, A. (1998) The ubiquitin sys\u2013tem, Annu. Rev. Biochem., 67, 425\u2013479.","journal-title":"Annu. Rev. Biochem."},{"key":"762_CR13","doi-asserted-by":"publisher","first-page":"873","DOI":"10.1016\/j.tibs.2017.09.002","volume":"42","author":"Y. T. Kwon","year":"2017","unstructured":"Kwon, Y. T., and Ciechanover, A. (2017) The ubiquitin code in the ubiquitin\u2013proteasome system and autophagy, Trends Biochem. Sci., 42, 873\u2013886.","journal-title":"Trends Biochem. Sci."},{"key":"762_CR14","doi-asserted-by":"publisher","first-page":"193","DOI":"10.1146\/annurev-biochem-061516-044908","volume":"86","author":"I. Dikic","year":"2017","unstructured":"Dikic, I. (2017) Proteasomal and autophagic degradation systems, Annu. Rev. Biochem., 86, 193\u2013224.","journal-title":"Annu. Rev. Biochem."},{"key":"762_CR15","doi-asserted-by":"publisher","first-page":"844","DOI":"10.1002\/pmic.201400341","volume":"15","author":"D. Scott","year":"2015","unstructured":"Scott, D., Oldham, N. J., Strachan, J., Searle, M. S., and Layfield, R. (2015) Ubiquitin\u2013binding domains: mecha\u2013nisms of ubiquitin recognition and use as tools to investi\u2013gate ubiquitin\u2013modified proteomes, Proteomics, 15, 844\u2013861.","journal-title":"Proteomics"},{"key":"762_CR16","doi-asserted-by":"publisher","first-page":"3497","DOI":"10.1007\/s00018-016-2255-5","volume":"73","author":"G. L. Grice","year":"2016","unstructured":"Grice, G. L., and Nathan, J. A. (2016) The recognition of ubiquitinated proteins by the proteasome, Cell. Mol. Life Sci., 73, 3497\u20133506.","journal-title":"Cell. Mol. Life Sci."},{"key":"762_CR17","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1146\/annurev-biochem-061516-044518","volume":"86","author":"F. U. Hartl","year":"2017","unstructured":"Hartl, F. U. (2017) Protein misfolding diseases, Annu. Rev. Biochem., 86, 1\u20136.","journal-title":"Annu. Rev. Biochem."},{"key":"762_CR18","doi-asserted-by":"publisher","first-page":"761","DOI":"10.1016\/S0092-8674(94)90462-6","volume":"78","author":"K. L. Rock","year":"1994","unstructured":"Rock, K. L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., and Goldberg, A. L. (1994) Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules, Cell, 78, 761\u2013771.","journal-title":"Cell"},{"key":"762_CR19","doi-asserted-by":"publisher","first-page":"1743","DOI":"10.2741\/1363","volume":"1","author":"J. Maupin\u2013Furlow","year":"2004","unstructured":"Maupin\u2013Furlow, J., Gil, M., and Karadzic, I. (2004) Proteasomes: perspectives from the Archaea, Front. Biosci., 1, 1743\u20131758.","journal-title":"Front. Biosci."},{"key":"762_CR20","doi-asserted-by":"publisher","first-page":"132","DOI":"10.1016\/j.abb.2015.12.012","volume":"591","author":"B. Dahlmann","year":"2016","unstructured":"Dahlmann, B. (2016) Mammalian proteasome subtypes: their diversity in structure and function, Arch. Biochem. Biophys., 591, 132\u2013140.","journal-title":"Arch. Biochem. Biophys."},{"key":"762_CR21","doi-asserted-by":"publisher","first-page":"22123","DOI":"10.1074\/jbc.274.32.22123","volume":"274","author":"G. N. DeMartino","year":"1999","unstructured":"DeMartino, G. N., and Slaughter, C. A. (1999) The pro\u2013teasome, a novel protease regulated by multiple mecha\u2013nisms, J. Biol. Chem., 274, 22123\u201322126.","journal-title":"J. Biol. Chem."},{"key":"762_CR22","doi-asserted-by":"publisher","first-page":"14336","DOI":"10.1074\/jbc.275.19.14336","volume":"275","author":"N. Tanahashi","year":"2000","unstructured":"Tanahashi, N., Murakami, Y., Minami, Y., Shimbara, N., Hendil, K. B., and Tanaka, K. (2000) Hybrid proteasomes. Induction by interferon\u2013gamma and contribution to ATP\u2013dependent proteolysis, J. Biol. Chem., 275, 14336\u201314345.","journal-title":"J. Biol. Chem."},{"key":"762_CR23","doi-asserted-by":"publisher","first-page":"687","DOI":"10.1074\/mcp.M112.023317","volume":"12","author":"B. Fabre","year":"2013","unstructured":"Fabre, B., Lambour, T., Delobel, J., Amalric, F., Monsarrat, B., Burlet\u2013Schiltz, O., and Bousquet\u2013Dubouch, M.\u2013P. (2013) Subcellular distribution and dynamics of active proteasome complexes unraveled by a workflow combining in vivo complex cross\u2013linking and quantitative proteomics, Mol. Cell. Proteomics, 12, 687\u2013699.","journal-title":"Mol. Cell. Proteomics"},{"key":"762_CR24","doi-asserted-by":"publisher","first-page":"439","DOI":"10.1126\/science.1261197","volume":"347","author":"S. Asano","year":"2015","unstructured":"Asano, S., Fukuda, Y., Beck, F., Aufderheide, A., Forster, F., Danev, R., and Baumeister, W. (2015) A molecular cen\u2013sus of 26S proteasomes in intact neurons, Science, 347, 439\u2013442.","journal-title":"Science"},{"key":"762_CR25","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1016\/j.tcb.2004.11.003","volume":"15","author":"M. Rechsteiner","year":"2005","unstructured":"Rechsteiner, M., and Hill, C. P. (2005) Mobilizing the pro\u2013teolytic machine: cell biological roles of proteasome activa\u2013tors and inhibitors, Trends Cell Biol., 15, 27\u201333.","journal-title":"Trends Cell Biol."},{"key":"762_CR26","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1038\/nsmb.3389","volume":"24","author":"K. V. Ramachandran","year":"2017","unstructured":"Ramachandran, K. V., and Margolis, S. S. (2017) A mam\u2013malian nervous\u2013system\u2013specific plasma membrane protea\u2013some complex that modulates neuronal function, Nat. Struct. Mol. Biol., 24, 419\u2013430.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"762_CR27","doi-asserted-by":"publisher","first-page":"463","DOI":"10.1038\/386463a0","volume":"386","author":"M. Groll","year":"1997","unstructured":"Groll, M., Ditzel, L., Lowe, J., Stock, D., Bochtler, M., Bartunik, H. D., and Huber, R. (1997) Structure of 20S proteasome from yeast at 2.4 \u00c5 resolution, Nature, 386, 463\u2013471.","journal-title":"Nature"},{"key":"762_CR28","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1016\/j.bbamcr.2004.09.025","volume":"1695","author":"M. Groll","year":"2004","unstructured":"Groll, M., and Huber, R. (2004) Inhibitors of the eukaryot\u2013ic 20S proteasome core particle: a structural approach, Biochim. Biophys. Acta, 1695, 33\u201344.","journal-title":"Biochim. Biophys. Acta"},{"key":"762_CR29","doi-asserted-by":"publisher","first-page":"222","DOI":"10.1002\/cbic.200400313","volume":"6","author":"M. Groll","year":"2005","unstructured":"Groll, M., Bochtler, M., Brandstetter, H., Clausen, T., and Huber, R. (2005) Molecular machines for protein degrada\u2013tion, Chembiochem, 6, 222\u2013256.","journal-title":"Chembiochem"},{"key":"762_CR30","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1016\/S0014-5793(96)01403-2","volume":"400","author":"F. Zuhl","year":"1997","unstructured":"Zuhl, F., Tamura, T., Dolenc, I., Cejka, Z., Nagy, I., De Mot, R., and Baumeister, W. (1997) Subunit topology of the Rhodococcus proteasome, FEBS Lett., 400, 83\u201390.","journal-title":"FEBS Lett."},{"key":"762_CR31","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1016\/S0092-8674(00)80929-0","volume":"92","author":"W. Baumeister","year":"1998","unstructured":"Baumeister, W., Walz, J., Zuhl, F., and Seemuller, E. (1998) The proteasome: paradigm of a self\u2013compartmentalizing protease, Cell, 92, 367\u2013380.","journal-title":"Cell"},{"key":"762_CR32","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1016\/j.bbamcr.2013.03.008","volume":"1843","author":"M. J. Kunjappu","year":"2014","unstructured":"Kunjappu, M. J., and Hochstrasser, M. (2014) Assembly of the 20S proteasome, Biochim. Biophys. Acta, 1843, 2\u201312.","journal-title":"Biochim. Biophys. Acta"},{"key":"762_CR33","doi-asserted-by":"publisher","first-page":"1137","DOI":"10.1016\/j.str.2009.06.011","volume":"17","author":"P. A. Osmulski","year":"2009","unstructured":"Osmulski, P. A., Hochstrasser, M., and Gaczynska, M. (2009) A tetrahedral transition state at the active sites of the 20S proteasome is coupled to opening of the alpha\u2013ring channel, Structure, 17, 1137\u20131147.","journal-title":"Structure"},{"key":"762_CR34","doi-asserted-by":"publisher","first-page":"360","DOI":"10.1016\/j.molcel.2008.03.004","volume":"30","author":"J. Rabl","year":"2008","unstructured":"Rabl, J., Smith, D. M., Yu, Y., Chang, S.\u2013C., Goldberg, A. L., and Cheng, Y. (2008) Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases, Mol. Cell, 30, 360\u2013368.","journal-title":"Mol. Cell"},{"key":"762_CR35","doi-asserted-by":"publisher","first-page":"2240","DOI":"10.1021\/acschembio.7b00489","volume":"12","author":"C. L. Jones","year":"2017","unstructured":"Jones, C. L., Njomen, E., Sjogren, B., Dexheimer, T. S., and Tepe, J. J. (2017) Small molecule enhancement of 20S proteasome activity targets intrinsically disordered pro\u2013teins, ACS Chem. Biol., 12, 2240\u20132247.","journal-title":"ACS Chem. Biol."},{"key":"762_CR36","doi-asserted-by":"publisher","first-page":"895","DOI":"10.1038\/nature02263","volume":"426","author":"A. L. Goldberg","year":"2003","unstructured":"Goldberg, A. L. (2003) Protein degradation and protection against misfolded or damaged proteins, Nature, 426, 895\u2013899.","journal-title":"Nature"},{"key":"762_CR37","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1046\/j.1471-4159.2003.01642.x","volume":"85","author":"S. Keck","year":"2003","unstructured":"Keck, S., Nitsch, R., Grune, T., and Ullrich, O. (2003) Proteasome inhibition by paired helical filament\u2013tau in brains of patients with Alzheimer\u2019s disease, J. Neurochem., 85, 115\u2013122.","journal-title":"J. Neurochem."},{"key":"762_CR38","doi-asserted-by":"publisher","first-page":"10963","DOI":"10.1038\/ncomms10963","volume":"7","author":"W. H. d Choi","year":"2016","unstructured":"Choi, W. H., de Poot, S. A. H., Lee, J. H., Kim, J. H., Han, D. H., Kim, Y. K., Finley, D., and Lee, M. J. (2016) Open\u2013gate mutants of the mammalian proteasome show enhanced ubiquitin\u2013conjugate degradation, Nat. Commun., 7, 10963.","journal-title":"Nat. Commun."},{"key":"762_CR39","first-page":"840","volume":"9","author":"V. A. Kulichkova","year":"2010","unstructured":"Kulichkova, V. A., Fedorova, O. A., Tsimokha, A. S., Moiseeva, T. N., Bottril, A., Lezina, L., Gauze, L. N., Konstantinova, I. M., Mittenberg, A. G., and Barlev, N. (2010) 26S proteasome exhibits endoribonuclease activity controlled by extracellular stimuli, Cell Cycle, 9, 840\u2013849.","journal-title":"26S proteasome exhibits endoribonuclease activity controlled by extracellular stimuli, Cell Cycle"},{"key":"762_CR40","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1007\/s10930-015-9642-x","volume":"35","author":"A. G. Mittenberg","year":"2016","unstructured":"Mittenberg, A. G., Moiseeva, T. N., Kuzyk, V. O., and Barlev, N. A. (2016) Regulation of endoribonuclease activ\u2013ity of alpha\u2013type proteasome subunits in proery\u2013throleukemia K562 upon hemin\u2013induced differentiation, Protein J., 35, 17\u201323.","journal-title":"Protein J."},{"key":"762_CR41","doi-asserted-by":"publisher","first-page":"661","DOI":"10.1038\/ni1090","volume":"5","author":"P. M. Kloetzel","year":"2004","unstructured":"Kloetzel, P. M. (2004) Generation of major histocompati\u2013bility complex class I antigens: functional interplay between proteasomes and TPPII, Nat. Immunol., 5, 661\u2013669.","journal-title":"Nat. Immunol."},{"key":"762_CR42","doi-asserted-by":"publisher","first-page":"1491","DOI":"10.1007\/s00018-011-0657-y","volume":"68","author":"E. J. A. M. Sijts","year":"2011","unstructured":"Sijts, E. J. A. M., and Kloetzel, P.\u2013M. M. (2011) The role of the proteasome in the generation of MHC class I ligands and immune responses, Cell Mol. Life Sci., 68, 1491\u20131502.","journal-title":"Cell Mol. Life Sci."},{"key":"762_CR43","doi-asserted-by":"publisher","first-page":"4111","DOI":"10.1093\/emboj\/19.15.4111","volume":"19","author":"M. Chatterjee\u2013Kishore","year":"2000","unstructured":"Chatterjee\u2013Kishore, M., Wright, K. L., Ting, J. P., and Stark, G. R. (2000) How Stat1 mediates constitutive gene expression: a complex of unphosphorylated Stat1 and IRF1 supports transcription of the LMP2 gene, EMBO J., 19, 4111\u20134122.","journal-title":"EMBO J."},{"key":"762_CR44","doi-asserted-by":"publisher","first-page":"1053","DOI":"10.4049\/jimmunol.176.2.1053","volume":"176","author":"J. Chapiro","year":"2006","unstructured":"Chapiro, J., Claverol, S., Piette, F., Ma, W., Stroobant, V., Guillaume, B., Gairin, J.\u2013E., Morel, S., Burlet\u2013Schiltz, O., Monsarrat, B., Boon, T., and van den Eynde, B. J. (2006) Destructive cleavage of antigenic peptides either by the immunoproteasome or by the standard proteasome results in differential antigen presentation, J. Immunol., 176, 1053\u20131061.","journal-title":"J. Immunol."},{"key":"762_CR45","doi-asserted-by":"publisher","first-page":"1319","DOI":"10.1084\/jem.193.11.1319","volume":"193","author":"W. Chen","year":"2001","unstructured":"Chen, W., Norbury, C., and Cho, Y. (2001) Immunoproteasomes shape immunodominance hierar\u2013chies of antiviral CD8+ T cells at the levels of T cell reper\u2013toire and presentation of viral antigens, J. Exp. Med., 193, 1319\u20131326.","journal-title":"J. Exp. Med."},{"key":"762_CR46","doi-asserted-by":"publisher","first-page":"24032","DOI":"10.1038\/srep24032","volume":"6","author":"F. Ebstein","year":"2016","unstructured":"Ebstein, F., Textoris\u2013Taube, K., Keller, C., Golnik, R., Vigneron, N., Van Den Eynde, B. J., Schuler\u2013Thurner, B., Schadendorf, D., Lorenz, F. K. M., Uckert, W., Urban, S., Lehmann, A., Albrecht\u2013Koepke, N., Janek, K., Henklein, P., Niewienda, A., Kloetzel, P. M., and Mishto, M. (2016) Proteasomes generate spliced epitopes by two different mechanisms and as efficiently as non\u2013spliced epitopes, Sci. Rep., 6, 24032.","journal-title":"Sci. Rep."},{"key":"762_CR47","doi-asserted-by":"publisher","first-page":"4075","DOI":"10.4049\/jimmunol.1402454","volume":"195","author":"C. R. d Berkers","year":"2015","unstructured":"Berkers, C. R., de Jong, A., Schuurman, K. G., Linnemann, C., Geenevasen, J. A. J., Schumacher, T. N. M., Rodenko, B., and Ovaa, H. (2015) Peptide splicing in the proteasome creates a novel type of antigen with an isopeptide linkage, J. Immunol., 195, 4075\u20134084.","journal-title":"J. Immunol."},{"key":"762_CR48","doi-asserted-by":"publisher","first-page":"4085","DOI":"10.4049\/jimmunol.1402455","volume":"195","author":"C. R. d Berkers","year":"2015","unstructured":"Berkers, C. R., de Jong, A., Schuurman, K. G., Linnemann, C., Meiring, H. D., Janssen, L., Neefjes, J. J., Schumacher, T. N. M., Rodenko, B., and Ovaa, H. (2015) Definition of proteasomal peptide splicing rules for high\u2013efficiency spliced peptide presentation by MHC class I molecules, J. Immunol., 195, 4085\u20134095.","journal-title":"J. Immunol."},{"key":"762_CR49","doi-asserted-by":"publisher","first-page":"354","DOI":"10.1126\/science.aaf4384","volume":"354","author":"J. Liepe","year":"2016","unstructured":"Liepe, J., Marino, F., Sidney, J., Jeko, A., Bunting, D. E., Sette, A., Kloetzel, P. M., Stumpf, M. P. H., Heck, A. J. R., and Mishto, M. (2016) A large fraction of HLA class I lig\u2013ands are proteasome\u2013generated spliced peptides, Science, 354, 354\u2013358.","journal-title":"Science"},{"key":"762_CR50","doi-asserted-by":"publisher","first-page":"2087","DOI":"10.1016\/j.bbamcr.2012.06.016","volume":"1823","author":"N. Qureshi","year":"2012","unstructured":"Qureshi, N., Morrison, D. C., and Reis, J. (2012) Proteasome protease mediated regulation of cytokine induction and inflammation, Biochim. Biophys. Acta Mol. Cell Res., 1823, 2087\u20132093.","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"762_CR51","doi-asserted-by":"publisher","first-page":"12365","DOI":"10.1074\/jbc.M114.558866","volume":"289","author":"H. Uechi","year":"2014","unstructured":"Uechi, H., Hamazaki, J., and Murata, S. (2014) Characterization of the testis\u2013specific proteasome subunit \u03b14s in mammals, J. Biol. Chem., 289, 12365\u201312374.","journal-title":"J. Biol. Chem."},{"key":"762_CR52","doi-asserted-by":"publisher","first-page":"5186","DOI":"10.1182\/blood-2008-11-187633","volume":"113","author":"U. Tomaru","year":"2009","unstructured":"Tomaru, U., Ishizu, A., Murata, S., Miyatake, Y., Suzuki, S., Takahashi, S., Kazamaki, T., Ohara, J., Baba, T., Iwasaki, S., Fugo, K., Otsuka, N., Tanaka, K., and Kasahara, M. (2009) Exclusive expression of proteasome subunit 5t in the human thymic cortex, Blood, 113, 5186\u20135191.","journal-title":"Blood"},{"key":"762_CR53","doi-asserted-by":"publisher","first-page":"192","DOI":"10.1016\/j.coi.2008.03.002","volume":"20","author":"S. Murata","year":"2008","unstructured":"Murata, S., Takahama, Y., and Tanaka, K. (2008) Thymoproteasome: probable role in generating positively selecting peptides, Curr. Opin. Immunol., 20, 192\u2013196.","journal-title":"Curr. Opin. Immunol."},{"key":"762_CR54","doi-asserted-by":"publisher","first-page":"795","DOI":"10.1016\/j.chembiol.2010.05.027","volume":"17","author":"B. I. Florea","year":"2010","unstructured":"Florea, B. I., Verdoes, M., Li, N., van der Linden, W. A., Geurink, P. P., van den Elst, H., Hofmann, T., de Ru, A., van Veelen, P. A., Tanaka, K., Sasaki, K., Murata, S., den Dulk, H., Brouwer, J., Ossendorp, F. A., Kisselev, A. F., and Overkleeft, H. S. (2010) Activity\u2013based profiling reveals reactivity of the murine thymoproteasome\u2013specific subunit \u03b25t, Chem. Biol., 17, 795\u2013801.","journal-title":"Chem. Biol."},{"key":"762_CR55","doi-asserted-by":"publisher","first-page":"1349","DOI":"10.1126\/science.1141915","volume":"316","author":"S. Murata","year":"2007","unstructured":"Murata, S., Sasaki, K., Kishimoto, T., Niwa, S., Hayashi, H., Takahama, Y., and Tanaka, K. (2007) Regulation of CD8+ T cell development by thymus\u2013specific proteasomes, Science, 316, 1349\u20131353.","journal-title":"Science"},{"key":"762_CR56","doi-asserted-by":"publisher","first-page":"587","DOI":"10.1146\/annurev-biochem-060408-172623","volume":"80","author":"R. T. Sauer","year":"2011","unstructured":"Sauer, R. T., and Baker, T. A. (2011) AAA+ proteases: ATP\u2013fueled machines of protein destruction, Annu. Rev. Biochem., 80, 587\u2013612.","journal-title":"Annu. Rev. Biochem."},{"key":"762_CR57","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1016\/j.molcel.2010.02.035","volume":"38","author":"R. J. Tomko","year":"2010","unstructured":"Tomko, R. J., Funakoshi, M., Schneider, K., Wang, J., and Hochstrasser, M. (2010) Heterohexameric ring arrange\u2013ment of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly, Mol. Cell, 38, 393\u2013403.","journal-title":"Mol. Cell"},{"key":"762_CR58","doi-asserted-by":"publisher","first-page":"548","DOI":"10.1038\/nature06924","volume":"453","author":"P. Schreiner","year":"2008","unstructured":"Schreiner, P., Chen, X., Husnjak, K., Randles, L., Zhang, N., Elsasser, S., Finley, D., Dikic, I., Walters, K. J., and Groll, M. (2008) Ubiquitin docking at the proteasome through a novel pleckstrin\u2013homology domain interaction, Nature, 453, 548\u2013552.","journal-title":"Nature"},{"key":"762_CR59","doi-asserted-by":"publisher","first-page":"481","DOI":"10.1038\/nature06926","volume":"453","author":"K. Husnjak","year":"2008","unstructured":"Husnjak, K., Elsasser, S., Zhang, N., Chen, X., Randles, L., Shi, Y., Hofmann, K., Walters, K. J., Finley, D., and Dikic, I. (2008) Proteasome subunit Rpn13 is a novel ubiq\u2013uitin receptor, Nature, 453, 481\u2013488.","journal-title":"Nature"},{"key":"762_CR60","volume-title":"Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the pro\u2013teasome","author":"Y. Shi","year":"2016","unstructured":"Shi, Y., Chen, X., Elsasser, S., Stocks, B. B., Tian, G., Lee, B.\u2013H., Shi, Y., Zhang, N., de Poot, S. A. H., Tuebing, F., Sun, S., Vannoy, J., Tarasov, S. G., Engen, J. R., Finley, D., and Walters, K. J. (2016) Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the pro\u2013teasome, Science, 351, aad9421."},{"key":"762_CR61","doi-asserted-by":"publisher","first-page":"611","DOI":"10.1126\/science.1075898","volume":"298","author":"R. Verma","year":"2002","unstructured":"Verma, R., Aravind, L., Oania, R., McDonald, W. H., Yates, J. R., Koonin, E. V., and Deshaies, R. J. (2002) Role of Rpn11 metalloprotease in deubiquitination and degrada\u2013tion by the 26S proteasome, Science, 298, 611\u2013615.","journal-title":"Science"},{"key":"762_CR62","doi-asserted-by":"publisher","first-page":"615","DOI":"10.1016\/S0092-8674(00)81603-7","volume":"94","author":"M. H. Glickman","year":"1998","unstructured":"Glickman, M. H., Rubin, D. M., Coux, O., Wefes, I., Pfeifer, G., Cjeka, Z., Baumeister, W., Fried, V. A., and Finley, D. (1998) A subcomplex of the proteasome regula\u2013tory particle required for ubiquitin\u2013conjugate degradation and related to the COP9\u2013signalosome and eIF3, Cell, 94, 615\u2013623.","journal-title":"Cell"},{"key":"762_CR63","doi-asserted-by":"publisher","first-page":"781","DOI":"10.1038\/nsmb.2616","volume":"20","author":"M. E. Matyskiela","year":"2013","unstructured":"Matyskiela, M. E., Lander, G. C., and Martin, A. (2013) Conformational switching of the 26S proteasome enables substrate degradation, Nat. Struct. Mol. Biol., 20, 781\u2013788.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"762_CR64","doi-asserted-by":"publisher","first-page":"7264","DOI":"10.1073\/pnas.1305782110","volume":"110","author":"P. Sledz","year":"2013","unstructured":"Sledz, P., Unverdorben, P., Beck, F., Pfeifer, G., Schweitzer, A., Forster, F., and Baumeister, W. (2013) Structure of the 26S proteasome with ATP\u2013\u03b3S bound pro\u2013vides insights into the mechanism of nucleotide\u2013dependent substrate translocation, Proc. Natl. Acad. Sci. USA, 110, 7264\u20137269.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"762_CR65","doi-asserted-by":"publisher","first-page":"186","DOI":"10.1038\/nature10774","volume":"482","author":"G. C. Lander","year":"2012","unstructured":"Lander, G. C., Estrin, E., Matyskiela, M. E., Bashore, C., Nogales, E., and Martin, A. (2012) Complete subunit architecture of the proteasome regulatory particle, Nature, 482, 186\u2013191.","journal-title":"Nature"},{"key":"762_CR66","doi-asserted-by":"publisher","first-page":"7816","DOI":"10.1073\/pnas.1608050113","volume":"113","author":"A. Schweitzer","year":"2016","unstructured":"Schweitzer, A., Aufderheide, A., Rudack, T., Beck, F., Pfeifer, G., Plitzko, J. M., Sakata, E., Schulten, K., Forster, F., and Baumeister, W. (2016) Structure of the human 26S proteasome at a resolution of 3.9 \u00c5, Proc. Natl. Acad. Sci. USA, 113, 7816\u20137821.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"762_CR67","doi-asserted-by":"publisher","first-page":"580","DOI":"10.1016\/j.molcel.2009.04.030","volume":"34","author":"S. Djuranovic","year":"2009","unstructured":"Djuranovic, S., Hartmann, M. D., Habeck, M., Ursinus, A., Zwickl, P., Martin, J., Lupas, A. N., and Zeth, K. (2009) Structure and activity of the N\u2013terminal substrate recognition domains in proteasomal ATPases, Mol. Cell, 34, 580\u2013590.","journal-title":"Mol. Cell"},{"key":"762_CR68","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1073\/pnas.1117648108","volume":"109","author":"G. R. Pathare","year":"2012","unstructured":"Pathare, G. R., Nagy, I., Bohn, S., Unverdorben, P., Hubert, A., Korner, R., Nickell, S., Lasker, K., Sali, A., Tamura, T., Nishioka, T., Forster, F., Baumeister, W., and Bracher, A. (2012) The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcom\u2013plexes together, Proc. Natl. Acad. Sci. USA, 109, 149\u2013154.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"762_CR69","doi-asserted-by":"publisher","first-page":"219","DOI":"10.1038\/nsmb.1547","volume":"16","author":"D. Bech\u2013Otschir","year":"2009","unstructured":"Bech\u2013Otschir, D., Helfrich, A., Enenkel, C., Consiglieri, G., Seeger, M., Holzhutter, H.\u2013G., Dahlmann, B., and Kloetzel, P.\u2013M. (2009) Polyubiquitin substrates allosteri\u2013cally activate their own degradation by the 26S proteasome, Nat. Struct. Mol. Biol., 16, 219\u2013225.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"762_CR70","doi-asserted-by":"publisher","DOI":"10.1126\/scisignal.2001232","volume-title":"Regulation of the 26S proteasome complex during oxidative stress","author":"X. Wang","year":"2010","unstructured":"Wang, X., Yen, J., Kaiser, P., and Huang, L. (2010) Regulation of the 26S proteasome complex during oxidative stress, Sci. Signal., 3, ra88."},{"key":"762_CR71","doi-asserted-by":"publisher","first-page":"1355","DOI":"10.1016\/j.freeradbiomed.2011.06.015","volume":"51","author":"T. Grune","year":"2011","unstructured":"Grune, T., Catalgol, B., Licht, A., Ermak, G., Pickering, A. M., Ngo, J. K., and Davies, K. J. A. (2011) HSP70 mediates dissociation and reassociation of the 26S protea\u2013some during adaptation to oxidative stress, Free Radic. Biol. Med., 51, 1355\u20131364.","journal-title":"Free Radic. Biol. Med."},{"key":"762_CR72","doi-asserted-by":"publisher","first-page":"11272","DOI":"10.1074\/jbc.M113.537175","volume":"289","author":"P. Tsvetkov","year":"2014","unstructured":"Tsvetkov, P., Myers, N., Eliav, R., Adamovich, Y., Hagai, T., Adler, J., Navon, A., and Shaul, Y. (2014) NADH binds and stabilizes the 26S proteasomes independent of ATP, J. Biol. Chem., 289, 11272\u201311281.","journal-title":"J. Biol. Chem."},{"key":"762_CR73","doi-asserted-by":"publisher","first-page":"12161","DOI":"10.1074\/jbc.M113.464552","volume":"288","author":"Q. Huang","year":"2013","unstructured":"Huang, Q., Wang, H., Perry, S. W., and Figueiredo\u2013Pereira, M. E. (2013) Negative regulation of 26S proteasome stabil\u2013ity via calpain\u2013mediated cleavage of Rpn10 subunit upon mitochondrial dysfunction in neurons, J. Biol. Chem., 288, 12161\u201312174.","journal-title":"J. Biol. Chem."},{"key":"762_CR74","doi-asserted-by":"publisher","first-page":"733","DOI":"10.1016\/j.molcel.2010.05.001","volume":"38","author":"M. Isasa","year":"2010","unstructured":"Isasa, M., Katz, E. J., Kim, W., Yugo, V., Gonzalez, S., Kirkpatrick, D. S., Thomson, T. M., Finley, D., Gygi, S. P., and Crosas, B. (2010) Monoubiquitination of Rpn10 regu\u2013lates substrate recruitment to the proteasome, Mol. Cell, 38, 733\u2013745.","journal-title":"Mol. Cell"},{"key":"762_CR75","doi-asserted-by":"publisher","first-page":"2769","DOI":"10.1002\/pmic.200900283","volume":"10","author":"J. Kikuchi","year":"2010","unstructured":"Kikuchi, J., Iwafune, Y., Akiyama, T., Okayama, A., Nakamura, H., Arakawa, N., Kimura, Y., and Hirano, H. (2010) Co\u2013and post\u2013translational modifications of the 26S proteasome in yeast, Proteomics, 10, 2769\u20132779.","journal-title":"Proteomics"},{"key":"762_CR76","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1016\/j.jprot.2015.11.016","volume":"134","author":"H. Hirano","year":"2016","unstructured":"Hirano, H., Kimura, Y., and Kimura, A. (2016) Biological significance of co\u2013and post\u2013translational modifications of the yeast 26S proteasome, J. Proteomics, 134, 37\u201346.","journal-title":"J. Proteomics"},{"key":"762_CR77","doi-asserted-by":"publisher","first-page":"614","DOI":"10.1016\/j.cell.2013.03.040","volume":"153","author":"P. F. Cho\u2013Park","year":"2013","unstructured":"Cho\u2013Park, P. F., and Steller, H. (2013) Proteasome regula\u2013tion by ADP\u2013ribosylation, Cell, 153, 614\u2013627.","journal-title":"Cell"},{"key":"762_CR78","doi-asserted-by":"publisher","first-page":"715","DOI":"10.1016\/S0092-8674(03)00974-7","volume":"115","author":"F. Zhang","year":"2003","unstructured":"Zhang, F., Su, K., Yang, X., Bowe, D. B., Paterson, A. J., and Kudlow, J. E. (2003) O\u2013GlcNAc modification is an endogenous inhibitor of the proteasome, Cell, 115, 715\u2013725.","journal-title":"Cell"},{"key":"762_CR79","doi-asserted-by":"publisher","first-page":"8856","DOI":"10.1021\/bi3007862","volume":"51","author":"A. Kimura","year":"2012","unstructured":"Kimura, A., Kato, Y., and Hirano, H. (2012) N\u2013myristoy\u2013lation of the Rpt2 subunit regulates intracellular localiza\u2013tion of the yeast 26S proteasome, Biochemistry, 51, 8856\u20138866.","journal-title":"Biochemistry"},{"key":"762_CR80","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1042\/bj20031122","volume":"378","author":"S. Bose","year":"2004","unstructured":"Bose, S., Stratford, F. L. L., Broadfoot, K. I., Mason, G. G. F., and Rivett, A. J. (2004) Phosphorylation of 20S protea\u2013some alpha subunit C8 (alpha7) stabilizes the 26S protea\u2013some and plays a role in the regulation of proteasome com\u2013plexes by gamma\u2013interferon, Biochem. J., 378, 177\u2013184.","journal-title":"Biochem. J."},{"key":"762_CR81","doi-asserted-by":"publisher","DOI":"10.1016\/j.molimm.2017.11.030","volume-title":"The 20S immunoproteasome and constitutive proteasome bind with the same affinity to PA28\u03b1\u03b2 and equally degrade FAT10","author":"G. Schmidtke","year":"2017","unstructured":"Schmidtke, G., Schregle, R., Alvarez, G., Huber, E. M., and Groettrup, M. (2017) The 20S immunoproteasome and constitutive proteasome bind with the same affinity to PA28\u03b1\u03b2 and equally degrade FAT10, Mol. Immunol., doi: 10.1016\/j.molimm.2017.11.030."},{"key":"762_CR82","doi-asserted-by":"publisher","first-page":"5126","DOI":"10.1523\/JNEUROSCI.4427-11.2012","volume":"32","author":"S. N. Djakovic","year":"2012","unstructured":"Djakovic, S. N., Marquez\u2013Lona, E. M., Jakawich, S. K., Wright, R., Chu, C., Sutton, M. A., and Patrick, G. N. (2012) Phosphorylation of Rpt6 regulates synaptic strength in hippocampal neurons, J. Neurosci., 32, 5126\u20135131.","journal-title":"J. Neurosci."},{"key":"762_CR83","doi-asserted-by":"publisher","first-page":"26655","DOI":"10.1074\/jbc.M109.021956","volume":"284","author":"S. N. Djakovic","year":"2009","unstructured":"Djakovic, S. N., Schwarz, L. A., Barylko, B., DeMartino, G. N., and Patrick, G. N. (2009) Regulation of the protea\u2013some by neuronal activity and calcium\/calmodulin\u2013dependent protein kinase II, J. Biol. Chem., 284, 26655\u201326665.","journal-title":"J. Biol. Chem."},{"key":"762_CR84","first-page":"115","volume":"7","author":"T. Jarome","year":"2013","unstructured":"Jarome, T., Kwapis, J. L., Ruenzel, W. L., and Helmstetter, F. J. (2013) CaMKII, but not protein kinase A, regulates Rpt6 phosphorylation and proteasome activity during the forma\u2013tion of long\u2013term memories, Front. Behav. Neurosci., 7, 115.","journal-title":"Front. Behav. Neurosci."},{"key":"762_CR85","first-page":"7176","volume":"112","author":"S. Lokireddy","year":"2015","unstructured":"Lokireddy, S., Kukushkin, N. V., and Goldberg, A. L. (2015) cAMP\u2013induced phosphorylation of 26S protea\u2013somes on Rpn6\/PSMD11 enhances their activity and the degradation of misfolded proteins, Proc. Natl. Acad. Sci. USA, 112, 7176\u20137185.","journal-title":"cAMP\u2013induced phosphorylation of 26S protea\u2013somes on Rpn6\/PSMD11 enhances their activity and the degradation of misfolded proteins, Proc. Natl. Acad. Sci. USA"},{"key":"762_CR86","doi-asserted-by":"publisher","first-page":"1824","DOI":"10.1091\/mbc.e13-10-0585","volume":"25","author":"A. D. Jacobson","year":"2014","unstructured":"Jacobson, A. D., MacFadden, A., Wu, Z., Peng, J., and Liu, C.\u2013W. (2014) Autoregulation of the 26S proteasome by in situ ubiquitination, Mol. Biol. Cell, 25, 1824\u20131835.","journal-title":"Mol. Biol. Cell"},{"key":"762_CR87","doi-asserted-by":"publisher","first-page":"1159","DOI":"10.1002\/embj.201386906","volume":"33","author":"H. C. Besche","year":"2014","unstructured":"Besche, H. C., Sha, Z., Kukushkin, N. V., Peth, A., Hock, E.\u2013M., Kim, W., Gygi, S., Gutierrez, J. A., Liao, H., Dick, L., and Goldberg, A. L. (2014) Autoubiquitination of the 26S proteasome on Rpn13 regulates breakdown of ubiqui\u2013tin conjugates, EMBO J., 33, 1159\u20131176.","journal-title":"EMBO J."},{"key":"762_CR88","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1038\/ncb1354","volume":"8","author":"D. Hoeller","year":"2006","unstructured":"Hoeller, D., Crosetto, N., Blagoev, B., Raiborg, C., Tikkanen, R., Wagner, S., Kowanetz, K., Breitling, R., Mann, M., Stenmark, H., and Dikic, I. (2006) Regulation of ubiquitin\u2013binding proteins by monoubiquitination, Nat. Cell Biol., 8, 163\u2013169.","journal-title":"Nat. Cell Biol."},{"key":"762_CR89","doi-asserted-by":"publisher","first-page":"2636","DOI":"10.1093\/emboj\/21.11.2636","volume":"21","author":"P. Cascio","year":"2002","unstructured":"Cascio, P., Call, M., Petre, B. M., Walz, T., and Goldberg, A. L. (2002) Properties of the hybrid form of the 26S pro\u2013teasome containing both 19S and PA28 complexes, EMBO J., 21, 2636\u20132645.","journal-title":"EMBO J."},{"key":"762_CR90","doi-asserted-by":"publisher","first-page":"195","DOI":"10.1046\/j.1365-2443.1997.d01-308.x","volume":"2","author":"N. Tanahashi","year":"1997","unstructured":"Tanahashi, N., Yokota, K., Ahn, J. Y., Chung, C. H., Fujiwara, T., Takahashi, E., DeMartino, G. N., Slaughter, C. A., Toyonaga, T., Yamamura, K., Shimbara, N., and Tanaka, K. (1997) Molecular properties of the proteasome activator PA28 family proteins and gamma\u2013interferon reg\u2013ulation, Genes Cells, 2, 195\u2013211.","journal-title":"Genes Cells"},{"key":"762_CR91","doi-asserted-by":"publisher","first-page":"7815","DOI":"10.4049\/jimmunol.174.12.7815","volume":"174","author":"F. Ossendorp","year":"2005","unstructured":"Ossendorp, F., Fu, N., Camps, M., Granucci, F., Gobin, S. J. P., van den Elsen, P. J., Schuurhuis, D., Adema, G. J., Lipford, G. B., Chiba, T., Sijts, A., Kloetzel, P.\u2013M., Ricciardi\u2013Castagnoli, P., and Melief, C. J. M. (2005) Differential expression regulation of the alpha and beta subunits of the PA28 proteasome activator in mature den\u2013dritic cells, J. Immunol., 174, 7815\u20137822.","journal-title":"J. Immunol."},{"key":"762_CR92","doi-asserted-by":"publisher","first-page":"883","DOI":"10.1096\/fj.10-160895","volume":"25","author":"J. Li","year":"2011","unstructured":"Li, J., Powell, S. R., and Wang, X. (2011) Enhancement of proteasome function by PA28\u03b1 overexpression protects against oxidative stress, FASEB J., 25, 883\u2013893.","journal-title":"FASEB J."},{"key":"762_CR93","doi-asserted-by":"publisher","first-page":"470","DOI":"10.1016\/j.chembiol.2014.02.006","volume":"21","author":"M. Raule","year":"2014","unstructured":"Raule, M., Cerruti, F., Benaroudj, N., Migotti, R., Kikuchi, J., Bachi, A., Navon, A., Dittmar, G., and Cascio, P. (2014) PA28\u03b1\u03b2 reduces size and increases hydrophilicity of 20S immunoproteasome peptide prod\u2013ucts, Chem. Biol., 21, 470\u2013480.","journal-title":"Chem. Biol."},{"key":"762_CR94","doi-asserted-by":"publisher","first-page":"831","DOI":"10.1016\/j.molcel.2007.05.028","volume":"26","author":"X. Li","year":"2007","unstructured":"Li, X., Amazit, L., Long, W., Lonard, D. M., Monaco, J. J., and O\u2019Malley, B. W. (2007) Ubiquitin\u2013and ATP\u2013inde\u2013pendent proteolytic turnover of p21 by the REGgamma\u2013proteasome pathway, Mol. Cell, 26, 831\u2013842.","journal-title":"Mol. Cell"},{"key":"762_CR95","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1016\/j.abb.2012.04.018","volume":"523","author":"A. M. Pickering","year":"2012","unstructured":"Pickering, A. M., and Davies, K. J. A. (2012) Differential roles of proteasome and immunoproteasome regulators Pa28\u03b1\u03b2, Pa28\u03b3 and Pa200 in the degradation of oxidized proteins, Arch. Biochem. Biophys., 523, 181\u2013190.","journal-title":"Pa28\u03b3 and Pa200 in the degradation of oxidized proteins, Arch. Biochem. Biophys."},{"key":"762_CR96","doi-asserted-by":"publisher","first-page":"585","DOI":"10.1042\/BJ20100878","volume":"432","author":"A. M. Pickering","year":"2010","unstructured":"Pickering, A. M., Koop, A. L., Teoh, C. Y., Ermak, G., Grune, T., and Davies, K. J. A. (2010) The immunoprotea\u2013some, the 20S proteasome and the PA28\u03b1\u03b2 proteasome regulator are oxidative\u2013stress\u2013adaptive proteolytic com\u2013plexes, Biochem. J., 432, 585\u2013595.","journal-title":"Biochem. J."},{"key":"762_CR97","doi-asserted-by":"publisher","first-page":"1383","DOI":"10.1074\/jbc.M007379200","volume":"276","author":"P. Masson","year":"2001","unstructured":"Masson, P., Andersson, O., Petersen, U. M., and Young, P. (2001) Identification and characterization of a Drosophila nuclear proteasome regulator. A homolog of human 11S REGgamma (PA28gamma), J. Biol. Chem., 276, 1383\u20131390.","journal-title":"J. Biol. Chem."},{"key":"762_CR98","doi-asserted-by":"publisher","first-page":"381","DOI":"10.1016\/j.cell.2005.11.037","volume":"124","author":"X. Li","year":"2006","unstructured":"Li, X., Lonard, D. M., Jung, S. Y., Malovannaya, A., Feng, Q., Qin, J., Tsai, S. Y., Tsai, M.\u2013J., and O\u2019Malley, B. W. (2006) The SRC\u20133\/AIB1 coactivator is degraded in a ubiquitin\u2013and ATP\u2013independent manner by the REG\u03b3 proteasome, Cell, 124, 381\u2013392.","journal-title":"Cell"},{"key":"762_CR99","doi-asserted-by":"publisher","first-page":"10237","DOI":"10.1128\/JVI.77.19.10237-10249.2003","volume":"77","author":"K. Moriishi","year":"2003","unstructured":"Moriishi, K., Okabayashi, T., Nakai, K., Moriya, K., Koike, K., Murata, S., Chiba, T., Tanaka, K., Suzuki, R., Suzuki, T., Miyamura, T., and Matsuura, Y. (2003) Proteasome activator PA28gamma\u2013dependent nuclear retention and degradation of hepatitis C virus core protein, J. Virol., 77, 10237\u201310249.","journal-title":"J. Virol."},{"key":"762_CR100","doi-asserted-by":"publisher","first-page":"843","DOI":"10.1016\/j.molcel.2007.05.022","volume":"26","author":"X. Chen","year":"2007","unstructured":"Chen, X., Barton, L. F., Chi, Y., Clurman, B. E., and Roberts, J. M. (2007) Ubiquitin\u2013independent degradation of cell\u2013cycle inhibitors by the REG\u03b3 proteasome, Mol. Cell, 26, 843\u2013852.","journal-title":"Mol. Cell"},{"key":"762_CR101","doi-asserted-by":"publisher","first-page":"38211","DOI":"10.1074\/jbc.274.53.38211","volume":"274","author":"S. Murata","year":"1999","unstructured":"Murata, S., Kawahara, H., Tohma, S., Yamamoto, K., Kasahara, M., Nabeshima, Y., Tanaka, K., and Chiba, T. (1999) Growth retardation in mice lacking the proteasome activator PA28gamma, J. Biol. Chem., 274, 38211\u201338215.","journal-title":"J. Biol. Chem."},{"key":"762_CR102","doi-asserted-by":"publisher","first-page":"3948","DOI":"10.4049\/jimmunol.172.6.3948","volume":"172","author":"L. F. Barton","year":"2004","unstructured":"Barton, L. F., Runnels, H. A., Schell, T. D., Cho, Y., Gibbons, R., Tevethia, S. S., Deepe, G. S., and Monaco, J. J. (2004) Immune defects in 28\u2013kDa proteasome activa\u2013tor gamma\u2013deficient mice, J. Immunol., 172, 3948\u20133954.","journal-title":"J. Immunol."},{"key":"762_CR103","doi-asserted-by":"publisher","first-page":"3516","DOI":"10.1093\/emboj\/cdf333","volume":"21","author":"V. Ustrell","year":"2002","unstructured":"Ustrell, V., Hoffman, L., Pratt, G., and Rechsteiner, M. (2002) PA200, a nuclear proteasome activator involved in DNA repair, EMBO J., 21, 3516\u20133525.","journal-title":"EMBO J."},{"key":"762_CR104","doi-asserted-by":"publisher","first-page":"1021","DOI":"10.1002\/yea.1146","volume":"21","author":"K. Doherty","year":"2004","unstructured":"Doherty, K., Pramanik, A., Pride, L., Lukose, J., and Wood Moore, C. (2004) Expression of the expanded YFL007w ORF and assignment of the gene name BLM10, Yeast, 21, 1021\u20131023.","journal-title":"Yeast"},{"key":"762_CR105","doi-asserted-by":"publisher","first-page":"611","DOI":"10.1126\/science.1075898","volume":"298","author":"R. Verma","year":"2002","unstructured":"Verma, R., Aravind, L., Oania, R., McDonald, W. H., Yates, J. R., Koonin, E. V., and Deshaies, R. J. (2002) Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome, Science, 298, 611\u2013615.","journal-title":"Science"},{"key":"762_CR106","doi-asserted-by":"publisher","first-page":"663","DOI":"10.1667\/RR0690.1","volume":"167","author":"J. Blickwedehl","year":"2007","unstructured":"Blickwedehl, J., McEvoy, S., Wong, I., Kousis, P., Clements, J., Elliott, R., Cresswell, P., Liang, P., and Bangia, N. (2007) Proteasomes and proteasome activator 200 kDa (PA200) accumulate on chromatin in response to ionizing radiation, Radiat. Res., 167, 663\u2013674.","journal-title":"Radiat. Res."},{"key":"762_CR107","doi-asserted-by":"publisher","first-page":"728","DOI":"10.1016\/j.molcel.2010.02.002","volume":"37","author":"K. Sadre\u2013Bazzaz","year":"2010","unstructured":"Sadre\u2013Bazzaz, K., Whitby, F. G., Robinson, H., Formosa, T., and Hill, C. P. (2010) Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening, Mol. Cell, 37, 728\u2013735.","journal-title":"Mol. Cell"},{"key":"762_CR108","doi-asserted-by":"publisher","first-page":"2999","DOI":"10.1128\/MCB.26.8.2999-3007.2006","volume":"26","author":"B. Khor","year":"2006","unstructured":"Khor, B., Bredemeyer, A. L., Huang, C.\u2013Y., Turnbull, I. R., Evans, R., Maggi, L. B., White, J. M., Walker, L. M., Carnes, K., Hess, R. A., and Sleckman, B. P. (2006) Proteasome activator PA200 is required for normal sper\u2013matogenesis, Mol. Cell Biol., 26, 2999\u20133007.","journal-title":"Mol. Cell Biol."},{"key":"762_CR109","doi-asserted-by":"publisher","first-page":"16165","DOI":"10.1073\/pnas.0803145105","volume":"105","author":"J. Blickwedehl","year":"2008","unstructured":"Blickwedehl, J., Agarwal, M., Seong, C., Pandita, R. K., Melendy, T., Sung, P., Pandita, T. K., and Bangia, N. (2008) Role for proteasome activator PA200 and postglu\u2013tamyl proteasome activity in genomic stability, Proc. Natl. Acad. Sci. USA, 105, 16165\u201316170.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"762_CR110","doi-asserted-by":"publisher","first-page":"1012","DOI":"10.1016\/j.cell.2013.04.032","volume":"153","author":"M.X. Qian","year":"2013","unstructured":"Qian, M.\u2013X., Pang, Y., Liu, C. H., Haratake, K., Du, B.\u2013Y., Ji, D.\u2013Y., Wang, G.\u2013F., Zhu, Q.\u2013Q., Song, W., Yu, Y., Zhang, X.\u2013X., Huang, H.\u2013T., Miao, S., Chen, L.\u2013B., Zhang, Z.\u2013H., Liang, Y.\u2013N., Liu, S., Cha, H., Yang, D., Zhai, Y., Komatsu, T., Tsuruta, F., Li, H., Cao, C., Li, W., Li, G.\u2013H., Cheng, Y., Chiba, T., Wang, L., Goldberg, A. L., Shen, Y., and Qiu, X.\u2013B. (2013) Acetylation\u2013mediated proteasomal degradation of core histones during DNA repair and spermatogenesis, Cell, 153, 1012\u20131024.","journal-title":"Cell"},{"key":"762_CR111","first-page":"23171","volume":"6","author":"L. Huang","year":"2016","unstructured":"Huang, L., Haratake, K., Miyahara, H., and Chiba, T. (2016) Proteasome activators, PA28\u03b3 and PA200, play indispensable roles in male fertility, Sci. Rep., 6, 23171.","journal-title":"PA28\u03b3 and PA200, play indispensable roles in male fertility, Sci. Rep."},{"key":"762_CR112","doi-asserted-by":"publisher","first-page":"12145","DOI":"10.1074\/jbc.M114.554105","volume":"289","author":"K. Tar","year":"2014","unstructured":"Tar, K., Dange, T., Yang, C., Yao, Y., Bulteau, A.\u2013L., Salcedo, E. F., Braigen, S., Bouillaud, F., Finley, D., and Schmidt, M. (2014) Proteasomes associated with the Blm10 activator protein antagonize mitochondrial fission through degradation of the fission protein Dnm1, J. Biol. Chem., 289, 12145\u201312156.","journal-title":"J. Biol. Chem."},{"key":"762_CR113","doi-asserted-by":"publisher","first-page":"528","DOI":"10.1091\/mbc.e10-04-0352","volume":"22","author":"A. D. Lopez","year":"2011","unstructured":"Lopez, A. D., Tar, K., Krugel, U., Dange, T., Ros, I. G., and Schmidt, M. (2011) Proteasomal degradation of Sfp1 contributes to the repression of ribosome biogenesis during starvation and is mediated by the proteasome activator Blm10, Mol. Biol. Cell, 22, 528\u2013540.","journal-title":"Mol. Biol. Cell"},{"key":"762_CR114","doi-asserted-by":"publisher","first-page":"333","DOI":"10.1016\/S0014-5793(99)01072-8","volume":"457","author":"D. M. Zaiss","year":"1999","unstructured":"Zaiss, D. M., Standera, S., Holzhutter, H., Kloetzel, P., and Sijts, A. J. (1999) The proteasome inhibitor PI31 com\u2013petes with PA28 for binding to 20S proteasomes, FEBS Lett., 457, 333\u2013338.","journal-title":"FEBS Lett."},{"key":"762_CR115","doi-asserted-by":"publisher","first-page":"14344","DOI":"10.1073\/pnas.212257299","volume":"99","author":"D. M. W. Zaiss","year":"2002","unstructured":"Zaiss, D. M. W., Standera, S., Kloetzel, P.\u2013M., and Sijts, A. J. A. M. (2002) PI31 is a modulator of proteasome for\u2013mation and antigen processing, Proc. Natl. Acad. Sci. USA, 99, 14344\u201314349.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"762_CR116","doi-asserted-by":"publisher","first-page":"29467","DOI":"10.1074\/jbc.M113.491662","volume":"288","author":"A. De La Mota\u2013Peynado","year":"2013","unstructured":"De La Mota\u2013Peynado, A., Lee, S. Y.\u2013C., Pierce, B. M., Wani, P., Singh, C. R., and Roelofs, J. (2013) The protea\u2013some\u2013associated protein Ecm29 inhibits proteasomal ATPase activity and in vivo protein degradation by the pro\u2013teasome, J. Biol. Chem., 288, 29467\u201329481.","journal-title":"J. Biol. Chem."},{"key":"762_CR117","doi-asserted-by":"publisher","first-page":"879","DOI":"10.1016\/j.molcel.2010.06.016","volume":"38","author":"A. Lehmann","year":"2010","unstructured":"Lehmann, A., Niewienda, A., Jechow, K., Janek, K., and Enenkel, C. (2010) Ecm29 fulfils quality control functions in proteasome assembly, Mol. Cell, 38, 879\u2013888.","journal-title":"Mol. Cell"},{"key":"762_CR118","doi-asserted-by":"publisher","first-page":"36652","DOI":"10.1074\/jbc.M111.285924","volume":"286","author":"S. Park","year":"2011","unstructured":"Park, S., Kim, W., Tian, G., Gygi, S. P., and Finley, D. (2011) Structural defects in the regulatory particle\u2013core particle interface of the proteasome induce a novel proteasome stress response, J. Biol. Chem., 286, 36652\u201336666.","journal-title":"J. Biol. Chem."},{"key":"762_CR119","doi-asserted-by":"publisher","first-page":"1053","DOI":"10.1016\/j.molcel.2015.04.023","volume":"58","author":"R. S. Marshall","year":"2015","unstructured":"Marshall, R. S., Li, F., Gemperline, D. C., Book, A. J., and Vierstra, R. D. (2015) Autophagic degradation of the 26S proteasome is mediated by the dual ATG8\/ubiquitin receptor RPN10 in arabidopsis, Mol. Cell, 58, 1053\u20131066.","journal-title":"Mol. Cell"},{"key":"762_CR120","doi-asserted-by":"publisher","first-page":"1717","DOI":"10.1016\/j.celrep.2016.07.015","volume":"16","author":"R. S. Marshall","year":"2016","unstructured":"Marshall, R. S., McLoughlin, F., and Vierstra, R. D. (2016) Autophagic turnover of inactive 26S proteasomes in yeast is directed by the ubiquitin receptor Cue5 and the Hsp42 chaperone, Cell Rep., 16, 1717\u20131732.","journal-title":"Cell Rep."},{"key":"762_CR121","doi-asserted-by":"publisher","first-page":"3239","DOI":"10.1074\/jbc.M115.699124","volume":"291","author":"K. A. Waite","year":"2016","unstructured":"Waite, K. A., Mota\u2013Peynado, A. D.\u2013L., Vontz, G., and Roelofs, J. (2016) Starvation induces proteasome autophagy with different pathways for core and regulatory particles, J. Biol. Chem., 291, 3239\u20133253.","journal-title":"J. Biol. Chem."},{"key":"762_CR122","doi-asserted-by":"publisher","first-page":"830","DOI":"10.1038\/nsmb814","volume":"11","author":"S. Prakash","year":"2004","unstructured":"Prakash, S., Tian, L., Ratliff, K. S., Lehotzky, R. E., and Matouschek, A. (2004) An unstructured initiation site is required for efficient proteasome\u2013mediated degradation, Nat. Struct. Mol. Biol., 11, 830\u2013837.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"762_CR123","doi-asserted-by":"publisher","first-page":"319","DOI":"10.1038\/nrm2673","volume":"10","author":"B. A. Schulman","year":"2009","unstructured":"Schulman, B. A., and Wade Harper, J. (2009) Ubiquitin\u2013like protein activation by E1 enzymes: the apex for down\u2013stream signalling pathways, Nat. Rev. Mol. Cell Biol., 10, 319\u2013331.","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"762_CR124","doi-asserted-by":"publisher","first-page":"615","DOI":"10.1038\/nature08595","volume":"462","author":"N. W. Pierce","year":"2009","unstructured":"Pierce, N. W., Kleiger, G., Shan, S., and Deshaies, R. J. (2009) Detection of sequential polyubiquitylation on a millisecond timescale, Nature, 462, 615\u2013619.","journal-title":"Nature"},{"key":"762_CR125","doi-asserted-by":"publisher","first-page":"86","DOI":"10.1016\/j.bbamcr.2013.07.007","volume":"1843","author":"A. Ciechanover","year":"2014","unstructured":"Ciechanover, A., and Stanhill, A. (2014) The complexity of recognition of ubiquitinated substrates by the 26S protea\u2013some, Biochim. Biophys. Acta, 1843, 86\u201396.","journal-title":"Biochim. Biophys. Acta"},{"key":"762_CR126","doi-asserted-by":"publisher","first-page":"1071","DOI":"10.15252\/embr.201540891","volume":"16","author":"L. Herhaus","year":"2015","unstructured":"Herhaus, L., and Dikic, I. (2015) Expanding the ubiquitin code through post\u2013translational modification, EMBO Rep., 16, 1071\u20131083.","journal-title":"EMBO Rep."},{"key":"762_CR127","doi-asserted-by":"publisher","first-page":"550","DOI":"10.1038\/nrm2731","volume":"10","author":"D. Komander","year":"2009","unstructured":"Komander, D., Clague, M. J., and Urbe, S. (2009) Breaking the chains: structure and function of the deubiq\u2013uitinases, Nat. Rev. Mol. Cell Biol., 10, 550\u2013563.","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"762_CR128","doi-asserted-by":"publisher","first-page":"399","DOI":"10.1146\/annurev.biochem.78.101807.093809","volume":"78","author":"R. J. Deshaies","year":"2009","unstructured":"Deshaies, R. J., and Joazeiro, C. A. P. (2009) RING domain E3 ubiquitin ligases, Annu. Rev. Biochem., 78, 399\u2013434.","journal-title":"Annu. Rev. Biochem."},{"key":"762_CR129","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1016\/j.cell.2005.10.032","volume":"124","author":"M. Rape","year":"2006","unstructured":"Rape, M., Reddy, S. K., and Kirschner, M. W. (2006) The processivity of multiubiquitination by the APC determines the order of substrate degradation, Cell, 124, 89\u2013103.","journal-title":"Cell"},{"key":"762_CR130","doi-asserted-by":"publisher","first-page":"325","DOI":"10.1016\/j.molcel.2011.08.025","volume":"44","author":"W. Kim","year":"2011","unstructured":"Kim, W., Bennett, E. J., Huttlin, E. L., Guo, A., Li, J., Possemato, A., Sowa, M. E., Rad, R., Rush, J., Comb, M. J., Harper, J. W., and Gygi, S. P. (2011) Systematic and quantitative assessment of the ubiquitin\u2013modified pro\u2013teome, Mol. Cell, 44, 325\u2013340.","journal-title":"Mol. Cell"},{"key":"762_CR131","doi-asserted-by":"publisher","first-page":"359","DOI":"10.1038\/emboj.2008.305","volume":"28","author":"Y. Saeki","year":"2009","unstructured":"Saeki, Y., Kudo, T., Sone, T., Kikuchi, Y., Yokosawa, H., Toh\u2013e, A., and Tanaka, K. (2009) Lysine 63\u2013linked polyu\u2013biquitin chain may serve as a targeting signal for the 26S proteasome, EMBO J., 28, 359\u2013371.","journal-title":"EMBO J."},{"key":"762_CR132","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1016\/j.molcel.2012.07.011","volume":"48","author":"N. Shabek","year":"2012","unstructured":"Shabek, N., Herman\u2013Bachinsky, Y., Buchsbaum, S., Lewinson, O., Haj\u2013Yahya, M., Hejjaoui, M., Lashuel, H. A., Sommer, T., Brik, A., and Ciechanover, A. (2012) The size of the proteasomal substrate determines whether its degradation will be mediated by mono\u2013or polyubiquityla\u2013tion, Mol. Cell, 48, 87\u201397.","journal-title":"Mol. Cell"},{"key":"762_CR133","doi-asserted-by":"publisher","first-page":"552","DOI":"10.1038\/emboj.2012.354","volume":"32","author":"J. A. Nathan","year":"2013","unstructured":"Nathan, J. A., Kim, H. T., Ting, L., Gygi, S. P., and Goldberg, A. L. (2013) Why do cellular proteins linked to K63\u2013polyubiquitin chains not associate with proteasomes? EMBO J., 32, 552\u2013565.","journal-title":"EMBO J."},{"key":"762_CR134","doi-asserted-by":"publisher","first-page":"660","DOI":"10.1016\/j.molcel.2015.02.020","volume":"58","author":"A. Ordureau","year":"2015","unstructured":"Ordureau, A., Munch, C., and Harper, J. W. (2015) Quantifying ubiquitin signaling, Mol. Cell, 58, 660\u2013676.","journal-title":"Mol. Cell"},{"key":"762_CR135","doi-asserted-by":"publisher","first-page":"691","DOI":"10.1038\/nmeth.1649","volume":"8","author":"S. E. Kaiser","year":"2011","unstructured":"Kaiser, S. E., Riley, B. E., Shaler, T. A., Trevino, R. S., Becker, C. H., Schulman, H., and Kopito, R. R. (2011) Protein standard absolute quantification (PSAQ) method for the measurement of cellular ubiquitin pools, Nat. Methods., 8, 691\u2013696.","journal-title":"Nat. Methods."},{"key":"762_CR136","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1016\/j.cell.2009.01.041","volume":"137","author":"P. Xu","year":"2009","unstructured":"Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D., Xie, Y., Robert, J., Rush, J., Hochstrasser, M., Finley, D., and Peng, J. (2009) Quantitative proteomics reveals the func\u2013tion of unconventional ubiquitin chains in proteasomal degradation, Cell, 137, 133\u2013145.","journal-title":"Cell"},{"key":"762_CR137","doi-asserted-by":"publisher","first-page":"1250834","DOI":"10.1126\/science.1250834","volume":"348","author":"Y. L. B.\u2013H. Lu","year":"2015","unstructured":"Lu, Y., Lee, B.\u2013H., King, R. W., Finley, D., and Kirschner, M. W. (2015) Substrate degradation by the proteasome: a single\u2013molecule kinetic analysis, Science, 348, 1250834.","journal-title":"Science"},{"key":"762_CR138","doi-asserted-by":"publisher","first-page":"1248737","DOI":"10.1126\/science.1248737","volume":"348","author":"Y. Lu","year":"2015","unstructured":"Lu, Y., Wang, W., and Kirschner, M. W. (2015) Specificity of the anaphase\u2013promoting complex: a single\u2013molecule study, Science, 348, 1248737.","journal-title":"Science"},{"key":"762_CR139","doi-asserted-by":"publisher","first-page":"700","DOI":"10.1038\/ncb1436","volume":"8","author":"D. S. Kirkpatrick","year":"2006","unstructured":"Kirkpatrick, D. S., Hathaway, N. A., Hanna, J., Elsasser, S., Rush, J., Finley, D., King, R. W., and Gygi, S. P. (2006) Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology, Nat. Cell Biol., 8, 700\u2013710.","journal-title":"Nat. Cell Biol."},{"key":"762_CR140","doi-asserted-by":"publisher","first-page":"1898","DOI":"10.1021\/acs.biochem.5b01310","volume":"55","author":"K. Martinez\u2013Fonts","year":"2016","unstructured":"Martinez\u2013Fonts, K., and Matouschek, A. (2016) A rapid and versatile method for generating proteins with defined ubiquitin chains, Biochemistry, 55, 1898\u20131908.","journal-title":"Biochemistry"},{"key":"762_CR141","doi-asserted-by":"publisher","first-page":"634","DOI":"10.1038\/ncb1143","volume":"6","author":"K. Flick","year":"2004","unstructured":"Flick, K., Ouni, I., Wohlschlegel, J. A., Capati, C., McDonald, W. H., Yates, J. R., and Kaiser, P. (2004) Proteolysis\u2013independent regulation of the transcription factor Met4 by a single Lys 48\u2013linked ubiquitin chain, Nat. Cell Biol., 6, 634\u2013641.","journal-title":"Nat. Cell Biol."},{"key":"762_CR142","doi-asserted-by":"publisher","first-page":"214","DOI":"10.1038\/nsmb.2958","volume":"22","author":"S. Fishbain","year":"2015","unstructured":"Fishbain, S., Inobe, T., Israeli, E., Chavali, S., Yu, H., Kago, G., Babu, M. M., and Matouschek, A. (2015) Sequence composition of disordered regions fine\u2013tunes protein half\u2013life, Nat. Struct. Mol. Biol., 22, 214\u2013221.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"762_CR143","doi-asserted-by":"publisher","first-page":"910","DOI":"10.1016\/j.cell.2014.03.037","volume":"157","author":"H.J. Meyer","year":"2014","unstructured":"Meyer, H.\u2013J., and Rape, M. (2014) Enhanced protein degradation by branched ubiquitin chains, Cell, 157, 910\u2013921.","journal-title":"Cell"},{"key":"762_CR144","doi-asserted-by":"publisher","first-page":"545","DOI":"10.1016\/j.celrep.2015.06.061","volume":"12","author":"G. L. Grice","year":"2015","unstructured":"Grice, G. L., Lobb, I. T., Weekes, M. P., Gygi, S. P., Antrobus, R., and Nathan, J. A. (2015) The proteasome distinguishes between heterotypic and homotypic lysine\u201311\u2013linked polyubiquitin chains, Cell Rep., 12, 545\u2013553.","journal-title":"Cell Rep."},{"key":"762_CR145","doi-asserted-by":"publisher","first-page":"210","DOI":"10.1111\/j.1600-0854.2009.01011.x","volume":"11","author":"J. M. Boname","year":"2010","unstructured":"Boname, J. M., Thomas, M., Stagg, H. R., Xu, P., Peng, J., and Lehner, P. J. (2010) Efficient internalization of MHC I requires lysine\u201311 and lysine\u201363 mixed linkage polyubiquitin chains, Traffic, 11, 210\u2013220.","journal-title":"Traffic"},{"key":"762_CR146","doi-asserted-by":"publisher","first-page":"10457","DOI":"10.1074\/jbc.M110.149633","volume":"286","author":"E. B. Dammer","year":"2011","unstructured":"Dammer, E. B., Na, C. H., Xu, P., Seyfried, N. T., Duong, D. M., Cheng, D., Gearing, M., Rees, H., Lah, J. J., Levey, A. I., Rush, J., and Peng, J. (2011) Polyubiquitin linkage profiles in three models of proteolytic stress suggest the etiology of alzheimer disease, J. Biol. Chem., 286, 10457\u201310465.","journal-title":"J. Biol. Chem."},{"key":"762_CR147","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1016\/j.molcel.2016.09.014","volume":"64","author":"F. Ohtake","year":"2016","unstructured":"Ohtake, F., Saeki, Y., Ishido, S., Kanno, J., and Tanaka, K. (2016) The K48\u2013K63 branched ubiquitin chain regu\u2013lates NF\u2013\u03baB signaling, Mol. Cell, 64, 251\u2013266.","journal-title":"Mol. Cell"},{"key":"762_CR148","doi-asserted-by":"publisher","first-page":"918","DOI":"10.1016\/j.cell.2017.09.040","volume":"171","author":"R. G. Yau","year":"2017","unstructured":"Yau, R. G., Doerner, K., Castellanos, E. R., Haakonsen, D. L., Werner, A., Wang, N., Yang, X. W., Martinez\u2013Martin, N., Matsumoto, M. L., Dixit, V. M., and Rape, M. (2017) Assembly and function of heterotypic ubiquitin chains in cell\u2013cycle and protein quality control, Cell, 171, 918\u2013933.","journal-title":"Cell"},{"key":"762_CR149","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1016\/S0076-6879(05)99014-9","volume":"399","author":"Y. Saeki","year":"2005","unstructured":"Saeki, Y., Isono, E., and Toh\u2013E, A. (2005) Preparation of ubiquitinated substrates by the PY motif\u2013insertion method for monitoring 26S proteasome activity, Methods Enzymol., 399, 215\u2013227.","journal-title":"Methods Enzymol."},{"key":"762_CR150","doi-asserted-by":"publisher","first-page":"94","DOI":"10.1093\/emboj\/19.1.94","volume":"19","author":"J. S. Thrower","year":"2000","unstructured":"Thrower, J. S., Hoffman, L., Rechsteiner, M., and Pickart, C. M. (2000) Recognition of the polyubiquitin proteolytic signal, EMBO J., 19, 94\u2013102.","journal-title":"EMBO J."},{"key":"762_CR151","doi-asserted-by":"publisher","first-page":"422","DOI":"10.1038\/nature12638","volume":"503","author":"B. Stieglitz","year":"2013","unstructured":"Stieglitz, B., Rana, R. R., Koliopoulos, M. G., Morris\u2013Davies, A. C., Schaeffer, V., Christodoulou, E., Howell, S., Brown, N. R., Dikic, I., and Rittinger, K. (2013) Structural basis for ligase\u2013specific conjugation of linear ubiquitin chains by HOIP, Nature, 503, 422\u2013426.","journal-title":"Nature"},{"key":"762_CR152","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1038\/nature09814","volume":"471","author":"F. Ikeda","year":"2011","unstructured":"Ikeda, F., Deribe, Y. L., Skanland, S. S., Stieglitz, B., Grabbe, C., Franz\u2013Wachtel, M., van Wijk, S. J. L., Goswami, P., Nagy, V., Terzic, J., Tokunaga, F., Androulidaki, A., Nakagawa, T., Pasparakis, M., Iwai, K., Sundberg, J. P., Schaefer, L., Rittinger, K., Macek, B., and Dikic, I. (2011) SHARPIN forms a linear ubiquitin ligase complex regulating NF\u2013\u03baB activity and apoptosis, Nature, 471, 637\u2013641.","journal-title":"Nature"},{"key":"762_CR153","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1038\/nature09816","volume":"471","author":"B. Gerlach","year":"2011","unstructured":"Gerlach, B., Cordier, S. M., Schmukle, A. C., Emmerich, C. H., Rieser, E., Haas, T. L., Webb, A. I., Rickard, J. A., Anderton, H., Wong, W. W.\u2013L., Nachbur, U., Gangoda, L., Warnken, U., Purcell, A. W., Silke, J., and Walczak, H. (2011) Linear ubiquitination prevents inflammation and regulates immune signalling, Nature, 471, 591\u2013596.","journal-title":"Nature"},{"key":"762_CR154","doi-asserted-by":"publisher","first-page":"633","DOI":"10.1038\/nature09815","volume":"471","author":"F. Tokunaga","year":"2011","unstructured":"Tokunaga, F., Nakagawa, T., Nakahara, M., Saeki, Y., Taniguchi, M., Sakata, S., Tanaka, K., Nakano, H., and Iwai, K. (2011) SHARPIN is a component of the NF\u2013\u03baB\u2013activating linear ubiquitin chain assembly complex, Nature, 471, 633\u2013636.","journal-title":"Nature"},{"key":"762_CR155","doi-asserted-by":"publisher","first-page":"318","DOI":"10.1038\/nature12296","volume":"498","author":"E. Rivkin","year":"2013","unstructured":"Rivkin, E., Almeida, S. M., Ceccarelli, D. F., Juang, Y.\u2013C., MacLean, T. A., Srikumar, T., Huang, H., Dunham, W. H., Fukumura, R., Xie, G., Gondo, Y., Raught, B., Gingras, A.\u2013C., Sicheri, F., and Cordes, S. P. (2013) The linear ubiquitin\u2013specific deubiquitinase gumby regulates angiogenesis, Nature, 498, 318\u2013324.","journal-title":"Nature"},{"key":"762_CR156","doi-asserted-by":"publisher","first-page":"4877","DOI":"10.1038\/sj.emboj.7601360","volume":"25","author":"T. Kirisako","year":"2006","unstructured":"Kirisako, T., Kamei, K., Murata, S., Kato, M., Fukumoto, H., Kanie, M., Sano, S., Tokunaga, F., Tanaka, K., and Iwai, K. (2006) A ubiquitin ligase complex assembles lin\u2013ear polyubiquitin chains, EMBO J., 25, 4877\u20134887.","journal-title":"EMBO J."},{"key":"762_CR157","doi-asserted-by":"publisher","first-page":"7704","DOI":"10.1073\/pnas.0908764107","volume":"107","author":"S. Zhao","year":"2010","unstructured":"Zhao, S., and Ulrich, H. D. (2010) Distinct consequences of posttranslational modification by linear versus K63\u2013linked polyubiquitin chains, Proc. Natl. Acad. Sci. USA, 107, 7704\u20137709.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"762_CR158","doi-asserted-by":"publisher","first-page":"354","DOI":"10.1016\/j.molcel.2010.12.029","volume":"41","author":"K.S. Inn","year":"2011","unstructured":"Inn, K.\u2013S., Gack, M. U., Tokunaga, F., Shi, M., Wong, L.\u2013Y., Iwai, K., and Jung, J. U. (2011) Linear ubiquitin assembly complex negatively regulates RIG\u2013I\u2013and TRIM25\u2013mediated type I interferon induction, Mol. Cell, 41, 354\u2013365.","journal-title":"Mol. Cell"},{"key":"762_CR159","doi-asserted-by":"publisher","first-page":"504","DOI":"10.1038\/nmeth.4228","volume":"14","author":"K. Kliza","year":"2017","unstructured":"Kliza, K., Taumer, C., Pinzuti, I., Franz\u2013Wachtel, M., Kunzelmann, S., Stieglitz, B., Macek, B., and Husnjak, K. (2017) Internally tagged ubiquitin: a tool to identify lin\u2013ear polyubiquitin\u2013modified proteins by mass spectrometry, Nat. Methods, 14, 504\u2013512.","journal-title":"Nat. Methods"},{"key":"762_CR160","doi-asserted-by":"publisher","first-page":"496","DOI":"10.1016\/j.molcel.2009.01.023","volume":"33","author":"Y. Kravtsova\u2013Ivantsiv","year":"2009","unstructured":"Kravtsova\u2013Ivantsiv, Y., Cohen, S., and Ciechanover, A. (2009) Modification by single ubiquitin moieties rather than polyubiquitination is sufficient for proteasomal processing of the p105 NF\u2013kappaB precursor, Mol. Cell, 33, 496\u2013504.","journal-title":"Mol. Cell"},{"key":"762_CR161","doi-asserted-by":"publisher","first-page":"4639","DOI":"10.1073\/pnas.1608644113","volume":"113","author":"O. Braten","year":"2016","unstructured":"Braten, O., Livneh, I., Ziv, T., Admon, A., Kehat, I., Caspi, L. H., Gonen, H., Bercovich, B., Godzik, A., Jahandideh, S., Jaroszewski, L., Sommer, T., Kwon, Y. T., Guharoy, M., Tompa, P., and Ciechanover, A. (2016) Numerous proteins with unique characteristics are degrad\u2013ed by the 26S proteasome following monoubiquitination, Proc. Natl. Acad. Sci. USA, 113, 4639\u20134647.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"762_CR162","doi-asserted-by":"publisher","first-page":"796","DOI":"10.1021\/pr200668y","volume":"11","author":"K. Oshikawa","year":"2012","unstructured":"Oshikawa, K., Matsumoto, M., Oyamada, K., and Nakayama, K. I. (2012) Proteome\u2013wide identification of ubiquitylation sites by conjugation of engineered lysine\u2013less ubiquitin, J. Proteome Res., 11, 796\u2013807.","journal-title":"J. Proteome Res."},{"key":"762_CR163","first-page":"399","volume":"26","author":"K. N. Swatek","year":"2016","unstructured":"Swatek, K. N., and Komander, D. (2016) Ubiquitin mod\u2013ifications, Nat. Publ. Gr., 26, 399\u2013422.","journal-title":"Nat. Publ. Gr."},{"key":"762_CR164","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1038\/nature09299","volume":"467","author":"B.H. Lee","year":"2010","unstructured":"Lee, B.\u2013H., Lee, M. J., Park, S., Oh, D.\u2013C., Elsasser, S., Chen, P.\u2013C., Gartner, C., Dimova, N., Hanna, J., Gygi, S. P., Wilson, S. M., King, R. W., and Finley, D. (2010) Enhancement of proteasome activity by a small\u2013molecule inhibitor of USP14, Nature, 467, 179\u2013184.","journal-title":"Nature"},{"key":"762_CR165","doi-asserted-by":"publisher","first-page":"1636","DOI":"10.1038\/nm.2536","volume":"17","author":"P. D\u2019Arcy","year":"2011","unstructured":"D\u2019Arcy, P., Brnjic, S., Olofsson, M. H., Fryknas, M., Lindsten, K., De Cesare, M., Perego, P., Sadeghi, B., Hassan, M., Larsson, R., and Linder, S. (2011) Inhibition of proteasome deubiquitinating activity as a new cancer therapy, Nat. Med., 17, 1636\u20131640.","journal-title":"Nat. Med."},{"key":"762_CR166","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/j.chembiol.2012.01.003","volume":"19","author":"A. F. v d Kisselev","year":"2012","unstructured":"Kisselev, A. F., van der Linden, W. A., and Overkleeft, H. S. (2012) Proteasome inhibitors: an expanding army attacking a unique target, Chem. Biol., 19, 99\u2013115.","journal-title":"Chem. Biol."},{"key":"762_CR167","doi-asserted-by":"publisher","first-page":"487","DOI":"10.1083\/jcb.200401141","volume":"166","author":"J. McCullough","year":"2004","unstructured":"McCullough, J., Clague, M. J., and Urbe, S. (2004) AMSH is an endosome\u2013associated ubiquitin isopeptidase, J. Cell Biol., 166, 487\u2013492.","journal-title":"J. Cell Biol."},{"key":"762_CR168","doi-asserted-by":"publisher","first-page":"113","DOI":"10.1371\/journal.pbio.0020113","volume":"2","author":"X. I. Ambroggio","year":"2004","unstructured":"Ambroggio, X. I., Rees, D. C., and Deshaies, R. J. (2004) JAMM: a metalloprotease\u2013like zinc site in the proteasome and signalosome, PLoS Biol., 2, 113\u2013119.","journal-title":"PLoS Biol."},{"key":"762_CR169","doi-asserted-by":"publisher","first-page":"608","DOI":"10.1126\/science.1075901","volume":"298","author":"G. A. Cope","year":"2002","unstructured":"Cope, G. A., Suh, G. S. B., Aravind, L., Schwarz, S. E., Zipursky, S. L., Koonin, E. V., and Deshaies, R. J. (2002) Role of predicted metalloprotease motif of Jab1\/Csn5 in cleavage of Nedd8 from Cul1, Science, 298, 608\u2013611.","journal-title":"Science"},{"key":"762_CR170","doi-asserted-by":"publisher","first-page":"3199","DOI":"10.1021\/bi5003162","volume":"53","author":"R. K. Shrestha","year":"2014","unstructured":"Shrestha, R. K., Ronau, J. A., Davies, C. W., Guenette, R. G., Strieter, E. R., Paul, L. N., and Das, C. (2014) Insights into the mechanism of deubiquitination by JAMM deubiq\u2013uitinases from cocrystal structures of the enzyme with the substrate and product, Biochemistry, 53, 3199\u20133217.","journal-title":"Biochemistry"},{"key":"762_CR171","doi-asserted-by":"publisher","first-page":"275","DOI":"10.1042\/BJ20040008","volume":"381","author":"T. Rinaldi","year":"2004","unstructured":"Rinaldi, T., Pick, E., Gambadoro, A., Zilli, S., Maytal\u2013Kivity, V., Frontali, L., and Glickman, M. H. (2004) Participation of the proteasomal lid subunit Rpn11 in mitochondrial morphology and function is mapped to a distinct C\u2013terminal domain, Biochem. J., 381, 275\u2013285.","journal-title":"Biochem. J."},{"key":"762_CR172","doi-asserted-by":"publisher","first-page":"220","DOI":"10.1038\/nsmb.2771","volume":"21","author":"E. J. Worden","year":"2014","unstructured":"Worden, E. J., Padovani, C., and Martin, A. (2014) Structure of the Rpn11\u2013Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degrada\u2013tion, Nat. Struct. Mol. Biol., 21, 220\u2013227.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"762_CR173","doi-asserted-by":"publisher","first-page":"398","DOI":"10.1038\/nature17433","volume":"532","author":"B.H. Lee","year":"2016","unstructured":"Lee, B.\u2013H., Lu, Y., Prado, M. A., Shi, Y., Tian, G., Sun, S., Elsasser, S., Gygi, S. P., King, R. W., and Finley, D. (2016) USP14 deubiquitinates proteasome\u2013bound sub\u2013strates that are ubiquitinated at multiple sites, Nature, 532, 398\u2013401.","journal-title":"Nature"},{"key":"762_CR174","doi-asserted-by":"publisher","first-page":"220","DOI":"10.1038\/nsmb.2771","volume":"21","author":"E. J. Worden","year":"2014","unstructured":"Worden, E. J., Padovani, C., and Martin, A. (2014) Structure of the Rpn11\u2013Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degrada\u2013tion, Nat. Struct. Mol. Biol., 21, 220\u2013227.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"762_CR175","doi-asserted-by":"publisher","first-page":"2984","DOI":"10.1073\/pnas.1400546111","volume":"111","author":"G. R. Pathare","year":"2014","unstructured":"Pathare, G. R., Nagy, I., Sledz, P., Anderson, D. J., Zhou, H.\u2013J., Pardon, E., Steyaert, J., Forster, F., Bracher, A., and Baumeister, W. (2014) Crystal structure of the proteasomal deubiquitylation module Rpn8\u2013Rpn11, Proc. Natl. Acad. Sci. USA, 111, 2984\u20132989.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"762_CR176","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.13027","volume-title":"Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition","author":"C. M. Dambacher","year":"2016","unstructured":"Dambacher, C. M., Worden, E. J., Herzik, M. A., Martin, A., and Lander, G. C. (2016) Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition, Elife, 5, e13027."},{"key":"762_CR177","doi-asserted-by":"publisher","first-page":"799","DOI":"10.1016\/j.molcel.2017.07.023","volume":"67","author":"E. J. Worden","year":"2017","unstructured":"Worden, E. J., Dong, K. C., and Martin, A. (2017) An AAA motor\u2013driven mechanical switch in Rpn11 controls deubiquitination at the 26S proteasome, Mol. Cell, 67, 799\u2013811.","journal-title":"Mol. Cell"},{"key":"762_CR178","doi-asserted-by":"publisher","first-page":"477","DOI":"10.1146\/annurev.biochem.78.081507.101607","volume":"78","author":"D. Finley","year":"2009","unstructured":"Finley, D. (2009) Recognition and processing of ubiqui\u2013tin\u2013protein conjugates by the proteasome, Annu. Rev. Biochem., 78, 477\u2013513.","journal-title":"Annu. Rev. Biochem."},{"key":"762_CR179","doi-asserted-by":"publisher","first-page":"5187","DOI":"10.1093\/emboj\/20.18.5187","volume":"20","author":"A. Borodovsky","year":"2001","unstructured":"Borodovsky, A., Kessler, B. M., Casagrande, R., Overkleeft, H. S., Wilkinson, K. D., and Ploegh, H. L. (2001) A novel active site\u2013directed probe specific for deu\u2013biquitylating enzymes reveals proteasome association of USP14, EMBO J., 20, 5187\u20135196.","journal-title":"EMBO J."},{"key":"762_CR180","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/j.cell.2006.07.038","volume":"127","author":"J. Hanna","year":"2006","unstructured":"Hanna, J., Hathaway, N. A., Tone, Y., Crosas, B., Elsasser, S., Kirkpatrick, D. S., Leggett, D. S., Gygi, S. P., King, R. W., and Finley, D. (2006) Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degrada\u2013tion, Cell, 127, 99\u2013111.","journal-title":"Cell"},{"key":"762_CR181","doi-asserted-by":"publisher","first-page":"1729","DOI":"10.1074\/jbc.M307050200","volume":"279","author":"A. Guterman","year":"2004","unstructured":"Guterman, A., and Glickman, M. H. (2004) Complementary roles for Rpn11 and Ubp6 in deubiquiti\u2013nation and proteolysis by the proteasome, J. Biol. Chem., 279, 1729\u20131738.","journal-title":"J. Biol. Chem."},{"key":"762_CR182","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1016\/S1097-2765(02)00638-X","volume":"10","author":"D. S. Leggett","year":"2002","unstructured":"Leggett, D. S., Hanna, J., Borodovsky, A., Crosas, B., Schmidt, M., Baker, R. T., Walz, T., Ploegh, H., and Finley, D. (2002) Multiple associated proteins regulate proteasome structure and function, Mol. Cell, 10, 495\u2013507.","journal-title":"Mol. Cell"},{"key":"762_CR183","doi-asserted-by":"publisher","first-page":"9830","DOI":"10.1074\/jbc.M116.763128","volume":"292","author":"H. T. Kim","year":"2017","unstructured":"Kim, H. T., and Goldberg, A. L. (2017) The deubiquiti\u2013nating enzyme Usp14 allosterically inhibits multiple pro\u2013teasomal activities and ubiquitin\u2013independent proteolysis, J. Biol. Chem., 292, 9830\u20139839.","journal-title":"J. Biol. Chem."},{"key":"762_CR184","doi-asserted-by":"publisher","first-page":"712","DOI":"10.1038\/nsmb.3075","volume":"22","author":"C. Bashore","year":"2015","unstructured":"Bashore, C., Dambacher, C. M., Goodall, E. A., Matyskiela, M. E., Lander, G. C., and Martin, A. (2015) Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome, Nat. Struct. Mol. Biol., 22, 712\u2013719.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"762_CR185","doi-asserted-by":"publisher","first-page":"8626","DOI":"10.1073\/pnas.1510449112","volume":"112","author":"A. Aufderheide","year":"2015","unstructured":"Aufderheide, A., Beck, F., Stengel, F., Hartwig, M., Schweitzer, A., Pfeifer, G., Goldberg, A. L., Sakata, E., Baumeister, W., and Forster, F. (2015) Structural charac\u2013terization of the interaction of Ubp6 with the 26S protea\u2013some, Proc. Natl. Acad. Sci. USA, 112, 8626\u20138631.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"762_CR186","doi-asserted-by":"publisher","first-page":"4688","DOI":"10.1074\/jbc.M114.568295","volume":"290","author":"W. Mansour","year":"2015","unstructured":"Mansour, W., Nakasone, M. A., von Delbruck, M., Yu, Z., Krutauz, D., Reis, N., Kleifeld, O., Sommer, T., Fushman, D., and Glickman, M. H. (2015) Disassembly of Lys11 and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiqui\u2013tinases Rpn11 and Ubp6, J. Biol. Chem., 290, 4688\u20134704.","journal-title":"J. Biol. Chem."},{"key":"762_CR187","doi-asserted-by":"publisher","first-page":"649","DOI":"10.1002\/prot.23147","volume":"80","author":"S. E. Burgie","year":"2012","unstructured":"Burgie, S. E., Bingman, C. A., Soni, A. B., and Phillips, G. N., Jr. (2012) Structural characterization of human Uch37, Proteins, 80, 649\u2013654.","journal-title":"Proteins"},{"key":"762_CR188","doi-asserted-by":"publisher","first-page":"901","DOI":"10.1016\/j.molcel.2015.01.016","volume":"57","author":"R. T. VanderLinden","year":"2015","unstructured":"VanderLinden, R. T., Hemmis, C. W., Schmitt, B., Ndoja, A., Whitby, F. G., Robinson, H., Cohen, R. E., Yao, T., and Hill, C. P. (2015) Structural basis for the activation and inhibition of the UCH37 deubiquitylase, Mol. Cell, 57, 901\u2013911.","journal-title":"Mol. Cell"},{"key":"762_CR189","doi-asserted-by":"publisher","first-page":"887","DOI":"10.1016\/j.molcel.2014.12.039","volume":"57","author":"D. D. v Sahtoe","year":"2015","unstructured":"Sahtoe, D. D., van Dijk, W. J., El Oualid, F., Ekkebus, R., Ovaa, H., and Sixma, T. K. (2015) Mechanism of UCH\u2013L5 activation and inhibition by DEUBAD domains in RPN13 and INO80G, Mol. Cell, 57, 887\u2013900.","journal-title":"Mol. Cell"},{"key":"762_CR190","doi-asserted-by":"publisher","first-page":"404","DOI":"10.1016\/j.molcel.2010.04.019","volume":"38","author":"X. L. B.\u2013H. Chen","year":"2010","unstructured":"Chen, X., Lee, B.\u2013H., Finley, D., and Walters, K. J. (2010) Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2, Mol. Cell, 38, 404\u2013415.","journal-title":"Mol. Cell"},{"key":"762_CR191","doi-asserted-by":"publisher","first-page":"737","DOI":"10.1038\/385737a0","volume":"385","author":"Y. A. Lam","year":"1997","unstructured":"Lam, Y. A., Xu, W., DeMartino, G. N., and Cohen, R. E. (1997) Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome, Nature, 385, 737\u2013740.","journal-title":"Nature"},{"key":"762_CR192","doi-asserted-by":"publisher","first-page":"25540","DOI":"10.1074\/jbc.M111.260505","volume":"286","author":"N.Y. Zhang","year":"2011","unstructured":"Zhang, N.\u2013Y., Jacobson, A. D., MacFadden, A., and Liu, C.\u2013W. (2011) Ubiquitin chain trimming recycles the sub\u2013strate binding sites of the 26S proteasome and promotes degradation of lysine 48\u2013linked polyubiquitin conjugates, J. Biol. Chem., 286, 25540\u201325546.","journal-title":"J. Biol. Chem."},{"key":"762_CR193","doi-asserted-by":"publisher","first-page":"12991","DOI":"10.1073\/pnas.1614614113","volume":"113","author":"S. Chen","year":"2016","unstructured":"Chen, S., Wu, J., Lu, Y., Ma, Y.\u2013B., Lee, B.\u2013H., Yu, Z., Ouyang, Q., Finley, D. J., Kirschner, M. W., and Mao, Y. (2016) Structural basis for dynamic regulation of the human 26S proteasome, Proc. Natl. Acad. Sci. USA, 113, 12991\u201312996.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"762_CR194","doi-asserted-by":"publisher","first-page":"7781","DOI":"10.1074\/jbc.M112.441907","volume":"288","author":"A. Peth","year":"2013","unstructured":"Peth, A., Kukushkin, N., Bosse, M., and Goldberg, A. L. (2013) Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 homologs, J. Biol. Chem., 288, 7781\u20137790.","journal-title":"J. Biol. Chem."},{"key":"762_CR195","doi-asserted-by":"publisher","first-page":"2583","DOI":"10.1091\/mbc.10.8.2583","volume":"10","author":"S. Swaminathan","year":"1999","unstructured":"Swaminathan, S., Amerik, A. Y., and Hochstrasser, M. (1999) The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast, Mol. Biol. Cell, 10, 2583\u20132594.","journal-title":"Mol. Biol. Cell"},{"key":"762_CR196","doi-asserted-by":"publisher","first-page":"167","DOI":"10.1146\/annurev-biochem-051910-094049","volume":"81","author":"A. Varshavsky","year":"2012","unstructured":"Varshavsky, A. (2012) The ubiquitin system, an immense realm, Annu. Rev. Biochem., 81, 167\u2013176.","journal-title":"Annu. Rev. Biochem."},{"key":"762_CR197","doi-asserted-by":"publisher","first-page":"1401","DOI":"10.1016\/j.cell.2006.09.051","volume":"127","author":"B. Crosas","year":"2006","unstructured":"Crosas, B., Hanna, J., Kirkpatrick, D. S., Zhang, D. P., Tone, Y., Hathaway, N. A., Buecker, C., Leggett, D. S., Schmidt, M., King, R. W., Gygi, S. P. P., and Finley, D. (2006) Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activi\u2013ties, Cell, 127, 1401\u20131413.","journal-title":"Cell"},{"key":"762_CR198","doi-asserted-by":"publisher","first-page":"1045","DOI":"10.1038\/nsmb1018","volume":"12","author":"L. Tian","year":"2005","unstructured":"Tian, L., Holmgren, R. A., and Matouschek, A. (2005) A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF\u2013\u03baB, Nat. Struct. Mol. Biol., 12, 1045\u20131053.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"762_CR199","doi-asserted-by":"publisher","first-page":"985","DOI":"10.1128\/MCB.00909-09","volume":"30","author":"S. Aviram","year":"2010","unstructured":"Aviram, S., and Kornitzer, D. (2010) The ubiquitin ligase Hul5 promotes proteasomal processivity, Mol. Cell Biol., 30, 985\u2013994.","journal-title":"Mol. Cell Biol."},{"key":"762_CR200","doi-asserted-by":"publisher","first-page":"889","DOI":"10.1021\/acs.chemrev.6b00737","volume":"118","author":"L. Cappadocia","year":"2018","unstructured":"Cappadocia, L., and Lima, C. D. (2018) Ubiquitin\u2013like protein conjugation: structures, chemistry, and mecha\u2013nism, Chem. Rev., 118, 889\u2013918.","journal-title":"Chem. Rev."},{"key":"762_CR201","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1016\/S0962-8924(00)01785-2","volume":"10","author":"S. Jentsch","year":"2000","unstructured":"Jentsch, S., and Pyrowolakis, G. (2000) Ubiquitin and its kin: how close are the family ties? Trends Cell Biol., 10, 335\u2013342.","journal-title":"Trends Cell Biol."},{"key":"762_CR202","doi-asserted-by":"publisher","first-page":"1169","DOI":"10.1038\/sj.embor.7400025","volume":"4","author":"J. Luders","year":"2003","unstructured":"Luders, J., Pyrowolakis, G., and Jentsch, S. (2003) The ubiquitin\u2013like protein HUB1 forms SDS\u2013resistant com\u2013plexes with cellular proteins in the absence of ATP, EMBO Rep., 4, 1169\u20131174.","journal-title":"EMBO Rep."},{"key":"762_CR203","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1186\/1471-2105-6-22","volume":"6","author":"M. Novatchkova","year":"2005","unstructured":"Novatchkova, M., Bachmair, A., Eisenhaber, B., and Eisenhaber, F. (2005) Proteins with two SUMO\u2013like domains in chromatin\u2013associated complexes: the RENi (Rad60\u2013Esc2\u2013NIP45) family, BMC Bioinformatics, 6, 22.","journal-title":"BMC Bioinformatics"},{"key":"762_CR204","doi-asserted-by":"publisher","first-page":"779","DOI":"10.1016\/j.tibs.2015.09.006","volume":"40","author":"K. Eifler","year":"2015","unstructured":"Eifler, K., and Vertegaal, A. C. O. (2015) SUMOylation\u2013mediated regulation of cell cycle progression and cancer, Trends Biochem. Sci., 40, 779\u2013793.","journal-title":"Trends Biochem. Sci."},{"key":"762_CR205","doi-asserted-by":"publisher","first-page":"357","DOI":"10.1146\/annurev-biochem-061909-093311","volume":"82","author":"A. Flotho","year":"2013","unstructured":"Flotho, A., and Melchior, F. (2013) Sumoylation: a regu\u2013latory protein modification in health and disease, Annu. Rev. Biochem., 82, 357\u2013385.","journal-title":"Annu. Rev. Biochem."},{"key":"762_CR206","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1016\/j.bbamcr.2013.01.009","volume":"1843","author":"G. Schmidtke","year":"2014","unstructured":"Schmidtke, G., Aichem, A., and Groettrup, M. (2014) FAT10ylation as a signal for proteasomal degradation, Biochim. Biophys. Acta, 1843, 97\u2013102.","journal-title":"Biochim. Biophys. Acta"},{"key":"762_CR207","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/ncomms1012","volume":"1","author":"A. Aichem","year":"2010","unstructured":"Aichem, A., Pelzer, C., Lukasiak, S., Kalveram, B., Sheppard, P. W., Rani, N., Schmidtke, G., and Groettrup, M. (2010) USE1 is a bispecific conjugating enzyme for ubiquitin and FAT10, which FAT10ylates itself in cis, Nat. Commun., 1, 1\u201310.","journal-title":"Nat. Commun."},{"key":"762_CR208","doi-asserted-by":"publisher","first-page":"238","DOI":"10.1007\/978-1-4419-6676-6_19","volume":"54","author":"C. Pelzer","year":"2010","unstructured":"Pelzer, C., and Groettrup, M. (2010) FAT10: activated by UBA6 and functioning in protein degradation, Subcell Biochem., 54, 238\u2013246.","journal-title":"Subcell Biochem."},{"key":"762_CR209","doi-asserted-by":"publisher","first-page":"5313","DOI":"10.1073\/pnas.1323426111","volume":"111","author":"A. Canaan","year":"2014","unstructured":"Canaan, A., DeFuria, J., Perelman, E., Schultz, V., Seay, M., Tuck, D., Flavell, R. A., Snyder, M. P., Obin, M. S., and Weissman, S. M. (2014) Extended lifespan and reduced adiposity in mice lacking the FAT10 gene, Proc. Natl. Acad. Sci. USA, 111, 5313\u20135318.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"762_CR210","doi-asserted-by":"publisher","first-page":"5180","DOI":"10.1128\/MCB.00966-05","volume":"26","author":"A. Canaan","year":"2006","unstructured":"Canaan, A., Yu, X., Booth, C. J., Lian, J., Lazar, I., Gamfi, S. L., Castille, K., Kohya, N., Nakayama, Y., Liu, Y.\u2013C., Eynon, E., Flavell, R., and Weissman, S. M. (2006) FAT10\/diubiquitin\u2013like protein\u2013deficient mice exhibit minimal phenotypic differences, Mol. Cell Biol., 26, 5180\u20135189.","journal-title":"Mol. Cell Biol."},{"key":"762_CR211","doi-asserted-by":"publisher","first-page":"225","DOI":"10.1091\/mbc.e11-07-0609","volume":"23","author":"S. Buchsbaum","year":"2012","unstructured":"Buchsbaum, S., Bercovich, B., and Ciechanover, A. (2012) FAT10 is a proteasomal degradation signal that is itself reg\u2013ulated by ubiquitination, Mol. Biol. Cell, 23, 225\u2013232.","journal-title":"Mol. Biol. Cell"},{"key":"762_CR212","doi-asserted-by":"publisher","first-page":"1970","DOI":"10.1074\/jbc.273.4.1970","volume":"273","author":"H. Fu","year":"1998","unstructured":"Fu, H., Sadis, S., Rubin, D. M., Glickman, M., van Nocker, S., Finley, D., and Vierstra, R. D. (1998) Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26S proteasome subunit Mcb1, J. Biol. Chem., 273, 1970\u20131981.","journal-title":"J. Biol. Chem."},{"key":"762_CR213","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1038\/416763a","volume":"416","author":"Y. A. Lam","year":"2002","unstructured":"Lam, Y. A., Lawson, T. G., Velayutham, M., Zweier, J. L., and Pickart, C. M. (2002) A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal, Nature, 416, 763\u2013767.","journal-title":"Nature"},{"key":"762_CR214","doi-asserted-by":"publisher","first-page":"453","DOI":"10.1016\/j.molcel.2014.09.008","volume":"56","author":"K. Paraskevopoulos","year":"2014","unstructured":"Paraskevopoulos, K., Kriegenburg, F., Tatham, M. H., Rosner, H. I., Medina, B., Larsen, I. B., Brandstrup, R., Hardwick, K. G., Hay, R. T., Kragelund, B. B., Hartmann\u2013Petersen, R., and Gordon, C. (2014) Dss1 is a 26S proteasome ubiquitin receptor, Mol. Cell, 56, 453\u2013461.","journal-title":"Mol. Cell"},{"key":"762_CR215","doi-asserted-by":"crossref","first-page":"7059","DOI":"10.1016\/S0021-9258(17)37244-7","volume":"269","author":"Q. Deveraux","year":"1994","unstructured":"Deveraux, Q., Ustrell, V., Pickart, C., and Rechsteiner, M. (1994) A 26S protease subunit that binds ubiquitin conju\u2013gates, J. Biol. Chem., 269, 7059\u20137061.","journal-title":"J. Biol. Chem."},{"key":"762_CR216","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pgen.1005401","volume-title":"Redundant roles of Rpn10 and Rpn13 in recognition of ubiquitinated proteins and cellular homeostasis","author":"J. Hamazaki","year":"2015","unstructured":"Hamazaki, J., Hirayama, S., and Murata, S. (2015) Redundant roles of Rpn10 and Rpn13 in recognition of ubiquitinated proteins and cellular homeostasis, PLOS Genet., 11, e1005401."},{"key":"762_CR217","doi-asserted-by":"publisher","first-page":"415","DOI":"10.1016\/j.molcel.2008.10.011","volume":"32","author":"Y. Matiuhin","year":"2008","unstructured":"Matiuhin, Y., Kirkpatrick, D. S., Ziv, I., Kim, W., Dakshinamurthy, A., Kleifeld, O., Gygi, S. P., Reis, N., and Glickman, M. H. (2008) Extraproteasomal Rpn10 restricts access of the polyubiquitin\u2013binding protein Dsk2 to proteasome, Mol. Cell, 32, 415\u2013425.","journal-title":"Mol. Cell"},{"key":"762_CR218","doi-asserted-by":"publisher","first-page":"12960","DOI":"10.1038\/ncomms12960","volume":"7","author":"T. Z. Keren\u2013Kaplan","year":"2016","unstructured":"Keren\u2013Kaplan, T., Zeev Peters, L., Levin\u2013Kravets, O., Attali, I., Kleifeld, O., Shohat, N., Artzi, S., Zucker, O., Pilzer, I., Reis, N., Glickman, M. H., Ben\u2013Aroya, S., and Prag, G. (2016) Structure of ubiquitylated\u2013Rpn10 provides insight into its autoregulation mechanism, Nat. Commun., 7, 12960.","journal-title":"Nat. Commun."},{"key":"762_CR219","doi-asserted-by":"publisher","first-page":"1027","DOI":"10.1016\/j.jmb.2005.12.001","volume":"356","author":"Y. Kang","year":"2006","unstructured":"Kang, Y., Vossler, R. A., Diaz\u2013Martinez, L. A., Winter, N. S., Clarke, D. J., and Walters, K. J. (2006) UBL\/UBA ubiquitin receptor proteins bind a common tetraubiquitin chain, J. Mol. Biol., 356, 1027\u20131035.","journal-title":"J. Mol. Biol."},{"key":"762_CR220","doi-asserted-by":"publisher","first-page":"1246","DOI":"10.1038\/ncb1484","volume":"8","author":"T. Woelk","year":"2006","unstructured":"Woelk, T., Oldrini, B., Maspero, E., Confalonieri, S., Cavallaro, E., Di Fiore, P. P., and Polo, S. (2006) Molecular mechanisms of coupled monoubiquitination, Nat. Cell Biol., 8, 1246\u20131254.","journal-title":"Nat. Cell Biol."},{"key":"762_CR221","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/j.cell.2004.06.014","volume":"118","author":"R. Verma","year":"2004","unstructured":"Verma, R., Oania, R., Graumann, J., and Deshaies, R. J. (2004) Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin\u2013proteasome system, Cell, 118, 99\u2013110.","journal-title":"Cell"},{"key":"762_CR222","doi-asserted-by":"publisher","first-page":"727","DOI":"10.1016\/j.jmb.2005.03.007","volume":"348","author":"Q. Wang","year":"2005","unstructured":"Wang, Q., Young, P., and Walters, K. J. (2005) Structure of S5a bound to monoubiquitin provides a model for polyu\u2013biquitin recognition, J. Mol. Biol., 348, 727\u2013739.","journal-title":"J. Mol. Biol."},{"key":"762_CR223","doi-asserted-by":"publisher","first-page":"6020","DOI":"10.1128\/MCB.16.11.6020","volume":"16","author":"S. Van Nocker","year":"1996","unstructured":"Van Nocker, S., Sadis, S., Rubin, D. M., Glickman, M., Fu, H., Coux, O., Wefes, I., Finley, D., and Vierstra, R. D. (1996) The multiubiquitin\u2013chain\u2013binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate\u2013specific role in protein turnover, Mol. Cell. Biol., 16, 6020\u20136028.","journal-title":"Mol. Cell. Biol."},{"key":"762_CR224","doi-asserted-by":"publisher","first-page":"6629","DOI":"10.1128\/MCB.00509-07","volume":"27","author":"J. Hamazaki","year":"2007","unstructured":"Hamazaki, J., Sasaki, K., Kawahara, H., Hisanaga, S.\u2013I., Tanaka, K., and Murata, S. (2007) Rpn10\u2013mediated degradation of ubiquitinated proteins is essential for mouse development, Mol. Cell. Biol., 27, 6629\u20136638.","journal-title":"Mol. Cell. Biol."},{"key":"762_CR225","volume-title":"Regulators of the proteasome pathway","author":"A. Al\u2013Shami","year":"2010","unstructured":"Al\u2013Shami, A., Jhaver, K. G., Vogel, P., Wilkins, C., Humphries, J., Davis, J. J., Xu, N., Potter, D. G., Gerhardt, B., Mullinax, R., Shirley, C. R., Anderson, S. J., and Oravecz, T. (2010) Regulators of the proteasome pathway, Uch37 and Rpn13, play distinct roles in mouse development, PLoS One, 5, e13654."},{"key":"762_CR226","doi-asserted-by":"publisher","first-page":"641","DOI":"10.1023\/A:1006790912877","volume":"17","author":"A. B. Simins","year":"1999","unstructured":"Simins, A. B., Weighardt, H., Weidner, K. M., Weidle, U. H., and Holzmann, B. (1999) Functional cloning of ARM\u20131, an adhesion\u2013regulating molecule upregulated in metastatic tumor cells, Clin. Exp. Metastasis, 17, 641\u2013648.","journal-title":"Clin. Exp. Metastasis"},{"key":"762_CR227","doi-asserted-by":"publisher","first-page":"4524","DOI":"10.1038\/sj.emboj.7601338","volume":"25","author":"J. Hamazaki","year":"2006","unstructured":"Hamazaki, J., Iemura, S., Natsume, T., Yashiroda, H., Tanaka, K., and Murata, S. (2006) A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes, EMBO J., 25, 4524\u20134536.","journal-title":"EMBO J."},{"key":"762_CR228","doi-asserted-by":"publisher","first-page":"994","DOI":"10.1038\/ncb1460","volume":"8","author":"T. Yao","year":"2006","unstructured":"Yao, T., Song, L., Xu, W., DeMartino, G. N., Florens, L., Swanson, S. K., Washburn, M. P., Conaway, R. C., Conaway, J. W., and Cohen, R. E. (2006) Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1, Nat. Cell Biol., 8, 994\u20131002.","journal-title":"Nat. Cell Biol."},{"key":"762_CR229","doi-asserted-by":"publisher","first-page":"13854","DOI":"10.1073\/pnas.0913495107","volume":"107","author":"T. Mazumdar","year":"2010","unstructured":"Mazumdar, T., Gorgun, F. M., Sha, Y., Tyryshkin, A., Zeng, S., Hartmann\u2013Petersen, R., Jorgensen, J. P., Hendil, K. B., and Eissa, N. T. (2010) Regulation of NF\u2013kappaB activity and inducible nitric oxide synthase by reg\u2013ulatory particle non\u2013ATPase subunit 13 (Rpn13), Proc. Natl. Acad. Sci. USA, 107, 13854\u201313859.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"762_CR230","doi-asserted-by":"publisher","first-page":"959","DOI":"10.18632\/aging.100249","volume":"2","author":"Y. Huang","year":"2010","unstructured":"Huang, Y., and Ratovitski, E. A. (2010) Phospho\u2013\u0394Np63\u03b1\/Rpn13\u2013dependent regulation of LKB1 degrada\u2013tion modulates autophagy in cancer cells, Aging (Albany. NY), 2, 959\u2013968.","journal-title":"Aging (Albany. NY)"},{"key":"762_CR231","doi-asserted-by":"publisher","first-page":"1539","DOI":"10.1126\/science.1160794","volume":"322","author":"G. Sabio","year":"2008","unstructured":"Sabio, G., Das, M., Mora, A., Zhang, Z., Jun, J. Y., Ko, H. J., Barrett, T., Kim, J. K., and Davis, R. J. (2008) A stress signaling pathway in adipose tissue regulates hepatic insulin resistance, Science, 322, 1539\u20131543.","journal-title":"Science"},{"key":"762_CR232","doi-asserted-by":"publisher","first-page":"7492","DOI":"10.1074\/jbc.M114.614925","volume":"290","author":"M. A. Aguileta","year":"2015","unstructured":"Aguileta, M. A., Korac, J., Durcan, T. M., Trempe, J.\u2013F., Haber, M., Gehring, K., Elsasser, S., Waidmann, O., Fon, E. A., and Husnjak, K. (2015) The E3 ubiquitin ligase parkin is recruited to the 26S proteasome via the proteaso\u2013mal ubiquitin receptor Rpn13, J. Biol. Chem., 290, 7492\u20137505.","journal-title":"J. Biol. Chem."},{"key":"762_CR233","first-page":"283","volume":"28","author":"X. Miao","year":"2012","unstructured":"Miao, X., Miao, X., Wen, Y., Hu, J., Dai, W., and Yin, B. (2012) A possible connection between adhesion regulating molecule 1 overexpression and nuclear factor kappa B activity in hepatocarcinogenesis, Oncol. Rep., 28, 283\u2013290.","journal-title":"Oncol. Rep."},{"key":"762_CR234","doi-asserted-by":"publisher","first-page":"1877","DOI":"10.1038\/leu.2016.97","volume":"30","author":"Y. Song","year":"2016","unstructured":"Song, Y., Ray, A., Li, S., Das, D. S., Tai, Y. T., Carrasco, R. D., Chauhan, D., and Anderson, K. C. (2016) Targeting proteasome ubiquitin receptor Rpn13 in multi\u2013ple myeloma, Leukemia, 30, 1877\u20131886.","journal-title":"Leukemia"},{"key":"762_CR235","doi-asserted-by":"publisher","first-page":"3094","DOI":"10.3390\/ijms14023094","volume":"14","author":"M. Fejzo","year":"2013","unstructured":"Fejzo, M., Anderson, L., von Euw, E., Kalous, O., Avliyakulov, N., Haykinson, M., Konecny, G., Finn, R., and Slamon, D. (2013) Amplification target ADRM1: role as an oncogene and therapeutic target for ovarian cancer, Int. J. Mol. Sci., 14, 3094\u20133109.","journal-title":"Int. J. Mol. Sci."},{"key":"762_CR236","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1136\/gut.2007.143065","volume":"58","author":"B. Carvalho","year":"2009","unstructured":"Carvalho, B., Postma, C., Mongera, S., Hopmans, E., Diskin, S., van de Wiel, M. A., van Criekinge, W., Thas, O., Matthai, A., Cuesta, M. A., Droste, J. S. T. S., Craanen, M., Schrock, E., Ylstra, B., and Meijer, G. A. (2009) Multiple putative oncogenes at the chromosome 20q amplicon contribute to colorectal adenoma to carci\u2013noma progression, Gut, 58, 79\u201389.","journal-title":"Gut"},{"key":"762_CR237","doi-asserted-by":"publisher","first-page":"727","DOI":"10.1007\/s10585-014-9663-4","volume":"31","author":"S. H. Jang","year":"2014","unstructured":"Jang, S. H., Park, J. W., Kim, H. R., Seong, J. K., and Kim, H. K. (2014) ADRM1 gene amplification is a candi\u2013date driver for metastatic gastric cancers, Clin. Exp. Metastasis, 31, 727\u2013733.","journal-title":"Clin. Exp. Metastasis"},{"key":"762_CR238","doi-asserted-by":"publisher","first-page":"791","DOI":"10.1016\/j.ccr.2013.11.001","volume":"24","author":"R. K. Anchoori","year":"2013","unstructured":"Anchoori, R. K., Karanam, B., Peng, S., Wang, J. W., Jiang, R., Tanno, T., Orlowski, R. Z., Matsui, W., Zhao, M., Rudek, M. A., Hung, C., Chen, X., Walters, K. J., and Roden, R. B. S. (2013) A bis\u2013benzylidine piperidone tar\u2013geting proteasome ubiquitin receptor RPN13\/ADRM1 as a therapy for cancer, Cancer Cell, 24, 791\u2013805.","journal-title":"Cancer Cell"},{"key":"762_CR239","doi-asserted-by":"publisher","first-page":"6312","DOI":"10.1021\/jacs.5b02069","volume":"137","author":"D. J. Trader","year":"2015","unstructured":"Trader, D. J., Simanski, S., and Kodadek, T. (2015) A reversible and highly selective inhibitor of the proteasomal ubiquitin receptor Rpn13 is toxic to multiple myeloma cells, J. Am. Chem. Soc., 137, 6312\u20136319.","journal-title":"J. Am. Chem. Soc."},{"key":"762_CR240","doi-asserted-by":"publisher","first-page":"607","DOI":"10.2217\/fon.11.42","volume":"7","author":"M. L. Khan","year":"2011","unstructured":"Khan, M. L., and Stewart, A. K. (2011) Carfilzomib: a novel second\u2013generation proteasome inhibitor, Futur. Oncol., 7, 607\u2013612.","journal-title":"Futur. Oncol."},{"key":"762_CR241","doi-asserted-by":"publisher","first-page":"1257","DOI":"10.1016\/j.str.2016.05.018","volume":"24","author":"X. Chen","year":"2016","unstructured":"Chen, X., Randles, L., Shi, K., Tarasov, S. G., Aihara, H., and Walters, K. J. (2016) Structures of Rpn1T1:Rad23 and hRpn13:hPLIC2 reveal distinct binding mechanisms between substrate receptors and shuttle factors of the pro\u2013teasome, Structure, 24, 1257\u20131270.","journal-title":"Structure"},{"key":"762_CR242","doi-asserted-by":"publisher","first-page":"813","DOI":"10.1016\/S0006-291X(02)02002-8","volume":"296","author":"Y. Saeki","year":"2002","unstructured":"Saeki, Y., Sone, T., Toh\u2013e, A., and Yokosawa, H. (2002) Identification of ubiquitin\u2013like protein\u2013binding subunits of the 26S proteasome, Biochem. Biophys. Res. Commun., 296, 813\u2013819.","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"762_CR243","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1186\/1741-7007-9-33","volume":"9","author":"T. A. Gomez","year":"2011","unstructured":"Gomez, T. A., Kolawa, N., Gee, M., Sweredoski, M. J., and Deshaies, R. J. (2011) Identification of a functional docking site in the Rpn1 LRR domain for the UBA\u2013UBL domain protein Ddi1, BMC Biol., 9, 33.","journal-title":"BMC Biol."},{"key":"762_CR244","doi-asserted-by":"publisher","first-page":"428","DOI":"10.4161\/cib.15283","volume":"4","author":"A. Haapasalo","year":"2011","unstructured":"Haapasalo, A., Viswanathan, J., Kurkinen, K. M., Bertram, L., Soininen, H., Dantuma, N. P., Tanzi, R. E., and Hiltunen, M. (2011) Involvement of ubiquilin\u20131 tran\u2013script variants in protein degradation and accumulation, Commun. Integr. Biol., 4, 428\u2013432.","journal-title":"Commun. Integr. Biol."},{"key":"762_CR245","doi-asserted-by":"publisher","first-page":"708","DOI":"10.1038\/nsmb962","volume":"12","author":"S. Raasi","year":"2005","unstructured":"Raasi, S., Varadan, R., Fushman, D., and Pickart, C. M. (2005) Diverse polyubiquitin interaction properties of ubiquitin\u2013associated domains, Nat. Struct. Mol. Biol., 12, 708\u2013714.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"762_CR246","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1016\/j.cell.2004.11.013","volume":"120","author":"H. Richly","year":"2005","unstructured":"Richly, H., Rape, M., Braun, S., Rumpf, S., Hoege, C., and Jentsch, S. (2005) A series of ubiquitin binding factors connects CDC48\/p97 to substrate multiubiquitylation and proteasomal targeting, Cell, 120, 73\u201384.","journal-title":"Cell"},{"key":"762_CR247","doi-asserted-by":"publisher","first-page":"211","DOI":"10.1083\/jcb.200507149","volume":"172","author":"I. Kim","year":"2006","unstructured":"Kim, I., Ahn, J., Liu, C., Tanabe, K., Apodaca, J., Suzuki, T., and Rao, H. (2006) The Png1\u2013Rad23 complex regu\u2013lates glycoprotein turnover, J. Cell Biol., 172, 211\u2013219.","journal-title":"J. Cell Biol."},{"key":"762_CR248","doi-asserted-by":"publisher","first-page":"225","DOI":"10.1016\/j.molcel.2005.03.015","volume":"18","author":"S. Heessen","year":"2005","unstructured":"Heessen, S., Masucci, M. G., and Dantuma, N. P. (2005) The UBA2 domain functions as an intrinsic stabilization signal that protects rad23 from proteasomal degradation, Mol. Cell, 18, 225\u2013235.","journal-title":"Mol. Cell"},{"key":"762_CR249","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1038\/ncomms1179","volume":"2","author":"C. Heinen","year":"2011","unstructured":"Heinen, C., Acs, K., Hoogstraten, D., and Dantuma, N. P. (2011) C\u2013terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation, Nat. Commun., 2, 191.","journal-title":"Nat. Commun."},{"key":"762_CR250","first-page":"20235","volume":"271","author":"R. K. Vadlamudi","year":"1996","unstructured":"Vadlamudi, R. K., Joung, I., Strominger, J. L., and Shin, J. (1996) p62, a phosphotyrosine\u2013independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin\u2013binding proteins, J. Biol. Chem., 271, 20235\u201320237.","journal-title":"p62"},{"key":"762_CR251","doi-asserted-by":"publisher","first-page":"8055","DOI":"10.1128\/MCB.24.18.8055-8068.2004","volume":"24","author":"M. L. Seibenhener","year":"2004","unstructured":"Seibenhener, M. L., Babu, J. R., Geetha, T., Wong, H. C., Krishna, N. R., and Wooten, M. W. (2004) Sequestosome 1\/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation, Mol. Cell. Biol., 24, 8055\u20138068.","journal-title":"Mol. Cell. Biol."},{"key":"762_CR252","first-page":"24131","volume":"282","author":"S. Pankiv","year":"2007","unstructured":"Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.\u2013A., Outzen, H., Overvatn, A., Bjorkoy, G., and Johansen, T. (2007) p62\/SQSTM1 binds directly to Atg8\/LC3 to facilitate degradation of ubiquitinated pro\u2013tein aggregates by autophagy, J. Biol. Chem., 282, 24131\u201324145.","journal-title":"p62\/SQSTM1 binds directly to Atg8\/LC3 to facilitate degradation of ubiquitinated pro\u2013tein aggregates by autophagy, J. Biol. Chem."},{"key":"762_CR253","doi-asserted-by":"publisher","first-page":"857","DOI":"10.1016\/j.neuron.2010.11.036","volume":"68","author":"J. O. Johnson","year":"2010","unstructured":"Johnson, J. O., Mandrioli, J., Benatar, M., Abramzon, Y., Van Deerlin, V. M., Trojanowski, J. Q., Gibbs, J. R., Brunetti, M., Gronka, S., Wuu, J., Ding, J., McCluskey, L., Martinez\u2013Lage, M., Falcone, D., Hernandez, D. G., Arepalli, S., Chong, S., Schymick, J. C., Rothstein, J., Landi, F., Wang, Y.\u2013D., Calvo, A., Mora, G., Sabatelli, M., Monsurro, M. R., Battistini, S., Salvi, F., Spataro, R., Sola, P., Borghero, G., Galassi, G., Scholz, S. W., Taylor, J. P., Restagno, G., Chio, A., Traynor, B. J., and Traynor, B. J. (2010) Exome sequencing reveals VCP mutations as a cause of familial ALS, Neuron, 68, 857\u2013864.","journal-title":"Neuron"},{"key":"762_CR254","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1091\/mbc.9.1.131","volume":"9","author":"F. Madeo","year":"1998","unstructured":"Madeo, F., Schlauer, J., Zischka, H., Mecke, D., and Frohlich, K. U. (1998) Tyrosine phosphorylation regulates cell cycle\u2013dependent nuclear localization of Cdc48p, Mol. Biol. Cell, 9, 131\u2013141.","journal-title":"Mol. Biol. Cell"},{"key":"762_CR255","doi-asserted-by":"publisher","first-page":"653","DOI":"10.1016\/j.ccell.2015.10.002","volume":"28","author":"D. J. Anderson","year":"2015","unstructured":"Anderson, D. J., Le Moigne, R., Djakovic, S., Kumar, B., Rice, J., Wong, S., Wang, J., Yao, B., Valle, E., Kiss von Soly, S., Madriaga, A., Soriano, F., Menon, M.\u2013K., Wu, Z. Y., Kampmann, M., Chen, Y., Weissman, J. S., Aftab, B. T., Yakes, F. M., Shawver, L., Zhou, H.\u2013J., Wustrow, D., and Rolfe, M. (2015) Targeting the AAA ATPase p97 as an approach to treat cancer through disruption of pro\u2013tein homeostasis, Cancer Cell, 28, 653\u2013665.","journal-title":"Cancer Cell"},{"key":"762_CR256","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1016\/j.jsb.2006.01.005","volume":"156","author":"Y. Ye","year":"2006","unstructured":"Ye, Y. (2006) Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase, J. Struct. Biol., 156, 29\u201340.","journal-title":"J. Struct. Biol."},{"key":"762_CR257","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1038\/ncb2407","volume":"14","author":"H. Meyer","year":"2012","unstructured":"Meyer, H., Bug, M., and Bremer, S. (2012) Emerging functions of the VCP\/p97AAA\u2013ATPase in the ubiquitin system, Nat. Cell Biol., 14, 117\u2013123.","journal-title":"Nat. Cell Biol."},{"key":"762_CR258","doi-asserted-by":"publisher","first-page":"1164","DOI":"10.1038\/nsmb.2659","volume":"20","author":"R. Beckwith","year":"2013","unstructured":"Beckwith, R., Estrin, E., Worden, E. J., and Martin, A. (2013) Reconstitution of the 26S proteasome reveals func\u2013tional asymmetries in its AAA+ unfoldase, Nat. Struct. Mol. Biol., 20, 1164\u20131172.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"762_CR259","doi-asserted-by":"publisher","first-page":"161","DOI":"10.1038\/nchembio.521","volume":"7","author":"T. Inobe","year":"2011","unstructured":"Inobe, T., Fishbain, S., Prakash, S., and Matouschek, A. (2011) Defining the geometry of the two\u2013component pro\u2013teasome degron, Nat. Chem. Biol., 7, 161\u2013167.","journal-title":"Nat. Chem. Biol."},{"key":"762_CR260","doi-asserted-by":"publisher","first-page":"432","DOI":"10.1016\/j.sbi.2011.03.011","volume":"21","author":"M. M. Babu","year":"2011","unstructured":"Babu, M. M., van der Lee, R., de Groot, N. S., and Gsponer, J. (2011) Intrinsically disordered proteins: regu\u2013lation and disease, Curr. Opin. Struct. Biol., 21, 432\u2013440.","journal-title":"Curr. Opin. Struct. Biol."},{"key":"762_CR261","doi-asserted-by":"publisher","first-page":"1365","DOI":"10.1126\/science.1163581","volume":"322","author":"J. Gsponer","year":"2008","unstructured":"Gsponer, J., Futschik, M. E., Teichmann, S. A., and Babu, M. M. (2008) Tight regulation of unstructured proteins: from transcript synthesis to protein degradation, Science, 322, 1365\u20131368.","journal-title":"Science"},{"key":"762_CR262","doi-asserted-by":"publisher","first-page":"903","DOI":"10.1002\/prot.21773","volume":"71","author":"P. Tompa","year":"2008","unstructured":"Tompa, P., Prilusky, J., Silman, I., and Sussman, J. L. (2008) Structural disorder serves as a weak signal for intra\u2013cellular protein degradation, Proteins Struct. Funct. Bioinformatics, 71, 903\u2013909.","journal-title":"Proteins Struct. Funct. Bioinformatics"},{"key":"762_CR263","doi-asserted-by":"publisher","first-page":"918","DOI":"10.1126\/science.1160489","volume":"322","author":"H.\u2013C. S. Yen","year":"2008","unstructured":"Yen, H.\u2013C. S., Xu, Q., Chou, D. M., Zhao, Z., and Elledge, S. J. (2008) Global protein stability profiling in mammalian cells, Science, 322, 918\u2013923.","journal-title":"Science"},{"key":"762_CR264","doi-asserted-by":"publisher","first-page":"923","DOI":"10.1126\/science.1160462","volume":"322","author":"H.\u2013C. S. Yen","year":"2008","unstructured":"Yen, H.\u2013C. S., and Elledge, S. J. (2008) Identification of SCF ubiquitin ligase substrates by global protein stability profiling, Science, 322, 923\u2013929.","journal-title":"Science"},{"key":"762_CR265","doi-asserted-by":"publisher","first-page":"1285","DOI":"10.1002\/pro.657","volume":"20","author":"M. J. Suskiewicz","year":"2011","unstructured":"Suskiewicz, M. J., Sussman, J. L., Silman, I., and Shaul, Y. (2011) Context\u2013dependent resistance to proteolysis of intrinsically disordered proteins, Protein Sci., 20, 1285\u20131297.","journal-title":"Protein Sci."},{"key":"762_CR266","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1002\/prot.22555","volume":"78","author":"P. Radivojac","year":"2010","unstructured":"Radivojac, P., Vacic, V., Haynes, C., Cocklin, R. R., Mohan, A., Heyen, J. W., Goebl, M. G., and Iakoucheva, L. M. (2010) Identification, analysis, and prediction of protein ubiquitination sites, Proteins Struct. Funct. Bioinformatics, 78, 365\u2013380.","journal-title":"Proteins Struct. Funct. Bioinformatics"},{"key":"762_CR267","doi-asserted-by":"publisher","first-page":"319","DOI":"10.1016\/j.jmb.2011.07.024","volume":"412","author":"T. Hagai","year":"2011","unstructured":"Hagai, T., Azia, A., Toth\u2013Petroczy, A., and Levy, Y. (2011) Intrinsic disorder in ubiquitination substrates, J. Mol. Biol., 412, 319\u2013324.","journal-title":"J. Mol. Biol."},{"key":"762_CR268","doi-asserted-by":"publisher","first-page":"2001","DOI":"10.1073\/pnas.0912335107","volume":"107","author":"T. Hagai","year":"2010","unstructured":"Hagai, T., and Levy, Y. (2010) Ubiquitin not only serves as a tag but also assists degradation by inducing protein unfolding, Proc. Natl. Acad. Sci. USA, 107, 2001\u20132006.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"762_CR269","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1038\/nchembio.130","volume":"5","author":"S. Prakash","year":"2009","unstructured":"Prakash, S., Inobe, T., Hatch, A. J., and Matouschek, A. (2009) Substrate selection by the proteasome during degra\u2013dation of protein complexes, Nat. Chem. Biol., 5, 29\u201336.","journal-title":"Nat. Chem. Biol."},{"key":"762_CR270","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1038\/346287a0","volume":"346","author":"E. S. Johnson","year":"1990","unstructured":"Johnson, E. S., Gonda, D. K., and Varshavsky, A. (1990) Cis\u2013trans recognition and subunit\u2013specific degradation of short\u2013lived proteins, Nature, 346, 287\u2013291.","journal-title":"Nature"},{"key":"762_CR271","doi-asserted-by":"publisher","first-page":"697","DOI":"10.1016\/0092-8674(90)90481-S","volume":"61","author":"M. Hochstrasser","year":"1990","unstructured":"Hochstrasser, M., and Varshavsky, A. (1990) In vivo degra\u2013dation of a transcriptional regulator: the yeast alpha 2 repressor, Cell, 61, 697\u2013708.","journal-title":"Cell"},{"key":"762_CR272","doi-asserted-by":"publisher","first-page":"439","DOI":"10.1016\/S1097-2765(01)00308-2","volume":"8","author":"R. Verma","year":"2001","unstructured":"Verma, R., McDonald, H., Yates, J. R., and Deshaies, R. J. (2001) Selective degradation of ubiquitinated Sic1 by purified 26S proteasome yields active S phase cyclin\u2013Cdk, Mol. Cell, 8, 439\u2013448.","journal-title":"Mol. Cell"},{"key":"762_CR273","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1038\/46080","volume":"402","author":"K. Nasmyth","year":"1999","unstructured":"Nasmyth, K., Shirayama, M., Toth, A., and Galova, M. (1999) APC(Cdc20) promotes exit from mitosis by destroying the anaphase inhibitor Pds1 and cyclin Clb5, Nature, 402, 203\u2013207.","journal-title":"Nature"},{"key":"762_CR274","doi-asserted-by":"publisher","first-page":"1720","DOI":"10.1038\/sj.emboj.7601058","volume":"25","author":"M. A. Hoyt","year":"2006","unstructured":"Hoyt, M. A., Zich, J., Takeuchi, J., Zhang, M., Govaerts, C., and Coffino, P. (2006) Glycine\u2013alanine repeats impair proper substrate unfolding by the proteasome, EMBO J., 25, 1720\u20131729.","journal-title":"EMBO J."},{"key":"762_CR275","doi-asserted-by":"publisher","first-page":"333","DOI":"10.1016\/j.cell.2015.03.001","volume":"161","author":"Y. Kravtsova\u2013Ivantsiv","year":"2015","unstructured":"Kravtsova\u2013Ivantsiv, Y., Shomer, I., Cohen\u2013Kaplan, V., Snijder, B., Superti\u2013Furga, G., Gonen, H., Sommer, T., Ziv, T., Admon, A., Naroditsky, I., Jbara, M., Brik, A., Pikarsky, E., Kwon, Y. T., Doweck, I., and Ciechanover, A. (2015) KPC1\u2013mediated ubiquitination and proteasomal processing of NF\u2013\u03baB1 p105 to p50 restricts tumor growth, Cell, 161, 333\u2013347.","journal-title":"Cell"},{"key":"762_CR276","doi-asserted-by":"publisher","first-page":"814","DOI":"10.1016\/j.jmb.2008.12.081","volume":"386","author":"J. M. Baugh","year":"2009","unstructured":"Baugh, J. M., Viktorova, E. G., and Pilipenko, E. V. (2009) Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination, J. Mol. Biol., 386, 814\u2013827.","journal-title":"J. Mol. Biol."},{"key":"762_CR277","doi-asserted-by":"publisher","first-page":"2377","DOI":"10.1128\/MCB.13.4.2377","volume":"13","author":"X. Li","year":"1993","unstructured":"Li, X., and Coffino, P. (1993) Degradation of ornithine decarboxylase: exposure of the C\u2013terminal target by a polyamine\u2013inducible inhibitory protein, Mol. Cell. Biol., 13, 2377\u20132383.","journal-title":"Mol. Cell. Biol."},{"key":"762_CR278","doi-asserted-by":"publisher","first-page":"14738","DOI":"10.1038\/srep14738","volume":"5","author":"D. Wu","year":"2015","unstructured":"Wu, D., Kaan, H. Y. K., Zheng, X., Tang, X., He, Y., Vanessa Tan, Q., Zhang, N., and Song, H. (2015) Structural basis of ornithine decarboxylase inactivation and accelerated degradation by polyamine sensor Antizyme1, Sci. Rep., 5, 14738.","journal-title":"Sci. Rep."},{"key":"762_CR279","doi-asserted-by":"crossref","first-page":"15949","DOI":"10.1016\/S0021-9258(18)71571-8","volume":"264","author":"Z. Bercovich","year":"1989","unstructured":"Bercovich, Z., Rosenberg\u2013Hasson, Y., Ciechanover, A., and Kahana, C. (1989) Degradation of ornithine decar\u2013boxylase in reticulocyte lysate is ATP\u2013dependent but ubiq\u2013uitin\u2013independent, J. Biol. Chem., 264, 15949\u201315952.","journal-title":"J. Biol. Chem."},{"key":"762_CR280","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1038\/sj.emboj.7601476","volume":"26","author":"J. Takeuchi","year":"2007","unstructured":"Takeuchi, J., Chen, H., and Coffino, P. (2007) Proteasome substrate degradation requires association plus extended peptide, EMBO J., 26, 123\u2013131.","journal-title":"EMBO J."},{"key":"762_CR281","doi-asserted-by":"publisher","first-page":"417","DOI":"10.1038\/87575","volume":"8","author":"B. L. Bertolaet","year":"2001","unstructured":"Bertolaet, B. L., Clarke, D. J., Wolff, M., Watson, M. H., Henze, M., Divita, G., and Reed, S. I. (2001) UBA domains of DNA damage\u2013inducible proteins interact with ubiquitin, Nat. Struct. Biol., 8, 417\u2013422.","journal-title":"Nat. Struct. Biol."},{"key":"762_CR282","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1006\/abbi.2000.2036","volume":"383","author":"M. Orlowski","year":"2000","unstructured":"Orlowski, M., and Wilk, S. (2000) Catalytic activities of the 20S proteasome, a multicatalytic proteinase complex, Arch. Biochem. Biophys., 383, 1\u201316.","journal-title":"Arch. Biochem. Biophys."},{"key":"762_CR283","doi-asserted-by":"publisher","first-page":"216","DOI":"10.1016\/j.bbamcr.2013.05.008","volume":"1843","author":"J. Erales","year":"2014","unstructured":"Erales, J., and Coffino, P. (2014) Ubiquitin\u2013independent proteasomal degradation, Biochim. Biophys. Acta, 1843, 216\u2013221.","journal-title":"Biochim. Biophys. Acta"},{"key":"762_CR284","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1016\/B978-0-12-397863-9.00006-7","volume":"109","author":"A. M. Pickering","year":"2012","unstructured":"Pickering, A. M., and Davies, K. J. A. (2012) Degradation of damaged proteins\u2013the main function of the 20S pro\u2013teasome, Prog. Mol. Biol. Transl. Sci., 109, 227\u2013248.","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"key":"762_CR285","doi-asserted-by":"publisher","first-page":"6589","DOI":"10.1021\/cr400525m","volume":"114","author":"R. Van der Lee","year":"2014","unstructured":"Van der Lee, R., Buljan, M., Lang, B., Weatheritt, R. J., Daughdrill, G. W., Dunker, A. K., Fuxreiter, M., Gough, J., Gsponer, J., Jones, D. T., Kim, P. M., Kriwacki, R. W., Oldfield, C. J., Pappu, R. V., Tompa, P., Uversky, V. N., Wright, P. E., and Babu, M. M. (2014) Classification of intrinsically disordered regions and proteins, Chem. Rev., 114, 6589\u20136631.","journal-title":"Chem. Rev."},{"key":"762_CR286","volume-title":"Oxidative stress\u2013mediated regulation of proteasome complexes","author":"C. T. Aiken","year":"2011","unstructured":"Aiken, C. T., Kaake, R. M., Wang, X., and Huang, L. (2011) Oxidative stress\u2013mediated regulation of proteasome complexes, Mol. Cell. Proteomics, 10, R110.006924."},{"key":"762_CR287","doi-asserted-by":"publisher","first-page":"4797","DOI":"10.1016\/j.febslet.2005.07.060","volume":"579","author":"B. Alvarez\u2013Castelao","year":"2005","unstructured":"Alvarez\u2013Castelao, B., and Castano, J. G. (2005) Mechanism of direct degradation of I\u03baB\u03b1 by 20S protea\u2013some, FEBS Lett., 579, 4797\u20134802.","journal-title":"FEBS Lett."},{"key":"762_CR288","doi-asserted-by":"publisher","first-page":"668","DOI":"10.1016\/j.bbrc.2011.03.071","volume":"407","author":"W. Zhang","year":"2011","unstructured":"Zhang, W., and Wei, Q. (2011) Calcineurin stimulates the expression of inflammatory factors in RAW 264.7 cells by interacting with proteasome subunit alpha type 6, Biochem. Biophys. Res. Commun., 407, 668\u2013673.","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"762_CR289","doi-asserted-by":"publisher","first-page":"612","DOI":"10.1128\/JVI.00832-08","volume":"83","author":"K. Yuksek","year":"2009","unstructured":"Yuksek, K., Chen, W.\u2013L., Chien, D., and Ou, J.\u2013H. (2009) Ubiquitin\u2013independent degradation of hepatitis C virus F protein, J. Virol., 83, 612\u2013621.","journal-title":"J. Virol."},{"key":"762_CR290","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1515\/BC.2003.005","volume":"384","author":"R. Stohwasser","year":"2003","unstructured":"Stohwasser, R., Holzhutter, H.\u2013G., Lehmann, U., Henklein, P., and Kloetzel, P.\u2013M. (2003) Hepatitis B virus HBx peptide 116\u2013138 and proteasome activator PA28 compete for binding to the proteasome \u03b14\/MC6 subunit, Biol. Chem., 384, 39\u201349.","journal-title":"Biol. Chem."},{"key":"762_CR291","doi-asserted-by":"publisher","first-page":"21334","DOI":"10.1074\/jbc.M401022200","volume":"279","author":"J. Dong","year":"2004","unstructured":"Dong, J., Chen, W., Welford, A., and Wandinger\u2013Ness, A. (2004) The proteasome \u03b1\u2013subunit XAPC7 interacts specif\u2013ically with Rab7 and late endosomes, J. Biol. Chem., 279, 21334\u201321342.","journal-title":"J. Biol. Chem."},{"key":"762_CR292","doi-asserted-by":"publisher","first-page":"3913","DOI":"10.1016\/j.febslet.2005.06.003","volume":"579","author":"J. C. Dachsel","year":"2005","unstructured":"Dachsel, J. C., Lucking, C. B., Deeg, S., Schultz, E., Lalowski, M., Casademunt, E., Corti, O., Hampe, C., Patenge, N., Vaupel, K., Yamamoto, A., Dichgans, M., Brice, A., Wanker, E. E., Kahle, P. J., and Gasser, T. (2005) Parkin interacts with the proteasome subunit \u03b14, FEBS Lett., 579, 3913\u20133919.","journal-title":"FEBS Lett."},{"key":"762_CR293","doi-asserted-by":"publisher","first-page":"952","DOI":"10.1159\/000350113","volume":"31","author":"L. Yang","year":"2013","unstructured":"Yang, L., Tang, Z., Zhang, H., Kou, W., Lu, Z., Li, X., Li, Q., and Miao, Z. (2013) PSMA7 directly interacts with NOD1 and regulates its function, Cell. Physiol. Biochem., 31, 952\u2013959.","journal-title":"Cell. Physiol. Biochem."},{"key":"762_CR294","doi-asserted-by":"publisher","first-page":"2367","DOI":"10.1093\/emboj\/20.10.2367","volume":"20","author":"R. Touitou","year":"2001","unstructured":"Touitou, R., Richardson, J., Bose, S., Nakanishi, M., Rivett, J., and Allday, M. J. (2001) A degradation signal located in the C\u2013terminus of p21WAF1\/CIP1 is a binding site for the C8 alpha\u2013subunit of the 20S proteasome, EMBO J., 20, 2367\u20132375.","journal-title":"EMBO J."},{"key":"762_CR295","doi-asserted-by":"publisher","first-page":"16000","DOI":"10.1074\/jbc.M312264200","volume":"279","author":"Z. Zhang","year":"2004","unstructured":"Zhang, Z., Wang, H., Li, M., Agrawal, S., Chen, X., and Zhang, R. (2004) MDM2 is a negative regulator of p21WAF1\/CIP1, independent of p53, J. Biol. Chem., 279, 16000\u201316006.","journal-title":"J. Biol. Chem."},{"key":"762_CR296","doi-asserted-by":"publisher","first-page":"465","DOI":"10.1016\/j.molcel.2007.12.030","volume":"29","author":"P. Yi","year":"2008","unstructured":"Yi, P., Feng, Q., Amazit, L., Lonard, D. M., Tsai, S. Y., Tsai, M.\u2013J., and O\u2019Malley, B. W. (2008) Atypical protein kinase C regulates dual pathways for degradation of the oncogenic coactivator SRC\u20133\/AIB1, Mol. Cell, 29, 465\u2013476.","journal-title":"Mol. Cell"},{"key":"762_CR297","doi-asserted-by":"publisher","first-page":"699","DOI":"10.1016\/j.molcel.2005.10.017","volume":"20","author":"P. Sdek","year":"2005","unstructured":"Sdek, P., Ying, H., Chang, D. L. F., Qiu, W., Zheng, H., Touitou, R., Allday, M. J., and Jim Xiao, Z.\u2013X. (2005) MDM2 promotes proteasome\u2013dependent ubiquitin\u2013inde\u2013pendent degradation of retinoblastoma protein, Mol. Cell, 20, 699\u2013708.","journal-title":"Mol. Cell"},{"key":"762_CR298","doi-asserted-by":"publisher","first-page":"352","DOI":"10.1016\/j.bbamcr.2013.11.018","volume":"1843","author":"B. Alvarez\u2013Castelao","year":"2014","unstructured":"Alvarez\u2013Castelao, B., Goethals, M., Vandekerckhove, J., and Castano, J. G. (2014) Mechanism of cleavage of alpha\u2013synuclein by the 20S proteasome and modulation of its degradation by the RedOx state of the N\u2013terminal methionines, Biochim. Biophys. Acta Mol. Cell Res., 1843, 352\u2013365.","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"762_CR299","doi-asserted-by":"publisher","first-page":"555","DOI":"10.1042\/BSR20130013","volume":"33","author":"F. Yuan","year":"2013","unstructured":"Yuan, F., Ma, Y., You, P., Lin, W., Lu, H., Yu, Y., Wang, X., Jiang, J., Yang, P., Ma, Q., and Tao, T. (2013) A novel role of proteasomal \u03b21 subunit in tumorigenesis, Biosci. Rep., 33, 555\u2013565.","journal-title":"Biosci. Rep."},{"key":"762_CR300","doi-asserted-by":"publisher","first-page":"46533","DOI":"10.1074\/jbc.M105500200","volume":"276","author":"C. Gruendler","year":"2001","unstructured":"Gruendler, C., Lin, Y., Farley, J., and Wang, T. (2001) Proteasomal degradation of Smad1 induced by bone morphogenetic proteins, J. Biol. Chem., 276, 46533\u201346543.","journal-title":"J. Biol. Chem."},{"key":"762_CR301","first-page":"153","volume":"1786","author":"I. Jariel\u2013Encontre","year":"2008","unstructured":"Jariel\u2013Encontre, I., Bossis, G., and Piechaczyk, M. (2008) Ubiquitin\u2013independent degradation of proteins by the pro\u2013teasome, Biochim. Biophys. Acta, 1786, 153\u2013177.","journal-title":"Biochim. Biophys. Acta"},{"key":"762_CR302","first-page":"3767","volume":"30","author":"J. Adler","year":"2010","unstructured":"Adler, J., Reuven, N., Kahana, C., and Shaul, Y. (2010) c\u2013Fos proteasomal degradation is activated by a default mechanism, and its regulation by NAD(P)H:quinone oxi\u2013doreductase 1 determines c\u2013Fos serum response kinetics, Mol. Cell. Biol., 30, 3767\u20133778.","journal-title":"c\u2013Fos proteasomal degradation is activated by a default mechanism"},{"key":"762_CR303","doi-asserted-by":"publisher","first-page":"1817","DOI":"10.1038\/onc.2011.375","volume":"31","author":"J. L. Pakay","year":"2012","unstructured":"Pakay, J. L., Diesch, J., Gilan, O., Yip, Y.\u2013Y., Sayan, E., Kolch, W., Mariadason, J. M., Hannan, R. D., Tulchinsky, E., and Dhillon, A. S. (2012) A 19S proteaso\u2013mal subunit cooperates with an ERK MAPK\u2013regulated degron to regulate accumulation of Fra\u20131 in tumour cells, Oncogene, 31, 1817\u20131824.","journal-title":"Oncogene"},{"key":"762_CR304","doi-asserted-by":"publisher","first-page":"300","DOI":"10.1134\/S1607672913060070","volume":"453","author":"E. S. Kuzina","year":"2013","unstructured":"Kuzina, E. S., Chernolovskaya, E. L., Kudriaeva, A. A., Zenkova, M. A., Knorre, V. D., Surina, E. A., Ponomarenko, N. A., Bobik, T. V., Smirnov, I. V., Bacheva, A. V., Belogurov, A. A., Gabibov, A. G., and Vlasov, V. V. (2013) Immunoproteasome enhances intra\u2013cellular proteolysis of myelin basic protein, Dokl. Biochem. Biophys., 453, 300\u2013303.","journal-title":"Dokl. Biochem. Biophys."},{"key":"762_CR305","doi-asserted-by":"publisher","first-page":"17758","DOI":"10.1074\/jbc.M113.544247","volume":"289","author":"A. Belogurov","year":"2014","unstructured":"Belogurov, A., Kudriaeva, A., Kuzina, E., Smirnov, I., Bobik, T., Ponomarenko, N., Kravtsova\u2013Ivantsiv, Y., Ciechanover, A., and Gabibov, A. (2014) Multiple sclero\u2013sis autoantigen myelin basic protein escapes control by ubiquitination during proteasomal degradation, J. Biol. Chem., 289, 17758\u201317766.","journal-title":"J. Biol. Chem."},{"key":"762_CR306","doi-asserted-by":"publisher","first-page":"1901","DOI":"10.1096\/fj.14-259333","volume":"29","author":"A. Belogurov","year":"2015","unstructured":"Belogurov, A., Kuzina, E., Kudriaeva, A., Kononikhin, A., Kovalchuk, S., Surina, Y., Smirnov, I., Lomakin, Y., Bacheva, A., Stepanov, A., Karpova, Y., Lyupina, Y., Kharybin, O., Melamed, D., Ponomarenko, N., Sharova, N., Nikolaev, E., and Gabibov, A. (2015) Ubiquitin\u2013inde\u2013pendent proteosomal degradation of myelin basic protein contributes to development of neurodegenerative autoim\u2013munity, FASEB J., 29, 1901\u20131913.","journal-title":"FASEB J."},{"key":"762_CR307","doi-asserted-by":"publisher","first-page":"926394","DOI":"10.1155\/2014\/926394","volume":"2014","author":"E. Kuzina","year":"2014","unstructured":"Kuzina, E., Kudriaeva, A., Smirnov, I., Dubina, M. V., Gabibov, A., and Belogurov, A. (2014) Glatiramer acetate and nanny proteins restrict access of the multiple sclerosis autoantigen myelin basic protein to the 26S proteasome, Biomed. Res. Int., 2014, 926394.","journal-title":"Biomed. Res. Int."},{"key":"762_CR308","doi-asserted-by":"publisher","first-page":"1942","DOI":"10.1016\/j.bbamcr.2014.05.005","volume":"1843","author":"M. Raule","year":"2014","unstructured":"Raule, M., Cerruti, F., and Cascio, P. (2014) Enhanced rate of degradation of basic proteins by 26S immunopro\u2013teasomes, Biochim. Biophys. Acta, 1843, 1942\u20131947.","journal-title":"Biochim. Biophys. Acta"},{"key":"762_CR309","doi-asserted-by":"publisher","first-page":"42830","DOI":"10.1074\/jbc.M111.300178","volume":"286","author":"T. Dange","year":"2011","unstructured":"Dange, T., Smith, D., Noy, T., Rommel, P. C., Jurzitza, L., Cordero, R. J. B., Legendre, A., Finley, D., Goldberg, A. L., and Schmidt, M. (2011) Blm10 protein promotes proteasomal substrate turnover by an active gating mecha\u2013nism, J. Biol. Chem., 286, 42830\u201342839.","journal-title":"J. Biol. Chem."},{"key":"762_CR310","doi-asserted-by":"publisher","first-page":"36559","DOI":"10.1074\/jbc.M111.274258","volume":"286","author":"S. P. Melo","year":"2011","unstructured":"Melo, S. P., Barbour, K. W., and Berger, F. G. (2011) Cooperation between an intrinsically disordered region and a helical segment is required for ubiquitin\u2013independ\u2013ent degradation by the proteasome, J. Biol. Chem., 286, 36559\u201336567.","journal-title":"J. Biol. Chem."},{"key":"762_CR311","volume-title":"Direct ubiquitin independent recognition and degradation of a folded protein by the eukaryotic protea\u2013somes\u2013origin of intrinsic degradation signals","author":"A. K. Singh Gautam","year":"2012","unstructured":"Singh Gautam, A. K., Balakrishnan, S., and Venkatraman, P. (2012) Direct ubiquitin independent recognition and degradation of a folded protein by the eukaryotic protea\u2013somes\u2013origin of intrinsic degradation signals, PLoS One, 7, e34864."},{"key":"762_CR312","doi-asserted-by":"publisher","first-page":"12645","DOI":"10.1074\/jbc.M113.453027","volume":"288","author":"O. S. Alfassy","year":"2013","unstructured":"Alfassy, O. S., Cohen, I., Reiss, Y., Tirosh, B., and Ravid, T. (2013) Placing a disrupted degradation motif at the C terminus of proteasome substrates attenuates degradation without impairing ubiquitylation, J. Biol. Chem., 288, 12645\u201312653.","journal-title":"J. Biol. Chem."},{"key":"762_CR313","doi-asserted-by":"publisher","first-page":"778","DOI":"10.1038\/nchembio.233","volume":"5","author":"P. Tsvetkov","year":"2009","unstructured":"Tsvetkov, P., Reuven, N., and Shaul, Y. (2009) The nanny model for IDPs, Nat. Chem. Biol., 5, 778\u2013781.","journal-title":"Nat. Chem. Biol."},{"key":"762_CR314","doi-asserted-by":"publisher","first-page":"1500","DOI":"10.4161\/auto.25573","volume":"9","author":"X. J. Wang","year":"2013","unstructured":"Wang, X. J., Yu, J., Wong, S. H., Cheng, A. S., Chan, F. K., Ng, S. S., Cho, C. H., Sung, J. J., and Wu, W. K. (2013) A novel crosstalk between two major protein degra\u2013dation systems, Autophagy, 9, 1500\u20131508.","journal-title":"Autophagy"},{"key":"762_CR315","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1016\/j.neulet.2009.03.085","volume":"456","author":"L. Qiao","year":"2009","unstructured":"Qiao, L., and Zhang, J. (2009) Inhibition of lysosomal functions reduces proteasomal activity, Neurosci. Lett., 456, 15\u201319.","journal-title":"Neurosci. Lett."},{"key":"762_CR316","doi-asserted-by":"publisher","first-page":"517","DOI":"10.1016\/j.molcel.2009.01.021","volume":"33","author":"V. I. Korolchuk","year":"2009","unstructured":"Korolchuk, V. I., Mansilla, A., Menzies, F. M., and Rubinsztein, D. C. (2009) Autophagy inhibition compro\u2013mises degradation of ubiquitin\u2013proteasome pathway sub\u2013strates, Mol. Cell, 33, 517\u2013527.","journal-title":"Mol. Cell"},{"key":"762_CR317","doi-asserted-by":"publisher","first-page":"126","DOI":"10.4161\/auto.6.1.10928","volume":"6","author":"Z. Gao","year":"2010","unstructured":"Gao, Z., Gammoh, N., Wong, P.\u2013M., Erdjument\u2013Bromage, H., Tempst, P., and Jiang, X. (2010) Processing of autophagic protein LC3 by the 20S proteasome, Autophagy, 6, 126\u2013137.","journal-title":"Autophagy"}],"container-title":["Biochemistry (Moscow)"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1134\/S0006297919140104.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1134\/S0006297919140104","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1134\/S0006297919140104.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T00:13:24Z","timestamp":1773620004000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1134\/S0006297919140104"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,1]]},"references-count":317,"journal-issue":{"issue":"S1","published-print":{"date-parts":[[2019,1]]}},"alternative-id":["762"],"URL":"https:\/\/doi.org\/10.1134\/s0006297919140104","relation":{},"ISSN":["0006-2979","1608-3040"],"issn-type":[{"value":"0006-2979","type":"print"},{"value":"1608-3040","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,1]]},"assertion":[{"value":"10 August 2018","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"7 September 2018","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"7 September 2018","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"19 April 2019","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}}]}}