{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T07:22:46Z","timestamp":1781853766899,"version":"3.54.5"},"reference-count":107,"publisher":"Springer Science and Business Media LLC","issue":"3","license":[{"start":{"date-parts":[[2001,3,1]],"date-time":"2001-03-01T00:00:00Z","timestamp":983404800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nat Rev Mol Cell Biol"],"published-print":{"date-parts":[[2001,3]]},"DOI":"10.1038\/35056563","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T08:32:58Z","timestamp":1027672378000},"page":"169-178","source":"Crossref","is-referenced-by-count":1212,"title":["Themes and variations on ubiquitylation"],"prefix":"10.1038","volume":"2","author":[{"given":"Allan M.","family":"Weissman","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","reference":[{"key":"BF35056563_CR1","doi-asserted-by":"publisher","first-page":"94","DOI":"10.1093\/emboj\/19.1.94","volume":"19","author":"JS Thrower","year":"2000","unstructured":"Thrower, J. S., Hoffman, L., Rechsteiner, M. & Pickart, C. M. Recognition of the polyubiquitin proteolytic signal. EMBO J. 19, 94?102 (2000).","journal-title":"EMBO J."},{"key":"BF35056563_CR2","doi-asserted-by":"publisher","first-page":"8408","DOI":"10.1128\/MCB.14.12.8408","volume":"14","author":"KR Loeb","year":"1994","unstructured":"Loeb, K. R. & Haas, A. L. Conjugates of ubiquitin cross-reactive protein distribute in a cytoskeletal pattern. Mol. Cell. Biol. 14, 8408?8419 ( 1994).","journal-title":"Mol. Cell. Biol."},{"key":"BF35056563_CR3","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. & Pyrowolakis, G. Ubiquitin and its kin: how close are the family ties? Trends Cell Biol. 10, 335?342 (2000).","journal-title":"Trends Cell Biol."},{"key":"BF35056563_CR4","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/S0378-1119(00)00139-6","volume":"248","author":"ET Yeh","year":"2000","unstructured":"Yeh, E. T., Gong, L. & Kamitani, T. Ubiquitin-like proteins: new wines in new bottles. Gene 248, 1?14 ( 2000).","journal-title":"Gene"},{"key":"BF35056563_CR5","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1016\/S1097-2765(00)00040-X","volume":"6","author":"MF Kleijnen","year":"2000","unstructured":"Kleijnen, M. F. et al. The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome. Mol. Cell 6, 409?419 (2000).","journal-title":"Mol. Cell"},{"key":"BF35056563_CR6","doi-asserted-by":"publisher","first-page":"2563","DOI":"10.1073\/pnas.92.7.2563","volume":"92","author":"JM Huibregtse","year":"1995","unstructured":"Huibregtse, J. M., Scheffner, M., Beaudenon, S. & Howley, P. M. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl Acad. Sci. USA. 92, 2563 ?2567 (1995).","journal-title":"Proc. Natl Acad. Sci. USA."},{"key":"BF35056563_CR7","doi-asserted-by":"publisher","first-page":"549","DOI":"10.1016\/S0092-8674(00)00077-5","volume":"102","author":"CA Joazeiro","year":"2000","unstructured":"Joazeiro, C. A. & Weissman, A. M. RING finger proteins: mediators of ubiquitin ligase activity. Cell 102, 549?552 (2000).","journal-title":"Cell"},{"key":"BF35056563_CR8","doi-asserted-by":"publisher","first-page":"394","DOI":"10.1038\/338394a0","volume":"338","author":"D Finley","year":"1989","unstructured":"Finley, D., Bartel, B. & Varshavsky, A. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature 338, 394?401 ( 1989).","journal-title":"Nature"},{"key":"BF35056563_CR9","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1006\/scdb.2000.0164","volume":"11","author":"KD Wilkinson","year":"2000","unstructured":"Wilkinson, K. D. Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome. Semin. Cell. Dev. Biol. 11, 141?148 (2000).","journal-title":"Semin. Cell. Dev. Biol."},{"key":"BF35056563_CR10","doi-asserted-by":"crossref","first-page":"33171","DOI":"10.1016\/S0021-9258(20)30113-7","volume":"269","author":"PM Handley-Gearhart","year":"1994","unstructured":"Handley-Gearhart, P. M., Stephen, A. G., Trausch-Azar, J. S., Ciechanover, A. & Schwartz, A. L. Human ubiquitin-activating enzyme, E1. Indication of potential nuclear and cytoplasmic subpopulations using epitope-tagged cDNA constructs. J. Biol. Chem. 269, 33171?33178 (1994).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR11","doi-asserted-by":"crossref","first-page":"2145","DOI":"10.1242\/jcs.108.6.2145","volume":"108","author":"Y Nagai","year":"1995","unstructured":"Nagai, Y. et al. Ubiquitin-activating enzyme, E1, is phosphorylated in mammalian cells by the protein kinase Cdc2. J. Cell Sci. 108, 2145?2152 (1995).","journal-title":"J. Cell Sci."},{"key":"BF35056563_CR12","doi-asserted-by":"publisher","first-page":"701","DOI":"10.1042\/bj3000701","volume":"300","author":"SJ Grenfell","year":"1994","unstructured":"Grenfell, S. J., Trausch-Azar, J. S., Handley-Gearhart, P. M., Ciechanover, A. & Schwartz, A. L. Nuclear localization of the ubiquitin-activating enzyme, E1, is cell-cycle-dependent. Biochem. J. 300, 701?708 (1994).","journal-title":"Biochem. J."},{"key":"BF35056563_CR13","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1016\/0092-8674(84)90299-X","volume":"37","author":"D Finley","year":"1984","unstructured":"Finley, D., Ciechanover, A. & Varshavsky, A. Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85. Cell 37, 43?55 (1984).This is a landmark study that provided the first evidence of a role for the ubiquitin-conjugating system in cellular function.","journal-title":"Cell"},{"key":"BF35056563_CR14","doi-asserted-by":"publisher","first-page":"4040","DOI":"10.1074\/jbc.273.7.4040","volume":"273","author":"N Mathias","year":"1998","unstructured":"Mathias, N., Steussy, C. N. & Goebl, M. G. An essential domain within Cdc34p is required for binding to a complex containing Cdc4p and Cdc53p in Saccharomyces cerevisiae . J. Biol. Chem. 273, 4040? 4045 (1998).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR15","doi-asserted-by":"publisher","first-page":"6832","DOI":"10.1093\/emboj\/18.23.6832","volume":"18","author":"Y Xie","year":"1999","unstructured":"Xie, Y. & Varshavsky, A. The E2?E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain. EMBO J. 18, 6832 ?6844 (1999).This study establishes a role for the RING finger in the activity of the N-end rule E3.","journal-title":"EMBO J."},{"key":"BF35056563_CR16","doi-asserted-by":"publisher","first-page":"176","DOI":"10.1038\/365176a0","volume":"365","author":"T Sommer","year":"1993","unstructured":"Sommer, T. & Jentsch, S. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 365, 176?179 (1993). This study describes Ubc6 and provided the first suggestion of a linkage between the ubiquitin-conjugating system and the degradation of proteins from the endoplasmic reticulum.","journal-title":"Nature"},{"key":"BF35056563_CR17","doi-asserted-by":"publisher","first-page":"1415","DOI":"10.1083\/jcb.141.6.1415","volume":"141","author":"HP Hauser","year":"1998","unstructured":"Hauser, H. P., Bardroff, M., Pyrowolakis, G. & Jentsch, S. A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors. J. Cell Biol. 141, 1415?1422 (1998).","journal-title":"J. Cell Biol."},{"key":"BF35056563_CR18","doi-asserted-by":"publisher","first-page":"14823","DOI":"10.1074\/jbc.274.21.14823","volume":"274","author":"H Gonen","year":"1999","unstructured":"Gonen, H. et al. Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of I\u03baB\u03b1 . J. Biol. Chem. 274, 14823? 14830 (1999).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR19","doi-asserted-by":"publisher","first-page":"12148","DOI":"10.1074\/jbc.273.20.12148","volume":"273","author":"SE Schwarz","year":"1998","unstructured":"Schwarz, S. E., Rosa, J. L. & Scheffner, M. Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7. J. Biol. Chem. 273, 12148?12154 (1998).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR20","doi-asserted-by":"publisher","first-page":"1257","DOI":"10.1096\/fasebj.11.14.9409544","volume":"11","author":"AL Haas","year":"1997","unstructured":"Haas, A. L. & Siepmann, T. J. Pathways of ubiquitin conjugation . FASEB J. 11, 1257?1268 (1997).","journal-title":"FASEB J."},{"key":"BF35056563_CR21","doi-asserted-by":"publisher","first-page":"1321","DOI":"10.1126\/science.286.5443.1321","volume":"286","author":"L Huang","year":"1999","unstructured":"Huang, L. et al. Structure of an E6AP?UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science 286, 1321?1326 (1999).","journal-title":"Science"},{"key":"BF35056563_CR22","doi-asserted-by":"publisher","first-page":"533","DOI":"10.1016\/S0092-8674(00)00057-X","volume":"102","author":"N Zheng","year":"2000","unstructured":"Zheng, N., Wang, P., Jeffrey, P. D. & Pavletich, N. P. Structure of a c-Cbl?UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 102, 533? 539 (2000).References 21 and 22 describe the crystal structures of a HECT domain and a RING finger protein with an E2.","journal-title":"Cell"},{"key":"BF35056563_CR23","doi-asserted-by":"publisher","first-page":"7576","DOI":"10.1074\/jbc.274.11.7576","volume":"274","author":"U Nuber","year":"1999","unstructured":"Nuber, U. & Scheffner, M. Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction. J. Biol. Chem. 274, 7576?7582 (1999).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR24","doi-asserted-by":"publisher","first-page":"1621","DOI":"10.1021\/bi962639e","volume":"36","author":"WJ Cook","year":"1997","unstructured":"Cook, W. J., Martin, P. D., Edwards, B. F., Yamazaki, R. K. & Chau, V. Crystal structure of a class I ubiquitin conjugating enzyme (Ubc7) from Saccharomyces cerevisiae at 2.9 angstroms resolution. Biochemistry 36, 1621? 1627 (1997).","journal-title":"Biochemistry"},{"key":"BF35056563_CR25","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1016\/0092-8674(93)90384-3","volume":"75","author":"M Scheffner","year":"1993","unstructured":"Scheffner, M., Huibregtse, J. M., Vierstra, R. D. & Howley, P. M. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75, 495? 505 (1993).This is a seminal paper describing the characterization of E6-AP, the first described member of the HECT domain family of E3s.","journal-title":"Cell"},{"key":"BF35056563_CR26","doi-asserted-by":"publisher","first-page":"18785","DOI":"10.1074\/jbc.274.26.18785","volume":"274","author":"S Kumar","year":"1999","unstructured":"Kumar, S., Talis, A. L. & Howley, P. M. Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination. J. Biol. Chem. 274 , 18785?18792 (1999).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR27","doi-asserted-by":"publisher","first-page":"70","DOI":"10.1038\/ng0197-70","volume":"15","author":"T Kishino","year":"1997","unstructured":"Kishino, T., Lalande, M. & Wagstaff, J. UBE3A\/E6-AP mutations cause Angelman syndrome. Nature Genet. 15, 70?73 (1997).","journal-title":"Nature Genet."},{"key":"BF35056563_CR28","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1096\/fasebj.14.2.231","volume":"14","author":"BK Kay","year":"2000","unstructured":"Kay, B. K., Williamson, M. P. & Sudol, M. The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14, 231?241 ( 2000).","journal-title":"FASEB J."},{"key":"BF35056563_CR29","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s00232001079","volume":"176","author":"D Rotin","year":"2000","unstructured":"Rotin, D., Staub, O. & Haguenauer-Tsapis, R. Ubiquitination and endocytosis of plasma membrane proteins: role of Nedd4\/Rsp5p family of ubiquitin-protein ligases. J. Membr. Biol. 176, 1?17 ( 2000).","journal-title":"J. Membr. Biol."},{"key":"BF35056563_CR30","doi-asserted-by":"publisher","first-page":"1473","DOI":"10.1083\/jcb.149.7.1473","volume":"149","author":"PJ Plant","year":"2000","unstructured":"Plant, P. J. et al. Apical membrane targeting of Nedd4 is mediated by an association of its C2 domain with annexin XIIIb. J. Cell Biol. 149, 1473?1484 (2000).","journal-title":"J. Cell Biol."},{"key":"BF35056563_CR31","doi-asserted-by":"publisher","first-page":"577","DOI":"10.1016\/S0092-8674(00)00080-5","volume":"102","author":"T Hoppe","year":"2000","unstructured":"Hoppe, T. et al. Activation of a membrane-bound transcription factor by regulated ubiquitin\/proteasome-dependent processing. Cell 102 , 577?586 (2000).","journal-title":"Cell"},{"key":"BF35056563_CR32","doi-asserted-by":"publisher","first-page":"21707","DOI":"10.1074\/jbc.270.37.21707","volume":"270","author":"A Orian","year":"1995","unstructured":"Orian, A. et al. Ubiquitin-mediated processing of NF-\u03baB transcriptional activator precursor p105. Reconstitution of a cell-free system and identification of the ubiquitin-carrier protein, E2, and a novel ubiquitin-protein ligase, E3, involved in conjugation. J. Biol. Chem. 270, 21707?21714 (1995).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR33","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1146\/annurev.cellbio.14.1.19","volume":"14","author":"JS Bonifacino","year":"1998","unstructured":"Bonifacino, J. S. & Weissman, A. M. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu. Rev. Cell. Dev. Biol. 14, 19? 57 (1998).","journal-title":"Annu. Rev. Cell. Dev. Biol."},{"key":"BF35056563_CR34","doi-asserted-by":"publisher","first-page":"204","DOI":"10.1096\/fj.00-0191com","volume":"15","author":"E Kamynina","year":"2001","unstructured":"Kamynina, E., Debonneville, C., Bens, M., Vandewalle, A. & Staub, O. A novel mouse Nedd4 protein suppresses the activity of the epithelial Na+ channel. FASEB J. 15, 204?214 ( 2001).","journal-title":"FASEB J."},{"key":"BF35056563_CR35","doi-asserted-by":"publisher","first-page":"R84","DOI":"10.1016\/S0960-9822(00)00287-6","volume":"10","author":"PS Freemont","year":"2000","unstructured":"Freemont, P. S. RING for destruction? Curr. Biol. 10, R84 ?R87 (2000).","journal-title":"Curr. Biol."},{"key":"BF35056563_CR36","doi-asserted-by":"publisher","first-page":"657","DOI":"10.1126\/science.284.5414.657","volume":"284","author":"T Kamura","year":"1999","unstructured":"Kamura, T. et al. Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase. Science 284, 657? 661 (1999).","journal-title":"Science"},{"key":"BF35056563_CR37","doi-asserted-by":"publisher","first-page":"535","DOI":"10.1016\/S1097-2765(00)80482-7","volume":"3","author":"T Ohta","year":"1999","unstructured":"Ohta, T., Michel, J. J., Schottelius, A. J. & Xiong, Y. ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. Mol. Cell 3, 535?541 (1999).","journal-title":"Mol. Cell"},{"key":"BF35056563_CR38","doi-asserted-by":"publisher","first-page":"527","DOI":"10.1016\/S1097-2765(00)80481-5","volume":"3","author":"P Tan","year":"1999","unstructured":"Tan, P. et al. Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I\u03baB\u03b1. Mol. Cell 3, 527?533 (1999).","journal-title":"Mol. Cell"},{"key":"BF35056563_CR39","doi-asserted-by":"publisher","first-page":"662","DOI":"10.1126\/science.284.5414.662","volume":"284","author":"D Skowyra","year":"1999","unstructured":"Skowyra, D. et al. Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1. Science 284, 662?665 (1999).","journal-title":"Science"},{"key":"BF35056563_CR40","doi-asserted-by":"publisher","first-page":"1614","DOI":"10.1101\/gad.13.12.1614","volume":"13","author":"JH Seol","year":"1999","unstructured":"Seol, J. H. et al. Cdc53\/cullin and the essential hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme cdc34. Genes Dev. 13, 1614?1626 (1999).References 36 40 all describe the characterization of a small RING finger protein as an integral component of SCF E3s.","journal-title":"Genes Dev."},{"key":"BF35056563_CR41","doi-asserted-by":"publisher","first-page":"11364","DOI":"10.1073\/pnas.96.20.11364","volume":"96","author":"KL Lorick","year":"1999","unstructured":"Lorick, K. L. et al. RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination. Proc. Natl Acad. Sci. USA 96, 11364?11369 (1999). This study suggests a general role for RING fingers in ubiquitylation.","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BF35056563_CR42","doi-asserted-by":"publisher","first-page":"8945","DOI":"10.1074\/jbc.275.12.8945","volume":"275","author":"S Fang","year":"2000","unstructured":"Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H. & Weissman, A. M. Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J. Biol. Chem. 275, 8945?8951 (2000).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR43","doi-asserted-by":"publisher","first-page":"1473","DOI":"10.1038\/sj.onc.1203464","volume":"19","author":"R Honda","year":"2000","unstructured":"Honda, R. & Yasuda, H. Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase . Oncogene 19, 1473?1476 (2000).","journal-title":"Oncogene"},{"key":"BF35056563_CR44","doi-asserted-by":"publisher","first-page":"22151","DOI":"10.1074\/jbc.274.32.22151","volume":"274","author":"H Waterman","year":"1999","unstructured":"Waterman, H., Levkowitz, G., Alroy, I. & Yarden, Y. The RING finger of c-Cbl mediates desensitization of the epidermal growth factor receptor . J. Biol. Chem. 274, 22151? 22154 (1999).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR45","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1126\/science.286.5438.309","volume":"286","author":"CA Joazeiro","year":"1999","unstructured":"Joazeiro, C. A. et al. The tyrosine kinase negative regulator c-Cbl as a RING-type, E2- dependent ubiquitin-protein ligase. Science 286 , 309?312 (1999).","journal-title":"Science"},{"key":"BF35056563_CR46","doi-asserted-by":"publisher","first-page":"31707","DOI":"10.1074\/jbc.274.44.31707","volume":"274","author":"M Yokouchi","year":"1999","unstructured":"Yokouchi, M. et al. Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7. J. Biol. Chem. 274, 31707?31712 (1999).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR47","doi-asserted-by":"publisher","first-page":"724","DOI":"10.1128\/MCB.19.1.724","volume":"19","author":"G Hu","year":"1999","unstructured":"Hu, G. & Fearon, E. R. Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins. Mol. Cell. Biol. 19 , 724?732 (1999). References 42 47 demonstrate a role for the RING finger in a variety of known and suspected E3s.","journal-title":"Mol. Cell. Biol."},{"key":"BF35056563_CR48","doi-asserted-by":"publisher","first-page":"1216","DOI":"10.1126\/science.279.5354.1216","volume":"279","author":"W Zachariae","year":"1998","unstructured":"Zachariae, W. et al. Mass spectrometric analysis of the anaphase-promoting complex from yeast: identification of a subunit related to cullins. Science 279, 1216?1219 ( 1998).","journal-title":"Science"},{"key":"BF35056563_CR49","doi-asserted-by":"publisher","first-page":"7795","DOI":"10.1074\/jbc.273.14.7795","volume":"273","author":"PS Brzovic","year":"1998","unstructured":"Brzovic, P. S., Meza, J., King, M. C. & Klevit, R. E. The cancer-predisposing mutation C61G disrupts homodimer formation in the NH2-terminal BRCA1 RING finger domain. J. Biol. Chem. 273, 7795? 7799 (1998).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR50","doi-asserted-by":"publisher","first-page":"874","DOI":"10.1126\/science.288.5467.874","volume":"288","author":"Y Yang","year":"2000","unstructured":"Yang, Y., Fang, S., Jensen, J. P., Weissman, A. M. & Ashwell, J. D. Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 288, 874?877 ( 2000).","journal-title":"Science"},{"key":"BF35056563_CR51","doi-asserted-by":"crossref","first-page":"26661","DOI":"10.1016\/S0021-9258(19)61427-4","volume":"275","author":"HK Hwang","year":"2000","unstructured":"Hwang, H. K. et al. The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7 . J. Biol. Chem. 275, 26661? 26664 (2000).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR52","doi-asserted-by":"publisher","first-page":"302","DOI":"10.1038\/77060","volume":"25","author":"H Shimura","year":"2000","unstructured":"Shimura, H. et al. Familial Parkinson's disease gene product, Parkin, in a ubiquitin-protein ligase. Nature Genet. 25, 302? 305 (2000).","journal-title":"Nature Genet."},{"key":"BF35056563_CR53","doi-asserted-by":"publisher","first-page":"13354","DOI":"10.1073\/pnas.240347797","volume":"97","author":"Y Zhang","year":"2000","unstructured":"Zhang, Y. et al. Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1 . Proc. Natl Acad. Sci. USA 97, 13354? 13359 (2000).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BF35056563_CR54","doi-asserted-by":"publisher","first-page":"2315","DOI":"10.1091\/mbc.11.7.2315","volume":"11","author":"JD Leverson","year":"2000","unstructured":"Leverson, J. D. et al. The APC11 RING-H2 finger mediates E2-dependent ubiquitination . Mol. Biol. Cell 11, 2315? 2325 (2000).","journal-title":"Mol. Biol. Cell"},{"key":"BF35056563_CR55","doi-asserted-by":"publisher","first-page":"435","DOI":"10.1146\/annurev.cellbio.15.1.435","volume":"15","author":"RJ Deshaies","year":"1999","unstructured":"Deshaies, R. J. SCF and Cullin\/Ring H2-based ubiquitin ligases. Annu. Rev. Cell. Dev. Biol. 15, 435?467 ( 1999).","journal-title":"Annu. Rev. Cell. Dev. Biol."},{"key":"BF35056563_CR56","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1146\/annurev.biochem.68.1.583","volume":"68","author":"AM Page","year":"1999","unstructured":"Page, A. M. & Hieter, P. The anaphase-promoting complex: new subunits and regulators. Annu. Rev. Biochem. 68, 583?609 (1999).","journal-title":"Annu. Rev. Biochem."},{"key":"BF35056563_CR57","doi-asserted-by":"publisher","first-page":"54","DOI":"10.1016\/S0959-437X(99)00049-0","volume":"10","author":"M Tyers","year":"2000","unstructured":"Tyers, M. & Jorgensen, P. Proteolysis and the cell cycle: with this RING I do thee destroy. Curr. Opin. Genet. Dev. 10, 54?64 (2000).","journal-title":"Curr. Opin. Genet. Dev."},{"key":"BF35056563_CR58","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1016\/S0092-8674(00)80098-7","volume":"86","author":"C Bai","year":"1996","unstructured":"Bai, C. et al. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86 , 263?274 (1996).","journal-title":"Cell"},{"key":"BF35056563_CR59","doi-asserted-by":"publisher","first-page":"751","DOI":"10.1016\/S1097-2765(00)00074-5","volume":"6","author":"P Zhou","year":"2000","unstructured":"Zhou, P., Bogacki, R., McReynolds, L. & Howley, P. M. Harnessing the ubiquitination machinery to target the degradation of specific cellular proteins. Mol. Cell 6, 751? 756 (2000).","journal-title":"Mol. Cell"},{"key":"BF35056563_CR60","doi-asserted-by":"publisher","first-page":"303","DOI":"10.1016\/S0092-8674(00)00036-2","volume":"102","author":"P Kaiser","year":"2000","unstructured":"Kaiser, P., Flick, K., Wittenberg, C. & Reed, S. I. Regulation of transcription by ubiquitination without proteolysis: Cdc34\/SCFMet30-mediated inactivation of the transcription factor Met4. Cell 102, 303?314 ( 2000).","journal-title":"Cell"},{"key":"BF35056563_CR61","doi-asserted-by":"publisher","first-page":"1822","DOI":"10.1101\/gad.13.14.1822","volume":"13","author":"J Lisztwan","year":"1999","unstructured":"Lisztwan, J., Imbert, G., Wirbelauer, C., Gstaiger, M. & Krek, W. The von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity. Genes Dev. 13, 1822?1833 (1999).","journal-title":"Genes Dev."},{"key":"BF35056563_CR62","doi-asserted-by":"publisher","first-page":"12436","DOI":"10.1073\/pnas.96.22.12436","volume":"96","author":"K Iwai","year":"1999","unstructured":"Iwai, K. et al. Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex. Proc. Natl Acad. Sci. USA 96, 12436?12441 (1999).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BF35056563_CR63","doi-asserted-by":"publisher","first-page":"423","DOI":"10.1038\/35017054","volume":"2","author":"M Ohh","year":"2000","unstructured":"Ohh, M. et al. Ubiquitination of hypoxia-inducible factor requires direct binding to the \u03b2-domain of the von Hippel-Lindau protein. Nature Cell Biol. 2, 423?427 ( 2000).","journal-title":"Nature Cell Biol."},{"key":"BF35056563_CR64","doi-asserted-by":"publisher","first-page":"25733","DOI":"10.1074\/jbc.M002740200","volume":"275","author":"ME Cockman","year":"2000","unstructured":"Cockman, M. E. et al. Hypoxia inducible factor-\u03b1 binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein. J. Biol. Chem. 275, 25733?25741 ( 2000).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR65","doi-asserted-by":"publisher","first-page":"10430","DOI":"10.1073\/pnas.190332597","volume":"97","author":"T Kamura","year":"2000","unstructured":"Kamura, T. et al. Activation of HIF1\u03b1 ubiquitination by a reconstituted von hippel-lindau (VHL) tumor suppressor complex. Proc. Natl Acad. Sci. USA 97, 10430?10435 (2000).References 61?65 establish the VHL?CBC complex as an E3 and show that HIF1\u03b1 is a substrate.","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BF35056563_CR66","doi-asserted-by":"publisher","first-page":"3872","DOI":"10.1101\/gad.12.24.3872","volume":"12","author":"T Kamura","year":"1998","unstructured":"Kamura, T. et al. The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families. Genes Dev. 12, 3872? 3881 (1998).","journal-title":"Genes Dev."},{"key":"BF35056563_CR67","doi-asserted-by":"publisher","first-page":"633","DOI":"10.1006\/bbrc.1999.1880","volume":"266","author":"CH Chung","year":"1999","unstructured":"Chung, C. H. & Baek, S. H. Deubiquitinating enzymes: their diversity and emerging roles. Biochem. Biophys. Res. Commun. 266, 633?640 (1999).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"BF35056563_CR68","doi-asserted-by":"publisher","first-page":"313","DOI":"10.1038\/366313a0","volume":"366","author":"FR Papa","year":"1993","unstructured":"Papa, F. R. & Hochstrasser, M. The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene . Nature 366, 313?319 (1993).","journal-title":"Nature"},{"key":"BF35056563_CR69","doi-asserted-by":"publisher","first-page":"737","DOI":"10.1038\/385737a0","volume":"385","author":"YA Lam","year":"1997","unstructured":"Lam, Y. A., Xu, W., DeMartino, G. N. & Cohen, R. E. Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 385, 737?740 (1997).","journal-title":"Nature"},{"key":"BF35056563_CR70","doi-asserted-by":"publisher","first-page":"635","DOI":"10.1016\/S0092-8674(00)80574-7","volume":"96","author":"M Koegl","year":"1999","unstructured":"Koegl, M. et al. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96, 635? 644 (1999).","journal-title":"Cell"},{"key":"BF35056563_CR71","doi-asserted-by":"publisher","first-page":"1265","DOI":"10.1128\/MCB.15.3.1265","volume":"15","author":"J Spence","year":"1995","unstructured":"Spence, J., Sadis, S., Haas, A. L. & Finley, D. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol. 15, 1265?1273 (1995).","journal-title":"Mol. Cell. Biol."},{"key":"BF35056563_CR72","doi-asserted-by":"publisher","first-page":"645","DOI":"10.1016\/S0092-8674(00)80575-9","volume":"96","author":"RM Hofmann","year":"1999","unstructured":"Hofmann, R. M. & Pickart, C. M. Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell 96, 645? 653 (1999).","journal-title":"Cell"},{"key":"BF35056563_CR73","doi-asserted-by":"publisher","first-page":"23360","DOI":"10.1074\/jbc.272.37.23360","volume":"272","author":"V Bailly","year":"1997","unstructured":"Bailly, V., Lauder, S., Prakash, S. & Prakash, L. Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities. J. Biol. Chem. 272, 23360?23365 (1997).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR74","doi-asserted-by":"publisher","first-page":"3388","DOI":"10.1093\/emboj\/19.13.3388","volume":"19","author":"HD Ulrich","year":"2000","unstructured":"Ulrich, H. D. & Jentsch, S. Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. EMBO J. 19, 3388?3397 ( 2000).","journal-title":"EMBO J."},{"key":"BF35056563_CR75","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1016\/S0092-8674(00)00011-8","volume":"102","author":"J Spence","year":"2000","unstructured":"Spence, J. et al. Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain. Cell 102, 67? 76 (2000).This is provocative study that demonstrates a role for K63-linked multi-ubiquitin chains in regulating translation.","journal-title":"Cell"},{"key":"BF35056563_CR76","doi-asserted-by":"publisher","first-page":"351","DOI":"10.1016\/S0092-8674(00)00126-4","volume":"103","author":"L Deng","year":"2000","unstructured":"Deng, L. et al. Activation of the I\u03baB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103, 351?361 (2000).","journal-title":"Cell"},{"key":"BF35056563_CR77","doi-asserted-by":"publisher","first-page":"1576","DOI":"10.1126\/science.2538923","volume":"243","author":"V Chau","year":"1989","unstructured":"Chau, V. et al. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243, 1576? 1583 (1989).","journal-title":"Science"},{"key":"BF35056563_CR78","doi-asserted-by":"publisher","first-page":"376","DOI":"10.1074\/jbc.271.1.376","volume":"271","author":"L Baldi","year":"1996","unstructured":"Baldi, L., Brown, K., Franzoso, G. & Siebenlist, U. Critical role for lysines 21 and 22 in signal-induced, ubiquitin- mediated proteolysis of I\u03baB\u03b1. J. Biol. Chem. 271, 376 ?379 (1996).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR79","doi-asserted-by":"crossref","first-page":"14244","DOI":"10.1016\/S0021-9258(17)36780-7","volume":"269","author":"D Hou","year":"1994","unstructured":"Hou, D., Cenciarelli, C., Jensen, J. P., Nguyen, H. B. & Weissman, A. M. Activation-dependent ubiquitination a T cell antigen receptor subunit on multiple intracellular lysines. J. Biol. Chem. 269, 14244?14247 (1994).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR80","doi-asserted-by":"publisher","first-page":"787","DOI":"10.1016\/S0092-8674(94)90502-9","volume":"78","author":"M Treier","year":"1994","unstructured":"Treier, M., Staszewski, L. M. & Bohmann, D. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 78, 787?798 (1994).","journal-title":"Cell"},{"key":"BF35056563_CR81","doi-asserted-by":"publisher","first-page":"5964","DOI":"10.1093\/emboj\/17.20.5964","volume":"17","author":"K Breitschopf","year":"1998","unstructured":"Breitschopf, K., Bengal, E., Ziv, T., Admon, A. & Ciechanover, A. A novel site for ubiquitination: the N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein. EMBO J. 17, 5964? 5973 (1998).","journal-title":"EMBO J."},{"key":"BF35056563_CR82","doi-asserted-by":"publisher","first-page":"403","DOI":"10.1016\/S1097-2765(00)80435-9","volume":"5","author":"RJ Sheaff","year":"2000","unstructured":"Sheaff, R. J. et al. Proteasomal turnover of p21Cip1 does not require p21Cip1 ubiquitination. Mol. Cell 5, 403?410 (2000).This study provides strong evidence for ubiquitin-independent proteasomal degradation of a protein that is known to ubiquitylated.","journal-title":"Mol. Cell"},{"key":"BF35056563_CR83","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. et al. The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol. Cell. Biol. 16, 6020?6028 (1996).","journal-title":"Mol. Cell. Biol."},{"key":"BF35056563_CR84","doi-asserted-by":"publisher","first-page":"507","DOI":"10.1006\/scdb.1999.0321","volume":"10","author":"JL Brodsky","year":"1999","unstructured":"Brodsky, J. L. & McCracken, A. A. ER protein quality control and proteasome-mediated protein degradation. Semin. Cell Dev. Biol. 10, 507?513 (1999).","journal-title":"Semin. Cell Dev. Biol."},{"key":"BF35056563_CR85","doi-asserted-by":"publisher","first-page":"3205","DOI":"10.1038\/sj.onc.1202656","volume":"18","author":"T Unger","year":"1999","unstructured":"Unger, T. et al. Mutations in serines 15 and 20 of human p53 impair its apoptotic activity. Oncogene 18, 3205? 3212 (1999).","journal-title":"Oncogene"},{"key":"BF35056563_CR86","doi-asserted-by":"publisher","first-page":"1815","DOI":"10.1093\/emboj\/18.7.1815","volume":"18","author":"SY Shieh","year":"1999","unstructured":"Shieh, S. Y., Taya, Y. & Prives, C. DNA damage-inducible phosphorylation of p53 at N-terminal sites including a novel site, Ser20, requires tetramerization. EMBO J. 18, 1815?1823 ( 1999).","journal-title":"EMBO J."},{"key":"BF35056563_CR87","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1038\/35004057","volume":"2","author":"MA Lohrum","year":"2000","unstructured":"Lohrum, M. A., Ashcroft, M., Kubbutat, M. H. & Vousden, K. H. Identification of a cryptic nucleolar-localization signal in MDM2. Nature Cell Biol. 2, 179?181 (2000).","journal-title":"Nature Cell Biol."},{"key":"BF35056563_CR88","doi-asserted-by":"publisher","first-page":"2517","DOI":"10.1128\/MCB.20.7.2517-2528.2000","volume":"20","author":"JD Weber","year":"2000","unstructured":"Weber, J. D. et al. Cooperative signals governing ARF-mdm2 interaction and nucleolar localization of the complex. Mol. Cell. Biol. 20, 2517?2528 (2000).","journal-title":"Mol. Cell. Biol."},{"key":"BF35056563_CR89","doi-asserted-by":"publisher","first-page":"2312","DOI":"10.1038\/sj.onc.1203593","volume":"19","author":"CA Midgley","year":"2000","unstructured":"Midgley, C. A. et al. An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo. Oncogene 19, 2312?2323 ( 2000).","journal-title":"Oncogene"},{"key":"BF35056563_CR90","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1093\/emboj\/18.1.22","volume":"18","author":"R Honda","year":"1999","unstructured":"Honda, R. & Yasuda, H. Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53. EMBO J. 18, 22?27 (1999).","journal-title":"EMBO J."},{"key":"BF35056563_CR91","doi-asserted-by":"publisher","first-page":"1001","DOI":"10.1128\/MCB.20.3.1001-1007.2000","volume":"20","author":"MW Jackson","year":"2000","unstructured":"Jackson, M. W. & Berberich, S. J. MdmX protects p53 from Mdm2-mediated degradation. Mol. Cell. Biol. 20, 1001?1007 (2000).","journal-title":"Mol. Cell. Biol."},{"key":"BF35056563_CR92","doi-asserted-by":"publisher","first-page":"38189","DOI":"10.1074\/jbc.274.53.38189","volume":"274","author":"DA Sharp","year":"1999","unstructured":"Sharp, D. A., Kratowicz, S. A., Sank, M. J. & George, D. L. Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein. J. Biol. Chem. 274, 38189?38196 (1999).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR93","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1016\/S0014-5793(99)00254-9","volume":"447","author":"S Tanimura","year":"1999","unstructured":"Tanimura, S. et al. MDM2 interacts with MDMX through their RING finger domains . FEBS Lett. 447, 5?9 (1999).","journal-title":"FEBS Lett."},{"key":"BF35056563_CR94","doi-asserted-by":"publisher","first-page":"753","DOI":"10.1016\/S0092-8674(00)80887-9","volume":"101","author":"T Buschmann","year":"2000","unstructured":"Buschmann, T., Fuchs, S. Y., Lee, C.-G., Pan, Z.-Q. & Ronai, Z. SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53. Cell 101, 753?762 (2000).","journal-title":"Cell"},{"key":"BF35056563_CR95","doi-asserted-by":"publisher","first-page":"3923","DOI":"10.1038\/sj.onc.1202781","volume":"18","author":"E Balint","year":"1999","unstructured":"Balint, E., Bates, S. & Vousden, K. H. Mdm2 binds p73\u03b1 without targeting degradation . Oncogene 18, 3923?3929 (1999).","journal-title":"Oncogene"},{"key":"BF35056563_CR96","doi-asserted-by":"publisher","first-page":"2101","DOI":"10.1038\/sj.onc.1202512","volume":"18","author":"M Dobbelstein","year":"1999","unstructured":"Dobbelstein, M., Wienzek, S., Konig, C. & Roth, J. Inactivation of the p53-homologue p73 by the mdm2-oncoprotein. Oncogene 18, 2101?2106 (1999).","journal-title":"Oncogene"},{"key":"BF35056563_CR97","doi-asserted-by":"publisher","first-page":"3257","DOI":"10.1128\/MCB.19.5.3257","volume":"19","author":"X Zeng","year":"1999","unstructured":"Zeng, X. et al. MDM2 suppresses p73 function without promoting p73 degradation . Mol. Cell. Biol. 19, 3257? 3266 (1999).","journal-title":"Mol. Cell. Biol."},{"key":"BF35056563_CR98","doi-asserted-by":"publisher","first-page":"9902","DOI":"10.1073\/pnas.170173897","volume":"97","author":"YA Lam","year":"2000","unstructured":"Lam, Y. A. et al. Inhibition of the ubiquitin-proteasome system in Alzheimer's disease. Proc. Natl Acad. Sci. USA. 97, 9902?9906 (2000).","journal-title":"Proc. Natl Acad. Sci. USA."},{"key":"BF35056563_CR99","doi-asserted-by":"publisher","first-page":"1093","DOI":"10.1006\/bbrc.2000.2576","volume":"270","author":"M Morimoto","year":"2000","unstructured":"Morimoto, M., Nishida, T., Honda, R. & Yasuda, H. Modification of cullin-1 by ubiquitin-like protein Nedd8 enhances the activity of SCFskp2 toward p27kip1. Biochem. Biophys. Res. Commun. 270, 1093?1096 ( 2000).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"BF35056563_CR100","doi-asserted-by":"publisher","first-page":"3475","DOI":"10.1093\/emboj\/19.13.3475","volume":"19","author":"F Osaka","year":"2000","unstructured":"Osaka, F. et al. Covalent modifier NEDD8 is essential for SCF ubiquitin-ligase in fission yeast. EMBO J. 19, 3475? 3484 (2000).","journal-title":"EMBO J."},{"key":"BF35056563_CR101","doi-asserted-by":"publisher","first-page":"4579","DOI":"10.1073\/pnas.090465597","volume":"97","author":"VN Podust","year":"2000","unstructured":"Podust, V. N. et al. A Nedd8 conjugation pathway is essential for proteolytic targeting of p27Kip1 by ubiquitination. Proc. Natl Acad. Sci. USA 97, 4579?4584 (2000).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BF35056563_CR102","doi-asserted-by":"publisher","first-page":"2326","DOI":"10.1128\/MCB.20.7.2326-2333.2000","volume":"20","author":"MA Read","year":"2000","unstructured":"Read, M. A. et al. Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha. Mol. Cell. Biol. 20 , 2326?2333 (2000).","journal-title":"Mol. Cell. Biol."},{"key":"BF35056563_CR103","doi-asserted-by":"publisher","first-page":"17008","DOI":"10.1074\/jbc.275.22.17008","volume":"275","author":"H Wada","year":"2000","unstructured":"Wada, H., Yeh, E. T. & Kamitani, T. A dominant-negative UBC12 mutant sequesters NEDD8 and inhibits NEDD8 conjugation in vivo. J. Biol. Chem. 275, 17008?17015 (2000).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR104","doi-asserted-by":"publisher","first-page":"32317","DOI":"10.1074\/jbc.M004847200","volume":"275","author":"K Wu","year":"2000","unstructured":"Wu, K., Chen, A. & Pan, Z. Q. Conjugation of Nedd8 to CUL1 enhances the ability of the ROC1-CUL1 complex to promote ubiquitin polymerization. J. Biol. Chem. 275, 32317?32324 ( 2000).","journal-title":"J. Biol. Chem."},{"key":"BF35056563_CR105","doi-asserted-by":"publisher","first-page":"2208","DOI":"10.1093\/emboj\/17.8.2208","volume":"17","author":"D Liakopoulos","year":"1998","unstructured":"Liakopoulos, D., Doenges, G., Matuschewski, K. & Jentsch, S. A novel protein modification pathway related to the ubiquitin system. EMBO J. 17, 2208?2214 ( 1998).","journal-title":"EMBO J."},{"key":"BF35056563_CR106","doi-asserted-by":"publisher","first-page":"5510","DOI":"10.1073\/pnas.96.10.5510","volume":"96","author":"D Liakopoulos","year":"1999","unstructured":"Liakopoulos, D., Busgen, T., Brychzy, A., Jentsch, S. & Pause, A. Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor function. Proc. Natl Acad. Sci. USA 96, 5510?5515 (1999).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BF35056563_CR107","doi-asserted-by":"publisher","first-page":"8973","DOI":"10.1073\/pnas.97.16.8973","volume":"97","author":"M Gmachl","year":"2000","unstructured":"Gmachl, M., Gieffers, C., Podtelejnikov, A. V., Mann, M. & Peters, J. M. The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex. Proc. Natl Acad. Sci. USA 97, 8973 ?8978 (2000).","journal-title":"Proc. Natl Acad. Sci. USA"}],"container-title":["Nature Reviews Molecular Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/35056563.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/35056563","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/35056563.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,17]],"date-time":"2023-05-17T01:49:44Z","timestamp":1684288184000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/35056563"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001,3]]},"references-count":107,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2001,3]]}},"alternative-id":["BF35056563"],"URL":"https:\/\/doi.org\/10.1038\/35056563","relation":{},"ISSN":["1471-0072","1471-0080"],"issn-type":[{"value":"1471-0072","type":"print"},{"value":"1471-0080","type":"electronic"}],"subject":[],"published":{"date-parts":[[2001,3]]}}}