{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,24]],"date-time":"2026-04-24T13:47:55Z","timestamp":1777038475846,"version":"3.51.4"},"reference-count":33,"publisher":"Springer Science and Business Media LLC","issue":"10","license":[{"start":{"date-parts":[[2005,9,18]],"date-time":"2005-09-18T00:00:00Z","timestamp":1127001600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nat Cell Biol"],"published-print":{"date-parts":[[2005,10]]},"DOI":"10.1038\/ncb1299","type":"journal-article","created":{"date-parts":[[2005,9,23]],"date-time":"2005-09-23T11:32:56Z","timestamp":1127475176000},"page":"999-1006","source":"Crossref","is-referenced-by-count":272,"title":["Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation"],"prefix":"10.1038","volume":"7","author":[{"given":"Christian","family":"Schuberth","sequence":"first","affiliation":[]},{"given":"Alexander","family":"Buchberger","sequence":"additional","affiliation":[]}],"member":"297","published-online":{"date-parts":[[2005,9,18]]},"reference":[{"key":"BFncb1299_CR1","doi-asserted-by":"publisher","first-page":"476","DOI":"10.1016\/S0955-0674(02)00358-7","volume":"14","author":"RY Hampton","year":"2002","unstructured":"Hampton, R. Y. ER-associated degradation in protein quality control and cellular regulation. Curr. Opin. Cell Biol. 14, 476\u2013482 (2002).","journal-title":"Curr. Opin. Cell Biol."},{"key":"BFncb1299_CR2","doi-asserted-by":"publisher","first-page":"2309","DOI":"10.1093\/emboj\/cdg227","volume":"22","author":"Z Kostova","year":"2003","unstructured":"Kostova, Z. & Wolf, D. H. For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J. 22, 2309\u20132317 (2003).","journal-title":"EMBO J."},{"key":"BFncb1299_CR3","doi-asserted-by":"publisher","first-page":"24","DOI":"10.1038\/35050524","volume":"3","author":"NW Bays","year":"2001","unstructured":"Bays, N. W., Gardner, R. G., Seelig, L. P., Joazeiro, C. A. & Hampton, R. Y. Hrd1p\/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nature Cell Biol. 3, 24\u201329 (2001).","journal-title":"Nature Cell Biol."},{"key":"BFncb1299_CR4","doi-asserted-by":"publisher","first-page":"10663","DOI":"10.1074\/jbc.M008608200","volume":"276","author":"PM Deak","year":"2001","unstructured":"Deak, P. M. & Wolf, D. H. Membrane topology and function of Der3\/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation. J. Biol. Chem. 276, 10663\u201310669 (2001).","journal-title":"J. Biol. Chem."},{"key":"BFncb1299_CR5","doi-asserted-by":"publisher","first-page":"2660","DOI":"10.1101\/gad.933301","volume":"15","author":"R Swanson","year":"2001","unstructured":"Swanson, R., Locher, M. & Hochstrasser, M. A conserved ubiquitin ligase of the nuclear envelope\/endoplasmic reticulum that functions in both ER-associated and Mat\u03b12 repressor degradation. Genes Dev. 15, 2660\u20132674 (2001).","journal-title":"Genes Dev."},{"key":"BFncb1299_CR6","doi-asserted-by":"publisher","first-page":"4114","DOI":"10.1091\/mbc.12.12.4114","volume":"12","author":"NW Bays","year":"2001","unstructured":"Bays, N. W., Wilhovsky, S. K., Goradia, A., Hodgkiss-Harlow, K. & Hampton, R. Y. HRD4\/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Mol. Biol. Cell 12, 4114\u20134128 (2001).","journal-title":"Mol. Biol. Cell"},{"key":"BFncb1299_CR7","doi-asserted-by":"publisher","first-page":"652","DOI":"10.1038\/414652a","volume":"414","author":"Y Ye","year":"2001","unstructured":"Ye, Y., Meyer, H. H. & Rapoport, T. A. The AAA ATPase Cdc48\/p97 and its partners transport proteins from the ER into the cytosol. Nature 414, 652\u2013656 (2001).","journal-title":"Nature"},{"key":"BFncb1299_CR8","doi-asserted-by":"publisher","first-page":"615","DOI":"10.1093\/emboj\/21.4.615","volume":"21","author":"S Braun","year":"2002","unstructured":"Braun, S., Matuschewski, K., Rape, M., Thoms, S. & Jentsch, S. Role of the ubiquitin-selective CDC48(UFD1\/NPL4)chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J. 21, 615\u2013621 (2002).","journal-title":"EMBO J."},{"key":"BFncb1299_CR9","doi-asserted-by":"publisher","first-page":"134","DOI":"10.1038\/ncb746","volume":"4","author":"E Jarosch","year":"2002","unstructured":"Jarosch, E. et al. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nature Cell Biol. 4, 134\u2013139 (2002).","journal-title":"Nature Cell Biol."},{"key":"BFncb1299_CR10","doi-asserted-by":"publisher","first-page":"626","DOI":"10.1128\/MCB.22.2.626-634.2002","volume":"22","author":"E Rabinovich","year":"2002","unstructured":"Rabinovich, E., Kerem, A., Frohlich, K. U., Diamant, N. & Bar-Nun, S. AAA-ATPase p97\/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol. Cell. Biol. 22, 626\u2013634 (2002).","journal-title":"Mol. Cell. Biol."},{"key":"BFncb1299_CR11","doi-asserted-by":"publisher","first-page":"721","DOI":"10.1016\/j.femsyr.2004.02.003","volume":"4","author":"R Hitt","year":"2004","unstructured":"Hitt, R. & Wolf, D. H. Der1p, a protein required for degradation of malfolded soluble proteins of the endoplasmic reticulum: topology and Der1-like proteins. FEMS Yeast Res. 4, 721\u2013729 (2004).","journal-title":"FEMS Yeast Res."},{"key":"BFncb1299_CR12","doi-asserted-by":"publisher","first-page":"834","DOI":"10.1038\/nature02592","volume":"429","author":"BN Lilley","year":"2004","unstructured":"Lilley, B. N. & Ploegh, H. L. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429, 834\u2013840 (2004).","journal-title":"Nature"},{"key":"BFncb1299_CR13","doi-asserted-by":"publisher","first-page":"841","DOI":"10.1038\/nature02656","volume":"429","author":"Y Ye","year":"2004","unstructured":"Ye, Y., Shibata, Y., Yun, C., Ron, D. & Rapoport, T. A. A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429, 841\u2013847 (2004).","journal-title":"Nature"},{"key":"BFncb1299_CR14","doi-asserted-by":"publisher","first-page":"4283","DOI":"10.1242\/jcs.00817","volume":"116","author":"PG Woodman","year":"2003","unstructured":"Woodman, P. G. p97, a protein coping with multiple identities. J. Cell Sci. 116, 4283\u20134290 (2003).","journal-title":"J. Cell Sci."},{"key":"BFncb1299_CR15","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1016\/S0959-440X(02)00315-9","volume":"12","author":"X Zhang","year":"2002","unstructured":"Zhang, X., Beuron, F. & Freemont, P. S. Machinery of protein folding and unfolding. Curr. Opin. Struct. Biol. 12, 231\u2013238 (2002).","journal-title":"Curr. Opin. Struct. Biol."},{"key":"BFncb1299_CR16","doi-asserted-by":"publisher","first-page":"17442","DOI":"10.1074\/jbc.270.29.17442","volume":"270","author":"ES Johnson","year":"1995","unstructured":"Johnson, E. S., Ma, P. C., Ota, I. M. & Varshavsky, A. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270, 17442\u201317456 (1995).","journal-title":"J. Biol. Chem."},{"key":"BFncb1299_CR17","doi-asserted-by":"publisher","first-page":"4884","DOI":"10.1002\/j.1460-2075.1996.tb00869.x","volume":"15","author":"M Ghislain","year":"1996","unstructured":"Ghislain, M., Dohmen, R. J., Levy, F. & Varshavsky, A. Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. EMBO J. 15, 4884\u20134899 (1996).","journal-title":"EMBO J."},{"key":"BFncb1299_CR18","doi-asserted-by":"publisher","first-page":"667","DOI":"10.1016\/S0092-8674(01)00595-5","volume":"107","author":"M Rape","year":"2001","unstructured":"Rape, M. et al. Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1\/NPL4), a ubiquitin-selective chaperone. Cell 107, 667\u2013677 (2001).","journal-title":"Cell"},{"key":"BFncb1299_CR19","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1006\/jmbi.2000.4462","volume":"307","author":"A Buchberger","year":"2001","unstructured":"Buchberger, A., Howard, M. J., Proctor, M. & Bycroft, M. The UBX domain: a widespread ubiquitin-like module. J. Mol. Biol. 307, 17\u201324 (2001).","journal-title":"J. Mol. Biol."},{"key":"BFncb1299_CR20","doi-asserted-by":"publisher","first-page":"216","DOI":"10.1016\/S0962-8924(02)02269-9","volume":"12","author":"A Buchberger","year":"2002","unstructured":"Buchberger, A. From UBA to UBX: new words in the ubiquitin vocabulary. Trends Cell Biol. 12, 216\u2013221 (2002).","journal-title":"Trends Cell Biol."},{"key":"BFncb1299_CR21","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1002\/yea.1071","volume":"21","author":"A Decottignies","year":"2004","unstructured":"Decottignies, A., Evain, A. & Ghislain, M. Binding of Cdc48p to a ubiquitin-related UBX domain from novel yeast proteins involved in intracellular proteolysis and sporulation. Yeast 21, 127\u2013139 (2004).","journal-title":"Yeast"},{"key":"BFncb1299_CR22","doi-asserted-by":"publisher","first-page":"824","DOI":"10.1016\/j.cub.2004.04.029","volume":"14","author":"R Hartmann-Petersen","year":"2004","unstructured":"Hartmann-Petersen, R. et al. The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and nonproteolytic ubiquitin-dependent processes. Curr. Biol. 14, 824\u2013828 (2004).","journal-title":"Curr. Biol."},{"key":"BFncb1299_CR23","doi-asserted-by":"publisher","first-page":"818","DOI":"10.1038\/sj.embor.7400203","volume":"5","author":"C Schuberth","year":"2004","unstructured":"Schuberth, C., Richly, H., Rumpf, S. & Buchberger, A. Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation. EMBO Rep. 5, 818\u2013824 (2004).","journal-title":"EMBO Rep."},{"key":"BFncb1299_CR24","doi-asserted-by":"publisher","first-page":"973","DOI":"10.1083\/jcb.200401010","volume":"164","author":"Y Wang","year":"2004","unstructured":"Wang, Y., Satoh, A., Warren, G. & Meyer, H. H. VCIP135 acts as a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic Golgi fragments. J. Cell Biol. 164, 973\u2013978 (2004).","journal-title":"J. Cell Biol."},{"key":"BFncb1299_CR25","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1242\/jcs.00841","volume":"117","author":"C Wojcik","year":"2004","unstructured":"Wojcik, C., Yano, M. & DeMartino, G. N. RNA interference of valosin-containing protein (VCP\/p97) reveals multiple cellular roles linked to ubiquitin\/proteasome-dependent proteolysis. J. Cell Sci. 117, 281\u2013292 (2004).","journal-title":"J. Cell Sci."},{"key":"BFncb1299_CR26","doi-asserted-by":"publisher","first-page":"2181","DOI":"10.1093\/emboj\/19.10.2181","volume":"19","author":"HH Meyer","year":"2000","unstructured":"Meyer, H. H., Shorter, J. G., Seemann, J., Pappin, D. & Warren, G. A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J. 19, 2181\u20132192 (2000).","journal-title":"EMBO J."},{"key":"BFncb1299_CR27","doi-asserted-by":"publisher","first-page":"1725","DOI":"10.1126\/science.273.5282.1725","volume":"273","author":"MM Hiller","year":"1996","unstructured":"Hiller, M. M., Finger, A., Schweiger, M. & Wolf, D. H. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273, 1725\u20131728 (1996).","journal-title":"Science"},{"key":"BFncb1299_CR28","doi-asserted-by":"publisher","first-page":"2029","DOI":"10.1091\/mbc.7.12.2029","volume":"7","author":"RY Hampton","year":"1996","unstructured":"Hampton, R. Y., Gardner, R. G. & Rine, J. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 7, 2029\u20132044 (1996).","journal-title":"Mol. Biol. Cell"},{"key":"BFncb1299_CR29","doi-asserted-by":"publisher","first-page":"753","DOI":"10.1002\/j.1460-2075.1996.tb00411.x","volume":"15","author":"M Knop","year":"1996","unstructured":"Knop, M., Finger, A., Braun, T., Hellmuth, K. & Wolf, D. H. Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J. 15, 753\u2013763 (1996).","journal-title":"EMBO J."},{"key":"BFncb1299_CR30","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1083\/jcb.200309132","volume":"165","author":"S Vashist","year":"2004","unstructured":"Vashist, S. & Ng, D. T. Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control. J. Cell Biol. 165, 41\u201352 (2004).","journal-title":"J. Cell Biol."},{"key":"BFncb1299_CR31","doi-asserted-by":"publisher","first-page":"1035","DOI":"10.1016\/0092-8674(87)90711-2","volume":"48","author":"D Finley","year":"1987","unstructured":"Finley, D., Ozkaynak, E. & Varshavsky, A. The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses. Cell 48, 1035\u20131046 (1987).","journal-title":"Cell"},{"key":"BFncb1299_CR32","doi-asserted-by":"publisher","first-page":"259","DOI":"10.1002\/(SICI)1097-0061(19960315)12:3<259::AID-YEA901>3.0.CO;2-C","volume":"12","author":"A Wach","year":"1996","unstructured":"Wach, A. PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae. Yeast 12, 259\u2013265 (1996).","journal-title":"Yeast"},{"key":"BFncb1299_CR33","doi-asserted-by":"publisher","first-page":"963","DOI":"10.1002\/(SICI)1097-0061(199907)15:10B<963::AID-YEA399>3.0.CO;2-W","volume":"15","author":"M Knop","year":"1999","unstructured":"Knop, M. et al. Epitope tagging of yeast genes using a PCR-based strategy: more tags and improved practical routines. Yeast 15, 963\u2013972 (1999).","journal-title":"Yeast"}],"container-title":["Nature Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/ncb1299.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/ncb1299","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/ncb1299.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T19:27:02Z","timestamp":1684438022000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/ncb1299"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2005,9,18]]},"references-count":33,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2005,10]]}},"alternative-id":["BFncb1299"],"URL":"https:\/\/doi.org\/10.1038\/ncb1299","relation":{},"ISSN":["1465-7392","1476-4679"],"issn-type":[{"value":"1465-7392","type":"print"},{"value":"1476-4679","type":"electronic"}],"subject":[],"published":{"date-parts":[[2005,9,18]]}}}