{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,26]],"date-time":"2026-02-26T19:34:03Z","timestamp":1772134443051,"version":"3.50.1"},"reference-count":26,"publisher":"Springer Science and Business Media LLC","issue":"7133","license":[{"start":{"date-parts":[[2007,2,18]],"date-time":"2007-02-18T00:00:00Z","timestamp":1171756800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nature"],"published-print":{"date-parts":[[2007,3]]},"DOI":"10.1038\/nature05542","type":"journal-article","created":{"date-parts":[[2007,2,19]],"date-time":"2007-02-19T11:55:09Z","timestamp":1171886109000},"page":"333-337","source":"Crossref","is-referenced-by-count":178,"title":["A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate"],"prefix":"10.1038","volume":"446","author":[{"given":"Wei","family":"Li","sequence":"first","affiliation":[]},{"given":"Daqi","family":"Tu","sequence":"additional","affiliation":[]},{"given":"Axel T.","family":"Brunger","sequence":"additional","affiliation":[]},{"given":"Yihong","family":"Ye","sequence":"additional","affiliation":[]}],"member":"297","published-online":{"date-parts":[[2007,2,18]]},"reference":[{"key":"BFnature05542_CR1","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\u20131583 (1989)","journal-title":"Science"},{"key":"BFnature05542_CR2","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1038\/373081a0","volume":"373","author":"M Scheffner","year":"1995","unstructured":"Scheffner, M., Nuber, U. & Huibregtse, J. M. Protein ubiquitination involving an E1\u2013E2\u2013E3 enzyme ubiquitin thioester cascade. Nature 373, 81\u201383 (1995)","journal-title":"Nature"},{"key":"BFnature05542_CR3","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1016\/j.bbamcr.2004.09.019","volume":"1695","author":"CM Pickart","year":"2004","unstructured":"Pickart, C. M. & Eddins, M. J. Ubiquitin: structures, functions, mechanisms. Biochim. Biophys. Acta 1695, 55\u201372 (2004)","journal-title":"Biochim. Biophys. Acta"},{"key":"BFnature05542_CR4","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1016\/j.cell.2005.12.025","volume":"124","author":"M Hochstrasser","year":"2006","unstructured":"Hochstrasser, M. Lingering mysteries of ubiquitin-chain assembly. Cell 124, 27\u201334 (2006)","journal-title":"Cell"},{"key":"BFnature05542_CR5","doi-asserted-by":"publisher","first-page":"14422","DOI":"10.1073\/pnas.251401598","volume":"98","author":"S Fang","year":"2001","unstructured":"Fang, S. et al. The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc. Natl Acad. Sci. USA 98, 14422\u201314427 (2001)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature05542_CR6","doi-asserted-by":"publisher","first-page":"341","DOI":"10.1073\/pnas.0506618103","volume":"103","author":"B Chen","year":"2006","unstructured":"Chen, B. et al. The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site. Proc. Natl Acad. Sci. USA 103, 341\u2013346 (2006)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature05542_CR7","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1083\/jcb.200302169","volume":"162","author":"Y Ye","year":"2003","unstructured":"Ye, Y., Meyer, H. H. & Rapoport, T. A. Function of the p97\u2013Ufd1\u2013Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol. 162, 71\u201384 (2003)","journal-title":"J. Cell Biol."},{"key":"BFnature05542_CR8","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1107\/S1744309106009006","volume":"62","author":"R Arai","year":"2006","unstructured":"Arai, R. et al. Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2\/UBC7). Acta Crystallogr. F 62, 330\u2013334 (2006)","journal-title":"Acta Crystallogr. F"},{"key":"BFnature05542_CR9","doi-asserted-by":"publisher","first-page":"1107","DOI":"10.1016\/j.cell.2005.09.033","volume":"123","author":"MD Petroski","year":"2005","unstructured":"Petroski, M. D. & Deshaies, R. J. Mechanism of lysine 48-linked ubiquitin-chain synthesis by the cullin-RING ubiquitin-ligase complex SCF\u2013Cdc34. Cell 123, 1107\u20131120 (2005)","journal-title":"Cell"},{"key":"BFnature05542_CR10","doi-asserted-by":"publisher","first-page":"151","DOI":"10.1016\/S0014-5793(03)01009-3","volume":"553","author":"X Sai","year":"2003","unstructured":"Sai, X. et al. The ubiquitin-like domain of Herp is involved in Herp degradation, but not necessary for its enhancement of amyloid \u03b2-protein generation. FEBS Lett. 553, 151\u2013156 (2003)","journal-title":"FEBS Lett."},{"key":"BFnature05542_CR11","doi-asserted-by":"publisher","first-page":"457","DOI":"10.1111\/j.1356-9597.2004.00735.x","volume":"9","author":"O Hori","year":"2004","unstructured":"Hori, O. et al. Role of Herp in the endoplasmic reticulum stress response. Genes Cells 9, 457\u2013469 (2004)","journal-title":"Genes Cells"},{"key":"BFnature05542_CR12","doi-asserted-by":"publisher","first-page":"1021","DOI":"10.1016\/j.jmb.2005.10.020","volume":"354","author":"A Schulze","year":"2005","unstructured":"Schulze, A. et al. The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway. J. Mol. Biol. 354, 1021\u20131027 (2005)","journal-title":"J. Mol. Biol."},{"key":"BFnature05542_CR13","doi-asserted-by":"publisher","first-page":"32846","DOI":"10.1074\/jbc.M002063200","volume":"275","author":"K Kokame","year":"2000","unstructured":"Kokame, K., Agarwala, K. L., Kato, H. & Miyata, T. Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress. J. Biol. Chem. 275, 32846\u201332853 (2000)","journal-title":"J. Biol. Chem."},{"key":"BFnature05542_CR14","doi-asserted-by":"crossref","first-page":"24766","DOI":"10.1016\/S0021-9258(19)74530-X","volume":"268","author":"S van Nocker","year":"1993","unstructured":"van Nocker, S. & Vierstra, R. D. Multiubiquitin chains linked through lysine 48 are abundant in vivo and are competent intermediates in the ubiquitin proteolytic pathway. J. Biol. Chem. 268, 24766\u201324773 (1993)","journal-title":"J. Biol. Chem."},{"key":"BFnature05542_CR15","doi-asserted-by":"publisher","first-page":"1499","DOI":"10.1126\/science.1120160","volume":"310","author":"QP Vong","year":"2005","unstructured":"Vong, Q. P., Cao, K., Li, H. Y., Iglesias, P. A. & Zheng, Y. Chromosome alignment and segregation regulated by ubiquitination of survivin. Science 310, 1499\u20131504 (2005)","journal-title":"Science"},{"key":"BFnature05542_CR16","doi-asserted-by":"publisher","first-page":"3091","DOI":"10.1002\/j.1460-2075.1992.tb05381.x","volume":"11","author":"ET Silver","year":"1992","unstructured":"Silver, E. T., Gwozd, T. J., Ptak, C., Goebl, M. & Ellison, M. J. A chimeric ubiquitin conjugating enzyme that combines the cell cycle properties of CDC34 (UBC3) and the DNA repair properties of RAD6 (UBC2): implications for the structure, function and evolution of the E2s. EMBO J. 11, 3091\u20133098 (1992)","journal-title":"EMBO J."},{"key":"BFnature05542_CR17","doi-asserted-by":"publisher","first-page":"357","DOI":"10.1016\/0092-8674(93)90426-Q","volume":"74","author":"P Chen","year":"1993","unstructured":"Chen, P., Johnson, P., Sommer, T., Jentsch, S. & Hochstrasser, M. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT\u03b12 repressor. Cell 74, 357\u2013369 (1993)","journal-title":"Cell"},{"key":"BFnature05542_CR18","doi-asserted-by":"publisher","first-page":"5388","DOI":"10.1128\/MCB.23.15.5388-5400.2003","volume":"23","author":"X Varelas","year":"2003","unstructured":"Varelas, X., Ptak, C. & Ellison, M. J. Cdc34 self-association is facilitated by ubiquitin thiolester formation and is required for its catalytic activity. Mol. Cell. Biol. 23, 5388\u20135400 (2003)","journal-title":"Mol. Cell. Biol."},{"key":"BFnature05542_CR19","doi-asserted-by":"publisher","first-page":"915","DOI":"10.1038\/nsmb1148","volume":"13","author":"MJ Eddins","year":"2006","unstructured":"Eddins, M. J., Carlile, C. M., Gomez, K. M., Pickart, C. M. & Wolberger, C. Mms2\u2013Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation. Nature Struct. Mol. Biol. 13, 915\u2013920 (2006)","journal-title":"Nature Struct. Mol. Biol."},{"key":"BFnature05542_CR20","doi-asserted-by":"publisher","first-page":"15053","DOI":"10.1073\/pnas.0507646102","volume":"102","author":"S Gazdoiu","year":"2005","unstructured":"Gazdoiu, S. et al. Proximity-induced activation of human Cdc34 through heterologous dimerization. Proc. Natl Acad. Sci. USA 102, 15053\u201315058 (2005)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature05542_CR21","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\u201311369 (1999)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature05542_CR22","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\u2013312 (1999)","journal-title":"Science"},{"key":"BFnature05542_CR23","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\u2013CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I\u03baB\u03b1. Mol. Cell 3, 527\u2013533 (1999)","journal-title":"Mol. Cell"},{"key":"BFnature05542_CR24","doi-asserted-by":"crossref","first-page":"26661","DOI":"10.1016\/S0021-9258(19)61427-4","volume":"275","author":"H Huang","year":"2000","unstructured":"Huang, H. 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\u201326664 (2000)","journal-title":"J. Biol. Chem."},{"key":"BFnature05542_CR25","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":"BFnature05542_CR26","doi-asserted-by":"publisher","first-page":"945","DOI":"10.1016\/S1097-2765(02)00519-1","volume":"9","author":"Z Lu","year":"2002","unstructured":"Lu, Z., Xu, S., Joazeiro, C., Cobb, M. H. & Hunter, T. The PHD domain of MEKK1 acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1\/2. Mol. Cell 9, 945\u2013956 (2002)","journal-title":"Mol. Cell"}],"container-title":["Nature"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nature05542.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nature05542","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nature05542.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T14:02:04Z","timestamp":1684418524000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nature05542"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2007,2,18]]},"references-count":26,"journal-issue":{"issue":"7133","published-print":{"date-parts":[[2007,3]]}},"alternative-id":["BFnature05542"],"URL":"https:\/\/doi.org\/10.1038\/nature05542","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.1071845.524841","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.1071845.524774","asserted-by":"object"}]},"ISSN":["0028-0836","1476-4687"],"issn-type":[{"value":"0028-0836","type":"print"},{"value":"1476-4687","type":"electronic"}],"subject":[],"published":{"date-parts":[[2007,2,18]]}}}