{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,6]],"date-time":"2026-06-06T21:56:50Z","timestamp":1780783010021,"version":"3.54.1"},"reference-count":29,"publisher":"Springer Science and Business Media LLC","issue":"6700","license":[{"start":{"date-parts":[[1998,9,1]],"date-time":"1998-09-01T00:00:00Z","timestamp":904608000000},"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":[[1998,9]]},"DOI":"10.1038\/26506","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T08:39:15Z","timestamp":1027672755000},"page":"395-398","source":"Crossref","is-referenced-by-count":1437,"title":["A protein conjugation system essential for autophagy"],"prefix":"10.1038","volume":"395","author":[{"given":"Noboru","family":"Mizushima","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takeshi","family":"Noda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tamotsu","family":"Yoshimori","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yae","family":"Tanaka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tomoko","family":"Ishii","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael D.","family":"George","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel J.","family":"Klionsky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mariko","family":"Ohsumi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshinori","family":"Ohsumi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","reference":[{"key":"BF26506_CR1","doi-asserted-by":"publisher","first-page":"301","DOI":"10.1083\/jcb.119.2.301","volume":"119","author":"K Takeshige","year":"1992","unstructured":"Takeshige, K., Baba, M., Tsuboi, S., Noda, T. & Ohsumi, Y. Autophagy in yeast demonstrated with proteinase-deficient mutants and condtions for its induction. J. Cell Biol. 119, 301\u2013311 (1992).","journal-title":"J. Cell Biol."},{"key":"BF26506_CR2","doi-asserted-by":"publisher","first-page":"903","DOI":"10.1083\/jcb.124.6.903","volume":"124","author":"M Baba","year":"1994","unstructured":"Baba, M., Takeshige, K., Baba, N. & Ohsumi, Y. Ultrastructural analysis of the autophagic process in yeast: Detection of autophagosomes and their characterization. J. Cell Biol. 124, 903\u2013913 (1994).","journal-title":"J. Cell Biol."},{"key":"BF26506_CR3","doi-asserted-by":"publisher","first-page":"158","DOI":"10.1007\/BF01923509","volume":"48","author":"PO Seglen","year":"1992","unstructured":"Seglen, P. O. & Bohley, P. Autophagy and other vacuolar protein degradation mechanisms. Experientia 48, 158\u2013172 (1992).","journal-title":"Experientia"},{"key":"BF26506_CR4","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1016\/0962-8924(94)90069-8","volume":"4","author":"WAJ Dunn","year":"1994","unstructured":"Dunn, W. A. J Autophagy and related mechanisms of lysome-mediated protein degradation. Trends Cell Biol. 4, 139\u2013143 (1994).","journal-title":"Trends Cell Biol."},{"key":"BF26506_CR5","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1016\/0014-5793(93)80398-E","volume":"333","author":"M Tsukada","year":"1993","unstructured":"Tsukada, M. & Ohsumi, Y. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett. 333, 169\u2013174 (1993).","journal-title":"FEBS Lett."},{"key":"BF26506_CR6","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1016\/0378-1119(96)00354-X","volume":"178","author":"S Kametaka","year":"1996","unstructured":"Kametaka, S., Matsuura, A., Wada, Y. & Ohsumi, Y. Structural and functional analyses of APG5, a gene involved in autophagy in yeast. Gene 178, 139\u2013143 (1996).","journal-title":"Gene"},{"key":"BF26506_CR7","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1016\/S0378-1119(97)00084-X","volume":"192","author":"A Matsuura","year":"1997","unstructured":"Matsuura, A., Tsukada, M., Wada, Y. & Ohsumi, Y. Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae. Gene 192, 245\u2013250 (1997).","journal-title":"Gene"},{"key":"BF26506_CR8","doi-asserted-by":"publisher","first-page":"207","DOI":"10.1016\/S0378-1119(97)00031-0","volume":"192","author":"T Funakoshi","year":"1997","unstructured":"Funakoshi, T., Matsuura, A., Noda, T. & Ohsumi, Y. Analyses of APG13 gene involved in autophagy in yeast, Saccharomyces cerevisiae. Gene 192, 207\u2013213 (1997).","journal-title":"Gene"},{"key":"BF26506_CR9","unstructured":"Kametaka, S., Okano, T., Ohsumi, M. & Ohsumi, Y. Apg14p and Apg6p\/Vps30p form a protein complex essential for autophagy in the yeast Saccharomyces cerevisiae. J. Biol. Chem. (in the press)."},{"key":"BF26506_CR10","doi-asserted-by":"publisher","first-page":"126","DOI":"10.1006\/bbrc.1995.1636","volume":"210","author":"T Noda","year":"1995","unstructured":"Noda, T., Matsuura, A., Wada, Y. & Ohsumi, Y. Novel system for monitoring autophagy in the yeast Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 210, 126\u2013132 (1995).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"BF26506_CR11","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1083\/jcb.119.2.287","volume":"119","author":"DJ Klionsky","year":"1992","unstructured":"Klionsky, D. J., Cueva, R. & Yaver, D. S. Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway. J. Cell Biol. 119, 287\u2013299 (1992).","journal-title":"J. Cell Biol."},{"key":"BF26506_CR12","doi-asserted-by":"publisher","first-page":"1687","DOI":"10.1083\/jcb.139.7.1687","volume":"139","author":"M Baba","year":"1997","unstructured":"Baba, M., Osumi, M., Scott, S. V., Klionsky, D. J. & Ohsumi, Y. Two distinct pathways for targeting proteins from the cytoplasm to the vacuole\/lysome. J. Cell Biol. 139, 1687\u20131695 (1997).","journal-title":"J. Cell Biol."},{"key":"BF26506_CR13","doi-asserted-by":"publisher","first-page":"12304","DOI":"10.1073\/pnas.93.22.12304","volume":"93","author":"SV Scott","year":"1996","unstructured":"Scott, S. V. et al. Cytoplasm-to-vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole. Proc. Natl Acad. Sci. USA 93, 12304\u201312308 (1996).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BF26506_CR14","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1146\/annurev.genet.30.1.405","volume":"30","author":"M Hochstrasser","year":"1996","unstructured":"Hochstrasser, M. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405\u2013429 (1996).","journal-title":"Annu. Rev. Genet."},{"key":"BF26506_CR15","doi-asserted-by":"publisher","first-page":"383","DOI":"10.1016\/S0968-0004(97)01122-5","volume":"22","author":"A Varshavsky","year":"1997","unstructured":"Varshavsky, A. The ubiquitin system. Trends Biochem. Sci. 22, 383\u2013387 (1997).","journal-title":"Trends Biochem. Sci."},{"key":"BF26506_CR16","doi-asserted-by":"publisher","first-page":"189","DOI":"10.1016\/S0167-5699(97)84666-X","volume":"18","author":"AM Weissman","year":"1997","unstructured":"Weissman, A. M. Regulating protein degradation by ubiquitination. Immunol. Today 18, 189\u2013198 (1997).","journal-title":"Immunol. Today"},{"key":"BF26506_CR17","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1002\/j.1460-2075.1991.tb07940.x","volume":"10","author":"JP McGrath","year":"1991","unstructured":"McGrath, J. P., Jentsch, S. & Varshavsky, A. UBA1: an essential yeast gene encoding ubiquitin-activating enzyme. EMBO J. 10, 227\u2013236 (1991).","journal-title":"EMBO J."},{"key":"BF26506_CR18","doi-asserted-by":"publisher","first-page":"1457","DOI":"10.1083\/jcb.135.6.1457","volume":"135","author":"MJ Matunis","year":"1996","unstructured":"Matunis, M. J., Coutavas, E. & Blobel, G. Anovel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 135, 1457\u20131470 (1996).","journal-title":"J. Cell Biol."},{"key":"BF26506_CR19","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1016\/S0092-8674(00)81862-0","volume":"88","author":"R Mahajan","year":"1997","unstructured":"Mahajan, R., Delphin, C., Guan, T., Gerace, L. & Melchior, F. Asmall ubiquitin-related polypeptide involved in targeting RasGAP1 to nuclear pore complex protein RanBP2. Cell 88, 97\u2013107 (1997).","journal-title":"Cell"},{"key":"BF26506_CR20","doi-asserted-by":"publisher","first-page":"259","DOI":"10.1083\/jcb.140.2.259","volume":"140","author":"R Mahajan","year":"1998","unstructured":"Mahajan, R., Gerace, L. & Melchior, F. Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association. J. Cell Biol. 140, 259\u2013270 (1998).","journal-title":"J. Cell Biol."},{"key":"BF26506_CR21","doi-asserted-by":"publisher","first-page":"499","DOI":"10.1083\/jcb.140.3.499","volume":"140","author":"MJ Matunis","year":"1998","unstructured":"Matunis, M. J., Wu, J. & Blobel, G. SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex. J. Cell Biol. 140, 499\u2013509 (1998).","journal-title":"J. Cell Biol."},{"key":"BF26506_CR22","doi-asserted-by":"publisher","first-page":"5509","DOI":"10.1093\/emboj\/16.18.5509","volume":"16","author":"ES Johnson","year":"1997","unstructured":"Johnson, E. S., Schwienhorst, I., Dohmen, R. J. & Blobel, G. The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p\/Uba2p heterodimer. EMBO J. 16, 5509\u20135519 (1997).","journal-title":"EMBO J."},{"key":"BF26506_CR23","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. Anovel protein modification pathway related to the ubiquitin system. EMBO J. 17, 2208\u20132214 (1998).","journal-title":"EMBO J."},{"key":"BF26506_CR24","doi-asserted-by":"publisher","first-page":"914","DOI":"10.1101\/gad.12.7.914","volume":"12","author":"D Lammer","year":"1998","unstructured":"Lammer, D. et al. Modification of yeast Cdc53p by the ubiquitin-related protein Rub1p affects function of the SCFCdc4 complex. Genes Dev. 12, 914\u2013926 (1998).","journal-title":"Genes Dev."},{"key":"BF26506_CR25","unstructured":"Osaka, F. et al. Anew Nedd8-ligating system for cullin-4A. Genes Dev. (in the press)."},{"key":"BF26506_CR26","doi-asserted-by":"publisher","first-page":"391","DOI":"10.1016\/S0014-5793(98)00266-X","volume":"425","author":"EM Hammond","year":"1998","unstructured":"Hammond, E. M. et al. Homology between a human apoptosis specific protein and the product of APG5, a gene involved in autophagy in yeast. FEBS Lett. 425, 391\u2013395 (1998).","journal-title":"FEBS Lett."},{"key":"BF26506_CR27","doi-asserted-by":"publisher","first-page":"3963","DOI":"10.1074\/jbc.273.7.3963","volume":"273","author":"T Noda","year":"1998","unstructured":"Noda, T. & Ohsumi, Y. Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. J. Biol. Chem. 273, 3963\u20133966 (1998).","journal-title":"J. Biol. Chem."},{"key":"BF26506_CR28","doi-asserted-by":"publisher","first-page":"9193","DOI":"10.1074\/jbc.271.16.9193","volume":"271","author":"Y Kamada","year":"1996","unstructured":"Kamada, Y. et al. Activation of yeast protein kinase C by Rho1 GTPase. J. Biol. Chem. 271, 9193\u20139196 (1996).","journal-title":"J. Biol. Chem."},{"key":"BF26506_CR29","doi-asserted-by":"publisher","first-page":"633","DOI":"10.1091\/mbc.3.6.633","volume":"3","author":"A Antebi","year":"1992","unstructured":"Antebi, A. & Fink, G. R. The yeast Ca2+-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol. Biol. Cell 3, 633\u2013654 (1992).","journal-title":"Mol. Biol. Cell"}],"container-title":["Nature"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/26506.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/26506","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/26506.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,17]],"date-time":"2023-05-17T00:15:00Z","timestamp":1684282500000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/26506"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,9]]},"references-count":29,"journal-issue":{"issue":"6700","published-print":{"date-parts":[[1998,9]]}},"alternative-id":["BF26506"],"URL":"https:\/\/doi.org\/10.1038\/26506","relation":{},"ISSN":["0028-0836","1476-4687"],"issn-type":[{"value":"0028-0836","type":"print"},{"value":"1476-4687","type":"electronic"}],"subject":[],"published":{"date-parts":[[1998,9]]}}}