{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T20:02:50Z","timestamp":1792267370141,"version":"4.4.0"},"reference-count":38,"publisher":"Elsevier BV","issue":"28","license":[{"start":{"date-parts":[[2014,7,1]],"date-time":"2014-07-01T00:00:00Z","timestamp":1404172800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,10]],"date-time":"2020-09-10T00:00:00Z","timestamp":1599696000000},"content-version":"vor","delay-in-days":2263,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2014,7]]},"DOI":"10.1074\/jbc.m114.549915","type":"journal-article","created":{"date-parts":[[2014,6,3]],"date-time":"2014-06-03T05:56:11Z","timestamp":1401774971000},"page":"19714-19725","source":"Crossref","is-referenced-by-count":67,"title":["Endoplasmic Reticulum-associated Degradation of Niemann-Pick C1"],"prefix":"10.1016","volume":"289","author":[{"given":"Naoe","family":"Nakasone","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuko S.","family":"Nakamura","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katsumi","family":"Higaki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nao","family":"Oumi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kousaku","family":"Ohno","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haruaki","family":"Ninomiya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M114.549915_bib1","first-page":"3611","article-title":"Niemann-Pick disease type C: a lipid trafficking disorder","author":"Patterson","year":"2001"},{"key":"10.1074\/jbc.M114.549915_bib2","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1126\/science.277.5323.228","article-title":"Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis","volume":"277","author":"Carstea","year":"1997","journal-title":"Science"},{"key":"10.1074\/jbc.M114.549915_bib3","doi-asserted-by":"crossref","first-page":"2298","DOI":"10.1126\/science.290.5500.2298","article-title":"Identification of HE1 as the second gene of Niemann-Pick C disease","volume":"290","author":"Naureckiene","year":"2000","journal-title":"Science"},{"key":"10.1074\/jbc.M114.549915_bib4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/mgme.1999.2882","article-title":"Niemann-Pick C1 is a late endosome-resident protein that transiently associates with lysosomes and the trans-Golgi network","volume":"68","author":"Higgins","year":"1999","journal-title":"Mol. Genet. Metab"},{"key":"10.1074\/jbc.M114.549915_bib5","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.bbalip.2004.08.007","article-title":"Structure and function of the NPC2 protein","volume":"1685","author":"Vanier","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.M114.549915_bib6","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1093\/brain\/awl260","article-title":"The adult form of Niemann-Pick disease type C","volume":"130","author":"S\u00e9vin","year":"2007","journal-title":"Brain"},{"key":"10.1074\/jbc.M114.549915_bib7","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1136\/jmg.37.9.707","article-title":"Genotype-phenotype relationship of Niemann-Pick disease type C: a possible correlation between clinical onset and levels of NPC1 protein in isolated skin fibroblasts","volume":"37","author":"Yamamoto","year":"2000","journal-title":"J. Med. Genet"},{"key":"10.1074\/jbc.M114.549915_bib8","doi-asserted-by":"crossref","first-page":"1373","DOI":"10.1086\/320606","article-title":"Niemann-Pick C1 disease: correlations between NPC1 mutations, levels of NPC1 protein, and phenotypes emphasize the functional significance of the putative sterol-sensing domain and of the cysteine-rich luminal loop","volume":"68","author":"Millat","year":"2001","journal-title":"Am. J. Hum. Genet"},{"key":"10.1074\/jbc.M114.549915_bib9","doi-asserted-by":"crossref","first-page":"8229","DOI":"10.1074\/jbc.M708735200","article-title":"Niemann-Pick type C1 I1061T mutant encodes a functional protein that is selected for endoplasmic reticulum-associated degradation due to protein misfolding","volume":"283","author":"Gelsthorpe","year":"2008","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.549915_bib10","doi-asserted-by":"crossref","first-page":"12391","DOI":"10.1073\/pnas.221181998","article-title":"Accumulation of cholera toxin and GM1 ganglioside in the early endosome of Niemann-Pick C1-deficient cells","volume":"98","author":"Sugimoto","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.549915_bib11","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/S0387-7604(03)00162-1","article-title":"Increased NPC1 mRNA in skin fibroblasts from Niemann-Pick disease type C patients","volume":"26","author":"Yamamoto","year":"2004","journal-title":"Brain Dev"},{"key":"10.1074\/jbc.M114.549915_bib12","doi-asserted-by":"crossref","first-page":"3205","DOI":"10.1093\/hmg\/dds145","article-title":"Ryanodine receptor antagonists adapt NPC1 proteostasis to ameliorate lipid storage in Niemann-Pick type C disease fibroblasts","volume":"21","author":"Yu","year":"2012","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M114.549915_bib13","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1007\/8904_2011_49","article-title":"Treatment of human fibroblasts carrying NPC1 missense mutations with MG132 leads to an improvement of intracellular cholesterol trafficking","volume":"2","author":"Zampieri","year":"2012","journal-title":"JIMD Rep"},{"key":"10.1074\/jbc.M114.549915_bib14","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/j.chembiol.2013.02.009","article-title":"Discovery of oxysterol-derived pharmacological chaperones for NPC1: implication for the existence of second sterol-binding site","volume":"20","author":"Ohgane","year":"2013","journal-title":"Chem. Biol"},{"key":"10.1074\/jbc.M114.549915_bib15","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1016\/j.cell.2012.11.012","article-title":"Cleaning up: ER-associated degradation to the rescue","volume":"151","author":"Brodsky","year":"2012","journal-title":"Cell"},{"key":"10.1074\/jbc.M114.549915_bib16","doi-asserted-by":"crossref","first-page":"2447","DOI":"10.1016\/j.bbamcr.2013.03.018","article-title":"How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: the early history of ERAD","volume":"1833","author":"Needham","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.M114.549915_bib17","doi-asserted-by":"crossref","first-page":"24367","DOI":"10.1074\/jbc.M002184200","volume":"275","author":"Davies","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.549915_bib18","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1161\/CIRCRESAHA.110.227835","article-title":"Reciprocal control of hERG stability by Hsp70 and Hsc70 with implication for restoration of LQT2 mutant stability","volume":"108","author":"Li","year":"2011","journal-title":"Circ. Res"},{"key":"10.1074\/jbc.M114.549915_bib19","doi-asserted-by":"crossref","first-page":"34908","DOI":"10.1074\/jbc.M506288200","article-title":"Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models","volume":"280","author":"Fujimoto","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.549915_bib20","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.bbadis.2004.03.007","article-title":"N-Octyl-\u03b2-valienamine up-regulates activity of F213I mutant \u03b2-glucosidase in cultured cells: a potential chemical chaperone therapy for Gaucher disease","volume":"1689","author":"Lin","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.M114.549915_bib21","doi-asserted-by":"crossref","first-page":"2643","DOI":"10.1242\/jcs.02993","article-title":"Cholesterol depletion facilitates ubiquitination of NPC1 and its association with SKD1\/Vps4","volume":"119","author":"Ohsaki","year":"2006","journal-title":"J. Cell Sci"},{"key":"10.1074\/jbc.M114.549915_bib22","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1038\/ncb0805-736","article-title":"Protein quality control: chaperones culling corrupt conformations","volume":"7","author":"McClellan","year":"2005","journal-title":"Nat. Cell Biol"},{"key":"10.1074\/jbc.M114.549915_bib23","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1093\/embo-reports\/kve246","article-title":"CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein","volume":"2","author":"Murata","year":"2001","journal-title":"EMBO Rep"},{"key":"10.1074\/jbc.M114.549915_bib24","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1038\/ncb0805-766","article-title":"ERAD: the long road to destruction","volume":"7","author":"Meusser","year":"2005","journal-title":"Nat. Cell Biol"},{"key":"10.1074\/jbc.M114.549915_bib25","doi-asserted-by":"crossref","first-page":"31069","DOI":"10.1074\/jbc.M113.479345","article-title":"Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp\/c70 and the CHIP E3 ligase","volume":"288","author":"Matsumura","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.549915_bib26","doi-asserted-by":"crossref","first-page":"38673","DOI":"10.1074\/jbc.M507986200","article-title":"Regulation of the cytoplasmic quality control protein degradation pathway by BAG2","volume":"280","author":"Dai","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.549915_bib27","doi-asserted-by":"crossref","first-page":"5891","DOI":"10.1091\/mbc.e05-07-0660","article-title":"BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP","volume":"16","author":"Arndt","year":"2005","journal-title":"Mol. Biol. Cell"},{"key":"10.1074\/jbc.M114.549915_bib28","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1038\/35050509","article-title":"The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation","volume":"3","author":"Meacham","year":"2001","journal-title":"Nat. Cell Biol"},{"key":"10.1074\/jbc.M114.549915_bib29","doi-asserted-by":"crossref","first-page":"5817","DOI":"10.1073\/pnas.0507903103","article-title":"Differential effects of Hsc70 and Hsp70 on the intracellular trafficking and functional expression of epithelial sodium channels","volume":"103","author":"Goldfarb","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.549915_bib30","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1093\/cvr\/cvt200","article-title":"Hsp90 prevents interaction between CHIP and HERG proteins to facilitate maturation of wild-type and mutant HERG proteins","volume":"100","author":"Iwai","year":"2013","journal-title":"Cardiovasc. Res"},{"key":"10.1074\/jbc.M114.549915_bib31","doi-asserted-by":"crossref","first-page":"16801","DOI":"10.1073\/pnas.0506249102","article-title":"Pharmacological induction of heat-shock proteins alleviates polyglutamine-mediated motor neuron disease","volume":"102","author":"Katsuno","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.549915_bib32","doi-asserted-by":"crossref","first-page":"1832","DOI":"10.1111\/j.1476-5381.2011.01204.x","article-title":"Transcriptional activation of the anchoring protein SAP97 by heat shock factor (HSF)-1 stabilizes K(v) 1.5 channels in HL-1 cells","volume":"162","author":"Ting","year":"2011","journal-title":"Br. J. Pharmacol"},{"key":"10.1074\/jbc.M114.549915_bib33","doi-asserted-by":"crossref","first-page":"1458","DOI":"10.1021\/ac048834d","article-title":"Approach for determining protein ubiquitination sites by MALDI-TOF mass spectrometry","volume":"77","author":"Wang","year":"2005","journal-title":"Anal. Chem"},{"key":"10.1074\/jbc.M114.549915_bib34","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1016\/j.molcel.2005.08.009","article-title":"Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG-CoA reductase","volume":"19","author":"Song","year":"2005","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M114.549915_bib35","doi-asserted-by":"crossref","first-page":"5620","DOI":"10.1073\/pnas.1014890108","article-title":"Histone deacetylase inhibitor treatment dramatically reduces cholesterol accumulation in Niemann-Pick type C1 mutant human fibroblasts","volume":"108","author":"Pipalia","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.549915_bib36","doi-asserted-by":"crossref","first-page":"23842","DOI":"10.1074\/jbc.M111.227645","article-title":"An \u201cexacerbate-reverse\u201d strategy in yeast identifies histone deacetylase inhibition as a correction for cholesterol and sphingolipid transport defects in human Niemann-Pick type C disease","volume":"286","author":"Munkacsi","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.549915_bib37","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.molcel.2006.12.008","article-title":"An acetylation site in the middle domain of Hsp90 regulates chaperone function","volume":"25","author":"Scroggins","year":"2007","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M114.549915_bib38","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1038\/nchembio.275","article-title":"Reduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosis","volume":"6","author":"Hutt","year":"2010","journal-title":"Nat. Chem. Biol"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820477348?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820477348?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M114.549915","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,7,10]],"date-time":"2021-07-10T21:16:03Z","timestamp":1625951763000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820477348"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,7]]},"references-count":38,"journal-issue":{"issue":"28","published-print":{"date-parts":[[2014,7]]}},"alternative-id":["S0021925820477348"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m114.549915","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2014,7]]}}}