{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T06:16:37Z","timestamp":1740118597407,"version":"3.37.3"},"reference-count":27,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2016,6,1]],"date-time":"2016-06-01T00:00:00Z","timestamp":1464739200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japanese Society for the Promotion of Science","doi-asserted-by":"crossref","award":["#24249008"],"award-info":[{"award-number":["#24249008"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"published-print":{"date-parts":[[2016,6]]},"DOI":"10.1016\/j.bbagen.2016.03.026","type":"journal-article","created":{"date-parts":[[2016,3,22]],"date-time":"2016-03-22T23:15:19Z","timestamp":1458688519000},"page":"1326-1333","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":4,"title":["Whi2 enhances methylmercury toxicity in yeast via inhibition of Akr1 palmitoyltransferase activity"],"prefix":"10.1016","volume":"1860","author":[{"given":"Gi-Wook","family":"Hwang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Toru","family":"Fukumitsu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yousuke","family":"Ogiwara","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tsutomu","family":"Takahashi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nobuhiko","family":"Miura","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shusuke","family":"Kuge","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Akira","family":"Naganuma","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbagen.2016.03.026_bb0005","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1007\/BF03033386","article-title":"Neurotoxicity of organomercurial compounds","volume":"5","author":"Sanfeliu","year":"2003","journal-title":"Neurotox. Res."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0010","doi-asserted-by":"crossref","first-page":"1885","DOI":"10.1001\/jama.296.15.1885","article-title":"Fish intake, contaminants, and human health: evaluating the risks and the benefits","volume":"296","author":"Mozaffarian","year":"2006","journal-title":"JAMA"},{"key":"10.1016\/j.bbagen.2016.03.026_bb0015","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1096\/fj.01-0899fje","article-title":"A ubiquitin\u2013proteasome system is responsible for the protection of yeast and human cells against methylmercury","volume":"16","author":"Hwang","year":"2002","journal-title":"FASEB J."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0020","doi-asserted-by":"crossref","first-page":"6813","DOI":"10.1016\/j.febslet.2006.11.045","article-title":"Identification of F-box proteins that are involved in resistance to methylmercury in Saccharomyces cerevisiae","volume":"580","author":"Hwang","year":"2006","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0025","doi-asserted-by":"crossref","first-page":"413","DOI":"10.2131\/jts.34.413","article-title":"Overexpression of the novel F-box protein Ymr258c confers resistance to methylmercury in Saccharomyces cerevisiae","volume":"34","author":"Hwang","year":"2009","journal-title":"J. Toxicol. Sci."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0030","doi-asserted-by":"crossref","first-page":"2720","DOI":"10.1016\/j.febslet.2015.08.016","article-title":"Identification of substrates of F-box protein involved in methylmercury toxicity in yeast cells","volume":"589","author":"Lee","year":"2015","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0035","doi-asserted-by":"crossref","first-page":"301","DOI":"10.2131\/jts.38.301","article-title":"Deletion of the ubiquitin-conjugating enzyme Ubc2 confers resistance to methylmercury in budding yeast by promoting Whi2 degradation","volume":"38","author":"Hwang","year":"2013","journal-title":"J. Toxicol. Sci."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0040","doi-asserted-by":"crossref","first-page":"1283","DOI":"10.2131\/jts.37.1283","article-title":"Ubiquitin-conjugating enzyme Cdc34 mediates methylmercury resistance in Saccharomyces cerevisiae by increasing Whi2 degradation","volume":"37","author":"Hwang","year":"2012","journal-title":"J. Toxicol. Sci."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0045","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1002\/(SICI)1097-0061(19970630)13:8<707::AID-YEA130>3.0.CO;2-9","article-title":"Deregulation of CLN1 and CLN2 in the Saccharomyces cerevisiae whi2 mutant","volume":"13","author":"Radcliffe","year":"1997","journal-title":"Yeast"},{"key":"10.1016\/j.bbagen.2016.03.026_bb0050","doi-asserted-by":"crossref","first-page":"276","DOI":"10.2144\/04362RR02","article-title":"Labeling and quantifying sites of protein palmitoylation","volume":"36","author":"Drisdel","year":"2004","journal-title":"Biotechniques"},{"key":"10.1016\/j.bbagen.2016.03.026_bb0055","doi-asserted-by":"crossref","first-page":"5888","DOI":"10.1038\/srep05888","article-title":"The protein transportation pathway from Golgi to vacuoles via endosomes plays a role in enhancement of methylmercury toxicity","volume":"4","author":"Hwang","year":"2014","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0060","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/0003-2697(84)90782-6","article-title":"A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids","volume":"138","author":"Wessel","year":"1984","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0065","doi-asserted-by":"crossref","first-page":"861","DOI":"10.2131\/jts.39.861","article-title":"FBXO6 attenuates cadmium toxicity in HEK293 cells by inhibiting ER stress and JNK activation","volume":"39","author":"Du","year":"2014","journal-title":"J. Toxicol. Sci."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0070","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1016\/j.bbrc.2007.09.064","article-title":"Ubiquitin-conjugating enzyme Cdc34 mediates cadmium resistance in budding yeast through ubiquitination of the transcription factor Met4","volume":"363","author":"Hwang","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0075","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1242\/jcs.00989","article-title":"Model organisms lead the way to protein palmitoyltransferases","volume":"117","author":"Linder","year":"2004","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0080","first-page":"re14","article-title":"Palmitoylation of ligands, receptors, and intracellular signaling molecules","author":"Resh","year":"2006","journal-title":"Sci. STKE"},{"key":"10.1016\/j.bbagen.2016.03.026_bb0085","doi-asserted-by":"crossref","first-page":"9189","DOI":"10.1128\/MCB.25.21.9189-9197.2005","article-title":"Long-chain base kinase Lcb4 Is anchored to the membrane through its palmitoylation by Akr1","volume":"25","author":"Kihara","year":"2005","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0090","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1016\/j.cell.2006.03.042","article-title":"Global analysis of protein palmitoylation in yeast","volume":"125","author":"Roth","year":"2006","journal-title":"Cell"},{"key":"10.1016\/j.bbagen.2016.03.026_bb0095","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1083\/jcb.200206120","article-title":"The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase","volume":"159","author":"Roth","year":"2002","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0100","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1016\/j.freeradbiomed.2009.05.013","article-title":"Methylmercury neurotoxicity is associated with inhibition of the antioxidant enzyme glutathione peroxidase","volume":"47","author":"Franco","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0105","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1007\/s12640-014-9494-8","article-title":"Correlation between attenuation of protein disulfide isomerase activity through S-mercuration and neurotoxicity induced by methylmercury","volume":"27","author":"Makino","year":"2015","journal-title":"Neurotox. Res."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0110","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0006-8993(94)91808-2","article-title":"The role of -SH groups in methylmercuric chloride-induced d-aspartate and rubidium release from rat primary astrocyte cultures","volume":"641","author":"Mullaney","year":"1994","journal-title":"Brain Res."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0115","doi-asserted-by":"crossref","first-page":"1780","DOI":"10.1021\/tx5002332","article-title":"Glutathione adduct of methylmercury activates the Keap1\u2013Nrf2 pathway in SH-SY5Y cells","volume":"27","author":"Yoshida","year":"2014","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0120","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1091\/mbc.8.7.1317","article-title":"The ankyrin repeat-containing protein Akr1p is required for the endocytosis of yeast pheromone receptors","volume":"8","author":"Givan","year":"1997","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bbagen.2016.03.026_bb0125","doi-asserted-by":"crossref","first-page":"27138","DOI":"10.1074\/jbc.M403071200","article-title":"Akr1p-dependent palmitoylation of Yck2p yeast casein kinase 1 is necessary and sufficient for plasma membrane targeting","volume":"279","author":"Babu","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0130","doi-asserted-by":"crossref","first-page":"39935","DOI":"10.1074\/jbc.M609365200","article-title":"Expression of a novel marine viral single-chain serine palmitoyltransferase and construction of yeast and mammalian single-chain chimera","volume":"281","author":"Han","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2016.03.026_bb0135","doi-asserted-by":"crossref","first-page":"4142","DOI":"10.1093\/hmg\/ddu137","article-title":"The palmitoyl acyltransferase HIP14 shares a high proportion of interactors with huntingtin: implications for a role in the pathogenesis of Huntington's disease","volume":"23","author":"Butland","year":"2014","journal-title":"Hum. Mol. Genet."}],"container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416516300812?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416516300812?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,10,29]],"date-time":"2019-10-29T14:11:47Z","timestamp":1572358307000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0304416516300812"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,6]]},"references-count":27,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2016,6]]}},"alternative-id":["S0304416516300812"],"URL":"https:\/\/doi.org\/10.1016\/j.bbagen.2016.03.026","relation":{},"ISSN":["0304-4165"],"issn-type":[{"type":"print","value":"0304-4165"}],"subject":[],"published":{"date-parts":[[2016,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Whi2 enhances methylmercury toxicity in yeast via inhibition of Akr1 palmitoyltransferase activity","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - General Subjects","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbagen.2016.03.026","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}