{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T19:00:09Z","timestamp":1786993209717,"version":"build-2736575974"},"reference-count":46,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,3,1]],"date-time":"2020-03-01T00:00:00Z","timestamp":1583020800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,3,1]],"date-time":"2020-03-01T00:00:00Z","timestamp":1583020800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100003453","name":"Natural Science Foundation of Guangdong Province","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003453","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002858","name":"China Postdoctoral Science Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002858","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Proteomics"],"published-print":{"date-parts":[[2020,3]]},"DOI":"10.1016\/j.jprot.2020.103653","type":"journal-article","created":{"date-parts":[[2020,1,17]],"date-time":"2020-01-17T11:43:41Z","timestamp":1579261421000},"page":"103653","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":19,"special_numbering":"C","title":["Hepatic proteomic analysis of selenoprotein F knockout mice by iTRAQ: An implication for the roles of selenoprotein F in metabolism and diseases"],"prefix":"10.1016","volume":"215","author":[{"given":"Xiaoxiang","family":"Zheng","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3663-8180","authenticated-orcid":false,"given":"Bingyu","family":"Ren","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heng","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruikun","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jun","family":"Zhou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hongmei","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jing","family":"Tian","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kaixun","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jprot.2020.103653_bb0005","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1126\/science.1083516","article-title":"Characterization of mammalian Selenoproteomes","volume":"300","author":"Kryukov","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.jprot.2020.103653_bb0010","doi-asserted-by":"crossref","first-page":"8910","DOI":"10.1074\/jbc.273.15.8910","article-title":"A new human selenium-containing protein","volume":"273","author":"Gladyshev","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2020.103653_bb0015","doi-asserted-by":"crossref","first-page":"3536","DOI":"10.1074\/jbc.M511386200","article-title":"NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family","volume":"281","author":"Ferguson","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2020.103653_bb0020","doi-asserted-by":"crossref","first-page":"15330","DOI":"10.1074\/jbc.M009861200","article-title":"Association between the 15-kDa Selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells","volume":"276","author":"Korotkov","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2020.103653_bb0025","doi-asserted-by":"crossref","first-page":"37839","DOI":"10.1074\/jbc.M508685200","article-title":"A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose:glycoprotein glucosyltransferase","volume":"280","author":"Labunskyy","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2020.103653_bb0030","doi-asserted-by":"crossref","first-page":"1387","DOI":"10.1016\/j.celrep.2018.04.009","article-title":"Role of Selenof as a gatekeeper of secreted disulfide-rich glycoproteins","volume":"23","author":"Yim","year":"2018","journal-title":"Cell Rep."},{"key":"10.1016\/j.jprot.2020.103653_bb0035","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1007\/s00394-008-0696-9","article-title":"Lung Cancer risk associated with selenium status is modified in smoking individuals by Sep15 polymorphism","volume":"47","author":"Jablonska","year":"2008","journal-title":"Eur. J. Nutr."},{"key":"10.1016\/j.jprot.2020.103653_bb0040","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1016\/j.bbagen.2009.03.004","article-title":"Molecular mechanisms by which Selenoproteins affect Cancer risk and progression","volume":"1790","author":"Zhuo","year":"2009","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"10.1016\/j.jprot.2020.103653_bb0045","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1002\/pros.22892","article-title":"Selenoprotein and antioxidant genes and the risk of high-grade prostate cancer and prostate cancer recurrence","volume":"75","author":"Gerstenberger","year":"2015","journal-title":"Prostate"},{"key":"10.1016\/j.jprot.2020.103653_bb0050","first-page":"2307","article-title":"Distribution and functional consequences of nucleotide polymorphisms in the 3\u2019-untranslated region of the human Sep15 gene","volume":"61","author":"Hu","year":"2001","journal-title":"Cancer Res."},{"key":"10.1016\/j.jprot.2020.103653_bb0055","doi-asserted-by":"crossref","first-page":"33203","DOI":"10.1074\/jbc.M111.259218","article-title":"Roles of the 15-kDa Selenoprotein (Sep15) in redox homeostasis and cataract development revealed by the analysis of Sep 15 knockout mice","volume":"286","author":"Kasaikina","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2020.103653_bb0060","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1007\/s00775-015-1309-8","article-title":"Knockdown of 15-kDa selenoprotein (Sep15) increases hLE cells\u2019 susceptibility to tunicamycin-induced apoptosis","volume":"20","author":"Yin","year":"2015","journal-title":"JBIC J. Biol. Inorgan. Chem."},{"key":"10.1016\/j.jprot.2020.103653_bb0065","doi-asserted-by":"crossref","first-page":"1633","DOI":"10.1016\/j.bbamcr.2012.02.018","article-title":"Understanding Selenoprotein function and regulation through the use of rodent models","volume":"1823","author":"Kasaikina","year":"2012","journal-title":"Biochimica et Biophysica Acta (BBA)"},{"key":"10.1016\/j.jprot.2020.103653_bb0070","doi-asserted-by":"crossref","first-page":"3641","DOI":"10.1016\/j.febslet.2007.04.045","article-title":"ER chaperones in mammalian development and human diseases","volume":"581","author":"Ni","year":"2007","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jprot.2020.103653_bb0075","doi-asserted-by":"crossref","first-page":"D442","DOI":"10.1093\/nar\/gky1106","article-title":"The PRIDE database and related tools and resources in 2019: improving support for quantification data","volume":"47","author":"Perez-Riverol","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jprot.2020.103653_bb0080","doi-asserted-by":"crossref","first-page":"1619","DOI":"10.3390\/nu10111619","article-title":"Role of Selenoprotein F in protein folding and secretion: potential involvement in human disease","volume":"10","author":"Ren","year":"2018","journal-title":"Nutrients"},{"key":"10.1016\/j.jprot.2020.103653_bb0085","doi-asserted-by":"crossref","DOI":"10.1186\/s12986-017-0235-x","article-title":"The interaction of Selenoprotein F (SELENOF) with retinol dehydrogenase 11 (RDH11) implied a role of SELENOF in vitamin a metabolism","volume":"15","author":"Tian","year":"2018","journal-title":"Nutr Metab"},{"key":"10.1016\/j.jprot.2020.103653_bb0090","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0050574","article-title":"Knockout of the 15 kDa Selenoprotein protects against chemically-induced aberrant crypt formation in mice","volume":"7","author":"Tsuji","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.jprot.2020.103653_bb0095","doi-asserted-by":"crossref","DOI":"10.1016\/j.jprot.2019.103389","article-title":"ITRAQ-based proteomic analysis to identify molecular mechanisms of the selenium deficiency response in the Przewalski\u2019s gazelle","volume":"203","author":"Shen","year":"2019","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2020.103653_bb0100","doi-asserted-by":"crossref","first-page":"80","DOI":"10.3390\/nu8020080","article-title":"Selenium and metabolic disorders: an emphasis on type 2 diabetes risk","volume":"8","author":"Ogawa-Wong","year":"2016","journal-title":"Nutrients"},{"key":"10.1016\/j.jprot.2020.103653_bb0105","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1042\/BCJ20170920","article-title":"Emerging roles of endoplasmic reticulum-resident Selenoproteins in the regulation of cellular stress responses and the implications for metabolic disease","volume":"475","author":"Addinsall","year":"2018","journal-title":"Biochem. J."},{"key":"10.1016\/j.jprot.2020.103653_bb0110","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1007\/BF01797914","article-title":"The role of the liver in metabolic homeostasis: implications for inborn errors of metabolism","volume":"14","author":"van den Berghe","year":"1991","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.jprot.2020.103653_bb0115","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj2540001","article-title":"Physiological roles of nicotinamide nucleotide transhydrogenase","volume":"254","author":"Hoek","year":"1988","journal-title":"Biochem. J."},{"key":"10.1016\/j.jprot.2020.103653_bb0120","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1038\/ng.2299","article-title":"Mutations in NNT encoding nicotinamide nucleotide transhydrogenase cause familial glucocorticoid deficiency","volume":"44","author":"Meimaridou","year":"2012","journal-title":"Nat. Genet."},{"key":"10.1016\/j.jprot.2020.103653_bb0125","article-title":"Determination of the cytosolic NADPH\/NADP ratio in saccharomyces cerevisiae using shikimate dehydrogenase as sensor reaction","volume":"5","author":"Zhang","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jprot.2020.103653_bb0130","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1007\/s10863-011-9381-4","article-title":"Mammalian NADH:ubiquinone oxidoreductase (complex I) and nicotinamide nucleotide transhydrogenase (Nnt) together regulate the mitochondrial production of H2O2 implications for their role in disease, especially cancer","volume":"43","author":"Albracht","year":"2011","journal-title":"J. Bioenerg. Biomembr."},{"key":"10.1016\/j.jprot.2020.103653_bb0135","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1002\/iub.1017","article-title":"Glucose-6-phosphate dehydrogenase, NADPH, and cell survival","volume":"64","author":"Stanton","year":"2012","journal-title":"IUBMB Life"},{"key":"10.1016\/j.jprot.2020.103653_bb0140","doi-asserted-by":"crossref","first-page":"1276","DOI":"10.1016\/j.ejmech.2018.09.001","article-title":"ATP citrate Lyase (ACLY) inhibitors: an anti-cancer strategy at the crossroads of glucose and lipid metabolism","volume":"157","author":"Granchi","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.jprot.2020.103653_bb0145","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.semcdb.2015.08.004","article-title":"Pyruvate kinase: function","volume":"43","author":"Israelsen","year":"2015","journal-title":"Regul. Role Cancer Semin Cell Dev. Biol."},{"key":"10.1016\/j.jprot.2020.103653_bb0150","doi-asserted-by":"crossref","first-page":"1548","DOI":"10.1016\/j.freeradbiomed.2013.07.012","article-title":"Selenium and diabetes- evidence from animal studies","volume":"65","author":"Zhou","year":"2013","journal-title":"Free Radical Biol. Med."},{"key":"10.1016\/j.jprot.2020.103653_bb0155","doi-asserted-by":"crossref","first-page":"1874","DOI":"10.1007\/PL00000669","article-title":"Selenium: An Insulin Mimetic","volume":"57","author":"Stapleton","year":"2000","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.jprot.2020.103653_bb0160","doi-asserted-by":"crossref","first-page":"2327","DOI":"10.1089\/ars.2010.3526","article-title":"Both maximal expression of Selenoproteins and Selenoprotein deficiency can promote development of type 2 diabetes-like phenotype in mice","volume":"14","author":"Labunskyy","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.jprot.2020.103653_bb0165","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1079\/PHN2001143","article-title":"Selenium, Selenoproteins and human health: a review","volume":"4","author":"Brown","year":"2001","journal-title":"Public Health Nutr."},{"key":"10.1016\/j.jprot.2020.103653_bb0170","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/S0027-5107(01)00075-6","article-title":"The protective role of selenium on genetic damage and on Cancer","volume":"475","author":"El-Bayoumy","year":"2001","journal-title":"Mutation Res. Fund. Mol. Mech. Mutagenesis"},{"key":"10.1016\/j.jprot.2020.103653_bb0175","doi-asserted-by":"crossref","first-page":"35540","DOI":"10.1074\/jbc.M004014200","article-title":"Structure-expression relationships of the 15-kDa selenoprotein gene","volume":"275","author":"Kumaraswamy","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2020.103653_bb0180","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1158\/1940-6207.CAPR-10-0003","article-title":"Deficiency in the 15-kDa Selenoprotein inhibits Tumorigenicity and metastasis of Colon Cancer cells","volume":"3","author":"Irons","year":"2010","journal-title":"Cancer Prev. Res."},{"key":"10.1016\/j.jprot.2020.103653_bb0185","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1007\/s12263-010-0176-8","article-title":"Polymorphisms in the Selenoprotein S and 15-kDa selenoprotein genes are associated with altered susceptibility to colorectal cancer","volume":"5","author":"Sutherland","year":"2010","journal-title":"Genes Nutr."},{"key":"10.1016\/j.jprot.2020.103653_bb0190","doi-asserted-by":"crossref","first-page":"5032","DOI":"10.1038\/sj.onc.1207683","article-title":"Growth inhibition and induction of apoptosis in mesothelioma cells by selenium and dependence on Selenoprotein SEP15 genotype","volume":"23","author":"Apostolou","year":"2004","journal-title":"Oncogene"},{"key":"10.1016\/j.jprot.2020.103653_bb0195","doi-asserted-by":"crossref","first-page":"3709","DOI":"10.1158\/0008-5472.CAN-11-4112","article-title":"ATP-citrate Lyase: a key player in cancer metabolism","volume":"72","author":"Zaidi","year":"2012","journal-title":"Cancer Res."},{"key":"10.1016\/j.jprot.2020.103653_bb0200","doi-asserted-by":"crossref","first-page":"5977","DOI":"10.1158\/0008-5472.CAN-05-4673","article-title":"Fatty acid synthase and Cancer: new application of an old pathway: figure 1","volume":"66","author":"Kuhajda","year":"2006","journal-title":"Cancer Res."},{"key":"10.1016\/j.jprot.2020.103653_bb0205","doi-asserted-by":"crossref","first-page":"551","DOI":"10.2217\/fon.10.11","article-title":"Fatty acid synthase as a potential therapeutic target in Cancer","volume":"6","author":"Flavin","year":"2010","journal-title":"Future Oncol."},{"key":"10.1016\/j.jprot.2020.103653_bb0210","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1080\/00313020701329906","article-title":"Glutathione S-transferase Pi (GSTP1) Hypermethylation in prostate Cancer: review 2007","volume":"39","author":"Meiers","year":"2007","journal-title":"Pathology"},{"key":"10.1016\/j.jprot.2020.103653_bb0215","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2013\/843781","article-title":"Expression of Tra2\u03b2 in Cancer cells as a potential contributory factor to neoplasia and metastasis","volume":"2013","author":"Best","year":"2013","journal-title":"Int. J. Cell Biol."},{"key":"10.1016\/j.jprot.2020.103653_bb0220","first-page":"1","article-title":"Metallothioneins and Cancer","author":"Eckschlager","year":"2009","journal-title":"Curr. Protein Pept. Sci."},{"key":"10.1016\/j.jprot.2020.103653_bb0225","doi-asserted-by":"crossref","DOI":"10.3389\/fonc.2018.00022","article-title":"Posttranslational modifications of pyruvate kinase M2: tweaks that benefit cancer","volume":"8","author":"Prakasam","year":"2018","journal-title":"Front. Oncol."},{"key":"10.1016\/j.jprot.2020.103653_bb0230","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1038\/nrm1052","article-title":"Quality control in the endoplasmic reticulum","volume":"4","author":"Ellgaard","year":"2003","journal-title":"Nat. Rev. Mol. Cell Biol."}],"container-title":["Journal of Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S187439192030021X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S187439192030021X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T12:04:26Z","timestamp":1761739466000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S187439192030021X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,3]]},"references-count":46,"alternative-id":["S187439192030021X"],"URL":"https:\/\/doi.org\/10.1016\/j.jprot.2020.103653","relation":{},"ISSN":["1874-3919"],"issn-type":[{"value":"1874-3919","type":"print"}],"subject":[],"published":{"date-parts":[[2020,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Hepatic proteomic analysis of selenoprotein F knockout mice by iTRAQ: An implication for the roles of selenoprotein F in metabolism and diseases","name":"articletitle","label":"Article Title"},{"value":"Journal of Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jprot.2020.103653","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"103653"}}