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Lipid raft proteome reveals that oxidative phosphorylation system is associated with the plasma membrane

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dc.contributor.authorKim, Bong-Woo-
dc.contributor.authorLee, Chang Seok-
dc.contributor.authorYi, Jae-Sung-
dc.contributor.authorLee, Joo-Hyung-
dc.contributor.authorLee, Joong-Won-
dc.contributor.authorChoo, Hyo-Jung-
dc.contributor.authorJung, Soon-Young-
dc.contributor.authorKim, Min-Sik-
dc.contributor.authorLee, Sang-Won-
dc.contributor.authorLee, Myung-Shik-
dc.contributor.authorYoon, Gyesoon-
dc.contributor.authorKo, Young-Gyu-
dc.date.accessioned2021-09-07T22:40:14Z-
dc.date.available2021-09-07T22:40:14Z-
dc.date.created2021-06-14-
dc.date.issued2010-12-
dc.identifier.issn1478-9450-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/115277-
dc.description.abstractAlthough accumulating proteomic analyses have supported the fact that mitochondrial oxidative phosphorylation (OXPHOS) complexes are localized in lipid rafts, which mediate cell signaling, immune response and host pathogen interactions, there has been no in-depth study of the physiological functions of lipid-raft OXPHOS complexes. Here, we show that many subunits of OXPHOS complexes were identified from the lipid rafts of human adipocytes, C2C12 myotubes, Jurkat cells and surface biotin-labeled Jurkat cells via shotgun proteomic analysis. We discuss the findings of OXPHOS complexes in lipid rafts, the role of the surface ATP synthase complex as a receptor for various ligands and extracellular superoxide generation by plasma membrane oxidative phosphorylation complexes.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherTAYLOR & FRANCIS LTD-
dc.subjectENDOTHELIAL-CELL SURFACE-
dc.subjectF1F0 ATP-SYNTHASE-
dc.subjectGPI-ANCHORED PROTEINS-
dc.subjectHUMAN-ERYTHROCYTE ACETYLCHOLINESTERASE-
dc.subjectTANDEM MASS-SPECTROMETRY-
dc.subjectMOUSE SMALL-INTESTINE-
dc.subjectDOUBLE-BOND POSITION-
dc.subjectAPOLIPOPROTEIN-A-I-
dc.subjectEXTRACELLULAR ATP-
dc.subjectQUANTITATIVE PROTEOMICS-
dc.titleLipid raft proteome reveals that oxidative phosphorylation system is associated with the plasma membrane-
dc.typeArticle-
dc.contributor.affiliatedAuthorLee, Sang-Won-
dc.contributor.affiliatedAuthorKo, Young-Gyu-
dc.identifier.doi10.1586/EPR.10.87-
dc.identifier.scopusid2-s2.0-78650433384-
dc.identifier.wosid000285227400011-
dc.identifier.bibliographicCitationEXPERT REVIEW OF PROTEOMICS, v.7, no.6, pp.849 - 866-
dc.relation.isPartOfEXPERT REVIEW OF PROTEOMICS-
dc.citation.titleEXPERT REVIEW OF PROTEOMICS-
dc.citation.volume7-
dc.citation.number6-
dc.citation.startPage849-
dc.citation.endPage866-
dc.type.rimsART-
dc.type.docTypeReview-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiochemical Research Methods-
dc.subject.keywordPlusENDOTHELIAL-CELL SURFACE-
dc.subject.keywordPlusF1F0 ATP-SYNTHASE-
dc.subject.keywordPlusGPI-ANCHORED PROTEINS-
dc.subject.keywordPlusHUMAN-ERYTHROCYTE ACETYLCHOLINESTERASE-
dc.subject.keywordPlusTANDEM MASS-SPECTROMETRY-
dc.subject.keywordPlusMOUSE SMALL-INTESTINE-
dc.subject.keywordPlusDOUBLE-BOND POSITION-
dc.subject.keywordPlusAPOLIPOPROTEIN-A-I-
dc.subject.keywordPlusEXTRACELLULAR ATP-
dc.subject.keywordPlusQUANTITATIVE PROTEOMICS-
dc.subject.keywordAuthorATP synthase-
dc.subject.keywordAuthordetergent-resistant lipid rafts-
dc.subject.keywordAuthorextracellular ATP-
dc.subject.keywordAuthorextracellular superoxide-
dc.subject.keywordAuthoroxidative phosphorylation complexes-
dc.subject.keywordAuthoroxygen consumption-
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