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Byung Gyu, Kim
유전체 항상성 연구단
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Mitoquinone Inactivates Mitochondrial Chaperone TRAP1 by Blocking the Client Binding Site

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dc.contributor.authorYoon, Nam Gu-
dc.contributor.authorLee, Hakbong-
dc.contributor.authorKim, So-Yeon-
dc.contributor.authorHu, Sung-
dc.contributor.authorKim, Darong-
dc.contributor.authorYang, Sujae-
dc.contributor.authorHong, Ki Bum-
dc.contributor.authorLee, Ji Hoon-
dc.contributor.authorKang, Soosung-
dc.contributor.authorByung-Gyu Kim-
dc.contributor.authorKyungjae Myung-
dc.contributor.authorLee, Changwook-
dc.contributor.authorKang, Byoung Heon-
dc.date.accessioned2021-12-22T01:50:01Z-
dc.date.available2021-12-22T01:50:01Z-
dc.date.created2021-12-15-
dc.date.issued2021-12-01-
dc.identifier.issn0002-7863-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/10915-
dc.description.abstract© Heat shock protein 90 (Hsp90) family proteins are molecular chaperones that modulate the functions of various substrate proteins (clients) implicated in pro-tumorigenic pathways. In this study, the mitochondria-targeted antioxidant mitoquinone (MitoQ) was identified as a potent inhibitor of mitochondrial Hsp90, known as a tumor necrosis factor receptor-associated protein 1 (TRAP1). Structural analyses revealed an asymmetric bipartite interaction between MitoQ and the previously unrecognized drug binding sites located in the middle domain of TRAP1, believed to be a client binding region. MitoQ effectively competed with TRAP1 clients, and MitoQ treatment facilitated the identification of 103 TRAP1-interacting mitochondrial proteins in cancer cells. MitoQ and its redox-crippled SB-U014/SB-U015 exhibited more potent anticancer activity in vitro and in vivo than previously reported mitochondria-targeted TRAP1 inhibitors. The findings indicate that targeting the client binding site of Hsp90 family proteins offers a novel strategy for the development of potent anticancer drugs.-
dc.language영어-
dc.publisherAmerican Chemical Society-
dc.titleMitoquinone Inactivates Mitochondrial Chaperone TRAP1 by Blocking the Client Binding Site-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000750622600003-
dc.identifier.scopusid2-s2.0-85119488886-
dc.identifier.rimsid76883-
dc.contributor.affiliatedAuthorByung-Gyu Kim-
dc.contributor.affiliatedAuthorKyungjae Myung-
dc.identifier.doi10.1021/jacs.1c07099-
dc.identifier.bibliographicCitationJournal of the American Chemical Society, v.143, no.47, pp.19684 - 19696-
dc.relation.isPartOfJournal of the American Chemical Society-
dc.citation.titleJournal of the American Chemical Society-
dc.citation.volume143-
dc.citation.number47-
dc.citation.startPage19684-
dc.citation.endPage19696-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaChemistry-
dc.relation.journalWebOfScienceCategoryChemistry, Multidisciplinary-
dc.subject.keywordPlusREGULATES AUTOPHAGY-
dc.subject.keywordPlusHSP90 INHIBITORS-
dc.subject.keywordPlusPHOSPHORYLATION-
dc.subject.keywordPlusSPECIFICITY-
dc.subject.keywordPlusEFFICACY-
dc.subject.keywordPlusCELLS-
Appears in Collections:
Center for Genomic Integrity(유전체 항상성 연구단) > 1. Journal Papers (저널논문)
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