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Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis

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dc.contributor.authorRoh, Soung-Hun-
dc.contributor.authorKasembeli, Moses-
dc.contributor.authorBakthavatsalam, Deenadayalan-
dc.contributor.authorChiu, Wah-
dc.contributor.authorTweardy, David J.-
dc.date.accessioned2024-05-17T07:39:10Z-
dc.date.available2024-05-17T07:39:10Z-
dc.date.created2024-05-17-
dc.date.issued2015-11-
dc.identifier.citationInternational Journal of Molecular Sciences, Vol.16 No.11, pp.26706-26720-
dc.identifier.issn1661-6596-
dc.identifier.urihttps://hdl.handle.net/10371/203198-
dc.description.abstractThe folding of newly synthesized proteins and the maintenance of pre-existing proteins are essential in sustaining a living cell. A network of molecular chaperones tightly guides the folding, intracellular localization, and proteolytic turnover of proteins. Many of the key regulators of cell growth and differentiation have been identified as clients of molecular chaperones, which implies that chaperones are potential mediators of oncogenesis. In this review, we briefly provide an overview of the role of chaperones, including HSP70 and HSP90, in cancer. We further summarize and highlight the emerging the role of chaperonin TRiC (T-complex protein-1 ring complex, also known as CCT) in the development and progression of cancer mediated through its critical interactions with oncogenic clients that modulate growth deregulation, apoptosis, and genome instability in cancer cells. Elucidation of how TRiC modulates the folding and function of oncogenic clients will provide strategies for developing novel cancer therapies.-
dc.language영어-
dc.publisherMultidisciplinary Digital Publishing Institute (MDPI)-
dc.titleContribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis-
dc.typeArticle-
dc.identifier.doi10.3390/ijms161125975-
dc.citation.journaltitleInternational Journal of Molecular Sciences-
dc.identifier.wosid000365648300051-
dc.identifier.scopusid2-s2.0-84946887698-
dc.citation.endpage26720-
dc.citation.number11-
dc.citation.startpage26706-
dc.citation.volume16-
dc.description.isOpenAccessY-
dc.contributor.affiliatedAuthorRoh, Soung-Hun-
dc.type.docTypeReview-
dc.description.journalClass1-
dc.subject.keywordPlusHYPOXIA-INDUCIBLE FACTORS-
dc.subject.keywordPlusTUMOR-SUPPRESSOR PROTEIN-
dc.subject.keywordPlusHEAT-SHOCK PROTEINS-
dc.subject.keywordPlusANAPHASE-PROMOTING COMPLEX-
dc.subject.keywordPlusIN-VIVO-
dc.subject.keywordPlusCYTOPLASMIC CHAPERONIN-
dc.subject.keywordPlusMOLECULAR CHAPERONES-
dc.subject.keywordPlusGENETIC INSTABILITY-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusRNA-POLYMERASE-
dc.subject.keywordAuthorprotein-folding-
dc.subject.keywordAuthorproteostasis-
dc.subject.keywordAuthoroncogenesis-
dc.subject.keywordAuthorchaperone-
dc.subject.keywordAuthorchaperonin-
dc.subject.keywordAuthorHSP70-
dc.subject.keywordAuthor90-
dc.subject.keywordAuthorTRiC-
dc.subject.keywordAuthorCCT-
dc.subject.keywordAuthoroncoprotein-
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  • College of Natural Sciences
  • School of Biological Sciences
Research Area Cryogenic Electron Microscopy (Cryo-EM), Structural Biology, 분자생물학, 생물물리학, 생화학

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