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Dual roles of pin1 in cancer development and progression

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dc.contributor.authorHan, Hyeong-Jun-
dc.contributor.authorChoi, Bu Young-
dc.contributor.authorSurh, Young-Joon-
dc.date.accessioned2021-01-31T09:26:58Z-
dc.date.available2021-01-31T09:26:58Z-
dc.date.created2018-11-15-
dc.date.issued2017-08-
dc.identifier.citationCurrent Pharmaceutical Design, Vol.23 No.29, pp.4422-4425-
dc.identifier.issn1381-6128-
dc.identifier.other68936-
dc.identifier.urihttps://hdl.handle.net/10371/172685-
dc.description.abstractPin1 is a unique peptidyl-prolyl cis/trans isomerase (PPIase) that catalyzes the cis/trans isomerization of peptidyl-prolyl peptide bonds of its substrate proteins by binding to their specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. This alters the conformation of target proteins and consequently affects their stability, intracellular localization, and/or biological functions. The abnormal overexpression of Pin1 is observed in some malignancies, which is associated with cancer cell proliferation, migration and invasion. However, a role for Pin1 as a putative tumor suppressor has recently been suggested. Systematic dissection of pro-oncogenic vs. tumor suppressive functions of Pin1 will be necessary.-
dc.language영어-
dc.publisherBentham Science Publishers-
dc.titleDual roles of pin1 in cancer development and progression-
dc.typeArticle-
dc.contributor.AlternativeAuthor서영준-
dc.identifier.doi10.2174/1381612823666170703164711-
dc.citation.journaltitleCurrent Pharmaceutical Design-
dc.identifier.wosid000415378600016-
dc.identifier.scopusid2-s2.0-85038818183-
dc.citation.endpage4425-
dc.citation.number29-
dc.citation.startpage4422-
dc.citation.volume23-
dc.identifier.sci000415378600016-
dc.description.isOpenAccessN-
dc.contributor.affiliatedAuthorSurh, Young-Joon-
dc.type.docTypeReview-
dc.description.journalClass1-
dc.subject.keywordPlusPROLYL-ISOMERASE PIN1-
dc.subject.keywordPlusTUMOR-SUPPRESSOR-
dc.subject.keywordPlusBREAST-CANCER-
dc.subject.keywordPlusNUCLEAR TRANSLOCATION-
dc.subject.keywordPlusCYCLIN-E-
dc.subject.keywordPlusPHOSPHORYLATION-
dc.subject.keywordPlusDEGRADATION-
dc.subject.keywordPlusCELLS-
dc.subject.keywordPlusMITOSIS-
dc.subject.keywordPlusUBIQUITINATION-
dc.subject.keywordAuthorPin1-
dc.subject.keywordAuthorproline-directed protein kinases-
dc.subject.keywordAuthorphosphorylation-dependent peptidyl-prolyl isomerase-
dc.subject.keywordAuthorpSer/Thr-Pro motif-
dc.subject.keywordAuthorPPIase-
dc.subject.keywordAuthorproline isomerization-
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  • College of Pharmacy
  • Department of Pharmacy
Research Area Agricultural Sciences

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