Dual-site interactions of p53 protein transactivation domain with anti-apoptotic bcl-2 family proteins reveal a highly convergent mechanism of divergent p53 pathways

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dc.contributor.authorJi Hyang Ha-
dc.contributor.authorJ S Shin-
dc.contributor.authorMi Kyung Yoon-
dc.contributor.authorM S Lee-
dc.contributor.authorF He-
dc.contributor.authorKwang-Hee Bae-
dc.contributor.authorH S Yoon-
dc.contributor.authorC K Lee-
dc.contributor.authorSung Goo Park-
dc.contributor.authorY Muto-
dc.contributor.authorSeung-Wook Chi-
dc.date.accessioned2017-04-19T09:38:32Z-
dc.date.available2017-04-19T09:38:32Z-
dc.date.issued2013-
dc.identifier.issn0021-9258-
dc.identifier.uri10.1074/jbc.M112.400754ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/11268-
dc.description.abstractBackground: Interactions between p53 and Bcl-2 family proteins serve a critical role in transcription-independent p53 apoptosis. Results: We studied the interactions of p53TAD2 with anti-apoptotic Bcl-2 family proteins at the atomic level by NMR, mutagenesis, and structure calculation. Conclusion: Bcl-XL/Bcl-2, MDM2, and CBP/p300 share similar modes of binding to the dual p53TAD motifs. Significance: Dual-site interaction of p53TAD is a highly conserved mechanism in the transcription-dependent and transcription- independent p53 apoptotic pathways.-
dc.publisherAmer Soc Biochemistry Molecular Biology Inc-
dc.titleDual-site interactions of p53 protein transactivation domain with anti-apoptotic bcl-2 family proteins reveal a highly convergent mechanism of divergent p53 pathways-
dc.title.alternativeDual-site interactions of p53 protein transactivation domain with anti-apoptotic bcl-2 family proteins reveal a highly convergent mechanism of divergent p53 pathways-
dc.typeArticle-
dc.citation.titleJournal of Biological Chemistry-
dc.citation.number10-
dc.citation.endPage7398-
dc.citation.startPage7387-
dc.citation.volume288-
dc.contributor.affiliatedAuthorJi Hyang Ha-
dc.contributor.affiliatedAuthorMi Kyung Yoon-
dc.contributor.affiliatedAuthorM S Lee-
dc.contributor.affiliatedAuthorKwang-Hee Bae-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.affiliatedAuthorSeung-Wook Chi-
dc.contributor.alternativeName하지향-
dc.contributor.alternativeName신재선-
dc.contributor.alternativeName윤미경-
dc.contributor.alternativeName이민성-
dc.contributor.alternativeNameHe-
dc.contributor.alternativeName배광희-
dc.contributor.alternativeName윤호섭-
dc.contributor.alternativeName이종길-
dc.contributor.alternativeName박성구-
dc.contributor.alternativeNameMuto-
dc.contributor.alternativeName지승욱-
dc.identifier.bibliographicCitationJournal of Biological Chemistry, vol. 288, no. 10, pp. 7387-7398-
dc.identifier.doi10.1074/jbc.M112.400754-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Biomedical Research > 1. Journal Articles
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