Interaction between human angiogenin and the p53 TAD2 domain and its implication for inhibitor discovery
DC Field | Value | Language |
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dc.contributor.author | Yeo, Kwon Joo | - |
dc.contributor.author | Jee, Jun-Goo | - |
dc.contributor.author | Hwang, Eunha | - |
dc.contributor.author | Kim, Eun-Hee | - |
dc.contributor.author | Jeon, Young Ho | - |
dc.contributor.author | Cheong, Hae-Kap | - |
dc.date.accessioned | 2021-09-02T22:29:28Z | - |
dc.date.available | 2021-09-02T22:29:28Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2017-12 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/81405 | - |
dc.description.abstract | Interaction between angiogenin and the p53 TAD2 domain in cancer cells can inhibit the function of the p53 tumor suppressor and promote cell survival. Based on a model structure using NMR and mutational analysis, positively charged (RRR33)-R-31 and (KRSIK54)-K-50 motifs of human angiogenin were identified as p53-binding sites that could interact with negatively charged D48/E51 and E56 residues of the p53 TAD2 domain, respectively. These results suggest that (RRR33)-R-31 and (KRSIK54)-K-50 motifs of human angiogenin might play a critical role in the regulation of p53-mediated apoptosis and angiogenesis in cancer cells. This study identifies potential target sites for screening angiogenin-specific inhibitors that could not only inhibit p53 binding but could also simultaneously inhibit cell binding, internalization, DNA binding, and nuclear translocation of human angiogenin. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | WILEY | - |
dc.subject | TORSION ANGLE DYNAMICS | - |
dc.subject | TRANSACTIVATION DOMAIN | - |
dc.subject | ENDOTHELIAL-CELLS | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | PROTEIN | - |
dc.subject | EXPRESSION | - |
dc.subject | CANCER | - |
dc.subject | HEPARIN | - |
dc.subject | BINDING | - |
dc.subject | PROGRESSION | - |
dc.title | Interaction between human angiogenin and the p53 TAD2 domain and its implication for inhibitor discovery | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Yeo, Kwon Joo | - |
dc.contributor.affiliatedAuthor | Jeon, Young Ho | - |
dc.identifier.doi | 10.1002/1873-3468.12899 | - |
dc.identifier.scopusid | 2-s2.0-85034082468 | - |
dc.identifier.wosid | 000417760400010 | - |
dc.identifier.bibliographicCitation | FEBS LETTERS, v.591, no.23, pp.3916 - 3925 | - |
dc.relation.isPartOf | FEBS LETTERS | - |
dc.citation.title | FEBS LETTERS | - |
dc.citation.volume | 591 | - |
dc.citation.number | 23 | - |
dc.citation.startPage | 3916 | - |
dc.citation.endPage | 3925 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordPlus | TORSION ANGLE DYNAMICS | - |
dc.subject.keywordPlus | TRANSACTIVATION DOMAIN | - |
dc.subject.keywordPlus | ENDOTHELIAL-CELLS | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | CANCER | - |
dc.subject.keywordPlus | HEPARIN | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | PROGRESSION | - |
dc.subject.keywordAuthor | angiogenesis | - |
dc.subject.keywordAuthor | Angiogenin | - |
dc.subject.keywordAuthor | p53 | - |
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