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Cited 35 time in webofscience Cited 35 time in scopus
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N-Terminal Acetylation-Targeted N-End Rule Proteolytic System: The Ac/N-End Rule Pathway

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dc.contributor.authorLee, Kang-Eun-
dc.contributor.authorHeo, Ji-Eun-
dc.contributor.authorKim, Jeong-Mok-
dc.contributor.authorHwang, Cheol-Sang-
dc.date.accessioned2021-08-02T17:26:43Z-
dc.date.available2021-08-02T17:26:43Z-
dc.date.issued2016-03-
dc.identifier.issn1016-8478-
dc.identifier.issn0219-1032-
dc.identifier.urihttps://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/23859-
dc.description.abstractAlthough Na-terminal acetylation (Nt-acetylation) is a pervasive protein modification in eukaryotes, its general functions in a majority of proteins are poorly understood. In 2010, it was discovered that Nt-acetylation creates a specific protein degradation signal that is targeted by a new class of the N-end rule proteolytic system, called the Ac/N end rule pathway. Here, we review recent advances in our understanding of the mechanism and biological functions of the Ac/N-end rule pathway, and its crosstalk with the Arg/N-end rule pathway (the classical N-end rule pathway).-
dc.format.extent10-
dc.language영어-
dc.language.isoENG-
dc.publisher한국분자세포생물학회-
dc.titleN-Terminal Acetylation-Targeted N-End Rule Proteolytic System: The Ac/N-End Rule Pathway-
dc.typeArticle-
dc.publisher.location대한민국-
dc.identifier.doi10.14348/molcells.2016.2329-
dc.identifier.scopusid2-s2.0-84964929936-
dc.identifier.wosid000372889800001-
dc.identifier.bibliographicCitationMolecules and Cells, v.39, no.3, pp 169 - 178-
dc.citation.titleMolecules and Cells-
dc.citation.volume39-
dc.citation.number3-
dc.citation.startPage169-
dc.citation.endPage178-
dc.type.docType정기 학술지(Review)-
dc.identifier.kciidART002089267-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClasssci-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.description.journalRegisteredClasskci-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaCell Biology-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryCell Biology-
dc.subject.keywordPlusE3 UBIQUITIN LIGASE-
dc.subject.keywordPlusSACCHAROMYCES-CEREVISIAE IDENTIFICATION-
dc.subject.keywordPlusCOENZYME-A REDUCTASE-
dc.subject.keywordPlusIN-VIVO-
dc.subject.keywordPlusPROTEASOMAL DEGRADATION-
dc.subject.keywordPlusALPHA-ACETYLTRANSFERASE-
dc.subject.keywordPlusENDOPLASMIC-RETICULUM-
dc.subject.keywordPlusPROTEIN ACETYLATION-
dc.subject.keywordPlusEMERGING FUNCTIONS-
dc.subject.keywordPlusCELLULAR-PROTEINS-
dc.subject.keywordAuthordegron-
dc.subject.keywordAuthorN-end rule-
dc.subject.keywordAuthorN-terminal acetylation-
dc.subject.keywordAuthorproteolysis-
dc.subject.keywordAuthorubiquitin-
dc.identifier.urlhttps://www.molcells.org/journal/view.html?doi=10.14348/molcells.2016.2329-
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