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기정민

Kee, Jung-Min
Bioorganic and Chembio Lab.
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dc.citation.endPage 7485 -
dc.citation.number 52 -
dc.citation.startPage 7482 -
dc.citation.title CHEMICAL COMMUNICATIONS -
dc.citation.volume 55 -
dc.contributor.author Jung, Hoyoung -
dc.contributor.author Choi, Yigun -
dc.contributor.author Lee, Donghee -
dc.contributor.author Seo, Jeong Kon -
dc.contributor.author Kee, Jung-Min -
dc.date.accessioned 2023-12-21T19:06:27Z -
dc.date.available 2023-12-21T19:06:27Z -
dc.date.created 2019-06-04 -
dc.date.issued 2019-07 -
dc.description.abstract Protein arginine (Arg) phosphorylation regulates stress responses and virulence in bacteria. With fluorescent activity probes, we show that McsB, a protein Arg kinase, can dephosphorylate phophoarginine (pArg) residues to produce ATP from ADP, implicating the dynamic control of protein pArg levels by the kinase even without the phosphatase. -
dc.identifier.bibliographicCitation CHEMICAL COMMUNICATIONS, v.55, no.52, pp.7482 - 7485 -
dc.identifier.doi 10.1039/C9CC03285A -
dc.identifier.issn 1359-7345 -
dc.identifier.scopusid 2-s2.0-85068144939 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/26707 -
dc.identifier.url https://pubs.rsc.org/en/Content/ArticleLanding/2019/CC/C9CC03285A#!divAbstract -
dc.identifier.wosid 000472790500009 -
dc.language 영어 -
dc.publisher Royal Society of Chemistry -
dc.title Distinct phosphorylation and dephosphorylation dynamics of protein arginine kinases revealed by fluorescent activity probes -
dc.type Article -
dc.description.isOpenAccess FALSE -
dc.relation.journalWebOfScienceCategory Chemistry, Multidisciplinary -
dc.relation.journalResearchArea Chemistry -
dc.type.docType Article -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordPlus PHOSPHOARGININE -
dc.subject.keywordPlus ASSAY -
dc.subject.keywordPlus REAL-TIME -

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