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민두영

Min, Duyoung
Nano Bio Dynamics Lab
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dc.citation.endPage 1294 -
dc.citation.number 11 -
dc.citation.startPage 1291 -
dc.citation.title STRUCTURE -
dc.citation.volume 31 -
dc.contributor.author Kim, Eojin -
dc.contributor.author Min, Duyoung -
dc.date.accessioned 2023-12-29T14:35:11Z -
dc.date.available 2023-12-29T14:35:11Z -
dc.date.created 2023-12-29 -
dc.date.issued 2023-11 -
dc.description.abstract In this issue of Structure, Blaimschein et al. elucidate the chaperoning function of the insertase YidC during the insertion and folding of the melibiose permease MelB. Their single-molecule forced unfolding approach reveals that YidC significantly reduces the misfolding and enhances the folding of helices near the interface of two folding cores. -
dc.identifier.bibliographicCitation STRUCTURE, v.31, no.11, pp.1291 - 1294 -
dc.identifier.doi 10.1016/j.str.2023.10.003 -
dc.identifier.issn 0969-2126 -
dc.identifier.scopusid 2-s2.0-85175242868 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/67333 -
dc.identifier.wosid 001110061400001 -
dc.language 영어 -
dc.publisher CELL PRESS -
dc.title Chaperoning the major facilitator superfamily at single-molecule level -
dc.type Article -
dc.description.isOpenAccess FALSE -
dc.relation.journalWebOfScienceCategory Biochemistry & Molecular Biology;Biophysics;Cell Biology -
dc.relation.journalResearchArea Biochemistry & Molecular Biology;Biophysics;Cell Biology -
dc.type.docType Editorial -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordAuthor Biochemistry & Molecular Biology -
dc.subject.keywordAuthor Biophysics -
dc.subject.keywordAuthor Cell Biology -
dc.subject.keywordPlus Biochemistry & Molecular Biology -
dc.subject.keywordPlus Biophysics -
dc.subject.keywordPlus Cell Biology -

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