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Article: Genetically Encoded Photoaffinity Histone Marks

TitleGenetically Encoded Photoaffinity Histone Marks
Authors
Xie, XLi, XQin, FLin, JZhang, GZhao, JBao, XZhu, RSong, HLi, XDChen, PR
Issue Date2017
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
Citation
Journal of the American Chemical Society, 2017, v. 139 n. 19, p. 6522-6525 How to Cite?
DOI: http://dx.doi.org/10.1021/jacs.7b01431
AbstractPosttranslational modifications (PTMs) of lysine are crucial histone marks that regulate diverse biological processes. The functional roles and regulation mechanism of many newly identified lysine PTMs, however, remain yet to be understood. Here we report a photoaffinity crotonyl lysine (Kcr) analogue that can be genetically and site-specifically incorporated into histone proteins. This, in conjunction with the genetically encoded photo-lysine as a “control probe”, enables the capture and identification of enzymatic machinery and/or effector proteins for histone lysine crotonylation.
Persistent Identifierhttp://hdl.handle.net/10722/247282
ISSN
0002-7863
2021 Impact Factor: 16.383
2020 SCImago Journal Rankings: 7.115
ISI Accession Number ID
WOS:000401781900003

 

DC FieldValueLanguage
dc.contributor.authorXie, X-
dc.contributor.authorLi, X-
dc.contributor.authorQin, F-
dc.contributor.authorLin, J-
dc.contributor.authorZhang, G-
dc.contributor.authorZhao, J-
dc.contributor.authorBao, X-
dc.contributor.authorZhu, R-
dc.contributor.authorSong, H-
dc.contributor.authorLi, XD-
dc.contributor.authorChen, PR-
dc.date.accessioned2017-10-18T08:25:00Z-
dc.date.available2017-10-18T08:25:00Z-
dc.date.issued2017-
dc.identifier.citationJournal of the American Chemical Society, 2017, v. 139 n. 19, p. 6522-6525-
dc.identifier.issn0002-7863-
dc.identifier.urihttp://hdl.handle.net/10722/247282-
dc.description.abstractPosttranslational modifications (PTMs) of lysine are crucial histone marks that regulate diverse biological processes. The functional roles and regulation mechanism of many newly identified lysine PTMs, however, remain yet to be understood. Here we report a photoaffinity crotonyl lysine (Kcr) analogue that can be genetically and site-specifically incorporated into histone proteins. This, in conjunction with the genetically encoded photo-lysine as a “control probe”, enables the capture and identification of enzymatic machinery and/or effector proteins for histone lysine crotonylation.-
dc.languageeng-
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html-
dc.relation.ispartofJournal of the American Chemical Society-
dc.titleGenetically Encoded Photoaffinity Histone Marks-
dc.typeArticle-
dc.identifier.emailBao, X: baoxc@hku.hk-
dc.identifier.emailLi, XD: xiangli@hku.hk-
dc.identifier.authorityBao, X=rp02881-
dc.identifier.authorityLi, XD=rp01562-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/jacs.7b01431-
dc.identifier.pmid28459554-
dc.identifier.scopuseid_2-s2.0-85019609766-
dc.identifier.hkuros282087-
dc.identifier.volume139-
dc.identifier.issue19-
dc.identifier.spage6522-
dc.identifier.epage6525-
dc.identifier.eissn1520-5126-
dc.identifier.isiWOS:000401781900003-
dc.publisher.placeUnited States-
dc.identifier.issnl0002-7863-

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