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Article: Photo-lysine captures proteins that bind lysine posttranslational modifications

TitlePhoto-lysine captures proteins that bind lysine posttranslational modifications
Authors
Issue Date2016
Citation
Nature Chemical Biology, 2016, v. 12 n. 2, p. 70-72 How to Cite?
AbstractPost-translational modifications (PTMs) have key roles in regulating protein-protein interactions in living cells. However, it remains a challenge to identify these PTM-mediated interactions. Here we develop a new lysine-based photo-reactive amino acid, termed photo-lysine. We demonstrate that photo-lysine, which is readily incorporated into proteins by native mammalian translation machinery, can be used to capture and identify proteins that recognize lysine PTMs, including 'readers' and 'erasers' of histone modifications.
Persistent Identifierhttp://hdl.handle.net/10722/222443

 

DC FieldValueLanguage
dc.contributor.authorYANG, T-
dc.contributor.authorLI, X-
dc.contributor.authorBAO, X-
dc.contributor.authorFung, EYM-
dc.contributor.authorLi, X-
dc.date.accessioned2016-01-18T07:40:02Z-
dc.date.available2016-01-18T07:40:02Z-
dc.date.issued2016-
dc.identifier.citationNature Chemical Biology, 2016, v. 12 n. 2, p. 70-72-
dc.identifier.urihttp://hdl.handle.net/10722/222443-
dc.description.abstractPost-translational modifications (PTMs) have key roles in regulating protein-protein interactions in living cells. However, it remains a challenge to identify these PTM-mediated interactions. Here we develop a new lysine-based photo-reactive amino acid, termed photo-lysine. We demonstrate that photo-lysine, which is readily incorporated into proteins by native mammalian translation machinery, can be used to capture and identify proteins that recognize lysine PTMs, including 'readers' and 'erasers' of histone modifications.-
dc.languageeng-
dc.relation.ispartofNature Chemical Biology-
dc.titlePhoto-lysine captures proteins that bind lysine posttranslational modifications-
dc.typeArticle-
dc.identifier.emailFung, EYM: eva.fungym@hku.hk-
dc.identifier.emailLi, X: xiangli@hku.hk-
dc.identifier.authorityFung, EYM=rp01986-
dc.identifier.authorityLi, X=rp01562-
dc.identifier.doi10.1038/nchembio.1990-
dc.identifier.hkuros256644-

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