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Article: Identifying the proteins to which small-molecule probes and drugs bind in cells

TitleIdentifying the proteins to which small-molecule probes and drugs bind in cells
Authors
KeywordsSILAC
Small molecules
Target identification
Issue Date2009
PublisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.org
Citation
Proceedings of the National Academy of Sciences, 2009, v. 106 n. 12, p. 4617-4622 How to Cite?
AbstractMost small-molecule probes and drugs alter cell circuitry by interacting with 1 or more proteins. A complete understanding of the interacting proteins and their associated protein complexes, whether the compounds are discovered by cell-based phenotypic or target- based screens, is extremely rare. Such a capability is expected to be highly illuminating-providing strong clues to the mechanisms used by small-molecules to achieve their recognized actions and suggesting potential unrecognized actions. We describe a powerful method combining quantitative proteomics(SILAC) with affinity enrichment to provide unbiased, robust and comprehensive identification of the proteins that bind to small-molecule probes and drugs. The method is scalable and general, requiring little optimization across different compound classes, and has already had a transformative effect on our studies of small-molecule probes. Here, we describe in full detail the application of the method to identify targets of kinase inhibitors and immunophilin binders.
Persistent Identifierhttp://hdl.handle.net/10722/221461
ISSN
2015 Impact Factor: 9.423
2015 SCImago Journal Rankings: 6.883
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorOng, SE-
dc.contributor.authorSchenone, M-
dc.contributor.authorMargolin, AA-
dc.contributor.authorLi, X-
dc.contributor.authorDo, K-
dc.contributor.authorDoud, MK-
dc.contributor.authorMani, DR-
dc.contributor.authorKuai, L-
dc.contributor.authorWang, X-
dc.contributor.authorWood, JL-
dc.contributor.authorTolliday, NJ-
dc.contributor.authorKoehler, AN-
dc.contributor.authorMarcaurelle, LA-
dc.contributor.authorGolub, TR-
dc.contributor.authorGould, RJ-
dc.contributor.authorSchreiber, SL-
dc.contributor.authorCarr, SA-
dc.date.accessioned2015-11-26T08:07:36Z-
dc.date.available2015-11-26T08:07:36Z-
dc.date.issued2009-
dc.identifier.citationProceedings of the National Academy of Sciences, 2009, v. 106 n. 12, p. 4617-4622-
dc.identifier.issn0027-8424-
dc.identifier.urihttp://hdl.handle.net/10722/221461-
dc.description.abstractMost small-molecule probes and drugs alter cell circuitry by interacting with 1 or more proteins. A complete understanding of the interacting proteins and their associated protein complexes, whether the compounds are discovered by cell-based phenotypic or target- based screens, is extremely rare. Such a capability is expected to be highly illuminating-providing strong clues to the mechanisms used by small-molecules to achieve their recognized actions and suggesting potential unrecognized actions. We describe a powerful method combining quantitative proteomics(SILAC) with affinity enrichment to provide unbiased, robust and comprehensive identification of the proteins that bind to small-molecule probes and drugs. The method is scalable and general, requiring little optimization across different compound classes, and has already had a transformative effect on our studies of small-molecule probes. Here, we describe in full detail the application of the method to identify targets of kinase inhibitors and immunophilin binders.-
dc.languageeng-
dc.publisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.org-
dc.relation.ispartofProceedings of the National Academy of Sciences-
dc.rightsProceedings of the National Academy of Sciences. Copyright © National Academy of Sciences.-
dc.subjectSILAC-
dc.subjectSmall molecules-
dc.subjectTarget identification-
dc.titleIdentifying the proteins to which small-molecule probes and drugs bind in cells-
dc.typeArticle-
dc.identifier.emailLi, X: xiaoyuli@hku.hk-
dc.identifier.authorityLi, X=rp02080-
dc.identifier.doi10.1073/pnas.0900191106-
dc.identifier.pmid19255428-
dc.identifier.pmcid2649954-
dc.identifier.scopuseid_2-s2.0-63849172494-
dc.identifier.volume106-
dc.identifier.issue12-
dc.identifier.spage4617-
dc.identifier.epage4622-
dc.publisher.placeUnited States-
dc.identifier.f10001158172-

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