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dc.contributor.authorLambert, Jean-Philippeen_US
dc.contributor.authorIvosev, Gordanaen_US
dc.contributor.authorCouzens, Amber L.en_US
dc.contributor.authorLarsen, Bretten_US
dc.contributor.authorTaipale, Mikkoen_US
dc.contributor.authorLin, Zhen-Yuanen_US
dc.contributor.authorZhong, Quanen_US
dc.contributor.authorLindquist, Susanen_US
dc.contributor.authorVidal, Marcen_US
dc.contributor.authorAebersold, Ruedien_US
dc.contributor.authorPawson, Tonyen_US
dc.contributor.authorBonner, Ronen_US
dc.contributor.authorTate, Stephenen_US
dc.contributor.authorGingras, Anne-Claudeen_US
dc.date.accessioned2014-07-07T17:03:32Z
dc.date.issued2013en_US
dc.identifier.citationLambert, J., G. Ivosev, A. L. Couzens, B. Larsen, M. Taipale, Z. Lin, Q. Zhong, et al. 2013. “Mapping differential interactomes by affinity purification coupled with data independent mass spectrometry acquisition.” Nature methods 10 (12): 10.1038/nmeth.2702. doi:10.1038/nmeth.2702. http://dx.doi.org/10.1038/nmeth.2702.en
dc.identifier.issn1548-7091en
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:12406705
dc.description.abstractCharacterizing changes in protein-protein interactions associated with sequence variants (e.g. disease-associated mutations or splice forms) or following exposure to drugs, growth factors or hormones is critical to understanding how protein complexes are built, localized and regulated. Affinity purification (AP) coupled with mass spectrometry permits the analysis of protein interactions under near-physiological conditions, yet monitoring interaction changes requires the development of a robust and sensitive quantitative approach, especially for large-scale studies where cost and time are major considerations. To this end, we have coupled AP to data-independent mass spectrometric acquisition (SWATH), and implemented an automated data extraction and statistical analysis pipeline to score modulated interactions. Here, we use AP-SWATH to characterize changes in protein-protein interactions imparted by the HSP90 inhibitor NVP-AUY922 or melanoma-associated mutations in the human kinase CDK4. We show that AP-SWATH is a robust label-free approach to characterize such changes, and propose a scalable pipeline for systems biology studies.en
dc.language.isoen_USen
dc.relation.isversionofdoi:10.1038/nmeth.2702en
dc.relation.hasversionhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3882083/pdf/en
dash.licenseLAAen_US
dc.titleMapping differential interactomes by affinity purification coupled with data independent mass spectrometry acquisitionen
dc.typeJournal Articleen_US
dc.description.versionVersion of Recorden
dc.relation.journalNature methodsen
dash.depositing.authorVidal, Marcen_US
dc.date.available2014-07-07T17:03:32Z
dc.identifier.doi10.1038/nmeth.2702*
dash.authorsorderedfalse
dash.contributor.affiliatedVidal, Marc


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