Literature DB >> 27726338

K-CLASP: A Tool to Identify Phosphosite Specific Kinases and Interacting Proteins.

Pavithra M Dedigama-Arachchige1, Mary Kay H Pflum1.   

Abstract

Few methods are available to discover the cellular kinase that phosphorylates a specific amino acid, or phosphosite, on a protein. In addition, identifying the associated proteins bound near a phosphosite during phosphorylation would provide insights into cell biology and signaling. Here, we report K-CLASP (Kinase Catalyzed CrossLinking And Streptavidin Purification) as a method for both phosphosite-specific kinase identification and the discovery of kinase interacting proteins. K-CLASP offers a powerful tool to discover unanticipated protein-protein interactions in phosphorylation-mediated biological events.

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Year:  2016        PMID: 27726338      PMCID: PMC5481203          DOI: 10.1021/acschembio.6b00289

Source DB:  PubMed          Journal:  ACS Chem Biol        ISSN: 1554-8929            Impact factor:   5.100


  27 in total

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Review 2.  Photoaffinity labelling strategies for mapping the small molecule-protein interactome.

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6.  An Affinity-Based, Cysteine-Specific ATP Analog for Kinase-Catalyzed Crosslinking.

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