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10.1074/mcp.M114.041087 http://scihub22266oqcxt.onion/10.1074/mcp.M114.041087 C4256487!4256487!25154561     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mol+Cell+Proteomics 2014 ; 13 (12): 3332-42 Nephropedia Template TP {{tp|p=25154561|t=2014. Kinase Substrate Sensor (KISS), a Mammalian In Situ Protein Interaction Sensor* |pdf=|usr=}}{{25154561}} gab.com Text Kinase Substrate Sensor (KISS), a Mammalian In Situ Protein Interaction Sensor* JO: Mol Cell Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=25154561 #FOAvip Probably every cellular process is governed by protein-protein interaction (PPIs), which are often highly dynamic in nature being modulated by in- or external stimuli. Here we present KISS, for KInase Substrate Sensor, a mammalian two-hybrid approach designed to map intracellular PPIs and some of the dynamic features they exhibit. Benchmarking experiments indicate that in terms of sensitivity and specificity KISS is on par with other binary protein interaction technologies while being complementary with regard to the subset of PPIs it is able to detect. We used KISS to evaluate interactions between different types of proteins, including transmembrane proteins, expressed at their native subcellular location. In situ analysis of endoplasmic reticulum stress-induced clustering of the endoplasmic reticulum stress sensor ERN1 and ligand-dependent ?-arrestin recruitment to GPCRs illustrated the method's potential to study functional PPI modulation in complex cellular processes. Exploring its use as a tool for in cell evaluation of pharmacological interference with PPIs, we showed that reported effects of known GPCR antagonists and PPI inhibitors are properly recapitulated. In a three-hybrid setup, KISS was able to map interactions between small molecules and proteins. Taken together, we established KISS as a sensitive approach for in situ analysis of protein interactions and their modulation in a changing cellular context or in response to pharmacological challenges. Twit Text FOAVip Kinase Substrate Sensor (KISS), a Mammalian In Situ Protein Interaction Sensor* ????Mol Cell Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=25154561 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25154561 #FOAvip English Wikipedia <ref>{{Cite pmid|25154561}}</ref> Kinase Substrate Sensor (KISS), a Mammalian In Situ Protein Interaction Sensor* #MMPMID25154561 Lievens S; Gerlo S; Lemmens I; De Clercq DJH; Risseeuw MDP; Vanderroost N; De Smet AS; Ruyssinck E; Chevet E; Van Calenbergh S; Tavernier J Mol Cell Proteomics 2014[Dec]; 13 (12): 3332-42 PMID25154561show ga Probably every cellular process is governed by protein-protein interaction (PPIs), which are often highly dynamic in nature being modulated by in- or external stimuli. Here we present KISS, for KInase Substrate Sensor, a mammalian two-hybrid approach designed to map intracellular PPIs and some of the dynamic features they exhibit. Benchmarking experiments indicate that in terms of sensitivity and specificity KISS is on par with other binary protein interaction technologies while being complementary with regard to the subset of PPIs it is able to detect. We used KISS to evaluate interactions between different types of proteins, including transmembrane proteins, expressed at their native subcellular location. In situ analysis of endoplasmic reticulum stress-induced clustering of the endoplasmic reticulum stress sensor ERN1 and ligand-dependent ?-arrestin recruitment to GPCRs illustrated the method's potential to study functional PPI modulation in complex cellular processes. Exploring its use as a tool for in cell evaluation of pharmacological interference with PPIs, we showed that reported effects of known GPCR antagonists and PPI inhibitors are properly recapitulated. In a three-hybrid setup, KISS was able to map interactions between small molecules and proteins. Taken together, we established KISS as a sensitive approach for in situ analysis of protein interactions and their modulation in a changing cellular context or in response to pharmacological challenges. äKinase Substrate Sensor (KISS), a Mammalian In Situ Protein Interactio(epmc).pdf DeepDyve Pubget Overpricing