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10.1016/j.celrep.2017.03.019 http://scihub22266oqcxt.onion/10.1016/j.celrep.2017.03.019 C5382234!5382234!28355572     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Rep 2017 ; 18 (13): 3219-26 Nephropedia Template TP {{tp|p=28355572|t=2017. Precise Temporal Profiling of Signaling Complexes in Primary Cells Using SWATH Mass Spectrometry |pdf=|usr=}}{{28355572}} gab.com Text Precise Temporal Profiling of Signaling Complexes in Primary Cells Using SWATH Mass Spectrometry JO: Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=28355572 #FOAvip Spatiotemporal organization of protein interactions in cell signaling is a fundamental process that drives cellular functions. Given differential protein expression across tissues and developmental stages, the architecture and dynamics of signaling interaction proteomes is, likely, highly context dependent. However, current interaction information has been almost exclusively obtained from transformed cells. In this study, we applied an advanced and robust workflow combining mouse genetics and affinity purification (AP)-SWATH mass spectrometry to profile the dynamics of 53 high-confidence protein interactions in primary T cells, using the scaffold protein GRB2 as a model. The workflow also provided a sufficient level of robustness to pinpoint differential interaction dynamics between two similar, but functionally distinct, primary T cell populations. Altogether, we demonstrated that precise and reproducible quantitative measurements of protein interaction dynamics can be achieved in primary cells isolated from mammalian tissues, allowing resolution of the tissue-specific context of cell-signaling events. Twit Text FOAVip Precise Temporal Profiling of Signaling Complexes in Primary Cells Using SWATH Mass Spectrometry ????Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=28355572 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28355572 #FOAvip English Wikipedia <ref>{{Cite pmid|28355572}}</ref> Precise Temporal Profiling of Signaling Complexes in Primary Cells Using SWATH Mass Spectrometry #MMPMID28355572 Caron E; Roncagalli R; Hase T; Wolski WE; Choi M; Menoita MG; Durand S; García-Blesa A; Fierro-Monti I; Sajic T; Heusel M; Weiss T; Malissen M; Schlapbach R; Collins BC; Ghosh S; Kitano H; Aebersold R; Malissen B; Gstaiger M Cell Rep 2017[Mar]; 18 (13): 3219-26 PMID28355572show ga Spatiotemporal organization of protein interactions in cell signaling is a fundamental process that drives cellular functions. Given differential protein expression across tissues and developmental stages, the architecture and dynamics of signaling interaction proteomes is, likely, highly context dependent. However, current interaction information has been almost exclusively obtained from transformed cells. In this study, we applied an advanced and robust workflow combining mouse genetics and affinity purification (AP)-SWATH mass spectrometry to profile the dynamics of 53 high-confidence protein interactions in primary T cells, using the scaffold protein GRB2 as a model. The workflow also provided a sufficient level of robustness to pinpoint differential interaction dynamics between two similar, but functionally distinct, primary T cell populations. Altogether, we demonstrated that precise and reproducible quantitative measurements of protein interaction dynamics can be achieved in primary cells isolated from mammalian tissues, allowing resolution of the tissue-specific context of cell-signaling events. äPrecise Temporal Profiling of Signaling Complexes in Primary Cells Usi(epmc).pdf DeepDyve Pubget Overpricing