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10.1038/nmeth.3395 http://scihub22266oqcxt.onion/10.1038/nmeth.3395 C4449307!4449307!25938370     free     free     free       Nat+Methods 2015 ; 12 (6): 553-60 Nephropedia Template TP {{tp|p=25938370|t=2015. Rapid, Optimized Interactomic Screening |pdf=|usr=}}{{25938370}} gab.com Text Rapid, Optimized Interactomic Screening JO: Nat Methods http://www.kidney.de/pget.php?&tw=1&pmid=25938370 #FOAvip We must reliably map the interactomes of cellular macromolecular complexes in order to fully explore and understand biological systems. However, there are no methods to accurately predict how to capture a given macromolecular complex with its physiological binding partners. Here, we present a screen that comprehensively explores the parameters affecting the stability of interactions in affinity-captured complexes, enabling the discovery of physiological binding partners and the elucidation of their functional interactions in unparalleled detail. We have implemented this screen on several macromolecular complexes from a variety of organisms, revealing novel profiles even for well-studied proteins. Our approach is robust, economical and automatable, providing an inroad to the rigorous, systematic dissection of cellular interactomes. Twit Text FOAVip Rapid, Optimized Interactomic Screening ????Nat Methods http://www.kidney.de/pget.php?&tw=1&pmid=25938370 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25938370 #FOAvip English Wikipedia <ref>{{Cite pmid|25938370}}</ref> Rapid, Optimized Interactomic Screening #MMPMID25938370 Hakhverdyan Z; Domanski M; Hough L; Oroskar AA; Oroskar AR; Keegan S; Dilworth DJ; Molloy KR; Sherman V; Aitchison JD; Fenyö D; Chait BT; Jensen TH; Rout MP; LaCava J Nat Methods 2015[Jun]; 12 (6): 553-60 PMID25938370show ga We must reliably map the interactomes of cellular macromolecular complexes in order to fully explore and understand biological systems. However, there are no methods to accurately predict how to capture a given macromolecular complex with its physiological binding partners. Here, we present a screen that comprehensively explores the parameters affecting the stability of interactions in affinity-captured complexes, enabling the discovery of physiological binding partners and the elucidation of their functional interactions in unparalleled detail. We have implemented this screen on several macromolecular complexes from a variety of organisms, revealing novel profiles even for well-studied proteins. Our approach is robust, economical and automatable, providing an inroad to the rigorous, systematic dissection of cellular interactomes. äRapid, Optimized Interactomic Screening (epmc).pdf DeepDyve Pubget Overpricing