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10.1021/acs.chemrev.5b00548 http://scihub22266oqcxt.onion/10.1021/acs.chemrev.5b00548 C5342629!5342629!26922996     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Chem+Rev 2016 ; 116 (11): 6424-62 Nephropedia Template TP {{tp|p=26922996|t=2016. Dynamic protein interaction networks and new structural paradigms in signaling |pdf=|usr=}}{{26922996}} gab.com Text Dynamic protein interaction networks and new structural paradigms in signaling JO: Chem Rev http://www.kidney.de/pget.php?&tw=1&pmid=26922996 #FOAvip Understanding signaling and other complex biological processes requires elucidating the critical roles of intrinsically disordered proteins and regions (IDPs/IDRs), which represent ~30% of the proteome and enable unique regulatory mechanisms. In this review we describe the structural heterogeneity of disordered proteins that underpins these mechanisms and the latest progress in obtaining structural descriptions of ensembles of disordered proteins that are needed for linking structure and dynamics to function. We describe the diverse interactions of IDPs that can have unusual characteristics such as ?ultrasensitivity? and ?regulated folding and unfolding?. We also summarize the mounting data showing that large-scale assembly and protein phase separation occurs within a variety of signaling complexes and cellular structures. In addition, we discuss efforts to therapeutically target disordered proteins with small molecules. Overall, we interpret the remodeling of disordered state ensembles due to binding and post-translational modifications within an expanded framework for allostery that provides significant insights into how disordered proteins transmit biological information. Twit Text FOAVip Dynamic protein interaction networks and new structural paradigms in signaling ????Chem Rev http://www.kidney.de/pget.php?&tw=1&pmid=26922996 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26922996 #FOAvip English Wikipedia <ref>{{Cite pmid|26922996}}</ref> Dynamic protein interaction networks and new structural paradigms in signaling #MMPMID26922996 Csizmok V; Follis AV; Kriwacki RW; Forman-Kay JD Chem Rev 2016[Jun]; 116 (11): 6424-62 PMID26922996show ga Understanding signaling and other complex biological processes requires elucidating the critical roles of intrinsically disordered proteins and regions (IDPs/IDRs), which represent ~30% of the proteome and enable unique regulatory mechanisms. In this review we describe the structural heterogeneity of disordered proteins that underpins these mechanisms and the latest progress in obtaining structural descriptions of ensembles of disordered proteins that are needed for linking structure and dynamics to function. We describe the diverse interactions of IDPs that can have unusual characteristics such as ?ultrasensitivity? and ?regulated folding and unfolding?. We also summarize the mounting data showing that large-scale assembly and protein phase separation occurs within a variety of signaling complexes and cellular structures. In addition, we discuss efforts to therapeutically target disordered proteins with small molecules. Overall, we interpret the remodeling of disordered state ensembles due to binding and post-translational modifications within an expanded framework for allostery that provides significant insights into how disordered proteins transmit biological information. äDynamic protein interaction networks and new structural paradigms in s(epmc).pdf DeepDyve Pubget Overpricing