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10.1016/j.jmb.2016.11.030 http://scihub22266oqcxt.onion/10.1016/j.jmb.2016.11.030 C5350076!5350076!27939292     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Mol+Biol 2017 ; 429 (2): 237-48 Nephropedia Template TP {{tp|p=27939292|t=2017. Structural basis of Arp2/3 complex inhibition by GMF, Coronin, and Arpin |pdf=|usr=}}{{27939292}} gab.com Text Structural basis of Arp2/3 complex inhibition by GMF, Coronin, and Arpin JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=27939292 #FOAvip The evolutionarily conserved Arp2/3 complex plays a central role in nucleating the branched actin filament arrays that drive cell migration, endocytosis, and other processes. To better understand Arp2/3 complex regulation, we used single particle electron microscopy to compare the structures of Arp2/3 complex bound to three different inhibitory ligands: GMF, Coronin, and Arpin. Although the three inhibitors have distinct binding sites on Arp2/3 complex, they each induced an ?open? nucleation-inactive conformation. Coronin promoted a standard (previously described) open conformation of Arp2/3 complex, with the N-terminal ?-propeller domain of Coronin positioned near the p35/ARPC2 subunit of Arp2/3 complex. GMF induced two distinct open conformations of Arp2/3 complex, which correlated with two suggested binding sites for GMF. Further, GMF synergized with Coronin in inhibiting actin nucleation by Arp2/3 complex. Arpin, which uses VCA-related acidic (A) motifs to interact with the Arp2/3 complex, induced the standard open conformation, and two new masses appeared at positions near Arp2 and Arp3. Further, Arpin showed additive inhibitory effects on Arp2/3 complex with Coronin and GMF. Together, these data suggest that Arp2/3 complex conformation is highly polymorphic and that its activities can be controlled combinatorially by different inhibitory ligands. Twit Text FOAVip Structural basis of Arp2/3 complex inhibition by GMF, Coronin, and Arpin ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=27939292 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27939292 #FOAvip English Wikipedia <ref>{{Cite pmid|27939292}}</ref> Structural basis of Arp2/3 complex inhibition by GMF, Coronin, and Arpin #MMPMID27939292 Sokolova OS; Chemeris A; Guo S; Alioto SL; Gandhi M; Padrick S; Pechnikova E; David V; Gautreau A; Goode BL J Mol Biol 2017[Jan]; 429 (2): 237-48 PMID27939292show ga The evolutionarily conserved Arp2/3 complex plays a central role in nucleating the branched actin filament arrays that drive cell migration, endocytosis, and other processes. To better understand Arp2/3 complex regulation, we used single particle electron microscopy to compare the structures of Arp2/3 complex bound to three different inhibitory ligands: GMF, Coronin, and Arpin. Although the three inhibitors have distinct binding sites on Arp2/3 complex, they each induced an ?open? nucleation-inactive conformation. Coronin promoted a standard (previously described) open conformation of Arp2/3 complex, with the N-terminal ?-propeller domain of Coronin positioned near the p35/ARPC2 subunit of Arp2/3 complex. GMF induced two distinct open conformations of Arp2/3 complex, which correlated with two suggested binding sites for GMF. Further, GMF synergized with Coronin in inhibiting actin nucleation by Arp2/3 complex. Arpin, which uses VCA-related acidic (A) motifs to interact with the Arp2/3 complex, induced the standard open conformation, and two new masses appeared at positions near Arp2 and Arp3. Further, Arpin showed additive inhibitory effects on Arp2/3 complex with Coronin and GMF. Together, these data suggest that Arp2/3 complex conformation is highly polymorphic and that its activities can be controlled combinatorially by different inhibitory ligands. äStructural basis of Arp2/3 complex inhibition by GMF, Coronin, and Arp(epmc).pdf DeepDyve Pubget Overpricing