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10.1021/ja510028c http://scihub22266oqcxt.onion/10.1021/ja510028c C4291754!4291754 !25474128     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25474128 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Am+Chem+Soc 2014 ; 136 (51 ): 17692-701 Nephropedia Template TP {{tp|p=25474128 |t=2014. Principles of allosteric interactions in cell signaling |pdf=|usr=}}{{25474128 }} gab.com Text Principles of allosteric interactions in cell signaling JO: J Am Chem Soc http://www.kidney.de/pget.php?&tw=1&pmid=25474128 #FOAvip Linking cell signaling events to the fundamental physicochemical basis of the conformational behavior of single molecules and ultimately to cellular function is a key challenge facing the life sciences. Here we outline the emerging principles of allosteric interactions in cell signaling, with emphasis on the following points. (1) Allosteric efficacy is not a function of the chemical composition of the allosteric pocket but reflects the extent of the population shift between the inactive and active states. That is, the allosteric effect is determined by the extent of preferred binding, not by the overall binding affinity. (2) Coupling between the allosteric and active sites does not decide the allosteric effect; however, it does define the propagation pathways, the allosteric binding sites, and key on-path residues. (3) Atoms of allosteric effectors can act as "driver" or "anchor" and create attractive "pulling" or repulsive "pushing" interactions. Deciphering, quantifying, and integrating the multiple co-occurring events present daunting challenges to our scientific community. Twit Text FOAVip Principles of allosteric interactions in cell signaling ????J Am Chem Soc http://www.kidney.de/pget.php?&tw=1&pmid=25474128 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25474128 #FOAvip English Wikipedia <ref>{{Cite pmid|25474128 }}</ref> Principles of allosteric interactions in cell signaling #MMPMID25474128 Nussinov R ; Tsai CJ ; Liu J J Am Chem Soc 2014[Dec]; 136 (51 ): 17692-701 PMID25474128 show ga Linking cell signaling events to the fundamental physicochemical basis of the conformational behavior of single molecules and ultimately to cellular function is a key challenge facing the life sciences. Here we outline the emerging principles of allosteric interactions in cell signaling, with emphasis on the following points. (1) Allosteric efficacy is not a function of the chemical composition of the allosteric pocket but reflects the extent of the population shift between the inactive and active states. That is, the allosteric effect is determined by the extent of preferred binding, not by the overall binding affinity. (2) Coupling between the allosteric and active sites does not decide the allosteric effect; however, it does define the propagation pathways, the allosteric binding sites, and key on-path residues. (3) Atoms of allosteric effectors can act as "driver" or "anchor" and create attractive "pulling" or repulsive "pushing" interactions. Deciphering, quantifying, and integrating the multiple co-occurring events present daunting challenges to our scientific community. |*Allosteric Regulation [MESH] |*Signal Transduction [MESH] |Catalytic Domain [MESH]Principles of allosteric interactions in cell signaling (epmc).pdf DeepDyve Pubget Overpricing