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10.1016/j.ejmech.2014.09.047 http://scihub22266oqcxt.onion/10.1016/j.ejmech.2014.09.047 C4362920!4362920!25253637     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25253637.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Eur+J+Med+Chem 2015 ; 94 (ä): 480-8 Nephropedia Template TP {{tp|p=25253637|t=2015. Structure-Based Inhibition of Protein-Protein Interactions |pdf=|usr=}}{{25253637}} gab.com Text Structure-Based Inhibition of Protein-Protein Interactions JO: Eur J Med Chem http://www.kidney.de/pget.php?&tw=1&pmid=25253637 #FOAvip Protein-protein interactions (PPIs) are emerging as attractive targets for drug design because of their central role in directing normal and aberrant cellular functions. These interactions were once considered ?undruggable? because their large and dynamic interfaces make small molecule inhibitor design challenging. However, landmark advances in computational analysis, fragment screening and molecular design have enabled development of a host of promising strategies to address the fundamental molecular recognition challenge. An attractive approach for targeting PPIs involves mimicry of protein domains that are critical for complex formation. This approach recognizes that protein subdomains or protein secondary structures are often present at interfaces and serve as organized scaffolds for the presentation of side chain groups that engage the partner protein(s). Design of protein domain mimetics is in principle rather straightforward but is enabled by a host of computational strategies that provide predictions of important residues that should be mimicked. Herein we describe a workflow proceeding from interaction network analysis, to modeling a complex structure, to identifying a high-affinity sub-structure, to developing interaction inhibitors. We apply the design procedure to peptidomimetic inhibitors of Ras-mediated signaling. Twit Text FOAVip Structure-Based Inhibition of Protein-Protein Interactions ????Eur J Med Chem http://www.kidney.de/pget.php?&tw=1&pmid=25253637 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25253637 #FOAvip English Wikipedia <ref>{{Cite pmid|25253637}}</ref> Structure-Based Inhibition of Protein-Protein Interactions #MMPMID25253637 Watkins AM; Arora PS Eur J Med Chem 2015[Apr]; 94 (ä): 480-8 PMID25253637show ga Protein-protein interactions (PPIs) are emerging as attractive targets for drug design because of their central role in directing normal and aberrant cellular functions. These interactions were once considered ?undruggable? because their large and dynamic interfaces make small molecule inhibitor design challenging. However, landmark advances in computational analysis, fragment screening and molecular design have enabled development of a host of promising strategies to address the fundamental molecular recognition challenge. An attractive approach for targeting PPIs involves mimicry of protein domains that are critical for complex formation. This approach recognizes that protein subdomains or protein secondary structures are often present at interfaces and serve as organized scaffolds for the presentation of side chain groups that engage the partner protein(s). Design of protein domain mimetics is in principle rather straightforward but is enabled by a host of computational strategies that provide predictions of important residues that should be mimicked. Herein we describe a workflow proceeding from interaction network analysis, to modeling a complex structure, to identifying a high-affinity sub-structure, to developing interaction inhibitors. We apply the design procedure to peptidomimetic inhibitors of Ras-mediated signaling. äStructure-Based Inhibition of Protein-Protein Interactions (epmc).pdf DeepDyve Pubget Overpricing