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10.1016/j.sbi.2016.01.004 http://scihub22266oqcxt.onion/10.1016/j.sbi.2016.01.004 C4834252!4834252 !26829757     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26829757 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Curr+Opin+Struct+Biol 2016 ; 37 (ä): 115-22 Nephropedia Template TP {{tp|p=26829757 |t=2016. SPLINTS: small-molecule protein ligand interface stabilizers |pdf=|usr=}}{{26829757 }} gab.com Text SPLINTS: small-molecule protein ligand interface stabilizers JO: Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=26829757 #FOAvip Regulatory protein-protein interactions are ubiquitous in biology, and small molecule protein-protein interaction inhibitors are an important focus in drug discovery. Remarkably little attention has been given to the opposite strategy-stabilization of protein-protein interactions, despite the fact that several well-known therapeutics act through this mechanism. From a structural perspective, we consider representative examples of small molecules that induce or stabilize the association of protein domains to inhibit, or alter, signaling for nuclear hormone, GTPase, kinase, phosphatase, and ubiquitin ligase pathways. These SPLINTS (small-molecule protein ligand interface stabilizers) drive interactions that are in some cases physiologically relevant, and in others entirely adventitious. The diverse structural mechanisms employed suggest approaches for a broader and systematic search for such compounds in drug discovery. Twit Text FOAVip SPLINTS: small-molecule protein ligand interface stabilizers ????Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=26829757 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26829757 #FOAvip English Wikipedia <ref>{{Cite pmid|26829757 }}</ref> SPLINTS: small-molecule protein ligand interface stabilizers #MMPMID26829757 Fischer ES ; Park E ; Eck MJ ; Thomä NH Curr Opin Struct Biol 2016[Apr]; 37 (ä): 115-22 PMID26829757 show ga Regulatory protein-protein interactions are ubiquitous in biology, and small molecule protein-protein interaction inhibitors are an important focus in drug discovery. Remarkably little attention has been given to the opposite strategy-stabilization of protein-protein interactions, despite the fact that several well-known therapeutics act through this mechanism. From a structural perspective, we consider representative examples of small molecules that induce or stabilize the association of protein domains to inhibit, or alter, signaling for nuclear hormone, GTPase, kinase, phosphatase, and ubiquitin ligase pathways. These SPLINTS (small-molecule protein ligand interface stabilizers) drive interactions that are in some cases physiologically relevant, and in others entirely adventitious. The diverse structural mechanisms employed suggest approaches for a broader and systematic search for such compounds in drug discovery. |Cell Nucleus/chemistry [MESH] |GTP Phosphohydrolases/chemistry [MESH] |Guanine Nucleotide Exchange Factors/chemistry [MESH] |Hormones/chemistry [MESH] |Ligands [MESH] |Protein Binding [MESH] |Proteins/*chemistry [MESH]SPLINTS: small-molecule protein ligand interface stabilizers (epmc).pdf DeepDyve Pubget Overpricing