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10.1021/ml300394w http://scihub22266oqcxt.onion/10.1021/ml300394w C4027485!4027485!24900659     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Med+Chem+Lett 2013 ; 4 (2): 274-7 Nephropedia Template TP {{tp|p=24900659|t=2013. Probing the Binding Site of Abl Tyrosine Kinase Using in Situ Click Chemistry |pdf=|usr=}}{{24900659}} gab.com Text Probing the Binding Site of Abl Tyrosine Kinase Using in Situ Click Chemistry JO: ACS Med Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=24900659 #FOAvip Modern combinatorial chemistry is used to discover compounds with desired function by an alternative strategy, in which the biological target is directly involved in the choice of ligands assembled from a pool of smaller fragments. Herein, we present the first experimental result where the use of in situ click chemistry has been successfully applied to probe the ligand-binding site of Abl and the ability of this enzyme to form its inhibitor. Docking studies show that Abl is able to allow the in situ click chemistry between specific azide and alkyne fragments by binding to Abl-active sites. This report allows medicinal chemists to use protein-directed in situ click chemistry for exploring the conformational space of a ligand-binding pocket and the ability of the protein to guide its inhibitor. This approach can be a novel, valuable tool to guide drug design synthesis in the field of tyrosine kinases. Twit Text FOAVip Probing the Binding Site of Abl Tyrosine Kinase Using in Situ Click Chemistry ????ACS Med Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=24900659 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24900659 #FOAvip English Wikipedia <ref>{{Cite pmid|24900659}}</ref> Probing the Binding Site of Abl Tyrosine Kinase Using in Situ Click Chemistry #MMPMID24900659 Peruzzotti C; Borrelli S; Ventura M; Pantano R; Fumagalli G; Christodoulou M; Monticelli D; Luzzani M; Fallacara AL; Tintori C; Botta M; Passarella D ACS Med Chem Lett 2013[Feb]; 4 (2): 274-7 PMID24900659show ga Modern combinatorial chemistry is used to discover compounds with desired function by an alternative strategy, in which the biological target is directly involved in the choice of ligands assembled from a pool of smaller fragments. Herein, we present the first experimental result where the use of in situ click chemistry has been successfully applied to probe the ligand-binding site of Abl and the ability of this enzyme to form its inhibitor. Docking studies show that Abl is able to allow the in situ click chemistry between specific azide and alkyne fragments by binding to Abl-active sites. This report allows medicinal chemists to use protein-directed in situ click chemistry for exploring the conformational space of a ligand-binding pocket and the ability of the protein to guide its inhibitor. This approach can be a novel, valuable tool to guide drug design synthesis in the field of tyrosine kinases. äProbing the Binding Site of Abl Tyrosine Kinase Using in Situ Click Ch(epmc).pdf DeepDyve Pubget Overpricing