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10.1002/cmdc.201000449 http://scihub22266oqcxt.onion/10.1002/cmdc.201000449 21275051!7162187!21275051     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 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       ChemMedChem 2011 ; 6 (2): 273-8 Nephropedia Template TP {{tp|p=21275051|t=2011. Potent and selective inhibition of cysteine proteases from Plasmodium falciparum and Trypanosoma brucei |pdf=|usr=}}{{21275051}} gab.com Text Potent and selective inhibition of cysteine proteases from Plasmodium falciparum and Trypanosoma brucei JO: ChemMedChem http://www.kidney.de/pget.php?&tw=1&pmid=21275051 #FOAvip Treating tropical diseases: Structure-based design afforded highly active triazine nitrile inhibitors of the protozoan cysteine proteases falcipain-2 and rhodesain. Optimization of the occupancy of the S1, S2, and S3 pockets of these enzymes yielded inhibitory constants in the low nanomolar activity range. The new ligands are selective against other related proteases and exhibit in vitro activities against the protozoan parasites.[Image: see text] Twit Text FOAVip Potent and selective inhibition of cysteine proteases from Plasmodium falciparum and Trypanosoma brucei ????ChemMedChem http://www.kidney.de/pget.php?&tw=1&pmid=21275051 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=21275051 #FOAvip English Wikipedia <ref>{{Cite pmid|21275051}}</ref> Potent and selective inhibition of cysteine proteases from Plasmodium falciparum and Trypanosoma brucei #MMPMID21275051 Ehmke V; Heindl C; Rottmann M; Freymond C; Schweizer WB; Brun R; Stich A; Schirmeister T; Diederich F ChemMedChem 2011[Feb]; 6 (2): 273-8 PMID21275051show ga Treating tropical diseases: Structure-based design afforded highly active triazine nitrile inhibitors of the protozoan cysteine proteases falcipain-2 and rhodesain. Optimization of the occupancy of the S1, S2, and S3 pockets of these enzymes yielded inhibitory constants in the low nanomolar activity range. The new ligands are selective against other related proteases and exhibit in vitro activities against the protozoan parasites.[Image: see text] |Animals[MESH] |Crystallography, X-Ray[MESH] |Cysteine Proteases/chemistry/*metabolism[MESH] |Cysteine Proteinase Inhibitors/*pharmacology[MESH] |Models, Molecular[MESH] |Plasmodium falciparum/*enzymology[MESH]Potent and selective inhibition of cysteine proteases from Plasmodium (epmc).pdf DeepDyve Pubget Overpricing