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10.1021/ml300419r http://scihub22266oqcxt.onion/10.1021/ml300419r 23795240/?report=reader!3685428!23795240     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Med+Chem+Lett 2013 ; 4 (2): 278-282 Nephropedia Template TP {{tp|p=23795240|t=2013. Antimalarial and Structural Studies of Pyridine-containing Inhibitors of 1-Deoxyxylulose-5-phosphate Reductoisomerase |pdf=|usr=}}{{23795240}} gab.com Text Antimalarial and Structural Studies of Pyridine-containing Inhibitors of 1-Deoxyxylulose-5-phosphate Reductoisomerase JO: ACS Med Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=23795240 #FOAvip 1-Deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) in the non-mevalonate isoprene biosynthesis pathway is a target for developing antimalarial drugs. Fosmidomycin, a potent DXR inhibitor, showed safety as well as efficacy against P. falciparum malaria in clinical trials. Based on our previous quantitative structure activity relationship (QSAR) and crystallographic studies, several novel pyridine-containing fosmidomycin derivatives were designed, synthesized and found to be highly potent inhibitors of P. falciparum DXR (PfDXR) having K(i) values of 1.9 - 13 nM, with the best one being ~11x more active than fosmidomycin. These compounds also potently block the proliferation of multi-drug resistant P. falciparum with EC(50) values as low as 170 nM. A 2.3 A crystal structure of PfDXR in complex with one of the inhibitors is reported, showing the flexible loop of the protein undergoes conformational changes upon ligand binding and a hydrogen bond and favorable hydrophobic interactions between the pyridine group and PfDXR account for the enhanced activity. Twit Text FOAVip Antimalarial and Structural Studies of Pyridine-containing Inhibitors of 1-Deoxyxylulose-5-phosphate Reductoisomerase ????ACS Med Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=23795240 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23795240 #FOAvip English Wikipedia <ref>{{Cite pmid|23795240}}</ref> Antimalarial and Structural Studies of Pyridine-containing Inhibitors of 1-Deoxyxylulose-5-phosphate Reductoisomerase #MMPMID23795240 Xue J; Diao J; Cai G; Deng L; Zheng B; Yao Y; Song Y ACS Med Chem Lett 2013[Feb]; 4 (2): 278-282 PMID23795240show ga 1-Deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) in the non-mevalonate isoprene biosynthesis pathway is a target for developing antimalarial drugs. Fosmidomycin, a potent DXR inhibitor, showed safety as well as efficacy against P. falciparum malaria in clinical trials. Based on our previous quantitative structure activity relationship (QSAR) and crystallographic studies, several novel pyridine-containing fosmidomycin derivatives were designed, synthesized and found to be highly potent inhibitors of P. falciparum DXR (PfDXR) having K(i) values of 1.9 - 13 nM, with the best one being ~11x more active than fosmidomycin. These compounds also potently block the proliferation of multi-drug resistant P. falciparum with EC(50) values as low as 170 nM. A 2.3 A crystal structure of PfDXR in complex with one of the inhibitors is reported, showing the flexible loop of the protein undergoes conformational changes upon ligand binding and a hydrogen bond and favorable hydrophobic interactions between the pyridine group and PfDXR account for the enhanced activity. äAntimalarial and Structural Studies of Pyridine-containing Inhibitors (epmc).pdf DeepDyve Pubget Overpricing