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10.1021/cb200105d http://scihub22266oqcxt.onion/10.1021/cb200105d 21866942/?report=reader!3220786!21866942     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Chem+Biol 2011 ; 6 (11): 1214-22 Nephropedia Template TP {{tp|p=21866942|t=2011. A chemical genomic analysis of decoquinate, a Plasmodium falciparum cytochrome b inhibitor |pdf=|usr=}}{{21866942}} gab.com Text A chemical genomic analysis of decoquinate, a Plasmodium falciparum cytochrome b inhibitor JO: ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=21866942 #FOAvip Decoquinate has single-digit nanomolar activity against in vitro blood stage Plasmodium falciparum parasites, the causative agent of human malaria. In vitro evolution of decoquinate-resistant parasites and subsequent comparative genomic analysis to the drug-sensitive parental strain revealed resistance was conferred by two nonsynonymous single nucleotide polymorphisms in the gene encoding cytochrome b. The resultant amino acid mutations, A122T and Y126C, reside within helix C in the ubiquinol-binding pocket of cytochrome b, an essential subunit of the cytochrome bc(1) complex. As with other cytochrome bc(1) inhibitors, such as atovaquone, decoquinate has low nanomolar activity against in vitro liver stage P. yoelii and provides partial prophylaxis protection when administered to infected mice at 50 mg kg(-1). In addition, transgenic parasites expressing yeast dihydroorotate dehydrogenase are >200-fold less sensitive to decoquinate, which provides additional evidence that this drug inhibits the parasite's mitochondrial electron transport chain. Importantly, decoquinate exhibits limited cross-resistance to a panel of atovaquone-resistant parasites evolved to harbor various mutations in cytochrome b. The basis for this difference was revealed by molecular docking studies, in which both of these inhibitors were shown to have distinctly different modes of binding within the ubiquinol-binding site of cytochrome b. Twit Text FOAVip A chemical genomic analysis of decoquinate, a Plasmodium falciparum cytochrome b inhibitor ????ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=21866942 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=21866942 #FOAvip English Wikipedia <ref>{{Cite pmid|21866942}}</ref> A chemical genomic analysis of decoquinate, a Plasmodium falciparum cytochrome b inhibitor #MMPMID21866942 Nam TG; McNamara CW; Bopp S; Dharia NV; Meister S; Bonamy GM; Plouffe DM; Kato N; McCormack S; Bursulaya B; Ke H; Vaidya AB; Schultz PG; Winzeler EA ACS Chem Biol 2011[Nov]; 6 (11): 1214-22 PMID21866942show ga Decoquinate has single-digit nanomolar activity against in vitro blood stage Plasmodium falciparum parasites, the causative agent of human malaria. In vitro evolution of decoquinate-resistant parasites and subsequent comparative genomic analysis to the drug-sensitive parental strain revealed resistance was conferred by two nonsynonymous single nucleotide polymorphisms in the gene encoding cytochrome b. The resultant amino acid mutations, A122T and Y126C, reside within helix C in the ubiquinol-binding pocket of cytochrome b, an essential subunit of the cytochrome bc(1) complex. As with other cytochrome bc(1) inhibitors, such as atovaquone, decoquinate has low nanomolar activity against in vitro liver stage P. yoelii and provides partial prophylaxis protection when administered to infected mice at 50 mg kg(-1). In addition, transgenic parasites expressing yeast dihydroorotate dehydrogenase are >200-fold less sensitive to decoquinate, which provides additional evidence that this drug inhibits the parasite's mitochondrial electron transport chain. Importantly, decoquinate exhibits limited cross-resistance to a panel of atovaquone-resistant parasites evolved to harbor various mutations in cytochrome b. The basis for this difference was revealed by molecular docking studies, in which both of these inhibitors were shown to have distinctly different modes of binding within the ubiquinol-binding site of cytochrome b. |Animals[MESH] |Antimalarials/administration & dosage/chemistry/*pharmacology[MESH] |Crystallography, X-Ray[MESH] |Cytochromes b/*antagonists & inhibitors/genetics/metabolism[MESH] |Decoquinate/administration & dosage/chemistry/*pharmacology[MESH] |Drug Discovery[MESH] |Drug Resistance, Fungal/drug effects/genetics[MESH] |Female[MESH] |Humans[MESH] |Mice[MESH] |Mice, Inbred ICR[MESH] |Models, Molecular[MESH] |Molecular Structure[MESH] |Parasitic Sensitivity Tests[MESH] |Plasmodium falciparum/*drug effects/genetics[MESH]A chemical genomic analysis of decoquinate, a Plasmodium falciparum cy(epmc).pdf DeepDyve Pubget Overpricing