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10.1016/j.chembiol.2015.05.013 http://scihub22266oqcxt.onion/10.1016/j.chembiol.2015.05.013 C4475277!4475277!26091171     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Chem+Biol 2015 ; 22 (6): 785-92 Nephropedia Template TP {{tp|p=26091171|t=2015. Nitric Oxide Synthase as a Target for Methicillin Resistant Staphylococcus aureus |pdf=|usr=}}{{26091171}} gab.com Text Nitric Oxide Synthase as a Target for Methicillin Resistant Staphylococcus aureus JO: Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=26091171 #FOAvip Bacterial infections associated with methicillin-resistant Staphylococcus aureus (MRSA) are a major economic burden to hospitals and confer high rates of morbidity and mortality amongst those infected. Exploitation of novel therapeutic targets is thus necessary to combat this dangerous pathogen. Here we report on the identification and characterization, including crystal structures, of two nitric oxide synthase (NOS) inhibitors that function as antimicrobials against MRSA. These data provide the first evidence that bacterial NOS (bNOS) inhibitors can work synergistically with oxidative stress to enhance MRSA killing. Crystal structures show that each inhibitor contacts an active site Ile residue in bNOS that is Val in the mammalian NOS isoforms. Mutagenesis studies show that the additional nonpolar contacts provided by the Ile in bNOS contributes to tighter binding of the bacterial enzyme. Twit Text FOAVip Nitric Oxide Synthase as a Target for Methicillin Resistant Staphylococcus aureus ????Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=26091171 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26091171 #FOAvip English Wikipedia <ref>{{Cite pmid|26091171}}</ref> Nitric Oxide Synthase as a Target for Methicillin Resistant Staphylococcus aureus #MMPMID26091171 Holden JK; Kang S; Beasley FC; Cinelli MA; Li H; Roy SG; Dejam D; Edinger AL; Nizet V; Silverman RB; Poulos TL Chem Biol 2015[Jun]; 22 (6): 785-92 PMID26091171show ga Bacterial infections associated with methicillin-resistant Staphylococcus aureus (MRSA) are a major economic burden to hospitals and confer high rates of morbidity and mortality amongst those infected. Exploitation of novel therapeutic targets is thus necessary to combat this dangerous pathogen. Here we report on the identification and characterization, including crystal structures, of two nitric oxide synthase (NOS) inhibitors that function as antimicrobials against MRSA. These data provide the first evidence that bacterial NOS (bNOS) inhibitors can work synergistically with oxidative stress to enhance MRSA killing. Crystal structures show that each inhibitor contacts an active site Ile residue in bNOS that is Val in the mammalian NOS isoforms. Mutagenesis studies show that the additional nonpolar contacts provided by the Ile in bNOS contributes to tighter binding of the bacterial enzyme. äNitric Oxide Synthase as a Target for Methicillin Resistant Staphyloco(epmc).pdf DeepDyve Pubget Overpricing