Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1073/pnas.1417816112 http://scihub22266oqcxt.onion/10.1073/pnas.1417816112 C4284529!4284529!25512491     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       Proc+Natl+Acad+Sci+U+S+A 2014 ; 111 (52): 18572-7 Nephropedia Template TP {{tp|p=25512491|t=2014. Identification of S-nitroso-CoA reductases that regulate protein S-nitrosylation |pdf=|usr=}}{{25512491}} gab.com Text Identification of S-nitroso-CoA reductases that regulate protein S-nitrosylation JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25512491 #FOAvip Coenzyme A (CoA) is a small-molecular-weight thiol that plays a central role in cellular metabolism. We have discovered a novel, phylogenetically conserved class of enzymes that reduce S-nitroso-CoA (SNO-CoA) and thereby regulate protein S-nitrosylation. These denitrosylases, identified as alcohol dehydrogenase 6 (Adh6) in yeast and aldo-keto reductase 1A1 in mammals, may be analogized to deacetylases, which regulate CoA-mediated protein acetylation. In yeast, Adh6 (previously without ascribed cellular function) regulates endogenous protein S-nitrosylation (heretofore unknown) including function-altering S-nitrosylation that impacts CoA-related metabolism. Thus, our findings establish a novel role for CoA in protein S-nitrosylation (operating through SNO-CoA), which is governed by specific enzymes. This mechanism may regulate the influence of nitric oxide on cellular metabolism in health and disease. Twit Text FOAVip Identification of S-nitroso-CoA reductases that regulate protein S-nitrosylation ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25512491 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25512491 #FOAvip English Wikipedia <ref>{{Cite pmid|25512491}}</ref> Identification of S-nitroso-CoA reductases that regulate protein S-nitrosylation #MMPMID25512491 Anand P; Hausladen A; Wang YJ; Zhang GF; Stomberski C; Brunengraber H; Hess DT; Stamler JS Proc Natl Acad Sci U S A 2014[Dec]; 111 (52): 18572-7 PMID25512491show ga Coenzyme A (CoA) is a small-molecular-weight thiol that plays a central role in cellular metabolism. We have discovered a novel, phylogenetically conserved class of enzymes that reduce S-nitroso-CoA (SNO-CoA) and thereby regulate protein S-nitrosylation. These denitrosylases, identified as alcohol dehydrogenase 6 (Adh6) in yeast and aldo-keto reductase 1A1 in mammals, may be analogized to deacetylases, which regulate CoA-mediated protein acetylation. In yeast, Adh6 (previously without ascribed cellular function) regulates endogenous protein S-nitrosylation (heretofore unknown) including function-altering S-nitrosylation that impacts CoA-related metabolism. Thus, our findings establish a novel role for CoA in protein S-nitrosylation (operating through SNO-CoA), which is governed by specific enzymes. This mechanism may regulate the influence of nitric oxide on cellular metabolism in health and disease. äIdentification of S-nitroso-CoA reductases that regulate protein S-nit(epmc).pdf DeepDyve Pubget Overpricing