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.

10.1016/j.cmet.2017.03.006 http://scihub22266oqcxt.onion/10.1016/j.cmet.2017.03.006 C5399522!5399522!28380375     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Metab 2017 ; 25 (4): 823-837.e8 Nephropedia Template TP {{tp|p=28380375|t=2017. A Class of Reactive Acyl-CoA Species Reveals the Non-Enzymatic Origins of Protein Acylation |pdf=|usr=}}{{28380375}} gab.com Text A Class of Reactive Acyl-CoA Species Reveals the Non-Enzymatic Origins of Protein Acylation JO: Cell Metab http://www.kidney.de/pget.php?&tw=1&pmid=28380375 #FOAvip The mechanisms underlying the formation of acyl protein modifications remain poorly understood. By investigating the reactivity of endogenous acyl-CoA metabolites, we found a class of acyl-CoAs that undergoes intramolecular catalysis to form reactive intermediates which non-enzymatically modify proteins. Based on this mechanism, we predicted, validated, and characterized a protein modification: 3-hydroxy-3-methylglutaryl(HMG)-lysine. In a model of altered HMG-CoA metabolism, we found evidence of two additional protein modifications: 3-methylglutaconyl(MGc)-lysine and 3-methylglutaryl(MG)-lysine. Using quantitative proteomics, we compared the ?acylomes? of two reactive acyl-CoA species, namely HMG-CoA and glutaryl-CoA, which are generated in different pathways. We found proteins that are uniquely modified by each reactive metabolite, as well as common proteins and pathways. We identified the tricarboxylic acid cycle as a pathway commonly regulated by acylation, and validated malate dehydrogenase as a key target. These data uncover a fundamental relationship between reactive acyl-CoA species and proteins, and define a new regulatory paradigm in metabolism. Twit Text FOAVip A Class of Reactive Acyl-CoA Species Reveals the Non-Enzymatic Origins of Protein Acylation ????Cell Metab http://www.kidney.de/pget.php?&tw=1&pmid=28380375 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28380375 #FOAvip English Wikipedia <ref>{{Cite pmid|28380375}}</ref> A Class of Reactive Acyl-CoA Species Reveals the Non-Enzymatic Origins of Protein Acylation #MMPMID28380375 Wagner GR; Bhatt DP; O?Connell TM; Thompson JW; Dubois LG; Backos DS; Yang H; Mitchell GA; Ilkayeva OR; Stevens RD; Grimsrud PA; Hirschey MD Cell Metab 2017[Apr]; 25 (4): 823-837.e8 PMID28380375show ga The mechanisms underlying the formation of acyl protein modifications remain poorly understood. By investigating the reactivity of endogenous acyl-CoA metabolites, we found a class of acyl-CoAs that undergoes intramolecular catalysis to form reactive intermediates which non-enzymatically modify proteins. Based on this mechanism, we predicted, validated, and characterized a protein modification: 3-hydroxy-3-methylglutaryl(HMG)-lysine. In a model of altered HMG-CoA metabolism, we found evidence of two additional protein modifications: 3-methylglutaconyl(MGc)-lysine and 3-methylglutaryl(MG)-lysine. Using quantitative proteomics, we compared the ?acylomes? of two reactive acyl-CoA species, namely HMG-CoA and glutaryl-CoA, which are generated in different pathways. We found proteins that are uniquely modified by each reactive metabolite, as well as common proteins and pathways. We identified the tricarboxylic acid cycle as a pathway commonly regulated by acylation, and validated malate dehydrogenase as a key target. These data uncover a fundamental relationship between reactive acyl-CoA species and proteins, and define a new regulatory paradigm in metabolism. äA Class of Reactive Acyl-CoA Species Reveals the Non-Enzymatic Origins(epmc).pdf DeepDyve Pubget Overpricing