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.1420389111 http://scihub22266oqcxt.onion/10.1073/pnas.1420389111 C4260582!4260582!25404345     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 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 (48): 17116-21 Nephropedia Template TP {{tp|p=25404345|t=2014. Combinatorial regulation of a signal-dependent activator by phosphorylation and acetylation |pdf=|usr=}}{{25404345}} gab.com Text Combinatorial regulation of a signal-dependent activator by phosphorylation and acetylation JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25404345 #FOAvip Catecholamines regulate adipocyte function in part by CREB activation. Obesity displays enhanced cyclic AMP response element binding protein (CREB) activity despite reduced catecholamine signals. We report that obesity promotes CREB binding protein (CBP)-mediated CREB acetylation at Lys136 in the adipose tissue by means of reduced SirT1 levels. CREB Lys136 acetylation promotes binding with the bromodomain (BRD) of CBP, which can also bind phosphorylated Ser133, through its KIX domain, upon hormonal signals. This double recognition is reflected in potentiated CBP recruitment at promoters when CREB is doubly modified. Structural data show the formation of a ternary complex between CBP BRD and KIX domains when bound to phospho-Ser133 and acetylated-Lys136 CREB. Disruption of the BRD:CREB interaction with a small molecule reduced the enhanced CREB activity associated with acetylation. Twit Text FOAVip Combinatorial regulation of a signal-dependent activator by phosphorylation and acetylation ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25404345 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25404345 #FOAvip English Wikipedia <ref>{{Cite pmid|25404345}}</ref> Combinatorial regulation of a signal-dependent activator by phosphorylation and acetylation #MMPMID25404345 Paz JC; Park S; Phillips N; Matsumura S; Tsai WW; Kasper L; Brindle PK; Zhang G; Zhou MM; Wright PE; Montminy M Proc Natl Acad Sci U S A 2014[Dec]; 111 (48): 17116-21 PMID25404345show ga Catecholamines regulate adipocyte function in part by CREB activation. Obesity displays enhanced cyclic AMP response element binding protein (CREB) activity despite reduced catecholamine signals. We report that obesity promotes CREB binding protein (CBP)-mediated CREB acetylation at Lys136 in the adipose tissue by means of reduced SirT1 levels. CREB Lys136 acetylation promotes binding with the bromodomain (BRD) of CBP, which can also bind phosphorylated Ser133, through its KIX domain, upon hormonal signals. This double recognition is reflected in potentiated CBP recruitment at promoters when CREB is doubly modified. Structural data show the formation of a ternary complex between CBP BRD and KIX domains when bound to phospho-Ser133 and acetylated-Lys136 CREB. Disruption of the BRD:CREB interaction with a small molecule reduced the enhanced CREB activity associated with acetylation. äCombinatorial regulation of a signal-dependent activator by phosphoryl(epmc).pdf DeepDyve Pubget Overpricing