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.

10.1042/BJ20150325 http://scihub22266oqcxt.onion/10.1042/BJ20150325 C4676407!4676407 !26201515     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 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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26201515 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biochem+J 2015 ; 471 (1 ): 37-51 Nephropedia Template TP {{tp|p=26201515 |t=2015. Akt kinase C-terminal modifications control activation loop dephosphorylation and enhance insulin response |pdf=|usr=}}{{26201515 }} gab.com Text Akt kinase C-terminal modifications control activation loop dephosphorylation and enhance insulin response JO: Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=26201515 #FOAvip The Akt protein kinase, also known as protein kinase B, plays key roles in insulin receptor signalling and regulates cell growth, survival and metabolism. Recently, we described a mechanism to enhance Akt phosphorylation that restricts access of cellular phosphatases to the Akt activation loop (Thr(308) in Akt1 or protein kinase B isoform alpha) in an ATP-dependent manner. In the present paper, we describe a distinct mechanism to control Thr(308) dephosphorylation and thus Akt deactivation that depends on intramolecular interactions of Akt C-terminal sequences with its kinase domain. Modifications of amino acids surrounding the Akt1 C-terminal mTORC2 (mammalian target of rapamycin complex 2) phosphorylation site (Ser(473)) increased phosphatase resistance of the phosphorylated activation loop (pThr(308)) and amplified Akt phosphorylation. Furthermore, the phosphatase-resistant Akt was refractory to ceramide-dependent dephosphorylation and amplified insulin-dependent Thr(308) phosphorylation in a regulated fashion. Collectively, these results suggest that the Akt C-terminal hydrophobic groove is a target for the development of agents that enhance Akt phosphorylation by insulin. Twit Text FOAVip Akt kinase C-terminal modifications control activation loop dephosphorylation and enhance insulin response ????Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=26201515 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26201515 #FOAvip English Wikipedia <ref>{{Cite pmid|26201515 }}</ref> Akt kinase C-terminal modifications control activation loop dephosphorylation and enhance insulin response #MMPMID26201515 Chan TO ; Zhang J ; Tiegs BC ; Blumhof B ; Yan L ; Keny N ; Penny M ; Li X ; Pascal JM ; Armen RS ; Rodeck U ; Penn RB Biochem J 2015[Oct]; 471 (1 ): 37-51 PMID26201515 show ga The Akt protein kinase, also known as protein kinase B, plays key roles in insulin receptor signalling and regulates cell growth, survival and metabolism. Recently, we described a mechanism to enhance Akt phosphorylation that restricts access of cellular phosphatases to the Akt activation loop (Thr(308) in Akt1 or protein kinase B isoform alpha) in an ATP-dependent manner. In the present paper, we describe a distinct mechanism to control Thr(308) dephosphorylation and thus Akt deactivation that depends on intramolecular interactions of Akt C-terminal sequences with its kinase domain. Modifications of amino acids surrounding the Akt1 C-terminal mTORC2 (mammalian target of rapamycin complex 2) phosphorylation site (Ser(473)) increased phosphatase resistance of the phosphorylated activation loop (pThr(308)) and amplified Akt phosphorylation. Furthermore, the phosphatase-resistant Akt was refractory to ceramide-dependent dephosphorylation and amplified insulin-dependent Thr(308) phosphorylation in a regulated fashion. Collectively, these results suggest that the Akt C-terminal hydrophobic groove is a target for the development of agents that enhance Akt phosphorylation by insulin. |Animals [MESH] |Cell Line [MESH] |Enzyme Activation/physiology [MESH] |Insulin/genetics/*metabolism [MESH] |Mechanistic Target of Rapamycin Complex 1 [MESH] |Multiprotein Complexes/genetics/*metabolism [MESH] |Phosphorylation/physiology [MESH] |Protein Processing, Post-Translational/*physiology [MESH] |Proto-Oncogene Proteins c-akt/genetics/*metabolism [MESH] |Rats [MESH] |Signal Transduction/*physiology [MESH]Akt kinase C-terminal modifications control activation loop dephosphor(epmc).pdf DeepDyve Pubget Overpricing