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10.1016/j.febslet.2008.07.043 http://scihub22266oqcxt.onion/10.1016/j.febslet.2008.07.043 18675813!?!18675813 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=18675813&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       FEBS+Lett 2008 ; 582 (20): 2993-7 Nephropedia Template TP {{tp|p=18675813|t=2008. The alpha-kinases TRPM6 and TRPM7, but not eEF-2 kinase, phosphorylate the assembly domain of myosin IIA, IIB and IIC |pdf=|usr=}}{{18675813}} gab.com Text The alpha-kinases TRPM6 and TRPM7, but not eEF-2 kinase, phosphorylate the assembly domain of myosin IIA, IIB and IIC JO: FEBS Lett http://www.kidney.de/pget.php?&tw=1&pmid=18675813 #FOAvip TRPM6 and TRPM7 encode channel-kinases. While these channels share electrophysiological properties and cellular functions, TRPM6 and TRPM7 are non-redundant genes raising the possibility that the kinases have distinct substrates. Here, we demonstrate that TRPM6 and TRPM7 phosphorylate the assembly domain of myosin IIA, IIB and IIC on identical residues. Whereas phosphorylation of myosin IIA is restricted to the coiled-coil domain, TRPM6 and TRPM7 also phosphorylate the non-helical tails of myosin IIB and IIC. TRPM7 does not phosphorylate eukaryotic elongation factor-2 (eEF-2) and myosin II is a poor substrate for eEF-2 kinase. In conclusion, TRPM6 and TRPM7 share exogenous substrates among themselves but not with functionally distant alpha-kinases. Twit Text FOAVip The alpha-kinases TRPM6 and TRPM7, but not eEF-2 kinase, phosphorylate the assembly domain of myosin IIA, IIB and IIC ????FEBS Lett http://www.kidney.de/pget.php?&tw=1&pmid=18675813 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=18675813 #FOAvip English Wikipedia <ref>{{Cite pmid|18675813}}</ref> The alpha-kinases TRPM6 and TRPM7, but not eEF-2 kinase, phosphorylate the assembly domain of myosin IIA, IIB and IIC #MMPMID18675813 Clark K; Middelbeek J; Dorovkov MV; Figdor CG; Ryazanov AG; Lasonder E; van Leeuwen FN FEBS Lett 2008[Sep]; 582 (20): 2993-7 PMID18675813show ga TRPM6 and TRPM7 encode channel-kinases. While these channels share electrophysiological properties and cellular functions, TRPM6 and TRPM7 are non-redundant genes raising the possibility that the kinases have distinct substrates. Here, we demonstrate that TRPM6 and TRPM7 phosphorylate the assembly domain of myosin IIA, IIB and IIC on identical residues. Whereas phosphorylation of myosin IIA is restricted to the coiled-coil domain, TRPM6 and TRPM7 also phosphorylate the non-helical tails of myosin IIB and IIC. TRPM7 does not phosphorylate eukaryotic elongation factor-2 (eEF-2) and myosin II is a poor substrate for eEF-2 kinase. In conclusion, TRPM6 and TRPM7 share exogenous substrates among themselves but not with functionally distant alpha-kinases. |Amino Acid Sequence[MESH] |Cell Line[MESH] |Elongation Factor 2 Kinase/genetics/metabolism[MESH] |Humans[MESH] |Molecular Sequence Data[MESH] |Myosin Heavy Chains/*metabolism[MESH] |Myosin Type II/*metabolism[MESH] |Nonmuscle Myosin Type IIA/*metabolism[MESH] |Nonmuscle Myosin Type IIB/*metabolism[MESH] |Phosphorylation[MESH] |Protein Serine-Threonine Kinases[MESH] |Protein Structure, Tertiary[MESH]The alpha-kinases TRPM6 and TRPM7, but not eEF-2 kinase, phosphorylate(epmc).pdf DeepDyve Pubget Overpricing