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http://scihub22266oqcxt.onion/ 19137675!?!19137675 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=19137675&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 Warning: Undefined variable $yww in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 538 Warning: Undefined variable $yww in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 538       Biofizika 2008 ; 53 (6): 943-9 Nephropedia Template TP {{tp|p=19137675|t=2008. Effect of mutations imitating the phosphorylation by TRPM7 kinase on the function of the N-terminal domain of tropomodulin |pdf=|usr=}}{{19137675}} gab.com Text Effect of mutations imitating the phosphorylation by TRPM7 kinase on the function of the N-terminal domain of tropomodulin JO: Biofizika http://www.kidney.de/pget.php?&tw=1&pmid=19137675 #FOAvip It has been shown that tropomodulin 1 is phosphorylated at serine and threonine residues by TRPM7 kinase. The phosphorylation sites for TRPM7 kinase in the N-terminal functional domain of tropomodulin 1 have been identified, which include tropomyosin-binding and actin-capping regions. It has been found that the phosphorylation-mimicking mutation T54E resulted in the loss of the capping ability of the N-terminal tropomodulin domain; however, its tropomyosin-binding ability did not change. We further hypothesize that the phosphorylation of tropomodulin by TRPM7 kinase may play a role in the regulation of the dynamics of actin filaments. Twit Text FOAVip Effect of mutations imitating the phosphorylation by TRPM7 kinase on the function of the N-terminal domain of tropomodulin ????Biofizika http://www.kidney.de/pget.php?&tw=1&pmid=19137675 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=19137675 #FOAvip English Wikipedia <ref>{{Cite pmid|19137675}}</ref> Effect of mutations imitating the phosphorylation by TRPM7 kinase on the function of the N-terminal domain of tropomodulin #MMPMID19137675 Dorovkov MV; Beznosov SN; Shah S; Kotlianskaia L; Kostiukova AS Biofizika 2008[Nov]; 53 (6): 943-9 PMID19137675show ga It has been shown that tropomodulin 1 is phosphorylated at serine and threonine residues by TRPM7 kinase. The phosphorylation sites for TRPM7 kinase in the N-terminal functional domain of tropomodulin 1 have been identified, which include tropomyosin-binding and actin-capping regions. It has been found that the phosphorylation-mimicking mutation T54E resulted in the loss of the capping ability of the N-terminal tropomodulin domain; however, its tropomyosin-binding ability did not change. We further hypothesize that the phosphorylation of tropomodulin by TRPM7 kinase may play a role in the regulation of the dynamics of actin filaments. |Actins/chemistry[MESH] |Amino Acid Sequence[MESH] |Molecular Sequence Data[MESH] |Mutation[MESH] |Phosphorylation[MESH] |Protein Isoforms/chemistry[MESH] |Protein Kinases/*chemistry/genetics[MESH] |Transient Receptor Potential Channels/*chemistry/genetics[MESH] Effect of mutations imitating the phosphorylation by TRPM7 kinase on (epmc).pdf DeepDyve Pubget Overpricing