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10.1101/cshperspect.a020644 http://scihub22266oqcxt.onion/10.1101/cshperspect.a020644 C3996475!3996475!24789824     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24789824&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: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\24789824.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cold+Spring+Harb+Perspect+Biol 2014 ; 6 (5): ä Nephropedia Template TP {{tp|p=24789824|t=2014. The Genesis of Tyrosine Phosphorylation |pdf=|usr=}}{{24789824}} gab.com Text The Genesis of Tyrosine Phosphorylation JO: Cold Spring Harb Perspect Biol http://www.kidney.de/pget.php?&tw=1&pmid=24789824 #FOAvip Tyrosine phosphorylation of proteins was discovered in 1979, but this posttranslational modification had been ?invented? by evolution more than a billion years ago in single-celled eukaryotic organisms that were the antecedents of the first multicellular animals. Because sophisticated cell?cell communication is a sine qua non for the existence of multicellular organisms, the development of cell-surface receptor systems that use tyrosine phosphorylation for transmembrane signal transduction and intracellular signaling seems likely to have been a crucial event in the evolution of metazoans. Like all types of protein phosphorylation, tyrosine phosphorylation serves to regulate proteins in multiple ways, including causing electrostatic repulsion and inducing allosteric transitions, but the most important function of phosphotyrosine (P.Tyr) is to serve as a docking site that promotes a specific interaction between a tyrosine phosphorylated protein and another protein that contains a P.Tyr-binding domain, such as an SH2 or PTB domain. Such docking interactions are essential for signal transduction downstream from receptor tyrosine kinases (RTKs) on the cell surface, which are activated on binding a cognate extracellular ligand, and, as a consequence, elicit specific cellular outcomes. Twit Text FOAVip The Genesis of Tyrosine Phosphorylation ????Cold Spring Harb Perspect Biol http://www.kidney.de/pget.php?&tw=1&pmid=24789824 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24789824 #FOAvip English Wikipedia <ref>{{Cite pmid|24789824}}</ref> The Genesis of Tyrosine Phosphorylation #MMPMID24789824 Hunter T Cold Spring Harb Perspect Biol 2014[May]; 6 (5): ä PMID24789824show ga Tyrosine phosphorylation of proteins was discovered in 1979, but this posttranslational modification had been ?invented? by evolution more than a billion years ago in single-celled eukaryotic organisms that were the antecedents of the first multicellular animals. Because sophisticated cell?cell communication is a sine qua non for the existence of multicellular organisms, the development of cell-surface receptor systems that use tyrosine phosphorylation for transmembrane signal transduction and intracellular signaling seems likely to have been a crucial event in the evolution of metazoans. Like all types of protein phosphorylation, tyrosine phosphorylation serves to regulate proteins in multiple ways, including causing electrostatic repulsion and inducing allosteric transitions, but the most important function of phosphotyrosine (P.Tyr) is to serve as a docking site that promotes a specific interaction between a tyrosine phosphorylated protein and another protein that contains a P.Tyr-binding domain, such as an SH2 or PTB domain. Such docking interactions are essential for signal transduction downstream from receptor tyrosine kinases (RTKs) on the cell surface, which are activated on binding a cognate extracellular ligand, and, as a consequence, elicit specific cellular outcomes. äThe Genesis of Tyrosine Phosphorylation (epmc).pdf DeepDyve Pubget Overpricing