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10.1146/annurev-biophys-050511-102349 http://scihub22266oqcxt.onion/10.1146/annurev-biophys-050511-102349 C4041481!4041481 !23451893     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 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\23451893 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Annu+Rev+Biophys 2013 ; 42 (ä): 289-314 Nephropedia Template TP {{tp|p=23451893 |t=2013. Considering protonation as a posttranslational modification regulating protein structure and function |pdf=|usr=}}{{23451893 }} gab.com Text Considering protonation as a posttranslational modification regulating protein structure and function JO: Annu Rev Biophys http://www.kidney.de/pget.php?&tw=1&pmid=23451893 #FOAvip Posttranslational modification is an evolutionarily conserved mechanism for regulating protein activity, binding affinity, and stability. Compared with established posttranslational modifications such as phosphorylation or ubiquitination, posttranslational modification by protons within physiological pH ranges is a less recognized mechanism for regulating protein function. By changing the charge of amino acid side chains, posttranslational modification by protons can drive dynamic changes in protein conformation and function. Addition and removal of a proton is rapid and reversible and, in contrast to most other posttranslational modifications, does not require an enzyme. Signaling specificity is achieved by only a minority of sites in proteins titrating within the physiological pH range. Here, we examine the structural mechanisms and functional consequences of proton posttranslational modification of pH-sensing proteins regulating different cellular processes. Twit Text FOAVip Considering protonation as a posttranslational modification regulating protein structure and function ????Annu Rev Biophys http://www.kidney.de/pget.php?&tw=1&pmid=23451893 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23451893 #FOAvip English Wikipedia <ref>{{Cite pmid|23451893 }}</ref> Considering protonation as a posttranslational modification regulating protein structure and function #MMPMID23451893 Schönichen A ; Webb BA ; Jacobson MP ; Barber DL Annu Rev Biophys 2013[]; 42 (ä): 289-314 PMID23451893 show ga Posttranslational modification is an evolutionarily conserved mechanism for regulating protein activity, binding affinity, and stability. Compared with established posttranslational modifications such as phosphorylation or ubiquitination, posttranslational modification by protons within physiological pH ranges is a less recognized mechanism for regulating protein function. By changing the charge of amino acid side chains, posttranslational modification by protons can drive dynamic changes in protein conformation and function. Addition and removal of a proton is rapid and reversible and, in contrast to most other posttranslational modifications, does not require an enzyme. Signaling specificity is achieved by only a minority of sites in proteins titrating within the physiological pH range. Here, we examine the structural mechanisms and functional consequences of proton posttranslational modification of pH-sensing proteins regulating different cellular processes. |*Protein Processing, Post-Translational [MESH] |*Protons [MESH] |Animals [MESH] |Disease/genetics [MESH] |Eukaryotic Cells/metabolism [MESH] |Humans [MESH] |Hydrogen-Ion Concentration [MESH] |Prokaryotic Cells/metabolism [MESH]Considering protonation as a posttranslational modification regulating(epmc).pdf DeepDyve Pubget Overpricing