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10.1016/j.freeradbiomed.2014.11.013 http://scihub22266oqcxt.onion/10.1016/j.freeradbiomed.2014.11.013 C4355186!4355186!25433365     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Free+Radic+Biol+Med 2015 ; ä (ä): 148-57 Nephropedia Template TP {{tp|p=25433365|t=2015. The Basics of Thiols and Cysteines in Redox Biology and Chemistry |pdf=|usr=}}{{25433365}} gab.com Text The Basics of Thiols and Cysteines in Redox Biology and Chemistry JO: Free Radic Biol Med http://www.kidney.de/pget.php?&tw=1&pmid=25433365 #FOAvip Cysteine is one of the least abundant amino acids, yet it is frequently found as a highly conserved residue within functional (regulatory, catalytic or binding) sites in proteins. It is the unique chemistry of the thiol or thiolate group of cysteine that imparts functional sites with their specialized properties (e.g., nucleophilicity, high affinity metal binding, and/or ability to form disulfide bonds). Highlighted in this review are some of the basic biophysical and biochemical properties of cysteine groups and the equations that apply to them, particularly with respect to pKa and redox potential. Also summarized are the types of low molecular weight thiols present in high concentrations in most cells, as well as the ways in which modifications of cysteinyl residues can impart or regulate molecular functions important to cellular processes including signal transduction. Twit Text FOAVip The Basics of Thiols and Cysteines in Redox Biology and Chemistry ????Free Radic Biol Med http://www.kidney.de/pget.php?&tw=1&pmid=25433365 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25433365 #FOAvip English Wikipedia <ref>{{Cite pmid|25433365}}</ref> The Basics of Thiols and Cysteines in Redox Biology and Chemistry #MMPMID25433365 Poole LB Free Radic Biol Med 2015[Mar]; ä (ä): 148-57 PMID25433365show ga Cysteine is one of the least abundant amino acids, yet it is frequently found as a highly conserved residue within functional (regulatory, catalytic or binding) sites in proteins. It is the unique chemistry of the thiol or thiolate group of cysteine that imparts functional sites with their specialized properties (e.g., nucleophilicity, high affinity metal binding, and/or ability to form disulfide bonds). Highlighted in this review are some of the basic biophysical and biochemical properties of cysteine groups and the equations that apply to them, particularly with respect to pKa and redox potential. Also summarized are the types of low molecular weight thiols present in high concentrations in most cells, as well as the ways in which modifications of cysteinyl residues can impart or regulate molecular functions important to cellular processes including signal transduction. äThe Basics of Thiols and Cysteines in Redox Biology and Chemistry (epmc).pdf DeepDyve Pubget Overpricing