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10.1016/j.freeradbiomed.2014.07.037 http://scihub22266oqcxt.onion/10.1016/j.freeradbiomed.2014.07.037 C4312752!4312752!25091901     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Free+Radic+Biol+Med 2015 ; ä (ä): 171-82 Nephropedia Template TP {{tp|p=25091901|t=2015. Oxidative Protein Folding: from Thiol-disulfide Exchange Reactions to the Redox Poise of the Endoplasmic Reticulum |pdf=|usr=}}{{25091901}} gab.com Text Oxidative Protein Folding: from Thiol-disulfide Exchange Reactions to the Redox Poise of the Endoplasmic Reticulum JO: Free Radic Biol Med http://www.kidney.de/pget.php?&tw=1&pmid=25091901 #FOAvip This review examines oxidative protein folding within the mammalian endoplasmic reticulum (ER) from an enzymological perspective. In protein disulfide isomerase-first (PDI-first) pathways of oxidative protein folding, PDI is the immediate oxidant of reduced client proteins and then addresses disulfide mispairings in a second isomerization phase. In PDI-second pathways the initial oxidation is PDI-independent. Evidence for the rapid reduction of PDI by reduced glutathione is presented in the context of PDI-first pathways. Strategies and challenges are discussed for determination of the concentrations of reduced and oxidized glutathione and of the ratios of PDIred:PDIox. The preponderance of evidence suggests that the mammalian ER is more reducing than first envisaged. The average redox state of major PDI-family members is found to be largely to almost totally reduced. These observations are consistent with model studies showing that oxidative protein folding proceeds most efficiently at a reducing redox poise consistent with a stoichiometric insertion of disulfides into client proteins. Following a discussion of the use of natively-encoded fluorescent probes to report the glutathione redox poise of the ER, this review concludes with elaboration of a complementary strategy to discontinuously survey the redox state of as many redox-active disulfides that can be identified by ratiometric LC-MS-MS methods. Consortia of oxidoreductases which are in redox equilibrium can then be identified and compared to the glutathione redox poise of the ER to gain a more detailed understanding of the factors that influence oxidative protein folding within the secretory compartment. Twit Text FOAVip Oxidative Protein Folding: from Thiol-disulfide Exchange Reactions to the Redox Poise of the Endoplasmic Reticulum ????Free Radic Biol Med http://www.kidney.de/pget.php?&tw=1&pmid=25091901 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25091901 #FOAvip English Wikipedia <ref>{{Cite pmid|25091901}}</ref> Oxidative Protein Folding: from Thiol-disulfide Exchange Reactions to the Redox Poise of the Endoplasmic Reticulum #MMPMID25091901 Hudson DA; Gannon SA; Thorpe C Free Radic Biol Med 2015[Mar]; ä (ä): 171-82 PMID25091901show ga This review examines oxidative protein folding within the mammalian endoplasmic reticulum (ER) from an enzymological perspective. In protein disulfide isomerase-first (PDI-first) pathways of oxidative protein folding, PDI is the immediate oxidant of reduced client proteins and then addresses disulfide mispairings in a second isomerization phase. In PDI-second pathways the initial oxidation is PDI-independent. Evidence for the rapid reduction of PDI by reduced glutathione is presented in the context of PDI-first pathways. Strategies and challenges are discussed for determination of the concentrations of reduced and oxidized glutathione and of the ratios of PDIred:PDIox. The preponderance of evidence suggests that the mammalian ER is more reducing than first envisaged. The average redox state of major PDI-family members is found to be largely to almost totally reduced. These observations are consistent with model studies showing that oxidative protein folding proceeds most efficiently at a reducing redox poise consistent with a stoichiometric insertion of disulfides into client proteins. Following a discussion of the use of natively-encoded fluorescent probes to report the glutathione redox poise of the ER, this review concludes with elaboration of a complementary strategy to discontinuously survey the redox state of as many redox-active disulfides that can be identified by ratiometric LC-MS-MS methods. Consortia of oxidoreductases which are in redox equilibrium can then be identified and compared to the glutathione redox poise of the ER to gain a more detailed understanding of the factors that influence oxidative protein folding within the secretory compartment. äOxidative Protein Folding: from Thiol-disulfide Exchange Reactions to (epmc).pdf DeepDyve Pubget Overpricing