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10.1073/pnas.1504376112 http://scihub22266oqcxt.onion/10.1073/pnas.1504376112 C4491776!4491776!26080424     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       Proc+Natl+Acad+Sci+U+S+A 2015 ; 112 (26): 7960-5 Nephropedia Template TP {{tp|p=26080424|t=2015. A universal entropy-driven mechanism for thioredoxin?target recognition |pdf=|usr=}}{{26080424}} gab.com Text A universal entropy-driven mechanism for thioredoxin target recognition JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=26080424 #FOAvip Thioredoxin (Trx) is universally conserved thiol-oxidoreductase that regulates numerous cellular pathways under thiol-based redox control, and its activity is often upregulated in malignant cancer cells. Despite its central importance, the mechanism by which Trx recognizes its target proteins remains unknown. Herein, we address this longstanding question by investigating the noncovalent forces involved in Trx?target interactions. Using a combination of biochemical and quantitative biophysical methods, we identify favorable entropy as the major force in molecular recognition that drives target specificity. These findings, and others reported herein, afford considerable new insight into Trx?target recognition, which is critical to understanding its function in normal metabolism and represents a fundamental step toward the development of new pharmacological strategies to address redox-related disorders. Twit Text FOAVip A universal entropy-driven mechanism for thioredoxin target recognition ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=26080424 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26080424 #FOAvip English Wikipedia <ref>{{Cite pmid|26080424}}</ref> A universal entropy-driven mechanism for thioredoxin?target recognition #MMPMID26080424 Palde PB; Carroll KS Proc Natl Acad Sci U S A 2015[Jun]; 112 (26): 7960-5 PMID26080424show ga Thioredoxin (Trx) is universally conserved thiol-oxidoreductase that regulates numerous cellular pathways under thiol-based redox control, and its activity is often upregulated in malignant cancer cells. Despite its central importance, the mechanism by which Trx recognizes its target proteins remains unknown. Herein, we address this longstanding question by investigating the noncovalent forces involved in Trx?target interactions. Using a combination of biochemical and quantitative biophysical methods, we identify favorable entropy as the major force in molecular recognition that drives target specificity. These findings, and others reported herein, afford considerable new insight into Trx?target recognition, which is critical to understanding its function in normal metabolism and represents a fundamental step toward the development of new pharmacological strategies to address redox-related disorders. äA universal entropy-driven mechanism for thioredoxin?target recognitio(epmc).pdf DeepDyve Pubget Overpricing