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10.1016/j.freeradbiomed.2015.05.034 http://scihub22266oqcxt.onion/10.1016/j.freeradbiomed.2015.05.034 C4668279!4668279!26057936     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26057936.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Free+Radic+Biol+Med 2015 ; 88 (Pt B): 101-7 Nephropedia Template TP {{tp|p=26057936|t=2015. Structural basis of Keap1 interactions with Nrf2 |pdf=|usr=}}{{26057936}} gab.com Text Structural basis of Keap1 interactions with Nrf2 JO: Free Radic Biol Med http://www.kidney.de/pget.php?&tw=1&pmid=26057936 #FOAvip Keap1 is a highly redox-sensitive member of the BTB-Kelch family that assembles with the Cul3 protein to form a Cullin?RING E3 ligase complex for the degradation of Nrf2. Oxidative stress disables Keap1, allowing Nrf2 protein levels to accumulate for the transactivation of critical stress response genes. Consequently, the Keap1?Nrf2 system is extensively pursued for the development of protein?protein interaction inhibitors that will stabilize Nrf2 for therapeutic effect in conditions of neurodegeneration, inflammation, and cancer. Here we review current progress toward the structure determination of Keap1 and its protein complexes with Cul3, Nrf2 substrate, and small-molecule antagonists. Together the available structures establish a rational three-dimensional model to explain the two-site binding of Nrf2 as well as its efficient ubiquitination. Twit Text FOAVip Structural basis of Keap1 interactions with Nrf2 ????Free Radic Biol Med http://www.kidney.de/pget.php?&tw=1&pmid=26057936 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26057936 #FOAvip English Wikipedia <ref>{{Cite pmid|26057936}}</ref> Structural basis of Keap1 interactions with Nrf2 #MMPMID26057936 Canning P; Sorrell FJ; Bullock AN Free Radic Biol Med 2015[Nov]; 88 (Pt B): 101-7 PMID26057936show ga Keap1 is a highly redox-sensitive member of the BTB-Kelch family that assembles with the Cul3 protein to form a Cullin?RING E3 ligase complex for the degradation of Nrf2. Oxidative stress disables Keap1, allowing Nrf2 protein levels to accumulate for the transactivation of critical stress response genes. Consequently, the Keap1?Nrf2 system is extensively pursued for the development of protein?protein interaction inhibitors that will stabilize Nrf2 for therapeutic effect in conditions of neurodegeneration, inflammation, and cancer. Here we review current progress toward the structure determination of Keap1 and its protein complexes with Cul3, Nrf2 substrate, and small-molecule antagonists. Together the available structures establish a rational three-dimensional model to explain the two-site binding of Nrf2 as well as its efficient ubiquitination. �Structural basis of Keap1 interactions with Nrf2 (epmc).pdf DeepDyve Pubget Overpricing