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10.1016/j.trecan.2017.12.005 http://scihub22266oqcxt.onion/10.1016/j.trecan.2017.12.005 C5884165!5884165!29458964     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       Trends+Cancer 2018 ; 4 (2): 151-65 Nephropedia Template TP {{tp|p=29458964|t=2018. Metabolism, Activity, and Targeting of D-and L-2-Hydroxyglutarates |pdf=|usr=}}{{29458964}} gab.com Text Metabolism, Activity, and Targeting of D-and L-2-Hydroxyglutarates JO: Trends Cancer http://www.kidney.de/pget.php?&tw=1&pmid=29458964 #FOAvip Isocitrate dehydrogenases (IDH1/2) are frequently mutated in multiple types of human cancer, resulting in neomorphic enzymes that convert ?-ketoglutarate (?-KG) to 2-hydroxyglutarate (2-HG). The current view on the mechanism of IDH mutation holds that 2-HG acts as an antagonist of ?-KG to competitively inhibit the activity of ?-KG-dependent dioxygenases, including those involved in histone and DNA demethylation. Recent studies have implicated 2-HG in activities beyond epigenetic modification. Multiple enzymes have been discovered that lack mutations but that can nevertheless produce 2-HG promiscuously under hypoxic or acidic conditions. Therapies are being developed to treat IDH-mutant cancers by targeting either the mutant IDH enzymes directly or the pathways sensitized by 2-HG. Twit Text FOAVip Metabolism, Activity, and Targeting of D-and L-2-Hydroxyglutarates ????Trends Cancer http://www.kidney.de/pget.php?&tw=1&pmid=29458964 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29458964 #FOAvip English Wikipedia <ref>{{Cite pmid|29458964}}</ref> Metabolism, Activity, and Targeting of D-and L-2-Hydroxyglutarates #MMPMID29458964 Ye D; Guan KL; Xiong Y Trends Cancer 2018[Feb]; 4 (2): 151-65 PMID29458964show ga Isocitrate dehydrogenases (IDH1/2) are frequently mutated in multiple types of human cancer, resulting in neomorphic enzymes that convert ?-ketoglutarate (?-KG) to 2-hydroxyglutarate (2-HG). The current view on the mechanism of IDH mutation holds that 2-HG acts as an antagonist of ?-KG to competitively inhibit the activity of ?-KG-dependent dioxygenases, including those involved in histone and DNA demethylation. Recent studies have implicated 2-HG in activities beyond epigenetic modification. Multiple enzymes have been discovered that lack mutations but that can nevertheless produce 2-HG promiscuously under hypoxic or acidic conditions. Therapies are being developed to treat IDH-mutant cancers by targeting either the mutant IDH enzymes directly or the pathways sensitized by 2-HG. äMetabolism, Activity, and Targeting of D-and L-2-Hydroxyglutarates (epmc).pdf DeepDyve Pubget Overpricing