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10.1038/ncomms12673 http://scihub22266oqcxt.onion/10.1038/ncomms12673 C5007464!5007464!27561929     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2016 ; 7 (ä): ä Nephropedia Template TP {{tp|p=27561929|t=2016. Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases |pdf=|usr=}}{{27561929}} gab.com Text Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=27561929 #FOAvip The response to hypoxia in animals involves the expression of multiple genes regulated by the ??-hypoxia-inducible transcription factors (HIFs). The hypoxia-sensing mechanism involves oxygen limited hydroxylation of prolyl residues in the N- and C-terminal oxygen-dependent degradation domains (NODD and CODD) of HIF? isoforms, as catalysed by prolyl hydroxylases (PHD 1?3). Prolyl hydroxylation promotes binding of HIF? to the von Hippel?Lindau protein (VHL)?elongin B/C complex, thus signalling for proteosomal degradation of HIF?. We reveal that certain PHD2 variants linked to familial erythrocytosis and cancer are highly selective for CODD or NODD. Crystalline and solution state studies coupled to kinetic and cellular analyses reveal how wild-type and variant PHDs achieve ODD selectivity via different dynamic interactions involving loop and C-terminal regions. The results inform on how HIF target gene selectivity is achieved and will be of use in developing selective PHD inhibitors. Twit Text FOAVip Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=27561929 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27561929 #FOAvip English Wikipedia <ref>{{Cite pmid|27561929}}</ref> Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases #MMPMID27561929 Chowdhury R; Leung IKH; Tian YM; Abboud MI; Ge W; Domene C; Cantrelle FX; Landrieu I; Hardy AP; Pugh CW; Ratcliffe PJ; Claridge TDW; Schofield CJ Nat Commun 2016[]; 7 (ä): ä PMID27561929show ga The response to hypoxia in animals involves the expression of multiple genes regulated by the ??-hypoxia-inducible transcription factors (HIFs). The hypoxia-sensing mechanism involves oxygen limited hydroxylation of prolyl residues in the N- and C-terminal oxygen-dependent degradation domains (NODD and CODD) of HIF? isoforms, as catalysed by prolyl hydroxylases (PHD 1?3). Prolyl hydroxylation promotes binding of HIF? to the von Hippel?Lindau protein (VHL)?elongin B/C complex, thus signalling for proteosomal degradation of HIF?. We reveal that certain PHD2 variants linked to familial erythrocytosis and cancer are highly selective for CODD or NODD. Crystalline and solution state studies coupled to kinetic and cellular analyses reveal how wild-type and variant PHDs achieve ODD selectivity via different dynamic interactions involving loop and C-terminal regions. The results inform on how HIF target gene selectivity is achieved and will be of use in developing selective PHD inhibitors. äStructural basis for oxygen degradation domain selectivity of the HIF (epmc).pdf DeepDyve Pubget Overpricing