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10.3389/fcell.2016.00011 http://scihub22266oqcxt.onion/10.3389/fcell.2016.00011 C4763087!4763087!26942179     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Front+Cell+Dev+Biol 2016 ; 4 (ä): ä Nephropedia Template TP {{tp|p=26942179|t=2016. Hypoxia-Inducible Factors (HIFs) and Phosphorylation: Impact on Stability, Localization, and Transactivity |pdf=|usr=}}{{26942179}} gab.com Text Hypoxia-Inducible Factors (HIFs) and Phosphorylation: Impact on Stability, Localization, and Transactivity JO: Front Cell Dev Biol http://www.kidney.de/pget.php?&tw=1&pmid=26942179 #FOAvip The hypoxia-inducible factor ?-subunits (HIF?) are key transcription factors in the mammalian response to oxygen deficiency. The HIF? regulation in response to hypoxia occurs primarily on the level of protein stability due to posttranslational hydroxylation and proteasomal degradation. However, HIF ?-subunits also respond to various growth factors, hormones, or cytokines under normoxia indicating involvement of different kinase pathways in their regulation. Because these proteins participate in angiogenesis, glycolysis, programmed cell death, cancer, and ischemia, HIF? regulating kinases are attractive therapeutic targets. Although numerous kinases were reported to regulate HIF? indirectly, direct phosphorylation of HIF? affects HIF? stability, nuclear localization, and transactivity. Herein, we review the role of phosphorylation-dependent HIF? regulation with emphasis on protein stability, subcellular localization, and transactivation. Twit Text FOAVip Hypoxia-Inducible Factors (HIFs) and Phosphorylation: Impact on Stability, Localization, and Transactivity ????Front Cell Dev Biol http://www.kidney.de/pget.php?&tw=1&pmid=26942179 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26942179 #FOAvip English Wikipedia <ref>{{Cite pmid|26942179}}</ref> Hypoxia-Inducible Factors (HIFs) and Phosphorylation: Impact on Stability, Localization, and Transactivity #MMPMID26942179 Kietzmann T; Mennerich D; Dimova EY Front Cell Dev Biol 2016[]; 4 (ä): ä PMID26942179show ga The hypoxia-inducible factor ?-subunits (HIF?) are key transcription factors in the mammalian response to oxygen deficiency. The HIF? regulation in response to hypoxia occurs primarily on the level of protein stability due to posttranslational hydroxylation and proteasomal degradation. However, HIF ?-subunits also respond to various growth factors, hormones, or cytokines under normoxia indicating involvement of different kinase pathways in their regulation. Because these proteins participate in angiogenesis, glycolysis, programmed cell death, cancer, and ischemia, HIF? regulating kinases are attractive therapeutic targets. Although numerous kinases were reported to regulate HIF? indirectly, direct phosphorylation of HIF? affects HIF? stability, nuclear localization, and transactivity. Herein, we review the role of phosphorylation-dependent HIF? regulation with emphasis on protein stability, subcellular localization, and transactivation. äHypoxia-Inducible Factors (HIFs) and Phosphorylation: Impact on Stabil(epmc).pdf DeepDyve Pubget Overpricing