FIH permits NAA10 to catalyze the oxygen-dependent lysyl-acetylation of HIF-1α

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FIH permits NAA10 to catalyze the oxygen-dependent lysyl-acetylation of HIF-1α

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наукова стаття, опублікована в жовтні 2018

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FIH permits NAA10 to catalyze the oxygen-dependent lysyl-acetylation of HIF-1α

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FIH permits NAA10 to catalyze the oxygen-dependent lysyl-acetylation of HIF-1α

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FIH permits NAA10 to catalyze the oxygen-dependent lysyl-acetylation of HIF-1α

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FIH permits NAA10 to catalyze the oxygen-dependent lysyl-acetylation of HIF-1α

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FIH permits NAA10 to catalyze the oxygen-dependent lysyl-acetylation of HIF-1α

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FIH permits NAA10 to catalyze the oxygen-dependent lysyl-acetylation of HIF-1α

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P1476

FIH permits NAA10 to catalyze the oxygen-dependent lysyl-acetylation of HIF-1α

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P2093

Jengmin Kang

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Jong-Wan Park

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June Huh

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Yang-Sook Chun

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P2860

FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor

Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)

Human Naa50p (Nat5/San) displays both protein N alpha- and N epsilon-acetyltransferase activity

Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways

Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factor

Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase

Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains

Lysine acetylation targets protein complexes and co-regulates major cellular functions

Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation

Substrate-Trapped Interactors of PHD3 and FIH Cluster in Distinct Signaling Pathways

P304

364-374

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P31

scholarly article

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10.1016/J.REDOX.2018.09.002

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English

P478

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P577

2018-10-01T00:00:00Z

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30237125

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P932

6142190

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