about
FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factorSubstrate requirements of the oxygen-sensing asparaginyl hydroxylase factor-inhibiting hypoxia-inducible factorInteraction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathwaysHuman variants in the neuronal basic helix-loop-helix/Per-Arnt-Sim (bHLH/PAS) transcription factor complex NPAS4/ARNT2 disrupt functionFIH Regulates Cellular Metabolism through Hydroxylation of the Deubiquitinase OTUB1Defining the role for XAP2 in stabilization of the dioxin receptorAsparagine hydroxylation of the HIF transactivation domain a hypoxic switchConsequences of IkappaB alpha hydroxylation by the factor inhibiting HIF (FIH)The transcription factor encyclopediaOxygen-dependent asparagine hydroxylation.Hypoxia-inducible factor-2 is a novel regulator of aberrant CXCL12 expression in multiple myeloma plasma cells.The asparaginyl hydroxylase factor inhibiting HIF-1alpha is an essential regulator of metabolismHypoxic induction of the regulator of G-protein signalling 4 gene is mediated by the hypoxia-inducible factor pathway.Oxygen-dependent regulation of hypoxia-inducible factors by prolyl and asparaginyl hydroxylation.The hypoxia-inducible factors: key transcriptional regulators of hypoxic responses.Oxygen-dependent hydroxylation by FIH regulates the TRPV3 ion channel.Factor inhibiting HIF (FIH) recognizes distinct molecular features within hypoxia-inducible factor-α (HIF-α) versus ankyrin repeat substratesAnkyrin Repeat Proteins of Orf Virus Influence the Cellular Hypoxia Response PathwayHIF signalling: The eyes have it.Modulation of TRP Channel Activity by Hydroxylation and Its Therapeutic Potential.Reciprocal regulation of the basic helix-loop-helix/Per-Arnt-Sim partner proteins, Arnt and Arnt2, during neuronal differentiationRare variants in single-minded 1 (SIM1) are associated with severe obesity.Loss-of-function mutations in SIM1 contribute to obesity and Prader-Willi-like featuresTurn me on: regulating HIF transcriptional activity.From polyps to people: a highly familiar response to hypoxia.The emerging role of hypoxia, HIF-1 and HIF-2 in multiple myeloma.bHLH-PAS proteins in cancer.Cancer-like metabolism of the mammalian retina.Activity of hypoxia-inducible factor 2alpha is regulated by association with the NF-kappaB essential modulator.M-Type Pyruvate Kinase Isoforms and Lactate Dehydrogenase A in the Mammalian Retina: Metabolic Implications.Mammalian two-hybrid assay showing redox control of HIF-like factor.Characterization of human variants in obesity-related SIM1 protein identifies a hot-spot for dimerization with the partner protein ARNT2.Differences in hydroxylation and binding of Notch and HIF-1alpha demonstrate substrate selectivity for factor inhibiting HIF-1 (FIH-1).Characterization of ankyrin repeat-containing proteins as substrates of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible transcription factor.Oxygen-regulated gene expression in murine cumulus cells.Hormonally regulated follicle differentiation and luteinization in the mouse is associated with hypoxia inducible factor activity.MAGED1 is a novel regulator of a select subset of bHLH PAS transcription factors.Potential adverse effects to the retina of cancer therapy targeting pyruvate kinase M2.The conservation and functionality of the oxygen-sensing enzyme Factor Inhibiting HIF (FIH) in non-vertebratesA comparative study of covalently-bound fatty acids in keratinized tissues
P50
Q24300161-D7DD08E8-134F-4C11-BDDE-5719CA4B5A2BQ24305504-C62AF4B6-72D6-410D-AE2F-A73448FEAE18Q24317627-2BB43D23-5A88-4526-9F3F-23112B14B149Q28115497-8D90CEB4-46E4-4786-ADE5-3F1504F775F7Q28117562-2694C64D-01FB-4D03-A92D-C2CEC23F4EB0Q28184153-5FC473AB-EF43-4A76-93F6-E69DE8699CABQ28217194-6630A4D2-6728-41D3-9C7D-C09E92FC3807Q28590108-0501A361-8669-4FAA-B8A5-32115EEC47A3Q28727892-00890FF8-31F6-4F29-8A51-231A46965FCAQ33200919-D40371FA-C4A3-4ABB-906B-78D9D1F280DCQ33829094-08831948-F557-4933-A3F4-FC191C2003B6Q33945163-C00D2F75-13CE-47E5-AF10-7DF164F52E5EQ34412532-9B18A629-218F-4233-ACE2-CE997A3C9D68Q35072131-C768DB92-7BCF-4EBE-8DB3-2C420B7FC127Q35207434-23F224D4-AFA0-4F52-B180-EFC74DFDCE40Q35440816-82184CCE-FA9D-44C4-8A27-6E315AEFB0D6Q35841949-0960C9D5-E309-46E4-9CB4-22BFEC4B93A7Q36177999-6912291C-F258-4891-ACE6-E25D49E77F1AQ36313671-4DFE1BD2-64DA-468E-9807-7A2A727192F4Q36323671-284B9B72-310A-4B97-A108-CB05FC82B4FDQ36909723-4099905F-C727-443F-9C9F-F25DA021BCCAQ36966937-D0E1DAF1-E59C-42D4-B232-DA0505902FACQ36966943-8882566C-F4DD-4B89-A29D-E80E5F8CF577Q37059658-DB9D070E-D823-4185-8833-41F99FBE067BQ37618836-A708F00D-6EDA-4ED7-BE97-D138C06619A4Q37884379-44BF047E-1E67-4452-BFBE-33FF4B22C816Q38164994-5D599D41-B60D-44BC-9989-451537083588Q38261422-03EFA94F-03AB-4B4A-843B-56617F9C0B86Q38331952-D6893470-E4A6-4BE9-8E10-54FFA24DB246Q38802353-F4832283-4984-43C2-B29A-C6A17AB18D6DQ44037759-D6243706-366A-4A56-B74A-2C05832D6C94Q44180749-485B2DEC-A2A9-4287-8020-A1ACFD89026DQ46033185-D9FE8AB9-2B2C-4B23-B8B5-9059B9FBDB68Q46903405-21E24757-486D-477D-844B-1DBBADA58F9CQ48611289-DC79F9D1-B0AC-4777-9585-7AFD10328033Q50548053-6486BF35-409B-474A-AC99-C8313C9ED14DQ51606994-B90ED59E-04EF-48D5-83B7-0BFB108317D1Q54350455-165CA2FE-234C-4F50-BBC6-7CDA6EA81C91Q64082505-735CF8B5-8B59-4B2E-B7ED-B8FF3EDD86E4Q67538549-C6ECA864-F9DD-47E8-9FE6-F6DF25487DC5
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Daniel J Peet
@es
Daniel J Peet
@nl
Daniel J Peet
@sl
Daniel J. Peet
@en
type
label
Daniel J Peet
@es
Daniel J Peet
@nl
Daniel J Peet
@sl
Daniel J. Peet
@en
prefLabel
Daniel J Peet
@es
Daniel J Peet
@nl
Daniel J Peet
@sl
Daniel J. Peet
@en
P106
P1153
55746193900
P21
P31
P496
0000-0002-6085-8936