FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
about
Cloning and expression analysis of two distinct HIF-alpha isoforms--gcHIF-1alpha and gcHIF-4alpha--from the hypoxia-tolerant grass carp, Ctenopharyngodon idellusPIASy stimulates HIF1α SUMOylation and negatively regulates HIF1α activity in response to hypoxiaExpanding role of the jumonji C domain as an RNA hydroxylaseJMJD6 is a histone arginine demethylaseUbiquitin-specific protease 19 (USP19) regulates hypoxia-inducible factor 1α (HIF-1α) during hypoxiaEvidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygenIOP1, a novel hydrogenase-like protein that modulates hypoxia-inducible factor-1alpha activityThe LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activityCrystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modificationPosttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alphaMint3 enhances the activity of hypoxia-inducible factor-1 (HIF-1) in macrophages by suppressing the activity of factor inhibiting HIF-1MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathwaysAsparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factorStructure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alphaStructural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediatesTranscriptional activation of hypoxia-inducible factor-1alpha by HDAC4 and HDAC5 involves differential recruitment of p300 and FIH-1Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domainsRegulation of the prolyl hydroxylase domain protein 2 (phd2/egln-1) gene: identification of a functional hypoxia-responsive elementThe candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF).Suppression of hypoxia-inducible factor 1alpha (HIF-1alpha) transcriptional activity by the HIF prolyl hydroxylase EGLN1Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway.Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)The phosphatidylserine receptor from Hydra is a nuclear protein with potential Fe(II) dependent oxygenase activityHypoxic regulation of erythropoiesis and iron metabolismThe possible mechanisms underlying the impairment of HIF-1α pathway signaling in hyperglycemia and the beneficial effects of certain therapiesOncometabolite 2-hydroxyglutarate is a competitive inhibitor of α-ketoglutarate-dependent dioxygenasesThe VHL tumor suppressor: master regulator of HIFIdentification of an alternative mechanism of degradation of the hypoxia-inducible factor-1alphaRegulation of hypoxia-inducible factor-1alpha by NF-kappaBHIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxiaThe VHL protein recruits a novel KRAB-A domain protein to repress HIF-1alpha transcriptional activityHypoxia upregulates the expression of the NDRG1 gene leading to its overexpression in various human cancersMolecular responses to hypoxia in tumor cellsaHIF but not HIF-1alpha transcript is a poor prognostic marker in human breast cancerAscorbate depletion: a critical step in nickel carcinogenesis?Hypoxia-inducible factor-1alpha polymorphisms and TSC1/2 mutations are complementary in head and neck cancersHypoxia and its implications in rheumatoid arthritis
P2860
Q21263015-BD1EE7A6-1E2D-45FA-8855-040287889C7EQ24293208-A512176F-7FD0-49A2-BCFA-C43CB34E7AFAQ24297426-0D8FC8D7-7E18-493E-8C76-C062C66D4377Q24298169-5AEC5091-24B7-4173-9068-7E5B4B83AC50Q24298656-D72F4477-57A2-4CE9-BC5A-5FE820F67B3AQ24299724-E0C87145-0BE6-4D52-BBA2-CA4A4E4FEA5BQ24301670-1B6625B4-F7EA-4B52-B51E-3A1C5F42E101Q24303868-3D75D9D1-F850-46BC-B5C4-7603A7BD5135Q24304317-6EA08192-340A-4297-9881-413711F993F0Q24304828-FCE53064-4759-48AE-93FF-A544E5AC5C64Q24306213-91540656-3BDC-4C7B-8948-856BE8005317Q24308024-771967B9-A716-4EFA-AEF5-2BFCEEBB5BE9Q24312373-8AE35516-214F-4D3E-9AB8-F9090AC33E1CQ24315135-D51756CB-81FA-4CBA-A7C8-2851B7EF7572Q24317627-B10F020B-15A7-4599-8E62-9A53B734E393Q24319665-ECA7B58C-6D03-420A-9EDE-079A11F69B24Q24320267-85155D71-FE67-4EF3-B6A8-92024C96ACF9Q24321241-79355573-EB90-4A9C-8CFE-7928D1C3FF4EQ24324150-870135B3-7A84-4D1F-A117-2AAC8F2AE652Q24337743-3E60288C-A4C7-49D5-97A1-381618237C72Q24528175-EEFFA6FD-A948-4201-8074-0A28CE9071B5Q24529065-EC5751F9-4FA2-4B14-964C-09AE13BAA6F8Q24538799-B929BEDF-FECC-4500-8B06-6EC615BA8BDDQ24539006-F6799755-B2D4-4325-83D3-3FEB88BDFAE1Q24550960-1B51668E-24AB-481E-B000-FCF850E59448Q24561863-F17D639A-7BEA-4DCD-8E23-68FFA360353CQ24609166-10C2D520-863C-43B3-B862-A7FDEE3D6C6DQ24630072-EF2EE8F8-A16E-473E-AEC2-8A99F9782B3DQ24632807-94AFF4C6-4E69-4550-956E-742ABA8F6B95Q24634592-7585035A-DA00-4C88-8918-72B61659ACE7Q24651502-9BD9199D-3D72-4F29-8994-996AFFCA2F1DQ24657260-77A4AA17-AC7B-4CFE-8A04-C97276830AB5Q24671941-F5FD2679-67CD-4C94-A17B-BABA106725A4Q24676311-324FD0D6-4E08-4D4E-B852-C40753FF0275Q24794324-47E12F47-2204-4208-BEAC-889078A7BB03Q24797310-23C7068E-339D-484F-85DD-FCCB82672167Q24802904-ACE5190D-7D7C-40DC-8A62-A800EF6D8250Q24812869-B0893874-88FF-4141-934C-673443840108Q25255621-2596042E-1C75-4DB9-BEA2-F1A566F12DD0Q26739909-B6472393-F7CD-4184-9697-D85DC0321684
P2860
FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
description
2002 nî lūn-bûn
@nan
2002 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
FIH-1 is an asparaginyl hydrox ...... ty of hypoxia-inducible factor
@ast
FIH-1 is an asparaginyl hydrox ...... ty of hypoxia-inducible factor
@en
FIH-1 is an asparaginyl hydrox ...... ty of hypoxia-inducible factor
@en-gb
FIH-1 is an asparaginyl hydrox ...... ty of hypoxia-inducible factor
@nl
type
label
FIH-1 is an asparaginyl hydrox ...... ty of hypoxia-inducible factor
@ast
FIH-1 is an asparaginyl hydrox ...... ty of hypoxia-inducible factor
@en
FIH-1 is an asparaginyl hydrox ...... ty of hypoxia-inducible factor
@en-gb
FIH-1 is an asparaginyl hydrox ...... ty of hypoxia-inducible factor
@nl
prefLabel
FIH-1 is an asparaginyl hydrox ...... ty of hypoxia-inducible factor
@ast
FIH-1 is an asparaginyl hydrox ...... ty of hypoxia-inducible factor
@en
FIH-1 is an asparaginyl hydrox ...... ty of hypoxia-inducible factor
@en-gb
FIH-1 is an asparaginyl hydrox ...... ty of hypoxia-inducible factor
@nl
P2093
P2860
P921
P3181
P356
P1433
P1476
FIH-1 is an asparaginyl hydrox ...... ty of hypoxia-inducible factor
@en
P2093
Dean A Whelan
Jeffrey J Gorman
Murray L Whitelaw
Richard K Bruick
P2860
P304
P3181
P356
10.1101/GAD.991402
P407
P577
2002-06-15T00:00:00Z