Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.

Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.

FIH (Factor inhibiting hypoxia-inducible factor), an asparaginyl beta-hydroxylase belonging to the super-family of 2-oxoglutarate and Fe(II)-dependent dioxygenases, catalyses hydroxylation of Asn-803 of hypoxia-inducible factor, a transcription factor that regulates the mammalian hypoxic response. O...

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Bibliografiska uppgifter
Huvudupphovsmän:	Lancaster, D, McDonough, M, Schofield, C
Materialtyp:	Journal article
Språk:	English
Publicerad:	2004

Liknande verk

Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH).
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Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803.
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Inhibition of the oxygen-sensing asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor: a potential hypoxia response modulating strategy
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Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity.
av: Lancaster, D, et al.
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Genetic analysis of the role of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH) in regulating hypoxia-inducible factor (HIF) transcriptional target genes [corrected].
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MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH).
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The inhibition of factor inhibiting hypoxia-inducible factor (FIH) by beta-oxocarboxylic acids.
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Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor.
av: Coleman, M, et al.
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Inhibition of hypoxia inducible factor (HIF) hydroxylases
av: Conejo-Garcia, A, et al.
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Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family.
av: Hewitson, K, et al.
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Tuning the transcriptional response to hypoxia by inhibiting HIF prolyl- and asparaginyl-hydroxylases
av: Chan, M, et al.
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Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains.
av: Yang, M, et al.
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Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.
av: Cockman, M, et al.
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Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates.
av: Hewitson, K, et al.
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FIH-dependent asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.
av: Cockman, M, et al.
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Evidence that two enzyme-derived histidine ligands are sufficient for iron binding and catalysis by factor inhibiting HIF (FIH).
av: Hewitson, K, et al.
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Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases.
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Investigating the dependence of the hypoxia-inducible factor hydroxylases (factor inhibiting HIF and prolyl hydroxylase domain 2) on ascorbate and other reducing agents.
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Selective inhibition of factor inhibiting hypoxia-inducible factor.
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Biochemistry of the hypoxia-inducible factor hydroxylases
av: Fiorini, G, et al.
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Structural basis for binding of cyclic 2-oxoglutarate analogues to factor-inhibiting hypoxia-inducible factor
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Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1)
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Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1).
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Structural basis for binding of the renal carcinoma target hypoxia-inducible factor 2α to prolyl hydroxylase domain 2
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The FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity.
av: Masson, N, et al.
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The FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity
av: Masson, N, et al.
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Selective small molecule probes for the hypoxia inducible factor (HIF) prolyl hydroxylases.
av: Chowdhury, R, et al.
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Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor.
av: Yang, M, et al.
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Inhibition studies on hypoxia-inducible factor (HIF) hydroxylases
av: Chan, M
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Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2).
av: McDonough, M, et al.
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Fih attenuates the hypoxic tolerance of Megalobrama amblycephala by inhibiting the activity of hypoxia-inducible factor alpha (hif-α)
av: Jun Li, et al.
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Differential sensitivity of hypoxia inducible factor hydroxylation sites to hypoxia and hydroxylase inhibitors.
av: Tian, Y, et al.
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Hypoxia-inducible factor prolyl-hydroxylase: purification and assays of PHD2.
av: Hewitson, K, et al.
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Studies on the inhibition of human hypoxia inducible factor (HIF) hydroxylases
av: Yeoh, KK
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Evaluation of aspirin metabolites as inhibitors of hypoxia-inducible factor hydroxylases.
av: Lienard, B, et al.
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Kinetic rationale for selectivity toward N- and C-terminal oxygen-dependent degradation domain substrates mediated by a loop region of hypoxia-inducible factor prolyl hydroxylases.
av: Flashman, E, et al.
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Structural basis for binding of cyclic 2-oxoglutarate analogues to factor-inhibiting hypoxia-inducible factor.
av: Conejo-Garcia, A, et al.
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Investigating the role of factor inhibiting HIF (FIH) in tumourigenesis
av: Ma, J
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Structural and mechanistic studies on the peroxisomal oxygenase phytanoyl-CoA 2-hydroxylase (PhyH).
av: Schofield, C, et al.
Publicerad: (2007)

Substrate selectivity of prolyl hydroxylases
av: McDonough, M
Publicerad: (2018)