Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates (Q24321241)

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English	Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates	scientific article

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scholarly article

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Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates (English)

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Hypoxia inducible factor 1 subunit alpha inhibitor

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GOA release 2020-03-11

carboxylic acid binding

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GOA release 2020-03-11

Christopher J. Schofield

9

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object named as

Neil J Oldham

7

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Michael A McDonough

object named as

Michael A McDonough

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author name string

Kirsty S Hewitson

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Benoit M R Liénard

2

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Ian J Clifton

4

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Danica Butler

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Alexie S Soares

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Luke A McNeill

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language of work or name

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publication date

2 February 2007

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Journal of Biological Chemistry

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282

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5

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3293-301

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Hypoxia-inducible nuclear factors bind to an enhancer element located 3' to the human erythropoietin gene

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21 January 2018

HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing

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

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21 January 2018

The von Hippel-Lindau protein, HIF hydroxylation, and oxygen sensing

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Dioxygenases as O2-dependent regulators of the hypoxic response pathway

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Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl hydroxylases

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21 January 2018

Signalling hypoxia by HIF hydroxylases

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21 January 2018

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

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21 January 2018

Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins

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21 January 2018

FeII/alpha-ketoglutarate-dependent hydroxylases and related enzymes

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https://api.crossref.org/works/10.1074%2FJBC.M608337200

21 January 2018

C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

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21 January 2018

A conserved family of prolyl-4-hydroxylases that modify HIF

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21 January 2018

Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor

1 reference

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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

1 reference

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21 January 2018

HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia

1 reference

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21 January 2018

Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor

1 reference

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21 January 2018

Role of nitric oxide in the regulation of HIF-1alpha expression during hypoxia

1 reference

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Redistribution of intracellular oxygen in hypoxia by nitric oxide: effect on HIF1alpha

1 reference

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Nitric oxide impairs normoxic degradation of HIF-1alpha by inhibition of prolyl hydroxylases

1 reference

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Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: evidence for metal centered rearrangements

1 reference

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HIF overexpression correlates with biallelic loss of fumarate hydratase in renal cancer: novel role of fumarate in regulation of HIF stability

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Accumulation of Krebs cycle intermediates and over-expression of HIF1alpha in tumours which result from germline FH and SDH mutations

1 reference

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Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M608337200

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Reactive oxygen species generated at mitochondrial complex III stabilize hypoxia-inducible factor-1alpha during hypoxia: a mechanism of O2 sensing

1 reference

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21 January 2018

Mitochondrial reactive oxygen species trigger hypoxia-induced transcription

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Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing

1 reference

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Reactive oxygen species in the control of hypoxia-inducible factor-mediated gene expression.

1 reference

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Inhibition of mitochondrial respiration elevates oxygen concentration but leaves regulation of hypoxia-inducible factor (HIF) intact

1 reference

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21 January 2018

On the Origin of Cancer Cells

1 reference

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Tumor hypoxia: definitions and current clinical, biologic, and molecular aspects

1 reference

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Lactate dehydrogenase 5 (LDH5) relates to up-regulated hypoxia inducible factor pathway and metastasis in colorectal cancer

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Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1.

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Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase

1 reference

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Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Refinement of macromolecular structures by the maximum-likelihood method

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Automated protein model building combined with iterative structure refinement

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Selective inhibition of factor inhibiting hypoxia-inducible factor

1 reference

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Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)

1 reference

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Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate

1 reference

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Succinate complex crystal structures of the alpha-ketoglutarate-dependent dioxygenase AtsK: steric aspects of enzyme self-hydroxylation

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A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis

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10.1074/JBC.M608337200

1 reference

Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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