(Q27641363)

2

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Andrew L Kung

3

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Dennis S France

4

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Gerhard Wagner

5

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Michael J Eck

Nature structural biology

6

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publication date

July 2003

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published in

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volume

10

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issue

7

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page(s)

504-12

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cites work

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Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1 alpha

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Hypoxia-inducible factor 1: oxygen homeostasis and disease pathophysiology

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Suppression of tumor growth through disruption of hypoxia-inducible transcription

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Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension

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Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit

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Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1

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Physiology meets biophysics: visualizing the interaction of hypoxia-inducible factor 1 alpha with p300 and CBP

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Transcription. Oxygen sensing gets a second wind

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Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch

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FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity

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

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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

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Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803

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Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha

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Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response

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Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau

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Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling

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Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL

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Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway

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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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Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2

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Molecular cloning and chromosomal localization of the human CITED2 gene encoding p35srj/Mrg1.

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msg1, a novel melanocyte-specific gene, encodes a nuclear protein and is associated with pigmentation

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MRG1, the product of a melanocyte-specific gene related gene, is a cytokine-inducible transcription factor with transformation activity

31 March 2020

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The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors

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Selective coactivation of estrogen-dependent transcription by CITED1 CBP/p300-binding protein

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Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1

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The essential role of Cited2, a negative regulator for HIF-1alpha, in heart development and neurulation

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Cardiac malformations, adrenal agenesis, neural crest defects and exencephaly in mice lacking Cited2, a new Tfap2 co-activator

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CREB-binding protein and p300 in transcriptional regulation

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The atomic structure of protein-protein recognition sites

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Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP

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Molecular mechanism of hypoxia-inducible factor 1alpha -p300 interaction. A leucine-rich interface regulated by a single cysteine

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beta-catenin: molecular plasticity and drug design.

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Coupling of folding and binding for unstructured proteins

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Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling

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Structure of translation factor eIF4E bound to m7GDP and interaction with 4E-binding protein

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Processing of multi-dimensional NMR data with the new software PROSA

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The program XEASY for computer-supported NMR spectral analysis of biological macromolecules

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Protein backbone angle restraints from searching a database for chemical shift and sequence homology

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Torsion angle dynamics for NMR structure calculation with the new program DYANA

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Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding

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AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

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MOLMOL: a program for display and analysis of macromolecular structures

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Structures of DNA-binding mutant zinc finger domains: implications for DNA binding

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