Thiol-disulfide redox dependence of heme binding and heme ligand switching in nuclear hormone receptor rev-erbβ

Journal of Biological Chemistry

Volumn 286, Issue 6, 2011, Pages 4392-4403

  Gupta, Nirupama ^a   Ragsdale, Stephen W ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BROAD SPECTRUM; DITHIOLS; EPR SPECTROSCOPY; HEME BINDING; HIGH AFFINITY; LIGAND BINDING DOMAIN; LOW DISSOCIATION CONSTANTS; NUCLEAR HORMONE RECEPTOR; PROINFLAMMATORY RESPONSE; REDOX CONDITION; REDOX STATE OF IRON; REDOX SWITCH; REDOX-TRIGGERED SWITCH; SITE DIRECTED MUTAGENESIS; TARGET GENES; THIOL-DISULFIDE; TRANSCRIPTIONAL ACTIVITY; UV-VISIBLE;

AMINO ACIDS; CRYSTAL STRUCTURE; DISSOCIATION; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENDOCRINOLOGY; ENZYME ACTIVITY; GENE EXPRESSION; LIGANDS; METABOLISM; OXIDATION;

PORPHYRINS;

CARBON MONOXIDE; CYSTEINE; FERRIC ION; FERROUS ION; HEME; HEMOPROTEIN; HISTIDINE; HORMONE RECEPTOR; IMIDAZOLE; RECEPTOR REV ERB BETA; THIOPHENE; UNCLASSIFIED DRUG; CELL RECEPTOR; DISULFIDE; IRON; LIGAND; NR1D2 PROTEIN, HUMAN; REPRESSOR PROTEIN;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISSOCIATION CONSTANT; ELECTRON SPIN RESONANCE; INFLAMMATION; LIGAND BINDING; OXIDATION; OXIDATION REDUCTION STATE; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN METABOLISM; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; ULTRAVIOLET SPECTROSCOPY; CHEMISTRY; GENETIC TRANSCRIPTION; GENETICS; HUMAN; METABOLISM; OXIDATION REDUCTION REACTION; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE;

CYSTEINE; DISULFIDES; HEME; HUMANS; IRON; LIGANDS; OXIDATION-REDUCTION; OXIDATIVE STRESS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, CYTOPLASMIC AND NUCLEAR; REPRESSOR PROTEINS; TRANSCRIPTION, GENETIC;

EID: 79953012491     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.193466     Document Type: Article

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