Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Role of cysteines 640, 656, and 661 in steroid binding to rat glucocorticoid receptors.

The Journal of biological chemistry - 5 Jun 1992

Chakraborti P K, Garabedian M J, Yamamoto K R, Simons S S

Abstract excerpt

The involvement of a vicinally spaced dithiol group in steroid binding to the glucocorticoid receptor has been deduced from experiments with the thiol-specific reagent methyl methanethiolsulfonate and the vicinal dithiol-specific reagent sodium arsenite. The vicinally spaced dithiol appears to reside in the 16-kDa trypsin fragment of the receptor, which is thought to contain 3 cysteines (Cys-640, -656, and -661...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Base Sequence
Share to Blotting, Western
Share to Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Peptide Fragments

Share to Substrate Specificity

Source

Identifiers

PMID: 1597467

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of cysteines 640, 656, and 661 in steroid binding to rat glucocorticoid receptors.PMID 1597467Read ↗

Metal oxyanion stabilization of the rat glucocorticoid receptor is independent of thiols.Semantic proximity Read ↗

Identification of single amino acid substitutions of Cys-736 that affect the steroid-binding affinity and specificity of the glucocorticoid receptor using phenotypic screening in yeast.Semantic proximity Read ↗

Mutations at positions 547-553 of rat glucocorticoid receptors reveal that hsp90 binding requires the presence, but not defined composition, of a seven-amino acid sequence at the amino terminus of the ligand binding domain.Semantic proximity Read ↗

Evidence that the conserved region in the steroid binding domain of the glucocorticoid receptor is required for both optimal binding of hsp90 and protection from proteolytic cleavage. A two-site model for hsp90 binding to the steroid binding domain.Semantic proximity Read ↗

A critical region in the mineralocorticoid receptor for aldosterone binding and activation by cortisol: evidence for a common mechanism governing ligand binding specificity in steroid hormone receptors.Semantic proximity Read ↗

Novel Antipeptide Antibodies to the Human Glucocorticoid Receptor: Recognition of Multiple Receptor Forms<i>in Vitro</i>and Distinct Localization of Cytoplasmic and Nuclear ReceptorsSemantic proximity Read ↗

Unique sequences in the guinea pig glucocorticoid receptor induce constitutive transactivation and decrease steroid sensitivity.Semantic proximity Read ↗

Hormone binding domain of human glucocorticoid receptor. Enhancement of transactivation function by substitution mutants M565R and A573Q.Semantic proximity Read ↗

Comparison of the 90-kilodalton heat shock protein interaction with in vitro translated glucocorticoid and estrogen receptors.Semantic proximity Read ↗

Cysteine residues are involved in structure and function of melanocortin 1 receptor: Substitution of a cysteine residue in transmembrane segment two converts an agonist to antagonist.Semantic proximity Read ↗

Mapping the HSP90 binding region of the glucocorticoid receptor.Semantic proximity Read ↗

Cysteine 647 in the insulin receptor is required for normal covalent interaction between alpha- and beta-subunits and signal transduction.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.