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

Molecular origins for the dominant negative function of human glucocorticoid receptor beta.

Molecular and cellular biology - 1 Jun 2003

Yudt Matthew R, Jewell Christine M, Bienstock Rachelle J, Cidlowski John A

Abstract excerpt

This study molecularly elucidates the basis for the dominant negative mechanism of the glucocorticoid receptor (GR) isoform hGRbeta, whose overexpression is associated with human glucocorticoid resistance. Using a series of truncated hGRalpha mutants and sequential mutagenesis to generate a serie...

Read the complete abstract on PubMed

Topics

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

Share to Chloramphenicol O-Acetyltransferase
Share to COS Cells
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Resistance

Share to Glutathione Transferase

Share to Protein Isoforms

Share to Receptors, Glucocorticoid

Share to Transcriptional Activation

Source

Open in PubMed Open full text

Identifiers

PMID: 12773573
DOI: 10.1128/MCB.23.12.4319-4330.2003
PMCID: PMC156139

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-12773573-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular origins for the dominant negative function of human glucocorticoid receptor beta.PMID 12773573Read ↗

Identification of natural human glucocorticoid receptor (hGR) mutations or polymorphisms and their functional consequences at the hormone-receptor interaction level.Semantic proximity Read ↗

Natural variants of the beta isoform of the human glucocorticoid receptor do not alter sensitivity to glucocorticoids.Semantic proximity Read ↗

Natural glucocorticoid receptor mutants causing generalized glucocorticoid resistance: molecular genotype, genetic transmission, and clinical phenotype.Semantic proximity Read ↗

Functional characterization of the natural human glucocorticoid receptor (hGR) mutants hGRalphaR477H and hGRalphaG679S associated with generalized glucocorticoid resistance.Semantic proximity Read ↗

The Human Glucocorticoid Receptor Beta: From Molecular Mechanisms to Clinical ImplicationsSemantic proximity Read ↗

A Novel Point Mutation in the Ligand-Binding Domain (LBD) of the Human Glucocorticoid Receptor (hGR) Causing Generalized Glucocorticoid Resistance: The Importance of the C Terminus of hGR LBD in Conferring Transactivational ActivitySemantic proximity Read ↗

Pathologic human GR mutant has a transdominant negative effect on the wild-type GR by inhibiting its translocation into the nucleus: importance of the ligand-binding domain for intracellular GR trafficking.Semantic proximity Read ↗

A Novel Point Mutation in the Amino Terminal Domain of the Human Glucocorticoid Receptor (hGR) Gene Enhancing hGR-Mediated Gene ExpressionSemantic proximity Read ↗

Glucocorticoid receptor beta, a potential endogenous inhibitor of glucocorticoid action in humans.Semantic proximity Read ↗

Glucocorticoid resistance.Semantic proximity Read ↗

Naturally occurring C-terminal splice variants of nuclear receptorsSemantic proximity Read ↗

The origin and functions of multiple human glucocorticoid receptor isoforms.Semantic proximity Read ↗

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