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

Mutations flanking the polyglutamine repeat in the modulatory domain of rat glucocorticoid receptor lead to an increase in affinity for hormone.

Endocrine research - 1 Aug 2002

Heeley Robert P, Rusconi Sandro G, Sutcliffe Roger G, Kenyon Christopher J

Abstract excerpt

A polyglutamine repeat in the N-terminus of the rat glucocorticoid receptor shows polymorphism, with variants of Q2RQ5, Q2RQ15-21. We investigated whether these natural polymorphisms affect receptor function, and whether alleles with polyglutamine repeats shorter than Q2RQ5, between Q2RQ6-14, or longer than Q2RQ21 are not found naturally because they encode a dysfunctional receptor. Ligand binding and...

Read the complete abstract on PubMed

Topics

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

Share to Binding, Competitive
Share to Corticosterone

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

Share to Dexamethasone

Share to Glucocorticoids

Share to Hormones

Share to Receptors, Glucocorticoid

Share to Repetitive Sequences, Amino Acid

Share to Transcriptional Activation

Source

Identifiers

PMID: 12489571
DOI: 10.1081/erc-120015060

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

Mutations flanking the polyglutamine repeat in the modulatory domain of rat glucocorticoid receptor lead to an increase in affinity for hormone.PMID 12489571Read ↗

Polymorphisms of the glucocorticoid receptor gene in laboratory and wild rats: steroid binding properties of trinucleotide CAG repeat length variants.Semantic proximity Read ↗

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

Glucocorticoid receptor mutants: man-made tools for functional research.Semantic proximity Read ↗

[Glucocorticoid receptor gene].Semantic proximity Read ↗

Active, interactive, and inactive steroid receptor mutants.Semantic proximity Read ↗

Differential hormone-dependent transcriptional activation and -repression by naturally occurring human glucocorticoid receptor variants.Semantic proximity Read ↗

Glucocorticoid and mineralocorticoid receptors and associated diseases.Semantic proximity Read ↗

[Nucleotide sequence variants of the glucocorticoid receptor gene and their significance in determining glucocorticoid sensitivity].Semantic proximity Read ↗

A Natural Mutation in Helix 5 of the Ligand Binding Domain of Glucocorticoid Receptor Enhances Receptor-Ligand Interaction.Semantic proximity Read ↗

Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement.Semantic proximity Read ↗

Naturally occurring C-terminal splice variants of nuclear receptorsSemantic 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 ↗

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