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

Parallel regulation of membrane trafficking and dominant-negative effects by misrouted gonadotropin-releasing hormone receptor mutants.

The Journal of biological chemistry - 1 Jul 2005

Knollman Paul E, Janovick Jo Ann, Brothers Shaun P, Conn P Michael

Abstract excerpt

Gonadotropin-releasing hormone (GnRH) receptor mutants from patients with hypogonadotropic hypogonadism are frequently misrouted proteins that exert a dominant-negative (DN) effect on human (h) wild-type (WT) receptor, due to oligomerization and retention in the endoplasmic reticulum. Pharmacologic chaperones restore correct folding, rescuing mutants and WT receptor from this oligomer. Rat WT retains the ability...

Read the complete abstract on PubMed

Topics

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

Share to COS Cells
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gonadotropins

Share to Inositol Phosphates

Share to Lysine

Share to Protein Folding

Share to Receptors, LHRH

Share to Serine

Source

Identifiers

PMID: 15886197
DOI: 10.1074/jbc.M501978200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Parallel regulation of membrane trafficking and dominant-negative effects by misrouted gonadotropin-releasing hormone receptor mutants.PMID 15886197Read ↗

Human loss-of-function gonadotropin-releasing hormone receptor mutants retain wild-type receptors in the endoplasmic reticulum: molecular basis of the dominant-negative effect.Semantic proximity Read ↗

Dominant-Negative Action of Disease-Causing Gonadotropin-Releasing Hormone Receptor (GnRHR) Mutants: A Trait That Potentially Coevolved with Decreased Plasma Membrane Expression of GnRHR in HumansSemantic proximity Read ↗

Receptor-misrouting: an unexpectedly prevalent and rescuable etiology in gonadotropin-releasing hormone receptor-mediated hypogonadotropic hypogonadism.Semantic proximity Read ↗

G protein-coupled receptor trafficking in health and disease: lessons learned to prepare for therapeutic mutant rescue in vivo.Semantic proximity Read ↗

Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease.Semantic proximity Read ↗

Unexpected Effects of Epitope and Chimeric Tags on Gonadotropin-Releasing Hormone Receptors: Implications for Understanding the Molecular Etiology of Hypogonadotropic HypogonadismSemantic proximity Read ↗

Targeting trafficking as a therapeutic avenue for misfolded GPCRs leading to endocrine diseases.Semantic proximity Read ↗

Rescue of hypogonadotropic hypogonadism-causing and manufactured GnRH receptor mutants by a specific protein-folding template: misrouted proteins as a novel disease etiology and therapeutic target.Semantic proximity Read ↗

Mutations in G protein-coupled receptors that impact receptor trafficking and reproductive function.Semantic proximity Read ↗

Molecular mechanism of action of pharmacoperone rescue of misrouted GPCR mutants: the GnRH receptor.Semantic proximity Read ↗

Calnexin regulated gonadotropin-releasing hormone receptor plasma membrane expression.Semantic proximity Read ↗

Mutations in the human gonadotropin-releasing hormone receptor: insights into receptor biology and function.Semantic proximity Read ↗

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