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

FGFR3 dimer stabilization due to a single amino acid pathogenic mutation.

Journal of molecular biology - 24 Feb 2006

Li Edwin, You Min, Hristova Kalina

Abstract excerpt

Mutations in the transmembrane (TM) domains of receptor tyrosine kinases (RTKs) have been implicated in the induction of pathological phenotypes. These mutations are believed to stabilize the RTK dimers, and thus promote unregulated signaling. However, the energetics behind the pathology inductio...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Craniofacial Dysostosis
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescence Resonance Energy Transfer

Share to Glutamic Acid

Share to Liposomes

Share to Receptor, Fibroblast Growth Factor, Type 3

Share to Urinary Bladder Neoplasms

Source

Open in PubMed Open full text

Identifiers

PMID: 16384584
DOI: 10.1016/j.jmb.2005.11.077
PMCID: PMC3812913

Genes

FGFR3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16384584-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

FGFR3 dimer stabilization due to a single amino acid pathogenic mutation.PMID 16384584Read ↗

FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain.Semantic proximity Read ↗

The A391E mutation enhances FGFR3 activation in the absence of ligand.Semantic proximity Read ↗

Studies of receptor tyrosine kinase transmembrane domain interactions: the EmEx-FRET method.Semantic proximity Read ↗

Multiple consequences of a single amino acid pathogenic RTK mutation: the A391E mutation in FGFR3.Semantic proximity Read ↗

Effect of the achondroplasia mutation on FGFR3 dimerization and FGFR3 structural response to fgf1 and fgf2: A quantitative FRET study in osmotically derived plasma membrane vesicles.Semantic proximity Read ↗

The strong dimerization of the transmembrane domain of the fibroblast growth factor receptor (FGFR) is modulated by C-terminal juxtamembrane residues.Semantic proximity Read ↗

Effect of pathogenic cysteine mutations on FGFR3 transmembrane domain dimerization in detergents and lipid bilayers.Semantic proximity Read ↗

Direct assessment of the effect of the Gly380Arg achondroplasia mutation on FGFR3 dimerization using quantitative imaging FRET.Semantic proximity Read ↗

Primary and secondary dimer interfaces of the fibroblast growth factor receptor 3 transmembrane domain: characterization via multiscale molecular dynamics simulations.Semantic proximity Read ↗

Role of dimerization efficiency of transmembrane domains in activation of fibroblast growth factor receptor 3.Semantic proximity Read ↗

Mechanism of FGF receptor dimerization and activation.Semantic proximity Read ↗

Effect of the G375C and G346E achondroplasia mutations on FGFR3 activation.Semantic proximity Read ↗

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