ArticlePloS one2012
Direct assessment of the effect of the Gly380Arg achondroplasia mutation on FGFR3 dimerization using quantitative imaging FRET.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed, 53 citations in OpenAlex.
- Anesthetic management of children undergoing specialized orthopedic surgeries.Journal of clinical orthopaedics and trauma · 2025Review
- Application of family whole-exome sequencing for prenatal diagnosis-an analysis of 357 cases.Frontiers in medicine · 2025Article
- Dental characteristics of patients with four different types of skeletal dysplasias.Clinical oral investigations · 2023Article
- Measurement of FGFR3 signaling at the cell membrane via total internal reflection fluorescence microscopy to compare the activation of FGFR3 mutants.The Journal of biological chemistry · 2023Article
- Towards generalizable predictions for G protein-coupled receptor variant expression.Biophysical journal · 2022Article
- Psychomotor Delay in a Child withGlobal medical genetics · 2021Article
- Stoichiometry and regulation network of Bcl-2 family complexes quantified by live-cell FRET assay.Cellular and molecular life sciences : CMLS · 2020Article
- Contribution of Cotranslational Folding Defects to Membrane Protein Homeostasis.Journal of the American Chemical Society · 2019Article
- Applications of Single-Molecule Methods to Membrane Protein Folding Studies.Journal of molecular biology · 2018Review
- A New Method to Study Heterodimerization of Membrane Proteins and Its Application to Fibroblast Growth Factor Receptors.The Journal of biological chemistry · 2017Article
- 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.Biochimica et biophysica acta · 2016Article
- Unliganded fibroblast growth factor receptor 1 forms density-independent dimers.The Journal of biological chemistry · 2015Article
- Unliganded EphA3 dimerization promoted by the SAM domain.The Biochemical journal · 2015Article
- A Genetic-Pathophysiological Framework for Craniosynostosis.American journal of human genetics · 2015Review
- Characterization of membrane protein interactions in plasma membrane derived vesicles with quantitative imaging Förster resonance energy transfer.Accounts of chemical research · 2015Article
- Fluorophores, environments, and quantification techniques in the analysis of transmembrane helix interaction using FRET.Biopolymers · 2015Review
- Analytical characterization of plasma membrane-derived vesicles produced via osmotic and chemical vesiculation.Biochimica et biophysica acta · 2015Article
- Structural and physico-chemical effects of disease and non-disease nsSNPs on proteins.Current opinion in structural biology · 2015Review
- Analysis of the clinical and molecular characteristics of a child with achondroplasia: A case report.Experimental and therapeutic medicine · 2015Article
- On human disease-causing amino acid variants: statistical study of sequence and structural patterns.Human mutation · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Gly380Arg mutation in FGFR3 is the genetic cause for achondroplasia (ACH), the most common form of human dwarfism. The mutation has been proposed to increase FGFR3 dimerization, but the dimerization propensities of wild-type and mutant FGFR3 have not been compared. Here we use quantitative imaging FRET to characterize the dimerization of wild-type FGFR3 and the ACH mutant in plasma membrane-derived vesicles from HEK293T cells. We demonstrate a small, but statistically significant increase in FGFR3 dimerization due to the ACH mutation. The data are consistent with the idea that the ACH mutation causes a structural change which affects both the stability and the activity of FGFR3 dimers in the absence of ligand.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.