ArticleThe Journal of biological chemistry2010
Physical basis behind achondroplasia, the most common form of human dwarfism.
Article in The Journal of biological chemistry, 2010. 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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Who cites it
29 citing papers in PubMed, 45 citations in OpenAlex.
- Achondroplasia: aligning mouse model with human clinical studies shows crucial importance of immediate postnatal start of the therapy.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2024Article
- 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
- A registry of achondroplasia: a 6-year experience from the Czechia and Slovak Republic.Orphanet journal of rare diseases · 2022Article
- Functioning and well-being in older children and adolescents with achondroplasia: A qualitative study.American journal of medical genetics. Part A · 2022Article
- Psychomotor Delay in a Child withGlobal medical genetics · 2021Article
- A qualitative study of the impacts of having an infant or young child with achondroplasia on parent well-being.Orphanet journal of rare diseases · 2021Article
- Review
- Quantifying the strength of heterointeractions among receptor tyrosine kinases from different subfamilies: Implications for cell signaling.The Journal of biological chemistry · 2020Article
- The transition model of RTK activation: A quantitative framework for understanding RTK signaling and RTK modulator activity.Cytokine & growth factor reviews · 2019Review
- The RTK Interactome: Overview and Perspective on RTK Heterointeractions.Chemical reviews · 2019Review
- Identification and in silico characterization of p.G380R substitution in FGFR3, associated with achondroplasia in a non-consanguineous Pakistani family.Diagnostic pathology · 2017Article
- Pathogenic Cysteine Removal Mutations in FGFR Extracellular Domains Stabilize Receptor Dimers and Perturb the TM Dimer Structure.Journal of molecular biology · 2016Article
- 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
- Mechanism of FGF receptor dimerization and activation.Nature communications · 2016Article
- Fibroblast growth factor receptor signaling in hereditary and neoplastic disease: biologic and clinical implications.Cancer metastasis reviews · 2015Review
- Analytical characterization of plasma membrane-derived vesicles produced via osmotic and chemical vesiculation.Biochimica et biophysica acta · 2015Article
- FGFR3 unliganded dimer stabilization by the juxtamembrane domain.Journal of molecular biology · 2015Article
- FGFR3 induces degradation of BMP type I receptor to regulate skeletal development.Biochimica et biophysica acta · 2014Article
- New evidence for positive selection helps explain the paternal age effect observed in achondroplasia.Human molecular genetics · 2013Article
- FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Fibroblast growth factor receptor 3 (FGFR3) is a receptor tyrosine kinase that plays an important role in long bone development. The G380R mutation in FGFR3 transmembrane domain is known as the genetic cause for achondroplasia, the most common form of human dwarfism. Despite many studies, there is no consensus about the exact mechanism underlying the pathology. To gain further understanding into the physical basis behind the disorder, here we measure the activation of wild-type and mutant FGFR3 in mammalian cells using Western blots, and we analyze the activation within the frame of a physical-chemical model describing dimerization, ligand binding, and phosphorylation probabilities within the dimers. The data analysis presented here suggests that the mutation does not increase FGFR3 dimerization, as proposed previously. Instead, FGFR3 activity in achondroplasia is increased due to increased probability for phosphorylation of the unliganded mutant dimers. This finding has implications for the design of targeted molecular treatments for achondroplasia.
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Registered trials
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.