ArticleBiochimica et biophysica acta2014
Strong dimerization of wild-type ErbB2/Neu transmembrane domain and the oncogenic Val664Glu mutant in mammalian plasma membranes.
Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Predicting the impacts of mutations on protein-ligand binding affinity based on molecular dynamics simulations and machine learning methods.Computational and structural biotechnology journal · 2020Article
- Applications of Single-Molecule Methods to Membrane Protein Folding Studies.Journal of molecular biology · 2018Review
- 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 EphA3 dimerization promoted by the SAM domain.The Biochemical journal · 2015Article
- 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
- On human disease-causing amino acid variants: statistical study of sequence and structural patterns.Human mutation · 2015Article
- Effect of thanatophoric dysplasia type I mutations on FGFR3 dimerization.Biophysical journal · 2015Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Here, we study the homodimerization of the transmembrane domain of Neu, as well as an oncogenic mutant (V664E), in vesicles derived from the plasma membrane of mammalian cells. For the characterization, we use a Förster resonance energy transfer (FRET)-based method termed Quantitative Imaging-FRET (QI-FRET), which yields the donor and acceptor concentrations in addition to the FRET efficiencies in individual plasma membrane-derived vesicles. Our results demonstrate that both the wild-type and the mutant are 100% dimeric, suggesting that the Neu TM helix dimerizes more efficiently than other RTK TM domains in mammalian membranes. Furthermore, the data suggest that the V664E mutation causes a very small, but statistically significant change in dimer structure. This article is part of a Special Issue entitled: Interfacially Active Peptides and Proteins. Guest Editors: William C. Wimley and Kalina Hristova.
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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.