ArticleProceedings of the National Academy of Sciences of the United States of America2015
N-Glycosylation as determinant of epidermal growth factor receptor conformation in membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.
What it found
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Who cites it
103 citing papers in PubMed, 172 citations in OpenAlex.
- Molecular Determinants of Receptor-Specific Membrane Interactions in EphA1 and EphA2 from Coarse-Grained Simulations.Journal of chemical information and modeling · 2026Article
- Cis glycan-glycan interactions organize membrane nanodomains that tune receptor signaling.Nature communications · 2026Article
- Comparative Real-Time Kinetics of Ligand-Receptor Interactions Using Immobilization-Based Sensing Readouts.Analytical chemistry · 2026Article
- Review
- Enzymatically controlled release of proteins and peptides: A promising, alternative secretion approach.iScience · 2026Article
- Membrane Protein Glycosylation Revisited: Functional Dynamics and Emerging Clinical Insights.International journal of molecular sciences · 2026Review
- Spatial metabolomics and multiomics integration for breakthroughs in precision medicine for kidney disease.Nature reviews. Nephrology · 2026Review
- Effects of N361 Glycosylation on Epidermal Growth Factor Receptor Biological Function.Cancers · 2026Article
- Golgi Drivers of Cancer.Sub-cellular biochemistry · 2026Review
- From EGFR PTM network to TKI resistance: spatial subtypes and targeting in lung cancer.Cancer drug resistance (Alhambra, Calif.) · 2026Review
- Asparagine-linked glycosylation protein 1 (ALG1) promotes aggressive phenotypes of lung adenocarcinoma cells, A549, via modulating N-linked glycosylation and ER-Stress.Glycoconjugate journal · 2025Article
- Targeting DDOST improves the efficacy of lenvatinib and immunotherapy in hepatocellular carcinoma.Experimental & molecular medicine · 2025Article
- Metal Ion-Enhanced ZIC-cHILIC StageTip for N-Glycoproteomic and Phosphoproteomic Profiling in EGFR-Mutated Lung Cancer Cells.Molecular & cellular proteomics : MCP · 2025Article
- Article
- N-deglycosylation targeting chimera (DGlyTAC): a strategy for immune checkpoint proteins inactivation by specifically removing N-glycan.Signal transduction and targeted therapy · 2025Article
- Engineered Proteins and Chemical Tools to Probe the Cell Surface Proteome.Chemical reviews · 2025Review
- Spatial top-down proteomics for the functional characterization of human kidney.Clinical proteomics · 2025Article
- Single-Molecule Observation of Competitive Protein-Protein Interactions Utilizing a Nanopore.ACS nano · 2025Article
- Mapping O- and N-Glycosylation in Transmembrane and Interface Regions of Proteins: Insights from a Database Search Study.International journal of molecular sciences · 2025Article
- Ocular surface glycocalyx in health and disease.Frontiers in cell and developmental biology · 2025Review
43 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The epidermal growth factor receptor (EGFR) regulates several critical cellular processes and is an important target for cancer therapy. In lieu of a crystallographic structure of the complete receptor, atomistic molecular dynamics (MD) simulations have recently shown that they can excel in studies of the full-length receptor. Here we present atomistic MD simulations of the monomeric N-glycosylated human EGFR in biomimetic lipid bilayers that are, in parallel, also used for the reconstitution of full-length receptors. This combination enabled us to experimentally validate our simulations, using ligand binding assays and antibodies to monitor the conformational properties of the receptor reconstituted into membranes. We find that N-glycosylation is a critical determinant of EGFR conformation, and specifically the orientation of the EGFR ectodomain relative to the membrane. In the absence of a structure for full-length, posttranslationally modified membrane receptors, our approach offers new means to structurally define and experimentally validate functional properties of cell surface receptors in biomimetic membrane environments.
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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.