ArticleBiochemistry2003
Characterization of glycosylation sites of the epidermal growth factor receptor.
Article in Biochemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
What it found
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Who cites it
59 citing papers in PubMed, 122 citations in OpenAlex.
- 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
- Multiple glycoforms of TrkA interact with N-cadherin during trigeminal ganglion neurodevelopment.Journal of cell science · 2026Article
- Dose-Dependent Inhibition of Protein Glycosylation Reveals Crosstalk between Glycosylation and Phosphorylation in EGF Signaling Pathways.Analytical chemistry · 2026Article
- Effects of N361 Glycosylation on Epidermal Growth Factor Receptor Biological Function.Cancers · 2026Article
- Niemann-Pick type C1 protein regulates epidermal growth factor receptor stability in hepatic cells and facilitates the early steps of Hepatitis B virus infection.Frontiers in cellular and infection microbiology · 2026Article
- Ocular surface glycocalyx in health and disease.Frontiers in cell and developmental biology · 2025Review
- H Antigen expression modulates epidermal Keratinocyte Integrity and differentiation.Biological research · 2024Article
- Article
- Structural dynamics of the active HER4 and HER2/HER4 complexes is finely tuned by different growth factors and glycosylation.bioRxiv : the preprint server for biology · 2024Article
- Engineering of cell-surface receptors for analysis of receptor internalization and detection of receptor-specific glycosylation.Chemical science · 2024Article
- Diverse perspectives on proteomic posttranslational modifications to address EGFR-TKI resistance in non-small cell lung cancer.Frontiers in cell and developmental biology · 2024Review
- Orbitrap-Based Mass and Charge Analysis of Single Molecules.Accounts of chemical research · 2023Article
- Sialylation of EGFR by ST6GAL1 induces receptor activation and modulates trafficking dynamics.bioRxiv : the preprint server for biology · 2023Article
- Innovative Metrics for Reporting and Comparing the Glycan Structural Profile in Biotherapeutics.Molecules (Basel, Switzerland) · 2023Article
- Role of glycosyltransferases in carcinogenesis; growth factor signaling and EMT/MET programs.Glycoconjugate journal · 2022Review
- Altered glycosylation of several metastasis-associated glycoproteins with terminal GalNAc defines the highly invasive cancer cell phenotype.Oncotarget · 2022Article
- Dual role of fucosidase in cancers and its clinical potential.Journal of Cancer · 2022Review
- Glycosylation promotes the cancer regulator EGFR-ErbB2 heterodimer formation - molecular dynamics study.Journal of molecular modeling · 2021Article
- Terminal α2,6-sialylation of epidermal growth factor receptor modulates antibody therapy response of colorectal cancer cells.Cellular oncology (Dordrecht, Netherlands) · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha). In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry. Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells. We also confirm the partial glycosylation of an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells. We show that an additional canonical site in the secreted form of the receptor is fully glycosylated. While the pattern of glycosylation is the same for the sites shared by the full-length and the secreted forms of the receptor, the oligosaccharides of the full-length receptor are more extensively processed. Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
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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.