Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Magnitude of Ubiquitination Determines the Fate of Epidermal Growth Factor Receptor Upon Ligand Stimulation.

Journal of molecular biology - 15 Oct 2021

Akimov Vyacheslav, Fehling-Kaschek Mirjam, Barrio-Hernandez Inigo, Puglia Michele, Bunkenborg Jakob, Nielsen Mogens M, Timmer Jens, Dengjel Jörn, Blagoev Blagoy

Abstract excerpt

Receptor tyrosine kinases (RTK) bind growth factors and are critical for cell proliferation and differentiation. Their dysregulation leads to a loss of growth control, often resulting in cancer. Epidermal growth factor receptor (EGFR) is the prototypic RTK and can bind several ligands exhibiting distinct mitogenic potentials. Whereas the phosphorylation on individual EGFR sites and their roles for downstream...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Epidermal Growth Factor
Share to Epithelial Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heparin-binding EGF-like Growth Factor

Share to Ligands

Share to Protein Processing, Post-Translational

Share to Proteomics

Share to Transforming Growth Factor alpha

Share to Ubiquitination

Source

Identifiers

PMID: 34508725
DOI: 10.1016/j.jmb.2021.167240

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Magnitude of Ubiquitination Determines the Fate of Epidermal Growth Factor Receptor Upon Ligand Stimulation.PMID 34508725Read ↗

Multisite EGFR phosphorylation is regulated by adaptor protein abundances and dimer lifetimes.Semantic proximity Read ↗

Quantitative proteomics and phosphoproteomics reveal novel insights into complexity and dynamics of the EGFR signaling networkSemantic proximity Read ↗

EGF receptor ubiquitination is not necessary for its internalization.Semantic proximity Read ↗

Ubiquitination of nuclear receptorsSemantic proximity Read ↗

The epidermal growth factor receptor family as a central element for cellular signal transduction and diversification.Semantic proximity Read ↗

Quantification of ligand and mutation-induced bias in EGFR phosphorylation in direct response to ligand bindingSemantic proximity Read ↗

K63-Linked Ubiquitination in Kinase Activation and CancerSemantic proximity Read ↗

A threshold model for receptor tyrosine kinase signaling specificity and cell fate determinationSemantic proximity Read ↗

Quantification of ligand and mutation-induced bias in EGFR phosphorylation in direct response to ligand binding.Semantic proximity Read ↗

Cell and molecular biology of epidermal growth factor receptor.Semantic proximity Read ↗

An integrated mechanistic and data-driven computational model predicts cell responses to high- and low-affinity EGFR ligandsSemantic proximity Read ↗

Phosphoproteomics-based modeling defines the regulatory mechanism underlying aberrant EGFR signaling.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.