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

Identification of the minimal N-glycosylation on integrin α5β1 required for its inhibitory effect on EGFR signaling and cell proliferation.

Biochemical and biophysical research communications - 26 Feb 2020

Hou Sicong, Hang Qinglei, Isaji Tomoya, Fukuda Tomohiko, Gu Jianguo

Abstract excerpt

The N-glycosylation of integrin α5β1 is involved in multiple cell biological functions. Our group previously reported that the N-glycosylation of the Calf-1,2 domain on α5 subunit (S3-5,10-14) was important for its inhibitory effect on EGFR signaling through regulating α5-EGFR complex formation. In this follow-up study, we provide evidence that the N-glycosylation on integrin β1 subunit suppress cell growth by...

Read the complete abstract on PubMed

Topics

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

Share to Cell Adhesion
Share to Cell Proliferation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cells, Cultured

Share to ErbB Receptors

Share to Glycosylation

Share to Mutation

Share to Polysaccharides

Share to Signal Transduction

Source

Identifiers

PMID: 31858971
DOI: 10.1016/j.bbrc.2019.11.188

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

Identification of the minimal N-glycosylation on integrin α5β1 required for its inhibitory effect on EGFR signaling and cell proliferation.PMID 31858971Read ↗

Integrin α5 Suppresses the Phosphorylation of Epidermal Growth Factor Receptor and Its Cellular Signaling of Cell Proliferation via N-Glycosylation.Semantic proximity Read ↗

N-glycosylation of the beta-propeller domain of the integrin alpha5 subunit is essential for alpha5beta1 heterodimerization, expression on the cell surface, and its biological function.Semantic proximity Read ↗

The Roles of Integrin α5β1 in Human CancerSemantic proximity Read ↗

Role of Site-Specific Glycosylation in the I-Like Domain of Integrin β1 in Small Extracellular Vesicle-Mediated Malignant Behavior and FAK Activation.Semantic proximity Read ↗

An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1,4-N-acetylglucosaminyltransferase III.Semantic proximity Read ↗

Role of N-glycosylation in EGFR ectodomain ligand binding.Semantic proximity Read ↗

Functional impact of glycosylation of LRIG1 on EGFR proteostasis in cancer.Semantic proximity Read ↗

N-Glycosylation at Asn 402 Stabilizes N-Cadherin and Promotes Cell-Cell Adhesion of Glioma Cells.Semantic proximity Read ↗

Aberrant N-glycosylation in cancer: MGAT5 and β1,6-GlcNAc branched N-glycans as critical regulators of tumor development and progression.Semantic proximity Read ↗

Functional Impact of Glycosylation and Splicing Variants of LRIG1 on EGFR Proteostasis in CancerSemantic proximity Read ↗

Mutation of N-linked glycosylation in EpCAM affected cell adhesion in breast cancer cells.Semantic proximity Read ↗

The cellular microenvironment and cell adhesion: a role for O-glycosylation.Semantic proximity Read ↗

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