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

Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.

The Journal of biological chemistry - 12 Nov 2010

Kwak Tae Kyoung, Kim Hyeonjung, Jung Oisun, Lee Sin-Ae, Kang Minkyung, Kim Hyun Jeong, Park Ji-Min, Kim Sung-Hoon, Lee Jung Weon

Abstract excerpt

Protein-protein interactions and/or signaling activities at focal adhesions, where integrin-mediated adhesion to extracellular matrix occurs, are critical for the regulation of adhesion-dependent cellular functions. Although the phosphorylation and activities of focal adhesion molecules have been intensively studied, the effects of the O-GlcNAc modification of their Ser/Thr residues on cellular functions have...

Read the complete abstract on PubMed

Topics

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

Share to Acetylglucosamine
Share to Diabetes Mellitus, Experimental

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glucosamine

Share to Insulinoma

Share to Laminin

Share to Mice, Inbred ICR

Share to Paxillin

Share to Streptozocin

Source

Open in PubMed Open full text

Identifiers

PMID: 20829364
DOI: 10.1074/jbc.M110.129601
PMCID: PMC2975224

Genes

INS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.PMID 20829364Read ↗

Tyrosine phosphorylation of paxillin alpha is involved in temporospatial regulation of paxillin-containing focal adhesion formation and F-actin organization in motile cells.Semantic proximity Read ↗

Phosphorylation of actopaxin regulates cell spreading and migration.Semantic proximity Read ↗

MYPT1 O-GlcNAc modification controls the sensitivity of fibroblasts to sphingosine-1-phosphate mediated cellular contractionSemantic proximity Read ↗

Matrix nonenzymatic glycosylation leads to altered cellular phenotype and intracellular tyrosine phosphorylation.Semantic proximity Read ↗

Ras-induced serine phosphorylation of the focal adhesion protein paxillin is mediated by the Raf-->MEK-->ERK pathway.Semantic proximity Read ↗

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

The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling.Semantic proximity Read ↗

Modulation of Thr phosphorylation of integrin beta1 during muscle differentiation.Semantic proximity Read ↗

Paxillin enables attachment-independent tyrosine phosphorylation of focal adhesion kinase and transformation by RAS.Semantic proximity Read ↗

Glycosylation is a novel TGFβ1-independent post-translational modification of Smad2.Semantic proximity Read ↗

Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.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 ↗

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