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

Cancer-derived mutations in the fibronectin III repeats of PTPRT/PTPrho inhibit cell-cell aggregation.

Cell communication & adhesion - 1 Dec 2009

Zhang Peng, Becka Scott, Craig Sonya E L, Lodowski David T, Brady-Kalnay Susann M, Wang Zhenghe

Abstract excerpt

Abstract The receptor protein tyrosine phosphatase T PTPrho is the most frequently mutated tyrosine phosphatase in human cancer. PTPrho mediates homophilic cell-cell aggregation. In its extracellular region, PTPrho has cell adhesion molecule-like motifs, including a MAM domain, an immunoglobulin domain, and four fibronectin type III (FNIII) repeats. Tumor-derived mutations have been identified in all of these...

Read the complete abstract on PubMed

Topics

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

Share to Cell Aggregation
Share to Cell Line

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Fibronectins

Share to Models, Molecular

Share to Mutagenesis, Site-Directed

Share to Neoplasms

Share to Protein Structure, Tertiary

Share to Receptor-Like Protein Tyrosine Phosphatases, Class 2

Source

Open in PubMed Open full text

Identifiers

PMID: 20230342
DOI: 10.3109/15419061003653771
PMCID: PMC2921943

Genes

PTPRT

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Cancer-derived mutations in the fibronectin III repeats of PTPRT/PTPrho inhibit cell-cell aggregation.PMID 20230342Read ↗

Tumor-derived extracellular mutations of PTPRT /PTPrho are defective in cell adhesion.Semantic proximity Read ↗

Receptor protein tyrosine phosphatases and cancer: new insights from structural biology.Semantic proximity Read ↗

Tumour suppressor function of protein tyrosine phosphatase receptor-T.Semantic proximity Read ↗

RPTPα controls epithelial adherens junctions, linking E-cadherin engagement to c-Src-mediated phosphorylation of cortactin.Semantic proximity Read ↗

Reversible Disruption of Cell-Matrix and Cell-Cell Interactions by Overexpression of Sialomucin ComplexSemantic proximity Read ↗

The rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residue.Semantic proximity Read ↗

PTPRK negatively regulates transcriptional activity of wild type and mutated oncogenic beta-catenin and affects membrane distribution of beta-catenin/E-cadherin complexes in cancer cells.Semantic proximity Read ↗

Catalytically active membrane-distal phosphatase domain of receptor protein-tyrosine phosphatase alpha is required for Src activation.Semantic proximity Read ↗

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