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

PINCH-1 Is an Obligate Partner of Integrin-linked Kinase (ILK) Functioning in Cell Shape Modulation, Motility, and Survival

1 Dec 2003

Abstract excerpt

PINCH-1 is a widely expressed focal adhesion protein that forms a ternary complex with integrin-linked kinase (ILK) and CH-ILKBP/actopaxin/alpha-parvin (abbreviated as alpha-parvin herein). We have used RNA interference, a powerful approach of reverse genetics, to investigate the functions of PINCH-1 and ILK in human cells. We report here the following. First, PINCH-1 and ILK, but not alpha-parvin, are essential...

Read the complete abstract on PubMed

Topics

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

Share to Cell Adhesion Molecules Research
Share to Cellular Mechanics and Interactions
Share to NF-κB Signaling Pathways

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

Source

Identifiers

PMID: 14551191
DOI: 10.1074/jbc.m309122200

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 · 12 closest

PINCH-1 Is an Obligate Partner of Integrin-linked Kinase (ILK) Functioning in Cell Shape Modulation, Motility, and SurvivalPMID 14551191Read ↗

Distinct Roles of Two Structurally Closely Related Focal Adhesion Proteins, α-Parvins and β-Parvins, in Regulation of Cell Morphology and SurvivalSemantic proximity Read ↗

The gamma-parvin-integrin-linked kinase complex is critically involved in leukocyte-substrate interaction.Semantic proximity Read ↗

Integrin-linked kinase regulates migration and proliferation of human intestinal cells under a fibronectin-dependent mechanism.Semantic proximity Read ↗

Integrin-linked kinase (ILK): the known vs. the unknown and perspectivesSemantic proximity Read ↗

The Integrin-Mediated ILK-Parvin-αPix Signaling Axis Controls Differentiation in Mammary Epithelial Cells.Semantic proximity Read ↗

The role of integrin-linked kinase (ILK) in cancer progression.Semantic proximity Read ↗

Integrin-linked kinase – essential roles in physiology and cancer biologySemantic proximity Read ↗

Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes.Semantic proximity Read ↗

Targeted Ablation of PINCH1 and PINCH2 From Murine Myocardium Results in Dilated Cardiomyopathy and Early Postnatal LethalitySemantic proximity Read ↗

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

PINCH-1 Regulates the ERK-Bim Pathway and Contributes to Apoptosis Resistance in Cancer CellsSemantic proximity Read ↗

Parvin: A hub of intracellular signalling pathways regulating cellular behaviour and disease progressionSemantic proximity Read ↗

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