Evidence map›Paper›PMID 22763012›Full record

ReviewCurrent opinion in cell biology2012

ILK: a pseudokinase in the center stage of cell-matrix adhesion and signaling.

Jun Qin, Chuanyue Wu

Abstract readReview
In one paragraph

Review in Current opinion in cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
6.5field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

76 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
  2. ILK binding to β1 integrin is indirect and mediated by kindlin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Unlocking the Therapeutic Potential of Integrin-Linked Kinase Inhibitors in Bioengineered 3D Breast Tumor Stroma Models.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  5. Tnni3k Is Cardioprotective in Viral Myocarditis.Journal of cardiovascular development and disease · 2026
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Drosophila Nephrocyte as a Model for Studying Glomerular Basement Membrane Physiology.Journal of the American Society of Nephrology : JASN · 2024
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

16 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Jun QinDepartment of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA. qinj@ccf.org
Chuanyue Wu
Cleveland Clinic · USUniversity of Pittsburgh · US

Funding

STRUCTURES AND MECHANISMS OF ANK REPEAT BEARING PROTEINSR01HL058758 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI JUN QIN · 1999 to 2026
$9.0M
PINCH-1 Interactions and FunctionsR01GM065188 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI WU, CHUANYUE · 2002 to 2014
$3.3M
The PINCH-ILK-parvin complexes in glomerular cellsR01DK054639 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI WU, CHUANYUE · 1998 to 2010
$3.2M
NHLBI NIH HHS R01 HL058758NIDDK NIH HHS R01 DK054639NIGMS NIH HHS R01 GM065188
6 · The paper itself

Abstract

Integrin-linked kinase (ILK) is a widely expressed and evolutionally conserved component of cell-extracellular matrix (ECM) adhesions. Although initially named as a kinase, ILK contains an unusual pseudoactive site that is incapable of catalyzing phosphorylation. Instead, ILK acts as a central component of a heterotrimer (the PINCH-ILK-parvin complex) at ECM adhesions mediating interactions with a large number of proteins via multiple sites including its pseudoactive site. Through higher level protein-protein interactions, this scaffold links integrins to the actin cytoskeleton and catalytic proteins and thereby regulates focal adhesion assembly, cytoskeleton organization and signaling. This review summarizes recent advances in our understanding of the structure and functions of the PINCH-ILK-parvin complex, and discusses emerging new features of the molecular mechanisms by which it regulates diverse cellular, physiological and pathological processes.

Indexed as

Signal TransductionAnimalsCell-Matrix JunctionsDiseaseDNA-Binding ProteinsEmbryonic DevelopmentHumansIntegrinsMicrofilament ProteinsPhosphorylationProtein MultimerizationProtein Serine-Threonine KinasesScaffold Protein ILKDNA-Binding ProteinsIntegrinsMicrofilament ProteinsProtein Serine-Threonine KinasesScaffold Protein ILK

Identifiers

PMID22763012
PMCPMC3467332
OpenAlexW1986055287

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.