Evidence map›Paper›PMID 20033063›Full record

ReviewThe EMBO journal2010

The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase!

Sara A Wickström, Anika Lange, Eloi Montanez, Reinhard Fässler

Open access · bronzeAbstract readReview
In one paragraph

Review in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.

0numbers the graph read from it
0cells of the map it votes in
150citing papers in PubMed
11.6field-weighted citation impact, top 1% 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

150 citing papers in PubMed, 255 citations in OpenAlex.

  1. Trial
  2. Article
  3. 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
  4. Review
  5. Integrins in the kidney - beyond the matrix.Nature reviews. Nephrology · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Vascular mechanotransduction.Physiological reviews · 2023
    Review
  11. Article
  12. Cytoplasmic Tail of MT1-MMP: A Hub of MT1-MMP Regulation and Function.International journal of molecular sciences · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. ATP allosterically stabilizes integrin-linked kinase for efficient force generation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Understanding the molecular basis of cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2022
    Review
  20. Integrin-linked kinase (ILK): the known vs. the unknown and perspectives.Cellular and molecular life sciences : CMLS · 2022
    Review

90 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

4 authors at 2 institutions in 1 country.

Sara A WickströmDepartment for Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried, Germany.
Anika Lange
Eloi Montanez
Reinhard Fässler
Max Planck Society · DEMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dynamic interactions of cells with their environment regulate multiple aspects of tissue morphogenesis and function. Integrins are the major class of cell surface receptors that recognize and bind extracellular matrix proteins, resulting in the engagement and organization of the cytoskeleton as well as activation of signalling pathways to regulate cell behaviour and morphogenetic processes. The ternary complex of integrin-linked kinase (ILK), PINCH, and parvin (IPP complex), which was identified more than a decade ago, interacts with the cytoplasmic tail of beta integrins and couples them to the actin cytoskeleton. In addition, ILK has been shown to act as a serine/threonine kinase and to directly activate several signalling pathways downstream of integrins. However, the kinase activity of ILK and the precise functions of the IPP complex have remained elusive and controversial. This review focuses on the recent advances made towards understanding the specialized roles this complex and its individual components have acquired during evolution.

Indexed as

Amino Acid SequenceAnimalsDNA-Binding ProteinsHumansMicrofilament ProteinsMolecular Sequence DataMorphogenesisProtein Serine-Threonine KinasesScaffold Protein ILKSequence AlignmentDNA-Binding ProteinsMicrofilament ProteinsProtein Serine-Threonine KinasesScaffold Protein ILK

Identifiers

PMID20033063
PMCPMC2824469
OpenAlexW2068585362

What OpenQuestion holds

Textmetadata
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.