Evidence map›Paper›PMID 35167661›Full record

ReviewBlood2022

Molecular mechanisms of leukocyte β2 integrin activation.

Lai Wen, Markus Moser, Klaus Ley

Open access · bronzeAbstract readReview
In one paragraph

Review in Blood, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
8.3field-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

49 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Functional unfolding of the integrin αX transmembrane helix.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Tracing LYVE1bioRxiv : the preprint server for biology · 2025
    Article
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

3 authors at 2 institutions in 2 countries.

Lai WenCenter for Autoimmunity and Inflammation, La Jolla Institute for Immunology, La Jolla, CA.ORCID 0000-0001-9760-3403
Markus MoserInstitute of Experimental Hematology, School of Medicine, Technical University of Munich, Munich, Germany; and.ORCID 0000-0001-8825-5566
Klaus LeyCenter for Autoimmunity and Inflammation, La Jolla Institute for Immunology, La Jolla, CA.ORCID 0000-0001-9339-3672
La Jolla Institute for Immunology · USTechnical University of Munich · DE

Funding

The Interaction of TPO and Integrins in Hematopoiesis CellsP01HL078784 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GINSBERG, MARK HOWARD · 2005 to 2019
$28.3M
The Hemostasis, Thrombosis, and Inflammation Models CoreP01HL151433 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Mark HOWARD Ginsberg · 2020 to 2026
$16.4M
NHLBI NIH HHS P01 HL078784NHLBI NIH HHS P01 HL151433
6 · The paper itself

Abstract

Integrins are transmembrane receptors that mediate cell-cell and cell-extracellular matrix adhesion. Although all integrins can undergo activation (affinity change for ligands), the degree of activation is most spectacular for integrins on blood cells. The β2 integrins are exclusively expressed on the surface of all leukocytes including neutrophils, lymphocytes, and monocytes. They are essential for many leukocyte functions and are strictly required for neutrophil arrest from rolling. The inside-out integrin activation process receives input from chemokine receptors and adhesion molecules. The integrin activation pathway involves many cytoplasmic signaling molecules such as spleen tyrosine kinase, other kinases like Bruton's tyrosine kinase, phosphoinositide 3-kinases, phospholipases, Rap1 GTPases, and the Rap1-GTP-interacting adapter molecule. These signaling events ultimately converge on talin-1 and kindlin-3, which bind to the integrin β cytoplasmic domain and induce integrin conformational changes: extension and high affinity for ligand. Here, we review recent structural and functional insights into how talin-1 and kindlin-3 enable integrin activation, with a focus on the distal signaling components that trigger β2 integrin conformational changes and leukocyte adhesion under flow.

Indexed as

CD18 AntigensTalinCell AdhesionIntegrinsLeukocytesCD18 AntigensIntegrinsTalin

Identifiers

PMID35167661
PMCPMC10082358
OpenAlexW4213119767

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.