Evidence map›Paper›PMID 36782235›Full record

ReviewThrombosis journal2023

Structure, signal transduction, activation, and inhibition of integrin αIIbβ3.

Honglei Xin, Jiansong Huang, Zhiqun Song, Jianhua Mao, Xiaodong Xi, Xiaofeng Shi

Open access · goldAbstract readReview
In one paragraph

Review in Thrombosis journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Platelet Membrane Receptors and Signalling Pathways.Handbook of experimental pharmacology · 2026
    Review
  6. Article
  7. Review
  8. Prediction of αBiophysical journal · 2025
    Article
  9. MnBiophysical journal · 2025
    Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Contributions of the individual domains of αCytoskeleton (Hoboken, N.J.) · 2024
    Article
  15. 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

6 authors at 3 institutions in 1 country.

Honglei XinDepartment of Hematology, Second Affiliated Hospital of Nanjing Medical University, Nanjing, Jiangsu, 210003, China.
Jiansong HuangDepartment of Hematology, The First Affiliated Hospital, Zhejiang University School of Medicine, Zhejiang, Hangzhou, 310003, China.
Zhiqun SongJiangsu Province People's Hospital and Nanjing Medical University First Affiliated Hospital, Nanjing, Jiangsu, 210029, China.
Jianhua MaoShanghai Institute of Hematology, State Key Laboratory of Medical Genomics, Collaborative Innovation Center of Hematology, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200025, China.
Xiaodong XiShanghai Institute of Hematology, State Key Laboratory of Medical Genomics, Collaborative Innovation Center of Hematology, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200025, China. xixiaodong@shsmu.edu.cn.
Xiaofeng ShiDepartment of Hematology, Second Affiliated Hospital of Nanjing Medical University, Nanjing, Jiangsu, 210003, China. shixiaofeng1977@163.com.
Shanghai Jiao Tong University · CNNanjing Medical University · CNSecond Affiliated Hospital of Nanjing Medical University · CN

Funding

National Natural Science Foundation of China 81700130
6 · The paper itself

Abstract

Integrins are heterodimeric receptors comprising α and β subunits. They are expressed on the cell surface and play key roles in cell adhesion, migration, and growth. Several types of integrins are expressed on the platelets, including αvβ3, αIIbβ3, α2β1, α5β1, and α6β1. Among these, physically αIIbβ3 is exclusively expressed on the platelet surface and their precursor cells, megakaryocytes. αIIbβ3 adopts at least three conformations: i) bent-closed, ii) extended-closed, and iii) extended-open. The transition from conformation i) to iii) occurs when αIIbβ3 is activated by stimulants. Conformation iii) possesses a high ligand affinity, which triggers integrin clustering and platelet aggregation. Platelets are indispensable for maintaining vascular system integrity and preventing bleeding. However, excessive platelet activation can result in myocardial infarction (MI) and stroke. Therefore, finding a novel strategy to stop bleeding without accelerating the risk of thrombosis is important. Regulation of αIIbβ3 activation is vital for this strategy. There are a large number of molecules that facilitate or inhibit αIIbβ3 activation. The interference of these molecules can accurately control the balance between hemostasis and thrombosis. This review describes the structure and signal transduction of αIIbβ3, summarizes the molecules that directly or indirectly affect integrin αIIbβ3 activation, and discusses some novel antiαIIbβ3 drugs. This will advance our understanding of the activation of αIIbβ3 and its essential role in platelet function and tumor development.

Indexed as

HemostasisIntegrinsPlatelet activationThrombosisαIIbβ3

Identifiers

PMID36782235
PMCPMC9923933
OpenAlexW4320489702

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.