Evidence map›Paper›PMID 38579706›Full record

ArticleStructure (London, England : 1993)2024

Full-length αIIbβ3 cryo-EM structure reveals intact integrin initiate-activation intrinsic architecture.

Tong Huo, Hongjiang Wu, Zeinab Moussa, Mehmet Sen, Valerie Dalton, Zhao Wang

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Prediction of αBiophysical journal · 2025
    Article
  5. Article
  6. MnBiophysical journal · 2025
    Article
  7. Review
  8. Contributions of the individual domains of αCytoskeleton (Hoboken, N.J.) · 2024
    Article
  9. Article
  10. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Tong HuoVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Hongjiang WuVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA; Graduate School of Baylor College of Medicine, Baylor College of Medicine, Houston, TX 77030, USA.
Zeinab MoussaDepartment of Biology and Biochemistry, University of Houston, Houston, TX 77204, USA.
Mehmet SenDepartment of Biology and Biochemistry, University of Houston, Houston, TX 77204, USA.
Valerie DaltonVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Zhao WangVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA; Cryo-EM/ET CPRIT Core, Baylor College of Medicine, Houston, TX 77030, USA; Dan L Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX 77030, USA; Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA. Electronic address: zhaow@bcm.edu.

Funding

Molecular Assembly of Bacterial Tripartite Multidrug Efflux PumpsR01AI179879 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI Zhao Wang · 2024 to 2026
$1.9M
Molecular mechanism of Androgen Receptor mediated transcriptionR01GM143380 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI WANG, ZHAO · 2021 to 2025
$1.7M
Investigation of the Cellular and Molecular Mechanisms of Thrombocyte Integrin SignalingR01HL162842 · NHLBI · BAYLOR COLLEGE OF MEDICINE · PI WANG, ZHAO · 2022 to 2025
$1.6M
NHLBI NIH HHS R01 HL162842NIAID NIH HHS R01 AI179879NIGMS NIH HHS R01 GM143380
6 · The paper itself

Abstract

Integrin αIIbβ3 is the key receptor regulating platelet retraction and accumulation and a proven drug-target for antithrombotic therapies. Here we resolve the cryo-EM structures of the full-length αIIbβ3, which covers three distinct states along the activation pathway. Firstly, we obtain the αIIbβ3 structure at 3 Å resolution in the inactive state, revealing the overall topology of the heterodimer with the transmembrane (TM) helices and the ligand-binding domain tucked in a specific angle proximity to the TM region. After the addition of a Mn

Indexed as

Cryoelectron MicroscopyPlatelet Glycoprotein GPIIb-IIIa ComplexBinding SitesHumansIntegrin alpha2Integrin beta3ManganeseModels, MolecularProtein BindingProtein ConformationProtein MultimerizationIntegrin alpha2Integrin beta3ITGA2B protein, humanITGB3 protein, humanManganesePlatelet Glycoprotein GPIIb-IIIa ComplexcryoEMfull-length αIIbβ3integrinstructureTM region

Identifiers

PMID38579706
PMCPMC11246237

What OpenQuestion holds

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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.