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Plasma prothrombin antigenic levels across thrombotic and hemorrhagic phenotypes in triple-positive antiphospholipid patients with antiprothrombin antibodies.

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The folding pathway of prothrombin.

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Anti-β2GPI IgG display a broad reactivity against different β2GPI domains beyond domain 1: results from the APS ACTION and multi-center Italian cohorts.

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Related Experiment Video

Updated: Apr 21, 2026

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Prothrombin structure: unanticipated features and opportunities.

Nicola Pozzi1, Enrico Di Cera

  • 1Edward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, MO 63104, USA.

Expert Review of Proteomics
|October 21, 2014
PubMed
Summary
This summary is machine-generated.

The structure of prothrombin, a key clotting factor, has been revealed, showing unexpected flexibility. This breakthrough provides a framework for understanding its activation and developing new drugs.

Keywords:
blood coagulationdrug designproteaseprothrombinstructural biology

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Hematology

Background:

  • Prothrombin's structure was previously unknown, hindering understanding of its function.
  • Prothrombin is a crucial protein in the blood coagulation cascade.

Discussion:

  • The revealed structure highlights significant flexibility in prothrombin due to linker regions.
  • These linkers connect the gamma carboxyglutamic domain, kringles, and protease domain.

Key Insights:

  • A new structure-based framework elucidates the molecular mechanism of prothrombin activation.
  • The findings rationalize observed bleeding phenotypes in patients with prothrombin mutations.

Outlook:

  • The structural insights identify potential targets for novel anticoagulant or procoagulant drug design.
  • Further research can leverage this framework to explore prothrombin's role in thrombosis and hemostasis.