ArticleBiochimie2016
Structural transitions during prothrombin activation: On the importance of fragment 2.
Article in Biochimie, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- Prothrombinase processivity is conferred by substrate allostery.The EMBO journal · 2026Article
- Measurement of Active Thrombin Bound to Circulating D-Dimers as a Sensitive Biomarker for Prothrombotic Conditions.Journal of clinical laboratory analysis · 2026Article
- The Interconnected World of Coagulation Factors, Platelets and Plasminogen: A Novel Perspective on Biosynthetic Regulation.Life (Basel, Switzerland) · 2025Review
- Pro-Coagulant Lipids in Physiological Ratios Found in the Activated Platelet Membrane Do Not Impact Clot Structure or Fibrinolysis in Purified Assays.Journal of blood medicine · 2025Article
- New insight into the traditional model of the coagulation cascade and its regulation: illustrated review of a three-dimensional view.Research and practice in thrombosis and haemostasis · 2023Article
- Dabigatran and Wet AMD, Results From Retinal Pigment Epithelial Cell Monolayers, the Mouse Model of Choroidal Neovascularization, and Patients From the Medicare Data Base.Frontiers in immunology · 2022Article
- Identification and characterization of a factor Va-binding site on human prothrombin fragment 2.Scientific reports · 2019Article
- Structure of Coagulation Factor II: Molecular Mechanism of Thrombin Generation and Development of Next-Generation Anticoagulants.Frontiers in medicine · 2018Review
- Conformational diversity analysis reveals three functional mechanisms in proteins.PLoS computational biology · 2017Article
- The Fragment 1 Region of Prothrombin Facilitates the Favored Binding of Fragment 12 to Zymogen and Enforces Zymogen-like Character in the Proteinase.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Prothrombin is activated to thrombin by the prothrombinase complex through sequential cleavage at two distinct sites. This occurs at sites of vascular injury in a highly regulated cascade of serine protease and cofactor activation, where activated platelets provide a suitable surface for protease/cofactor/substrate assembly. The precise structural and conformational changes undergone during the transition from prothrombin to thrombin have been studied for decades, and several structures of prothrombin fragments along the activation pathway have been solved. Here we present a new structure analyzed in context of other recent structures and biochemical studies. What emerges is an unexpected mechanism that involves a change in the mode of binding of the F2 domain (fragment 2) on the catalytic domain after cleavage at Arg320, and a subsequent reorientation of the linker between the F2 and catalytic domain to present the Arg271 site for cleavage.
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Registered trials
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.