Evidence map›Paper›PMID 24928861›Full record

ReviewBlood2014

von Willebrand factor, Jedi knight of the bloodstream.

Timothy A Springer

Open access · bronzeAbstract readReview
In one paragraph

Review in Blood, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 228 papers.

0numbers the graph read from it
0cells of the map it votes in
228citing papers in PubMed
13.2field-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

228 citing papers in PubMed, 439 citations in OpenAlex.

  1. Seventh Åland Island Meeting on von Willebrand Disease.Haemophilia : the official journal of the World Federation of Hemophilia · 2026
    Article
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  5. Selective Inhibition of Integrin β3 Topology Provides a Safer Antithrombotic Strategy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Article
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  11. Article
  12. Von Willebrand disease: A century of progress.Research and practice in thrombosis and haemostasis · 2026
    Review
  13. Review
  14. Article
  15. Article
  16. Article
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  18. Article
  19. Stimulation of themBio · 2025
    Article
  20. Article

168 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Timothy A SpringerProgram in Cellular and Molecular Medicine and Division of Hematology, Department of Medicine, Boston Children's Hospital, and Department of Biological Chemistry and Pharmacology, Harvard Medical School, Boston, MA.ORCID http://orcid.org/0000-0001-6627-2904
Boston Children's Hospital · US

Funding

Structures of Alpha 4 Integrins, Ligands and AntagonistsP01HL103526 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI SPRINGER, TIMOTHY A · 2011 to 2015
$11.1M
Single molecule measurements on von Willebrand factor A1 and A2 domainsR01HL108248 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI SPRINGER, TIMOTHY A · 2011 to 2015
$2.4M
NHLBI NIH HHS HL-103526NHLBI NIH HHS HL-108248NHLBI NIH HHS P01 HL103526NHLBI NIH HHS R01 HL108248
6 · The paper itself

Abstract

When blood vessels are cut, the forces in the bloodstream increase and change character. The dark side of these forces causes hemorrhage and death. However, von Willebrand factor (VWF), with help from our circulatory system and platelets, harnesses the same forces to form a hemostatic plug. Force and VWF function are so closely intertwined that, like members of the Jedi Order in the movie Star Wars who learn to use "the Force" to do good, VWF may be considered the Jedi knight of the bloodstream. The long length of VWF enables responsiveness to flow. The shape of VWF is predicted to alter from irregularly coiled to extended thread-like in the transition from shear to elongational flow at sites of hemostasis and thrombosis. Elongational force propagated through the length of VWF in its thread-like shape exposes its monomers for multimeric binding to platelets and subendothelium and likely also increases affinity of the A1 domain for platelets. Specialized domains concatenate and compact VWF during biosynthesis. A2 domain unfolding by hydrodynamic force enables postsecretion regulation of VWF length. Mutations in VWF in von Willebrand disease contribute to and are illuminated by VWF biology. I attempt to integrate classic studies on the physiology of hemostatic plug formation into modern molecular understanding, and point out what remains to be learned.

Indexed as

Amino Acid SequenceAnimalsBiophysical PhenomenaHemorheologyHemostasisHumansMicroscopy, Electron, TransmissionModels, MolecularMolecular Sequence DataProtein MultimerizationProtein Structure, TertiarySequence Homology, Amino AcidThrombosisvon Willebrand Diseasesvon Willebrand Factorvon Willebrand Factor

Identifiers

PMID24928861
PMCPMC4148764
OpenAlexW1985726492

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.