Evidence map›Paper›PMID 21730834›Full record

ReviewCurrent opinion in hematology2011

A new look at blood coagulation factor V.

Rodney M Camire

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in hematology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Cryogenic electron microscopy and coagulation factors.Current opinion in hematology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. The Prothrombin-Prothrombinase Interaction.Sub-cellular biochemistry · 2024
    Review
  6. Article
  7. Article
  8. Cryo-EM structures of coagulation factors.Research and practice in thrombosis and haemostasis · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Down-regulation of the clotting cascade by the protein C pathway.Hematology education. European Hematology Association. Congress. Education Program · 2013
    Article
  18. 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

1 author at 1 institution in 1 country.

Rodney M CamireDivision of Hematology, Department of Pediatrics, Children's Hospital of Philadelphia and University of Pennsylvania, Perelman School of Medicine, Philadelphia, Pennsylvania, USA. rcamire@mail.med.upenn.edu
Children's Hospital of Philadelphia · US

Funding

Structural Correlates of Protease and Cofactor FunctionP01HL074124 · NHLBI · CHILDREN'S HOSP OF PHILADELPHIA · PI KRISHNASWAMY, SRIRAM · 2003 to 2013
$17.6M
Molecular Basis of Procofactor ActivationR01HL088010 · NHLBI · CHILDREN'S HOSP OF PHILADELPHIA · PI CAMIRE, RODNEY M · 2008 to 2012
$1.6M
NHLBI NIH HHS HL-74124NHLBI NIH HHS HL-88010NHLBI NIH HHS P01 HL074124NHLBI NIH HHS R01 HL088010
6 · The paper itself

Abstract

purpose of reviewFactor V plays an essential role in hemostasis and has a profound influence on thrombin generation. The aim of this review is to highlight recent advances in our understanding of the biology of factor V which shed light on the variable bleeding tendencies in severe factor V deficiency. Furthermore, new mechanistic insights responsible for maintaining factor V as an inactive procofactor will be discussed. RECENT

findingsThe bleeding manifestation of severe factor V-deficient patients varies dramatically. Phenotypic modifiers of the bleeding predisposition in these patients have recently been identified. These include platelet factor V and, surprisingly, plasma tissue factor pathway inhibitor, which is significantly reduced in these patients. An important step in robust thrombin generation is the activation of factor V to factor Va. In a mechanism distinct from factor VIII, factor V activation involves proteolytic removal of inhibitory and conserved sequences from the large central B domain which exposes binding sites for factor Xa and possibly prothrombin. Taking advantage of this mechanism, certain Australian snakes have a unique form of factor V in their venom with these inhibitory sequences removed, thereby creating a potent constitutively active procoagulant cofactor. SUMMARY: Basic biochemical and clinical studies continue to move our understanding of factor V forward. It is apparent that there is much to be learned about parahemophilia and factor V activation, two seemingly well studied areas of research. A full understanding of each may provide unanticipated insights into ways to modulate factor V/Va function for therapeutic benefit.

Indexed as

AnimalsFactor VFactor V DeficiencyHumansFactor V

Identifiers

PMID21730834
PMCPMC12742396
OpenAlexW2042840911

What OpenQuestion holds

Textmetadata
LicenceTDM
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.