Evidence map›Paper›PMID 22652793›Full record

ReviewFrontiers in bioscience (Landmark edition)2012

Structural biology of factor VIIa/tissue factor initiated coagulation.

Kanagasabai Vadivel, S Paul Bajaj

Abstract readReview
In one paragraph

Review in Frontiers in bioscience (Landmark edition), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Comparative sequence analysis of vitamin K-dependent coagulation factors.Journal of thrombosis and haemostasis : JTH · 2022
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Bradykinin: Inflammatory Product of the Coagulation System.Clinical reviews in allergy & immunology · 2016
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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

2 authors.

Kanagasabai VadivelProtein Science Laboratory, UCLA/Orthopaedic Hospital, Department of Orthopaedic Surgery, University of California, Los Angeles, CA 90095-1795, USA.
S Paul Bajaj

Funding

Efficacy of Kunitz Domain 1 variants of TFPI-2 as novel antifibrinolytic agentsR21HL089661 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BAJAJ, MADHU SATYA · 2009 to 2010
$424k
Biochemistry of Normal and Abnormal Variants of Factor IXR56HL036365 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BAJAJ, S PAUL · 2007 to 2007
$356k
NHLBI NIH HHS R21 HL089661NHLBI NIH HHS R56 HL036365
6 · The paper itself

Abstract

Factor VII (FVII) consists of an N-terminal gamma-carboxyglutamic acid domain followed by two epidermal growth factor-like (EGF1 and EGF2) domains and the C-terminal protease domain. Activation of FVII results in a two-chain FVIIa molecule consisting of a light chain (Gla-EGF1-EGF2 domains) and a heavy chain (protease domain) held together by a single disulfide bond. During coagulation, the complex of tissue factor (TF, a transmembrane glycoprotein) and FVIIa activates factor IX (FIX) and factor X (FX). FVIIa is structurally "zymogen-like" and when bound to TF, it is more "active enzyme-like." FIX and FX share structural homology with FVII. Three structural biology aspects of FVIIa/TF are presented in this review. One, regions in soluble TF (sTF) that interact with FVIIa as well as mapping of Ca2+, Mg2+, Na+ and Zn2+ sites in FVIIa and their functions; two, modeled interactive regions of Gla and EGF1 domains of FXa and FIXa with FVIIa/sTF; and three, incompletely formed oxyanion hole in FVIIa/sTF and its induction by substrate/inhibitor. Finally, an overview of the recognition elements in TF pathway inhibitor is provided.

Indexed as

Binding SitesBlood CoagulationBlood Coagulation FactorsCationsFactor VIIaHumansLipoproteinsModels, MolecularMultiprotein ComplexesProtein FoldingProtein Interaction Domains and MotifsThromboplastinBlood Coagulation FactorsCationsFactor VIIalipoprotein-associated coagulation inhibitorLipoproteinsMultiprotein ComplexesThromboplastin

Identifiers

PMID22652793
PMCPMC3383856

What OpenQuestion holds

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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.