Evidence map›Paper›PMID 19109562›Full record

ArticleBlood2009

The distal carboxyl-terminal domains of ADAMTS13 are required for regulation of in vivo thrombus formation.

Fumiaki Banno, Anil K Chauhan, Koichi Kokame, Jin Yang, Shigeki Miyata, Denisa D Wagner, Toshiyuki Miyata

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

39 citing papers in PubMed, 77 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Mechanisms of ADAMTS13 regulation.Journal of thrombosis and haemostasis : JTH · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. ADAMTS13 and von Willebrand factor interactions.Current opinion in hematology · 2015
    Article
  15. Article
  16. Review
  17. Allosteric activation of ADAMTS13 by von Willebrand factor.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  18. Article
  19. Von Willebrand Factor Abnormalities Studied in the Mouse Model: What We Learned about VWF Functions.Mediterranean journal of hematology and infectious diseases · 2013
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Fumiaki BannoResearch Institute, National Cardiovascular Center, Suita, Japan.
Anil K Chauhan
Koichi Kokame
Jin Yang
Shigeki Miyata
Denisa D Wagner
Toshiyuki Miyata
National Cerebral and Cardiovascular Center · JPHarvard University · US

Funding

Platelets in Cardiovascular Biology and PathologyP01HL066105 · NHLBI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HYNES, RICHARD O · 2001 to 2010
$28.4M
NHLBI NIH HHS P01 HL066105NHLBI NIH HHS P01-HL066105
6 · The paper itself

Abstract

ADAMTS13 is a multidomain protease that limits platelet thrombogenesis through the cleavage of von Willebrand factor (VWF). We previously identified 2 types of mouse Adamts13 gene: the 129/Sv-strain Adamts13 gene encodes the long-form ADAMTS13 having the same domains as human ADAMTS13, whereas the C57BL/6-strain Adamts13 gene encodes the short-form ADAMTS13 lacking the distal C-terminal domains. To assess the physiologic significance of the distal C-terminal domains of ADAMTS13, we generated and analyzed 129/Sv-genetic background congenic mice (Adamts13(S/S)) that carry the short-form ADAMTS13. Similar to wild-type 129/Sv mice (Adamts13(L/L)), Adamts13(S/S) did not have ultralarge VWF multimers in plasma, in contrast to 129/Sv-genetic background ADAMTS13-deficient mice (Adamts13(-/-)). However, in vitro thrombogenesis under flow at a shear rate of 5000 s(-1) was accelerated in Adamts13(S/S) compared with Adamts13(L/L). Both in vivo thrombus formation in ferric chloride-injured arterioles and thrombocytopenia induced by collagen plus epinephrine challenge were more dramatic in Adamts13(S/S) than in Adamts13(L/L) but less than in Adamts13(-/-). These results suggested that the C-terminally truncated ADAMTS13 exhibited decreased activity in the cleavage of VWF under high shear rate. Role of the C-terminal domains may become increasingly important under prothrombotic conditions.

Indexed as

ADAMTS13 ProteinAnimalsArteriolesChloridesFerric CompoundsMetalloendopeptidasesMiceMice, Inbred StrainsProtein Structure, TertiaryThrombocytopeniaThrombosisvon Willebrand FactorADAMTS13 ProteinADAMTS13 protein, mouseChloridesferric chlorideFerric CompoundsMetalloendopeptidasesvon Willebrand Factor

Identifiers

PMID19109562
PMCPMC2686194
OpenAlexW2128727430

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.