Evidence map›Paper›PMID 26186678›Full record

ArticleCurrent opinion in hematology2015

ADAMTS13 and von Willebrand factor interactions.

Catherine B Zander, Wenjing Cao, X Long Zheng

Abstract read
In one paragraph

Article in Current opinion in hematology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

28 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. ADAMTS-13 Behavior in Thrombocytopenia of Infectious Origin in ICU Patients.Indian journal of critical care medicine : peer-reviewed, official publication of Indian Society of Critical Care Medicine · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Reduced ADAMTS13 Activity in Correlation with Pathophysiology, Severity, and Outcome of COVID-19: A Retrospective Observational Study.International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases · 2022
    Observational
  15. Molecular Advances in Preeclampsia and HELLP Syndrome.International journal of molecular sciences · 2022
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Catherine B ZanderDivision of Laboratory Medicine, Department of Pathology, The University of Alabama at Birmingham, Birmingham, Alabama, USA.
Wenjing Cao
X Long Zheng
University of Alabama at Birmingham · US

Funding

Novel Therapeutics for Acquired Thrombotic Thrombocytopenic PurpuraR01HL115187 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI ZHENG, X. LONG · 2013 to 2016
$1.6M
NHLBI NIH HHS R01 HL115187NHLBI NIH HHS R01 HL115187-01A1
6 · The paper itself

Abstract

purpose of reviewADAMTS13 is a zinc-containing metalloprotease that cleaves von Willebrand factor (VWF). Deficiency of plasma ADAMTS13 activity is accountable for a potentially fatal blood disorder thrombotic thrombocytopenic purpura (TTP). Understanding of ADAMTS13-VWF interaction is essential for developing novel treatments to this disorder. RECENT

findingsDespite the proteolytic activity of ADAMTS13 being restricted to the metalloprotease domain, the ancillary proximal C-terminal domains including the disintegrin domain, first TSP-1 repeat, cysteine-rich region, and spacer domain are all required for cleavage of VWF and its analogs. Recent studies have added to our understandings of the role of the specific regions in the disintegrin domain, the cysteine-rich domain, and the spacer domain responsible for its interaction with VWF. Additionally, regulative functions of the distal portion of ADAMTS13 including the TSP-1 2-8 repeats and the CUB domains have been proposed. Finally, fine mapping of anti-ADAMTS13 antibody epitopes have provided further insight into the essential structural elements in ADAMTS13 for VWF binding and the mechanism of autoantibody-mediated TTP. SUMMARY: Significant progress has been made in our understandings of the structure-function relationship of ADAMTS13 in the past decade. To further investigate ADAMTS13-VWF interactions for medical applications, these interactions must be studied under physiological conditions in vivo.

Indexed as

Purpura, Thrombotic ThrombocytopenicADAM ProteinsADAMTS13 ProteinAntibody SpecificityAutoantibodiesHumansImmunodominant EpitopesProtein Structure, TertiaryProteolysisStructure-Activity Relationshipvon Willebrand FactorADAM ProteinsADAMTS13 ProteinADAMTS13 protein, humanAutoantibodiesImmunodominant Epitopesvon Willebrand Factor

Identifiers

PMID26186678
PMCPMC4824554
OpenAlexW2401660990

What OpenQuestion holds

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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.