Evidence map›Paper›PMID 28986431›Full record

ArticleThe Journal of biological chemistry2017

A novel antithrombin domain dictates the journey's end of a proteinase.

Ingrid M Verhamme

Open access · hybridAbstract readComment
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 43% 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

1 citing paper in PubMed, 10 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Ingrid M VerhammeFrom the Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, Tennessee 37232 Ingrid.verhamme@vanderbilt.edu.
Vanderbilt University Medical Center · US

Funding

Mechanisms of Glycosaminoglycan-Catalyzed Protease Inactivation by SerpinsR01HL130018 · NHLBI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI VERHAMME, INGRID M · 2016 to 2019
$1.6M
NHLBI NIH HHS R01 HL130018
6 · The paper itself

Abstract

Antithrombin (AT) is an anticoagulant serpin that irreversibly inactivates the clotting proteinases factor Xa and thrombin by forming covalent complexes with them. Mutations in its critical domains, such as those that impair the conformational rearrangement required for proteinase inactivation, increase the risk of venous thrombosis. Águila

Indexed as

Antithrombin IIIAntithrombinsFactor XaHeparinHumansPeptide HydrolasesThrombinAntithrombin IIIAntithrombinsFactor XaHeparinPeptide HydrolasesThrombin

Identifiers

PMID28986431
PMCPMC5633113
OpenAlexW2760822991

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.