Evidence map›Paper›PMID 31294329›Full record

ArticleResearch and practice in thrombosis and haemostasis2019

Crystal structure, epitope, and functional impact of an antibody against a superactive FVIIa provide insights into allosteric mechanism.

Longguang Jiang, Xie Xie, Jinyu Li, Egon Persson, Mingdong Huang

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Research and practice in thrombosis and haemostasis, 2019. 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 48% 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, 2 citations in OpenAlex.

  1. 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

5 authors at 3 institutions in 2 countries.

Longguang JiangCollege of Chemistry National & Local Joint Biomedical Engineering Research Center on Photodynamic Technologies Fuzhou University Fuzhou China.
Xie XieCollege of Chemistry National & Local Joint Biomedical Engineering Research Center on Photodynamic Technologies Fuzhou University Fuzhou China.
Jinyu LiCollege of Chemistry National & Local Joint Biomedical Engineering Research Center on Photodynamic Technologies Fuzhou University Fuzhou China.
Egon PerssonHaemophilia Biology Novo Nordisk A/S Novo Nordisk Park Måløv, Denmark.ORCID https://orcid.org/0000-0003-3005-4926
Mingdong HuangCollege of Chemistry National & Local Joint Biomedical Engineering Research Center on Photodynamic Technologies Fuzhou University Fuzhou China.
Fuzhou University · CNChinese Academy of Sciences · CNNovo Nordisk (Denmark) · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundBlood coagulation factor VIIa (FVIIa) plays its critical physiological role in the initiation of hemostasis. Even so, recombinant FVIIa is successfully used as a bypassing agent for factor VIII or IX in the treatment of bleeds in patients with severe hemophilia with inhibitors. To investigate the utility of more potent FVIIa variants with enhanced intrinsic activity, molecules such as V21D/E154V/M156Q-FVIIa (FVIIa

methodsSurface plasmon resonance was used to characterize the binding of mAb4F5 to FVIIa

resultsThe binding experiments, functional effects on FVIIa

conclusionThe binary complex explains and supports the selectivity and functional consequences of Fab4F5 association with FVIIa

Indexed as

antibodyblood coagulationcrystal structurefactor VIIainhibitionSAXS

Identifiers

PMID31294329
PMCPMC6611371
OpenAlexW2950443059

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.