Evidence map›Paper›PMID 31801825›Full record

ArticleThe Journal of biological chemistry2020

Beating tissue factor at its own game: Design and properties of a soluble tissue factor-independent coagulation factor VIIa.

Anders B Sorensen, Inga Tuneew, L Anders Svensson, Egon Persson, Henrik Østergaard, Michael Toft Overgaard, Ole H Olsen, Prafull S Gandhi

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
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  5. 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

8 authors.

Anders B SorensenGlobal Research, Novo Nordisk A/S, DK-2760 Måløv, Denmark; Department of Chemistry and Bioscience, Aalborg University, DK-9220 Aalborg, Denmark. Electronic address: abs@evaxion-biotech.com.
Inga TuneewGlobal Research, Novo Nordisk A/S, DK-2760 Måløv, Denmark.
L Anders SvenssonGlobal Research, Novo Nordisk A/S, DK-2760 Måløv, Denmark.
Egon PerssonGlobal Research, Novo Nordisk A/S, DK-2760 Måløv, Denmark.
Henrik ØstergaardGlobal Research, Novo Nordisk A/S, DK-2760 Måløv, Denmark.
Michael Toft OvergaardDepartment of Chemistry and Bioscience, Aalborg University, DK-9220 Aalborg, Denmark.
Ole H OlsenGlobal Research, Novo Nordisk A/S, DK-2760 Måløv, Denmark; Novo Nordisk Foundation Center for Basic Metabolic Research, Section for Metabolic Receptology, University of Copenhagen, Blegdamsvej 3b, DK-2200 Copenhagen N, Denmark.
Prafull S GandhiGlobal Research, Novo Nordisk A/S, DK-2760 Måløv, Denmark. Electronic address: pgan@novonordisk.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two decades of research have uncovered the mechanism by which the complex of tissue factor (TF) and the plasma serine protease factor VIIa (FVIIa) mediates the initiation of blood coagulation. Membrane-anchored TF directly interacts with substrates and induces allosteric effects in the protease domain of FVIIa. These properties are also recapitulated by the soluble ectodomain of TF (sTF). At least two interdependent allosteric activation pathways originate at the FVIIa:sTF interface are proposed to enhance FVIIa activity upon sTF binding. Here, we sought to engineer an sTF-independent FVIIa variant by stabilizing both proposed pathways, with one pathway terminating at segment 215-217 in the activation domain and the other pathway terminating at the N terminus insertion site. To stabilize segment 215-217, we replaced the flexible 170 loop of FVIIa with the more rigid 170 loop from trypsin and combined it with an L163V substitution (FVIIa-VY

Indexed as

Blood CoagulationProtein EngineeringAllosteric RegulationAmino Acid SequenceCrystallography, X-RayFactor VIIaHumansModels, MolecularMutagenesisProtein UnfoldingRecombinant ProteinsThromboplastinFactor VIIarecombinant FVIIaRecombinant ProteinsThromboplastinallosteric regulationblood clottingcoagulation factorcofactorinflammationprotein engineeringserine proteasetissue factortrypsinX-ray crystallography

Identifiers

PMID31801825
PMCPMC6956519

What OpenQuestion holds

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Registered trials

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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.