Evidence map›Paper›PMID 30409910›Full record

ArticleThe Journal of biological chemistry2019

Blocking the proteolytic activity of zymogen matriptase with antibody-based inhibitors.

Trine Tamberg, Zebin Hong, Daphné De Schepper, Signe Skovbjerg, Daniel M Dupont, Lars Vitved, Christine R Schar, Karsten Skjoedt, Lotte K Vogel, Jan K Jensen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. 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

10 authors at 3 institutions in 1 country.

Trine TambergDepartment of Molecular Biology and Genetics, Danish-Chinese Centre for Proteases and Cancer, Aarhus University, Gustav Wieds Vej 10C, Aarhus 8000, Denmark.
Zebin HongDepartment of Molecular Biology and Genetics, Danish-Chinese Centre for Proteases and Cancer, Aarhus University, Gustav Wieds Vej 10C, Aarhus 8000, Denmark.
Daphné De SchepperDepartment of Molecular Biology and Genetics, Danish-Chinese Centre for Proteases and Cancer, Aarhus University, Gustav Wieds Vej 10C, Aarhus 8000, Denmark.
Signe SkovbjergDepartment of Cellular and Molecular Medicine, University of Copenhagen, Copenhagen 1165, Denmark.
Daniel M DupontDepartment of Molecular Biology and Genetics, Danish-Chinese Centre for Proteases and Cancer, Aarhus University, Gustav Wieds Vej 10C, Aarhus 8000, Denmark.
Lars VitvedDepartment of Cancer and Inflammation, University of Southern Denmark, Odense 5230, Denmark.
Christine R ScharDepartment of Molecular Biology and Genetics, Danish-Chinese Centre for Proteases and Cancer, Aarhus University, Gustav Wieds Vej 10C, Aarhus 8000, Denmark.
Karsten SkjoedtDepartment of Cancer and Inflammation, University of Southern Denmark, Odense 5230, Denmark.
Lotte K VogelDepartment of Cellular and Molecular Medicine, University of Copenhagen, Copenhagen 1165, Denmark.
Jan K JensenDepartment of Molecular Biology and Genetics, Danish-Chinese Centre for Proteases and Cancer, Aarhus University, Gustav Wieds Vej 10C, Aarhus 8000, Denmark. Electronic address: jkj@mbg.au.dk.
Aarhus University · DKUniversity of Copenhagen · DKUniversity of Southern Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Matriptase is a member of the type-II transmembrane serine protease (TTSP) family and plays a crucial role in the development and maintenance of epithelial tissues. As all chymotrypsin-like serine proteases, matriptase is synthesized as a zymogen (proform), requiring a cleavage event for full activity. Recent studies suggest that the zymogen of matriptase possesses enough catalytic activity to not only facilitate autoactivation, but also carry out its

Indexed as

ProteolysisAntibodies, MonoclonalCrystallography, X-RayEnzyme PrecursorsHEK293 CellsHumansProtease InhibitorsProtein DomainsSerine EndopeptidasesAntibodies, MonoclonalEnzyme PrecursorsmatriptaseProtease InhibitorsSerine Endopeptidasescancer therapyenzyme inhibitorenzyme kineticsepitope mappingmatriptasemulti-domain proteinserine proteasesurface plasmon resonance (SPR)TTSPzymogen

Identifiers

PMID30409910
PMCPMC6322904
OpenAlexW2900106816

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.