Evidence map›Paper›PMID 30422384›Full record

ArticleThe FEBS journal2019

Propeptide glycosylation and galectin-3 binding decrease proteolytic activation of human proMMP-9/progelatinase B.

Lise Boon, Estefania Ugarte-Berzal, Erik Martens, Jennifer Vandooren, Vasily Rybakin, Didier Colau, Monica Gordon-Alonso, Pierre van der Bruggen, Walter Stöcker, Christoph Becker-Pauly and 5 more

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. 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

15 authors at 7 institutions in 3 countries.

Lise BoonLaboratory of Immunobiology, Rega Institute for Medical Research, KU Leuven, Belgium.ORCID 0000-0001-9937-6793
Estefania Ugarte-BerzalLaboratory of Immunobiology, Rega Institute for Medical Research, KU Leuven, Belgium.ORCID 0000-0001-5182-6361
Erik MartensLaboratory of Immunobiology, Rega Institute for Medical Research, KU Leuven, Belgium.
Jennifer VandoorenLaboratory of Immunobiology, Rega Institute for Medical Research, KU Leuven, Belgium.ORCID 0000-0002-7157-3370
Vasily RybakinLaboratory of Immunobiology, Rega Institute for Medical Research, KU Leuven, Belgium.ORCID 0000-0002-5093-1757
Didier ColauLudwig Institute for Cancer Research, Brussels, Belgium.
Monica Gordon-AlonsoInstitut de Duve, UCLouvain, Brussels, Belgium.
Pierre van der BruggenInstitut de Duve, UCLouvain, Brussels, Belgium.
Walter StöckerInstitute of Molecular Physiology, Johannes Gutenberg University, Mainz, Germany.
Christoph Becker-PaulyBiochemical Institute, University of Kiel, Germany.
Peter WittersDepartment of Pediatrics, University Hospitals Leuven, KU Leuven, Belgium.
Eva MoravaDepartment of Clinical Genomics, Mayo Clinic, Rochester, ON, USA.
Jaak JaekenDepartment of Pediatrics, University Hospitals Leuven, KU Leuven, Belgium.
Paul ProostLaboratory of Molecular Immunology, Rega Institute for Medical Research, KU Leuven, Belgium.ORCID 0000-0002-0133-5545
Ghislain OpdenakkerLaboratory of Immunobiology, Rega Institute for Medical Research, KU Leuven, Belgium.ORCID 0000-0003-1714-2294
Rega Institute for Medical Research · BEde Duve Institute · BEKU Leuven · BEChristian-Albrechts-Universität zu Kiel · DEJohannes Gutenberg University Mainz · DELudwig Cancer Research · BEMayo Clinic in Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Matrix metalloproteinases (MMPs) are secreted as proenzymes, containing propeptides that interact with the catalytic zinc, thereby controlling MMP activation. The MMP-9 propeptide is unique in the MMP family because of its post-translational modification with an N-linked oligosaccharide. ProMMP-9 activation by MMP-3 occurs stepwise by cleavage of the propeptide in an aminoterminal (pro-AT) and carboxyterminal (pro-CT) peptide. We chemically synthesized aglycosyl pro-AT and pro-CT and purified recombinant glycosylated pro-AT

Indexed as

Amino Acid SequenceBlood ProteinsCase-Control StudiesCongenital Disorders of GlycosylationEnzyme ActivationEnzyme PrecursorsGalectin 3GalectinsGelatinasesGlycosylationHumansLeukocyte ElastaseMatrix Metalloproteinase 3Matrix Metalloproteinase 9ProteolysisBlood ProteinsEnzyme PrecursorsGalectin 3GalectinsGelatinasesLeukocyte ElastaseLGALS3 protein, humanMatrix Metalloproteinase 3Matrix Metalloproteinase 9MMP3 protein, humanMMP9 protein, humanprogelatinasegalectin-3matrix metalloproteinase-9N-linked glycosylationpropeptideproteolytic activation

Identifiers

PMID30422384
PMCPMC7379967
OpenAlexW2901223338

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.