Evidence map›Paper›PMID 36102354›Full record

ArticleThe FEBS journal2023

New links for meprin β within the protease web.

Vahap Canbay, Ulrich Auf dem Keller

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 87% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

2 authors at 1 institution in 1 country.

Vahap CanbayDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark.
Ulrich Auf dem KellerDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark.ORCID 0000-0002-3431-7415
Technical University of Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteases are organised in interconnected networks, together forming the protease web whose disturbance can have detrimental consequences for tissue homeostasis and response to environmental insults. Membrane-anchored sheddases are proteases that themselves can be released into the pericellular space by ectodomain shedding. Werny et al. have uncovered unexpected promiscuity in ectodomain shedding of meprin β, a metalloprotease with critical functions in inflammation and fibrosis. These findings suggest new links within complex proteolytic networks like the epidermal protease network with potential implications for skin homeostasis, inflammation and response to injury. Comment on: https://doi.org/10.1111/febs.16586.

Indexed as

MetalloendopeptidasesPeptide HydrolasesMetalloproteasesProteolysismeprin BMetalloendopeptidasesMetalloproteasesPeptide HydrolasesADAMectodomain sheddingepidermismeprinMT1-MMPprotease web

Identifiers

PMID36102354
PMCPMC10087362
OpenAlexW4295664999

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.