Evidence map›Paper›PMID 28903388›Full record

ArticleOncotarget2017

Cancer-associated mutations in the canonical cleavage site do not influence CD99 shedding by the metalloprotease meprin β but alter cell migration

Tillmann Bedau, Neele Schumacher, Florian Peters, Johannes Prox, Philipp Arnold, Tomas Koudelka, Ole Helm, Frederike Schmidt, Björn Rabe, Marlene Jentzsch and 5 more

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.1field-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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Meprin β induces activities of A disintegrin and metalloproteinases 9, 10, and 17 by specific prodomain cleavage.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  7. Review
  8. Article
  9. 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 1 institution in 1 country.

Tillmann BedauUnit for Degradomics of the Protease Web, Institute of Biochemistry, University of Kiel, 24118 Kiel, Germany.
Neele SchumacherUnit for Degradomics of the Protease Web, Institute of Biochemistry, University of Kiel, 24118 Kiel, Germany.
Florian PetersUnit for Degradomics of the Protease Web, Institute of Biochemistry, University of Kiel, 24118 Kiel, Germany.
Johannes ProxUnit for Degradomics of the Protease Web, Institute of Biochemistry, University of Kiel, 24118 Kiel, Germany.
Philipp ArnoldAnatomical Institute, University of Kiel, 24118 Kiel, Germany.
Tomas KoudelkaInstitute of Experimental Medicine, University of Kiel, 24118 Kiel, Germany.
Ole HelmInstitute for Experimental Tumor Research, University of Kiel, 24118 Kiel, Germany.
Frederike SchmidtUnit for Degradomics of the Protease Web, Institute of Biochemistry, University of Kiel, 24118 Kiel, Germany.
Björn RabeUnit for Degradomics of the Protease Web, Institute of Biochemistry, University of Kiel, 24118 Kiel, Germany.
Marlene JentzschInstitute of Clinical Molecular Biology, University of Kiel, 24118 Kiel, Germany.
Philip RosenstielInstitute of Clinical Molecular Biology, University of Kiel, 24118 Kiel, Germany.
Susanne SebensInstitute for Experimental Tumor Research, University of Kiel, 24118 Kiel, Germany.
Andreas TholeyInstitute of Experimental Medicine, University of Kiel, 24118 Kiel, Germany.
Stefan Rose-JohnUnit for Degradomics of the Protease Web, Institute of Biochemistry, University of Kiel, 24118 Kiel, Germany.
Christoph Becker-PaulyUnit for Degradomics of the Protease Web, Institute of Biochemistry, University of Kiel, 24118 Kiel, Germany.
Kiel University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transendothelial cell migration (TEM) is crucial for inflammation and metastasis. The adhesion molecule CD99 was shown to be important for correct immune cell extravasation and is highly expressed on certain cancer cells. Recently, we demonstrated that ectodomain shedding of CD99 by the metalloprotease meprin β promotes TEM

Indexed as

CD99inflammationlung cancermeprin βproteolytic shedding

Identifiers

PMID28903388
PMCPMC5589627
OpenAlexW2730881053

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.