Evidence map›Paper›PMID 17702616›Full record

ReviewSeminars in cell & developmental biology2008

Membrane type 1-matrix metalloproteinase: substrate diversity in pericellular proteolysis.

Maria V Barbolina, M Sharon Stack

Open access · greenAbstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

76 citing papers in PubMed, 143 citations in OpenAlex.

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  15. Matrix metalloproteinase collagenolysis in health and disease.Biochimica et biophysica acta. Molecular cell research · 2017
    Review
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16 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Maria V BarbolinaDepartment of Chemical and Biological Engineering, Northwestern University, Evanston, IL 60208, USA.
M Sharon Stack
Northwestern University · USUniversity of Missouri Hospital · US

Funding

REGULATION OF OVARIAN CARCINOMA PROTEINASESR01CA086984 · NCI · UNIVERSITY OF NOTRE DAME · PI STACK, MARY SHARON · 2000 to 2014
$3.8M
NCI NIH HHS R01 CA086984NCI NIH HHS R01CA86984
6 · The paper itself

Abstract

Enzymes in the matrix metalloproteinase (MMP) family have been linked to key events in developmental biology for almost 50 years. Biochemical, cellular and in vivo analyses have established that pericellular proteolysis contributes to numerous aspects of ontogeny including ovulation, fertilization, implantation, cellular migration, tissue remodeling and repair. Surface anchoring of proteinase activity provides spatial restrictions on substrate targeting. This review will utilize membrane type 1 MMP (MT1-MMP) as an example to highlight substrate diversity in pericellular proteolysis catalyzed by a membrane anchored MMP.

Indexed as

Protein Processing, Post-TranslationalAnimalsCell Adhesion MoleculesExtracellular MatrixExtracellular SpaceHumansMatrix Metalloproteinase 14Membrane GlycoproteinsModels, BiologicalProteoglycansSubstrate SpecificityCell Adhesion MoleculesMatrix Metalloproteinase 14Membrane GlycoproteinsProteoglycans

Identifiers

PMID17702616
PMCPMC2685078
OpenAlexW2007724842

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.