Evidence map›Paper›PMID 25599938›Full record

ReviewMatrix biology : journal of the International Society for Matrix Biology

Matrix metalloproteinase interactions with collagen and elastin.

Steven R Van Doren

Open access · hybridAbstract readReview
In one paragraph

Review in Matrix biology : journal of the International Society for Matrix Biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 222 papers, 4 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
222citing papers in PubMed, 4 pooled it
7.8field-weighted citation impact, top 2% 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

222 citing papers in PubMed, 4 syntheses or guidelines pooled it, 441 citations in OpenAlex.

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162 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

1 author at 1 institution in 1 country.

Steven R Van DorenDepartment of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, USA. Electronic address: vandorens@missouri.edu.
University of Missouri · US

Funding

Mechanism &Inhibition of Collagenolytic ActivityR01CA098799 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI FIELDS, GREGG B · 2003 to 2017
$4.5M
TIMP/METALLOPROTEINASE STRUCTURE AND INTERACTIONSR01GM057289 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI VAN DOREN, STEVEN R · 1998 to 2014
$3.2M
NCI NIH HHS R01 CA098799NCI NIH HHS R01CA098799NIGMS NIH HHS R01 GM057289NIGMS NIH HHS R01GM057289
6 · The paper itself

Abstract

Most abundant in the extracellular matrix are collagens, joined by elastin that confers elastic recoil to the lung, aorta, and skin. These fibrils are highly resistant to proteolysis but can succumb to a minority of the matrix metalloproteinases (MMPs). Considerable inroads to understanding how such MMPs move to the susceptible sites in collagen and then unwind the triple helix of collagen monomers have been gained. The essential role in unwinding of the hemopexin-like domain of interstitial collagenases or the collagen binding domain of gelatinases is highlighted. Elastolysis is also facilitated by the collagen binding domain in the cases of MMP-2 and MMP-9, and remote exosites of the catalytic domain in the case of MMP-12.

Indexed as

Binding SitesCollagenElastinHumansMatrix MetalloproteinasesModels, MolecularProtein BindingProtein Structure, SecondaryProteolysisSubstrate SpecificityCollagenElastinMatrix MetalloproteinasesCollagen triple helixElastinExositeMatrix metalloproteinases

Identifiers

PMID25599938
PMCPMC4466143
OpenAlexW2100238813

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.