Evidence map›Paper›PMID 28442379›Full record

ReviewBiochimica et biophysica acta. Molecular cell research2017

Peripheral membrane associations of matrix metalloproteinases.

Steven R Van Doren, Tara C Marcink, Rama K Koppisetti, Alexander Jurkevich, Yan G Fulcher

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular cell research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. High-Resolution Relaxometry for Fragment Screening.Journal of medicinal chemistry · 2026
    Article
  2. Spider venom phospholipase D toxin structure: Interfacial binding site, mechanism, activation, and head group preference.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Heparan Sulfate Proteoglycan Signaling in Tumor Microenvironment.International journal of molecular sciences · 2020
    Review
  10. Article
  11. Article
  12. Estrogen Effects on Wound Healing.International journal of molecular sciences · 2017
    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

5 authors at 1 institution in 1 country.

Steven R Van DorenDepartment of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, United States. Electronic address: vandorens@missouri.edu.
Tara C MarcinkDepartment of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, United States.
Rama K KoppisettiDepartment of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, United States.
Alexander JurkevichMolecular Cytology Core, University of Missouri, 120 Bond Life Sciences Center, Columbia, 65211, United States.
Yan G FulcherDepartment of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, United States.
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
800 MHZ SPECTROMETER FOR BIOMOLECULAR NMR: STRUCTURAL BIOLOGYS10RR022341 · NCRR · UNIVERSITY OF MISSOURI-COLUMBIA · PI VAN DOREN, STEVEN R · 2006 to 2006
$500k
NCI NIH HHS R01 CA098799NCRR NIH HHS S10 RR022341NIGMS NIH HHS R01 GM057289
6 · The paper itself

Abstract

Water soluble matrix metalloproteinases (MMPs) have been regarded as diffusing freely in the extracellular matrix. Yet multiple MMPs are also observed at cell surfaces. Their membrane-proximal activities include sheddase activities, collagenolysis, bacterial killing, and intracellular trafficking reaching as far as the nucleus. The catalytic domains of MMP-7 and MMP-12 bind bilayers peripherally, each in two different orientations, by presenting positive charges and a few hydrophobic groups to the surface. Related peripheral membrane associations are predicted for other soluble MMPs. The peripheral membrane associations may support pericellular proteolysis and endocytosis. The isolated soluble domains of MT1-MMP can also associate with membranes. NMR assays suggest transient association of the hemopexin-like domains of MT1-MMP and MMP-12 with lipid bilayers. Peripheral association of soluble MMP domains with bilayers or heparin sulfate proteoglycans probably concentrates them near the membrane. This could increase the probability of forming complexes with membrane-associated proteins, such as those targeted for proteolysis. This article is part of a Special Issue entitled: Matrix Metalloproteinases edited by Rafael Fridman.

Indexed as

ProteolysisAnimalsCell MembraneHeparinHumansMatrix Metalloproteinase 12Matrix Metalloproteinase 14Matrix Metalloproteinase 7Nuclear Magnetic Resonance, BiomolecularProtein DomainsProteoglycansHeparinheparin proteoglycanMatrix Metalloproteinase 12Matrix Metalloproteinase 14Matrix Metalloproteinase 7MMP12 protein, humanMMP14 protein, humanMMP7 protein, humanProteoglycansCompartmentalizationMembrane recognitionMembrane traffickingPeripheral membrane proteinProteaseSheddase

Identifiers

PMID28442379
PMCPMC5605405
OpenAlexW2605560387

What OpenQuestion holds

Textmetadata
LicenceTDM
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.