Evidence map›Paper›PMID 11687497›Full record

ReviewAnnual review of cell and developmental biology2001

How matrix metalloproteinases regulate cell behavior.

M D Sternlicht, Z Werb

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of cell and developmental biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1,296 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
1,296citing papers in PubMed, 2 pooled it
59.6field-weighted citation impact, top 1% 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

1,296 citing papers in PubMed, 2 syntheses or guidelines pooled it, 3,914 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
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  12. Cerebrospinal fluid matrix-remodeling biomarkers in neonates with myelomeningocele: MMP-9, TIMP-1, and TGF-β1 expression.Child's nervous system : ChNS : official journal of the International Society for Pediatric Neurosurgery · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Residential Proximity to NPL Superfund Sites and High Particulate Matter Exposure Is Associated with Increased Likelihood of Triple-Negative Breast Cancer.Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology · 2026
    Article
  18. Matrix Metalloproteinase Inhibition in Melanoma.Experimental dermatology · 2026
    Review
  19. VaginalFrontiers in cellular and infection microbiology · 2026
    Article
  20. Review

1,236 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 1 institution in 1 country.

M D SternlichtDepartment of Anatomy, University of California, San Francisco, California 94143-0452, USA. sternli@itsa.ucsf.edu
Z Werb
University of California, San Francisco · US

Funding

Tissue and Outcomes CoreP50CA058207 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GRAY, JOE W. · 1992 to 2012
$32.7M
PROTEASES--TUMOR BIOLOGYP01CA072006 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WERB, ZENA · 1997 to 2007
$10.8M
MECHANISMS OF ANGIOGENESIS IN TRANSGENIC TUMORIGENESISR01CA037395 · NCI · CHILDREN'S HOSPITAL BOSTON · PI FOLKMAN, JUDAH · 1985 to 2004
$3.6M
MECHANISMS OF ANGIOGENESIS IN TRANSGENIC TUMORIGENESISR37CA037395 · NCI · CHILDREN'S HOSPITAL BOSTON · PI FOLKMAN, JUDAH · 1990 to 1999
–
NCI NIH HHS CA37395NCI NIH HHS CA58207NCI NIH HHS CA72006NCI NIH HHS P01 CA072006NCI NIH HHS P50 CA058207NCI NIH HHS R01 CA037395NCI NIH HHS R37 CA037395
6 · The paper itself

Abstract

The matrix metalloproteinases (MMPs) constitute a multigene family of over 25 secreted and cell surface enzymes that process or degrade numerous pericellular substrates. Their targets include other proteinases, proteinase inhibitors, clotting factors, chemotactic molecules, latent growth factors, growth factor-binding proteins, cell surface receptors, cell-cell adhesion molecules, and virtually all structural extracellular matrix proteins. Thus MMPs are able to regulate many biologic processes and are closely regulated themselves. We review recent advances that help to explain how MMPs work, how they are controlled, and how they influence biologic behavior. These advances shed light on how the structure and function of the MMPs are related and on how their transcription, secretion, activation, inhibition, localization, and clearance are controlled. MMPs participate in numerous normal and abnormal processes, and there are new insights into the key substrates and mechanisms responsible for regulating some of these processes in vivo. Our knowledge in the field of MMP biology is rapidly expanding, yet we still do not fully understand how these enzymes regulate most processes of development, homeostasis, and disease.

Indexed as

AnimalsBone and BonesCell CommunicationExtracellular MatrixExtracellular Matrix ProteinsHumansMatrix MetalloproteinasesNeoplasmsNeovascularization, PhysiologicProtein Processing, Post-TranslationalSignal TransductionTissue Inhibitor of MetalloproteinasesTranscription, GeneticExtracellular Matrix ProteinsMatrix MetalloproteinasesTissue Inhibitor of Metalloproteinases

Identifiers

PMID11687497
PMCPMC2792593
OpenAlexW2128049766

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.