Evidence map›Paper›PMID 26056585›Full record

ReviewMolecular and cellular therapies2014

Molecular mechanisms of tissue inhibitor of metalloproteinase 2 in the tumor microenvironment.

Taylor C Remillard, Gennady Bratslavsky, Sandra Jensen-Taubman, William G Stetler-Stevenson, Dimitra Bourboulia

Open access · greenAbstract readReview
In one paragraph

Review in Molecular and cellular therapies, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. TIMP-1 and its potential diagnostic and prognostic value in pulmonary diseases.Chinese medical journal pulmonary and critical care medicine · 2023
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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.

Taylor C RemillardDepartment of Urology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210 USA.
Gennady BratslavskyDepartment of Urology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210 USA.
Sandra Jensen-TaubmanRadiation Oncology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Advanced Technology Center, 8717 Grovemont Circle, Bethesda, MD 20892-4605 USA.
William G Stetler-StevensonRadiation Oncology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Advanced Technology Center, 8717 Grovemont Circle, Bethesda, MD 20892-4605 USA.
Dimitra BourbouliaDepartment of Urology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210 USA ; Department of Urology and Department of Biochemistry & Molecular Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210 USA.
SUNY Upstate Medical University · US

Funding

The Role of TIMPs in Cell Growth, Tumor Progression and MetastasisZIASC009179 · NCI · DIVISION OF CLINICAL SCIENCES - NCI · PI STETLER-STEVENSON, WILLIAM · 2009 to 2024
$9.7M
Intramural NIH HHS ZIA SC009179
6 · The paper itself

Abstract

There has been a recent paradigm shift in the way we target cancer, drawing a greater focus on the role of the tumor microenvironment (TME) in cancer development, progression and metastasis. Within the TME, there is a crosstalk in signaling and communication between the malignant cells and the surrounding extracellular matrix. Matrix metalloproteinases (MMPs) are zinc-dependent endoproteases that have the ability to degrade the matrix surrounding a tumor and mediate tumor growth, angiogenesis and metastatic disease. Their endogenous inhibitors, the Tissue Inhibitors of Metalloproteinases (TIMPs), primarily function to prevent degradation of the ECM via inhibition of MMPs. However, recent studies demonstrate that TIMP family members also possess MMP-independent functions. One TIMP member in particular, TIMP-2, has many distinct properties and functions, that occur independent of MMP inhibition, including the inhibition of tumor growth and reduction of angiogenesis through decreased endothelial cell proliferation and migration. The MMP-independent molecular mechanisms and signaling pathways elicited by TIMP-2 in the TME are described in this review.

Indexed as

AngiogenesisMatrix metalloproteinase (MMPs)Tissue inhibitor of metalloproteinase-2 (TIMP-2)Tumor microenvironment (TME)

Identifiers

PMID26056585
PMCPMC4452049
OpenAlexW2101600093

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.