ArticleMethods in molecular biology (Clifton, N.J.)2025
Gelatin Zymography to Quantify Levels of MMP-2 and MMP-9 in Complex Biological Samples.
Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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.
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.
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Who cites it
3 citing papers in PubMed.
- Matrix Metalloproteinase-9 (MMP-9) in Psoriasis: Integrating Extracellular Matrix Remodeling, Neutrophil-Endothelial Crosstalk and Biomarker Evidence.Medical sciences (Basel, Switzerland) · 2026Review
- Pantothenic Acid Derivatives Modulate Oxidative Stress and Hepatic Fibrosis in Bile Duct Ligation-Induced Cholestatic Liver Injury.Pathophysiology : the official journal of the International Society for Pathophysiology · 2026Article
- Intravenous leiomyomatosis manifesting as a cardiac mass: a case report.Frontiers in cardiovascular medicine · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases associated with many disease states and aid in the degradation of the extracellular matrix (ECM). Matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) are gelatinases with many physiological functions. These proteases actively participate in many pathological states by cleaving the ECM and degrading other non-ECM substrates, such as tight junction proteins, cytokines and chemokines, growth factors, and adhesion molecules. Gelatin substrate zymography uses gelatin copolymerized in SDS-polyacrylamide gels to semi-quantitatively measure the enzymatic activity of gelatinases upon gel incubation in a developing buffer and subsequent gel staining. The study of MMP-2 and MMP-9 activity using gelatin substrate zymography is a simple and effective way to quantify MMP-2 and MMP-9 in a variety of samples. Here, we describe a protocol for detecting MMP-2 and MMP-9 using gelatin substrate zymography. We provide representative results using various sample types, including cell culture media, cell protein lysate protein, human and mouse plasma, and mouse brain protein lysate.
Indexed as
Identifiers
40261613What Socratic holds
Registered trials
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 Socratic graph.