Evidence map›Paper›PMID 40261623›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

Zymography: A Simple and Powerful Tool for the Assessment of MMP-2 and MMP-9 in Pathological Conditions.

Joseph George

Abstract read
PubMed Publisher
In one paragraph

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. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Joseph GeorgeDepartment of Hepatology, Kanazawa Medical University, Uchinada, Ishikawa, Japan. georgej@kanazawa-med.ac.jp.ORCID https://orcid.org/0000-0001-5354-7884

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Zymography is an electrophoretic technique to measure the proteolytic activity of native enzymes on a nonreducing sodium dodecyl sulfate polyacrylamide gel. It is a simple and powerful tool to assess the amount of various proteases present in both physiological and pathological conditions. The concerned protease degrades the protein substrate that is incorporated with the gel and resolves during the incubation period. Staining with Coomassie brilliant blue (CBB) reveals the sites of proteolysis as clear white bands. The intensity and area of the bands are linearly related to the amount of protease present in the loaded sample. Matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9), also known as gelatinases, have the indigenous property to digest gelatin and several other protein molecules present in the extracellular matrix. Here, we describe the detailed protocols and methods of zymography, with a special emphasis on the determination of gelatinases present in conditioned culture media and tissue extracts.

Indexed as

Electrophoresis, Polyacrylamide GelEnzyme AssaysMatrix Metalloproteinase 2Matrix Metalloproteinase 9AnimalsCulture Media, ConditionedGelatinHumansProteolysisRosaniline DyesCulture Media, ConditionedGelatinMatrix Metalloproteinase 2Matrix Metalloproteinase 9Rosaniline DyesGelatinasesMatrix metalloproteinasesMMP-2MMP-9Polyacrylamide gel electrophoresisZymography

Identifiers

PMID40261623

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.