Evidence map›Paper›PMID 12366374›Full record

ReviewThe Biochemical journal2002

Transglutaminases: nature's biological glues.

Martin Griffin, Rita Casadio, Carlo M Bergamini

Open access · bronzeAbstract readReview
In one paragraph

Review in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 295 papers.

0numbers the graph read from it
0cells of the map it votes in
295citing papers in PubMed
27.6field-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

295 citing papers in PubMed, 1,031 citations in OpenAlex.

  1. Trial
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  11. Piceatannol Attenuates Benzo[Journal of agricultural and food chemistry · 2025
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  14. Metabolic profiles of meconium in preeclamptic and normotensive pregnancies.Metabolomics : Official journal of the Metabolomic Society · 2025
    Article
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235 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

3 authors at 2 institutions in 1 country.

Martin GriffinDepartment of Life Sciences, Nottingham Trent University, Nottingham, U.K.
Rita Casadio
Carlo M Bergamini
University of Bologna · ITUniversity of Ferrara · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transglutaminases (Tgases) are a widely distributed group of enzymes that catalyse the post-translational modification of proteins by the formation of isopeptide bonds. This occurs either through protein cross-linking via epsilon-(gamma-glutamyl)lysine bonds or through incorporation of primary amines at selected peptide-bound glutamine residues. The cross-linked products, often of high molecular mass, are highly resistant to mechanical challenge and proteolytic degradation, and their accumulation is found in a number of tissues and processes where such properties are important, including skin, hair, blood clotting and wound healing. However, deregulation of enzyme activity generally associated with major disruptions in cellular homoeostatic mechanisms has resulted in these enzymes contributing to a number of human diseases, including chronic neurodegeneration, neoplastic diseases, autoimmune diseases, diseases involving progressive tissue fibrosis and diseases related to the epidermis of the skin. In the present review we detail the structural and regulatory features important in mammalian Tgases, with particular focus on the ubiquitous type 2 tissue enzyme. Physiological roles and substrates are discussed with a view to increasing and understanding the pathogenesis of the diseases associated with transglutaminases. Moreover the ability of these enzymes to modify proteins and act as biological glues has not gone unnoticed by the commercial sector. As a consequence, we have included some of the present and future biotechnological applications of this increasingly important group of enzymes.

Indexed as

AnimalsAutoimmune DiseasesBiotechnologyCeliac DiseaseCell DeathEnzyme StabilityExtracellular MatrixGTP-Binding ProteinsHumansInflammationNerve DegenerationProtein ConformationProtein Glutamine gamma Glutamyltransferase 2Protein Processing, Post-TranslationalTransglutaminasesWounds and InjuriesGTP-Binding ProteinsProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID12366374
PMCPMC1223021
OpenAlexW2067403820

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.