Evidence map›Paper›PMID 30715061›Full record

ReviewMicromachines2018

Biocatalysis by Transglutaminases: A Review of Biotechnological Applications.

Maria Pia Savoca, Elisa Tonoli, Adeola G Atobatele, Elisabetta A M Verderio

Open access · goldAbstract readReview
In one paragraph

Review in Micromachines, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

38 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Enzymatic Encoding of Topology in an Intrinsically Disordered Single-Chain Protein.Angewandte Chemie (International ed. in English) · 2026
    Article
  3. Review
  4. The cross-linking activity of transglutaminase 2 drives α-Synuclein pathology in synucleinopathy models.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Smart responsiveFrontiers in bioengineering and biotechnology · 2024
    Review
  17. Review
  18. Article
  19. Review
  20. Review
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

4 authors at 1 institution in 1 country.

Maria Pia SavocaSchool of Science and Technology, Interdisciplinary Biomedical Research Centre, Nottingham Trent University, Nottingham NG11 8NS, UK. maria.savoca2016@my.ntu.ac.uk.
Elisa TonoliSchool of Science and Technology, Interdisciplinary Biomedical Research Centre, Nottingham Trent University, Nottingham NG11 8NS, UK. elisa.tonoli2015@my.ntu.ac.uk.ORCID 0000-0001-9774-1048
Adeola G AtobateleSchool of Science and Technology, Interdisciplinary Biomedical Research Centre, Nottingham Trent University, Nottingham NG11 8NS, UK. adeola.atobatele022014@my.ntu.ac.uk.
Elisabetta A M VerderioSchool of Science and Technology, Interdisciplinary Biomedical Research Centre, Nottingham Trent University, Nottingham NG11 8NS, UK. elisabetta.verderio-edwards@ntu.ac.uk.ORCID 0000-0001-9153-8997
Nottingham Trent University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biocatalytic activity of transglutaminases (TGs) leads to the synthesis of new covalent isopeptide bonds (crosslinks) between peptide-bound glutamine and lysine residues, but also the transamidation of primary amines to glutamine residues, which ultimately can result into protein polymerisation. Operating with a cysteine/histidine/aspartic acid (Cys/His/Asp) catalytic triad, TGs induce the post-translational modification of proteins at both physiological and pathological conditions (e.g., accumulation of matrices in tissue fibrosis). Because of the disparate biotechnological applications, this large family of protein-remodelling enzymes have stimulated an escalation of interest. In the past 50 years, both mammalian and microbial TGs polymerising activity has been exploited in the food industry for the improvement of aliments' quality, texture, and nutritive value, other than to enhance the food appearance and increased marketability. At the same time, the ability of TGs to crosslink extracellular matrix proteins, like collagen, as well as synthetic biopolymers, has led to multiple applications in biomedicine, such as the production of biocompatible scaffolds and hydrogels for tissue engineering and drug delivery, or DNA-protein bio-conjugation and antibody functionalisation. Here, we summarise the most recent advances in the field, focusing on the utilisation of TGs-mediated protein multimerisation in biotechnological and bioengineering applications.

Indexed as

biomedicinecrosslinkingfood industrypolymerisationtransglutaminases

Identifiers

PMID30715061
PMCPMC6265872
OpenAlexW2898821482

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.