Evidence map›Paper›PMID 24778599›Full record

ReviewTheScientificWorldJournal2014

Biological functionalities of transglutaminase 2 and the possibility of its compensation by other members of the transglutaminase family.

Benedict Onyekachi Odii, Peter Coussons

Open access · goldAbstract readReview
In one paragraph

Review in TheScientificWorldJournal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. The Role of Transglutaminase 2 in Cancer: An Update.International journal of molecular sciences · 2024
    Review
  7. Article
  8. Article
  9. Resolution of Eczema with Multivalent Peptides.JID innovations : skin science from molecules to population health · 2022
    Article
  10. Review
  11. Article
  12. Latent TGFβ complexes are transglutaminase cross-linked to fibrillin to facilitate TGFβ activation.Matrix biology : journal of the International Society for Matrix Biology · 2022
    Article
  13. Article
  14. Review
  15. Extracellular Matrix Remodeling in Chronic Liver Disease.Current tissue microenvironment reports · 2021
    Review
  16. Study of tumor transglutaminase 2 expression in gallbladder cancer -Annals of hepato-biliary-pancreatic surgery · 2020
    Article
  17. Article
  18. Review
  19. Article
  20. Article
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

2 authors at 1 institution in 1 country.

Benedict Onyekachi OdiiBiomedical Research Group, Department of Life Sciences, Faculty of Science & Technology, Anglia Ruskin University, East Road, Cambridge, CB1 1PT, UK.ORCID 0000-0001-6990-206X
Peter CoussonsBiomedical Research Group, Department of Life Sciences, Faculty of Science & Technology, Anglia Ruskin University, East Road, Cambridge, CB1 1PT, UK.
Anglia Ruskin University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transglutaminase 2 (TG2) is the most widely distributed and most abundantly expressed member of the transglutaminase family of enzymes, a group of intracellular and extracellular proteins that catalyze the Ca²⁺-dependent posttranslational modification of proteins. It is a unique member of the transglutaminase family owing to its specialized biochemical, structural and functional elements, ubiquitous tissue distribution and subcellular localization, and substrate specificity. The broad substrate specificity of TG2 and its flexible interaction with numerous other gene products may account for its multiple biological functions. In addition to the classic Ca²⁺-dependent transamidation of proteins, which is a hallmark of transglutaminase enzymes, additional Ca²⁺-independent enzymatic and nonenzymatic activities of TG2 have been identified. Many such activities have been directly or indirectly implicated in diverse cellular physiological events, including cell growth and differentiation, cell adhesion and morphology, extracellular matrix stabilization, wound healing, cellular development, receptor-mediated endocytosis, apoptosis, and disease pathology. Given the wide range of activities of the transglutaminase gene family it has been suggested that, in the absence of active versions of TG2, its function could be compensated for by other members of the transglutaminase family. It is in the light of this assertion that we review, herein, TG2 activities and the possibilities and premises for compensation for its absence.

Indexed as

AnimalsApoptosisAutoimmune DiseasesGTP-Binding ProteinsHumansInflammationIsoenzymesMice, KnockoutNeoplasmsProtein Glutamine gamma Glutamyltransferase 2Substrate SpecificityTransglutaminasesGTP-Binding ProteinsIsoenzymesProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID24778599
PMCPMC3981525
OpenAlexW2165301593

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.