Evidence map›Paper›PMID 31874171›Full record

ReviewAnalytical biochemistry2020

Substrates, inhibitors, and probes of mammalian transglutaminase 2.

Ruize Zhuang, Chaitan Khosla

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Analytical biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 42 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. Celiac disease: mechanisms and emerging therapeutics.Trends in pharmacological sciences · 2023
    Review
  14. Transglutaminase in Foods and Biotechnology.International journal of molecular sciences · 2023
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

2 authors at 1 institution in 1 country.

Ruize ZhuangDepartment of Chemical Engineering, Stanford University, Stanford, CA, USA.
Chaitan KhoslaDepartment of Chemical Engineering, Stanford University, Stanford, CA, USA; Department of Chemistry, Stanford University, Stanford, CA, USA; Stanford ChEM-H, Stanford University, Stanford, CA, USA. Electronic address: khosla@stanford.edu.
Stanford University · US

Funding

Role of Transglutaminase 2 in Celiac SprueR01DK063158 · NIDDK · STANFORD UNIVERSITY · PI CHAITAN KHOSLA · 2003 to 2026
$11.2M
NIDDK NIH HHS R01 DK063158
6 · The paper itself

Abstract

Transglutaminase 2 (TG2) is a ubiquitous but enigmatic mammalian protein to which a number of biological functions have been ascribed but not definitively proven. As a member of the transglutaminase family, TG2 can catalyze deamidation or alternatively transamidation of selected Gln residues in proteins and peptides. It is also known to harbor other enzymatic properties, including protein disulfide isomerase, GTP-dependent signal transduction, and ATP dependent protein kinase activity. Given its multifunctional chemistry, it is unsurprising that a long list of proteins from the mammalian proteome have been identified as substrates and/or binding partners; however, the biological relevance of none of these protein-protein interactions has been clarified as yet. Remarkably, the most definitive insights into the biology of TG2 stem from its pathophysiological role in gluten peptide deamidation in celiac disease. Meanwhile our understanding of TG2 chemistry has been leveraged to engineer a spectrum of inhibitors and other molecular probes of TG2 biology in vivo. This review summarizes our current knowledge of the enzymology and regulation of human TG2 with a focus on its physiological substrates as well as tool molecules whose engineering was inspired by their identities.

Indexed as

LigandsAnimalsBiocatalysisCeliac DiseaseGlutensGTP-Binding ProteinsHumansPeptidesProtein BindingProtein Glutamine gamma Glutamyltransferase 2TransglutaminasesGlutensGTP-Binding ProteinsLigandsPeptidesProtein Glutamine gamma Glutamyltransferase 2TransglutaminasesChemical biologyPost-translational modificationsTransglutaminase

Identifiers

PMID31874171
PMCPMC6948143
OpenAlexW2998637586

What OpenQuestion holds

Textmetadata
LicenceTDM
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.