Evidence map›Paper›PMID 29362136›Full record

ReviewDrug discovery today2018

The diamond anniversary of tissue transglutaminase: a protein of many talents.

William P Katt, Marc A Antonyak, Richard A Cerione

Abstract readReview
In one paragraph

Review in Drug discovery today, 2018. 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
–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

27 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
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  5. Review
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  11. Article
  12. Article
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  15. Article
  16. 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
  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

3 authors.

William P KattDepartment of Molecular Medicine, Cornell University, NY, USA.
Marc A AntonyakDepartment of Molecular Medicine, Cornell University, NY, USA.
Richard A CerioneDepartment of Molecular Medicine, Cornell University, NY, USA; Department of Chemistry and Chemical Biology, Cornell University, NY, USA. Electronic address: rac1@cornell.edu.

Funding

The unique roles of the GTP-binding/protein crosslinking enzyme transglutaminase-2 and signaling partners in aggressive cancersR01CA201402 · NCI · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2016 to 2024
$4.3M
NCI NIH HHS R01 CA201402
6 · The paper itself

Abstract

Tissue transglutaminase (tTG) is capable of binding and hydrolyzing GTP, as well as catalyzing an enzymatic transamidation reaction that crosslinks primary amines to glutamine residues. tTG adopts two vastly different conformations, depending on whether it is functioning as a GTP-binding protein or a crosslinking enzyme. It has been shown to have important roles in several different aspects of cancer progression, making it an attractive target for therapeutic intervention. Here, we highlight many of the major findings involving tTG since its discovery 60 years ago, and describe recent drug discovery efforts that target specific activities or conformations of this unique protein.

Indexed as

AminesAnimalsDisease ProgressionGlutamineGTP-Binding ProteinsHumansNeoplasmsTransglutaminasesAminesGlutamineGTP-Binding ProteinsTransglutaminases

Identifiers

PMID29362136
PMCPMC5864117

What Socratic 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 Socratic graph.