Evidence map›Paper›PMID 20964734›Full record

ReviewJournal of internal medicine2010

Type 2 transglutaminase in Huntington's disease: a double-edged sword with clinical potential.

P G Mastroberardino, M Piacentini

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of internal medicine, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Autophagic-lysosomal dysregulation downstream of cathepsin B inactivation in human skin fibroblasts exposed to UVA.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2012
    Article
  13. Cellular functions of tissue transglutaminase.International review of cell and molecular biology · 2012
    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 2 institutions in 3 countries.

P G MastroberardinoDepartment of Genetics, Erasmus MC, Rotterdam, The Netherlands.
M Piacentini
Erasmus MC · NLIstituto Nazionale per le Malattie Infettive Lazzaro Spallanzani · IT

Funding

Oxidative modification of brain proteins in pesticide intoxicationK99ES016352 · NIEHS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MASTROBERARDINO, PIER GIORGIO · 2007 to 2009
$270k
NIEHS NIH HHS K99 ES016352NIEHS NIH HHS K99-ES016352Telethon GGP06254
6 · The paper itself

Abstract

Huntington's disease (HD) is a dominant genetic neurodegenerative disorder. The pathology affects principally neurons in the basal ganglia circuits and terminates invariably in death. There is compelling necessity for safe and effective therapeutic strategies to arrest, or even retard the progression of the pathogenesis. Recent findings indicate the autophagy-lysosome systems as appealing targets for pharmacological intervention. Autophagy exerts a critical role in controlling neuronal protein homeostasis, which is perturbed in HD, and is compromised in the pathogenesis of several neurodegenerative diseases. Type 2 transglutaminase (TG2) plays an important role both in apoptosis and autophagy regulation, and accumulates at high levels in cells under stressful conditions. TG2 inhibition, achieved either via drug treatments or genetic approaches, has been shown to be beneficial for the treatment of HD in animal models. In this review we will discuss the relevance of TG2 to the pathogenesis of HD, in an effort to define novel therapeutic avenues.

Indexed as

AnimalsAutophagyCell DeathGTP-Binding ProteinsHumansHuntington DiseaseMiceMitochondriaModels, AnimalProtein Glutamine gamma Glutamyltransferase 2TransglutaminasesGTP-Binding ProteinsProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID20964734
PMCPMC3073231
OpenAlexW1801450666

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.