Evidence map›Paper›PMID 22015769›Full record

ReviewBiochimica et biophysica acta2012

Transglutaminase 2: a molecular Swiss army knife.

Soner Gundemir, Gozde Colak, Janusz Tucholski, Gail V W Johnson

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 141 papers.

0numbers the graph read from it
0cells of the map it votes in
141citing papers in PubMed
9.5field-weighted citation impact, top 2% 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

141 citing papers in PubMed, 238 citations in OpenAlex.

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81 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Soner GundemirDepartment of Pharmacology, University of Rochester, 601 Elmwood Ave., Rochester, NY 14642, USA.
Gozde Colak
Janusz Tucholski
Gail V W Johnson
University of Rochester · USUniversity of Alabama at Birmingham · US

Funding

The attenuation of ischemic injury by transglutaminase 2R01NS065825 · NINDS · UNIVERSITY OF ROCHESTER · PI JOHNSON, GAIL V. W. · 2011 to 2015
$1.8M
TISSUE TRANSGLUTAMINASE--REGULATION AND DYSREGULATIONR01AG012396 · NIA · UNIVERSITY OF ROCHESTER · PI JOHNSON, GAIL V. W. · 1994 to 2006
$1.6M
NIA NIH HHS AG012396NIA NIH HHS R01 AG012396NINDS NIH HHS NS065825NINDS NIH HHS R01 NS065825
6 · The paper itself

Abstract

Transglutaminase 2 (TG2) is the most widely distributed member of the transglutaminase family with almost all cell types in the body expressing TG2 to varying extents. In addition to being widely expressed, TG2 is an extremely versatile protein exhibiting transamidating, protein disulphide isomerase and guanine and adenine nucleotide binding and hydrolyzing activities. TG2 can also act as a protein scaffold or linker. This unique protein also undergoes extreme conformational changes and exhibits localization diversity. Being mainly a cytosolic protein; it is also found in the nucleus, associated with the cell membrane (inner and outer side) and with the mitochondria, and also in the extracellular matrix. These different activities, conformations and localization need to be carefully considered while assessing the role of TG2 in physiological and pathological processes. For example, it is becoming evident that the role of TG2 in cell death processes is dependent upon the cell type, stimuli, subcellular localization and conformational state of the protein. In this review we discuss in depth the conformational and functional diversity of TG2 in the context of its role in numerous cellular processes. In particular, we have highlighted how differential localization, conformation and activities of TG2 may distinctly mediate cell death processes.

Indexed as

AnimalsCatalytic DomainCell ProliferationCell SurvivalGene DuplicationGTP-Binding ProteinsGTP PhosphohydrolasesHumansModels, MolecularProtein ConformationProtein Glutamine gamma Glutamyltransferase 2Structure-Activity RelationshipTranscription, GeneticTransglutaminasesGTP-Binding ProteinsGTP PhosphohydrolasesProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID22015769
PMCPMC3265640
OpenAlexW2221930001

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.