Evidence map›Paper›PMID 22364871›Full record

ReviewInternational review of cell and molecular biology2012

Cellular functions of tissue transglutaminase.

Maria V Nurminskaya, Alexey M Belkin

Open access · greenAbstract readReview
In one paragraph

Review in International review of cell and molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
131citing papers in PubMed, 1 pooled it
94.9field-weighted citation impact, top 1% 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

131 citing papers in PubMed, 1 synthesis or guideline pooled it, 235 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
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  11. Article
  12. Review
  13. Article
  14. Structural and mechanistic analysis of CaProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Review
  17. Sitting leg vasculopathy: potential adaptations beyond the endothelium.American journal of physiology. Heart and circulatory physiology · 2024
    Review
  18. Review
  19. Transglutaminase 2 in breast cancer metastasis and drug resistance.Frontiers in cell and developmental biology · 2024
    Review
  20. Review

71 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

2 authors at 2 institutions in 1 country.

Maria V NurminskayaDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Alexey M Belkin
University of Maryland, Baltimore · USUniversity of Maryland Marlene and Stewart Greenebaum Comprehensive Cancer Center

Funding

Molecular mechanisms of medial calcification: regulation by transglutaminase 2R01HL093305 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI NURMINSKAYA, MARIA · 2009 to 2012
$1.3M
Regulation of osteoblast maturation by transglutaminasesR56DK071920 · NIDDK · UNIVERSITY OF MARYLAND BALTIMORE · PI NURMINSKAYA, MARIA · 2010 to 2010
$225k
Transglutaminase 2 in cartilage formationR03AR057126 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI NURMINSKAYA, MARIA · 2009 to 2011
$222k
NHLBI NIH HHS HL093305NHLBI NIH HHS R01 HL093305NIAMS NIH HHS AR057126NIAMS NIH HHS R03 AR057126NIDDK NIH HHS DK071920NIDDK NIH HHS R56 DK071920NIGMS NIH HHS GM062865
6 · The paper itself

Abstract

Transglutaminase 2 (TG2 or tissue transglutaminase) is a highly complex multifunctional protein that acts as transglutaminase, GTPase/ATPase, protein disulfide isomerase, and protein kinase. Moreover, TG2 has many well-documented nonenzymatic functions that are based on its noncovalent interactions with multiple cellular proteins. A vast array of biochemical activities of TG2 accounts for its involvement in a variety of cellular processes, including adhesion, migration, growth, survival, apoptosis, differentiation, and extracellular matrix organization. In turn, the impact of TG2 on these processes implicates this protein in various physiological responses and pathological states, contributing to wound healing, inflammation, autoimmunity, neurodegeneration, vascular remodeling, tumor growth and metastasis, and tissue fibrosis. TG2 is ubiquitously expressed and is particularly abundant in endothelial cells, fibroblasts, osteoblasts, monocytes/macrophages, and smooth muscle cells. The protein is localized in multiple cellular compartments, including the nucleus, cytosol, mitochondria, endolysosomes, plasma membrane, and cell surface and extracellular matrix, where Ca(2+), nucleotides, nitric oxide, reactive oxygen species, membrane lipids, and distinct protein-protein interactions in the local microenvironment jointly regulate its activities. In this review, we discuss the complex biochemical activities and molecular interactions of TG2 in the context of diverse subcellular compartments and evaluate its wide ranging and cell type-specific biological functions and their regulation.

Indexed as

AnimalsApoptosisCell AdhesionCell CompartmentationCell DifferentiationCell EnlargementCell MovementCell SurvivalExtracellular MatrixGene Expression Regulation, EnzymologicGTP-Binding ProteinsHumansProtein Glutamine gamma Glutamyltransferase 2TransglutaminasesGTP-Binding ProteinsProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID22364871
PMCPMC3746560
OpenAlexW2193938114

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.