Evidence map›Paper›PMID 11350930›Full record

ArticleThe EMBO journal2001

Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2.

U S Singh, M T Kunar, Y L Kao, K M Baker

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 88 citations in OpenAlex.

  1. The role of Rho GTPases in facial morphogenesis.Developmental dynamics : an official publication of the American Association of Anatomists · 2026
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  19. Diabetic complications in pregnancy: is resveratrol a solution?Experimental biology and medicine (Maywood, N.J.) · 2013
    Review
  20. Article
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 1 institution in 1 country.

U S SinghDivision of Molecular Cardiology, Cardiovascular Research Institute, The Texas A&M University System Health Science Center, College of Medicine, 1901 South 1st Street, Temple, TX 76504, USA. Usingh@medicine.tamu.edu
M T Kunar
Y L Kao
K M Baker
Texas A&M University System · US

Funding

ANGIOTENSIN II SIMULATED CARDIAC SIGNAL TRANSDUCTIONR01HL060529 · NHLBI · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI BAKER, KENNETH MELVIN · 1997 to 1999
–
NHLBI NIH HHS HL60529PHS HHS 58439
6 · The paper itself

Abstract

Transamidation is a post-translational modification of proteins mediated by tissue transglutaminase II (TGase), a GTP-binding protein, participating in signal transduction pathways as a non-conventional G-protein. Retinoic acid (RA), which is known to have a role in cell differentiation, is a potent activator of TGASE: The activation of TGase results in increased transamidation of RhoA, which is inhibited by monodansylcadaverine (MDC; an inhibitor of transglutaminase activity) and TGaseM (a TGase mutant lacking transglutaminase activity). Transamidated RhoA functions as a constitutively active G-protein, showing increased binding to its downstream target, RhoA-associated kinase-2 (ROCK-2). Upon binding to RhoA, ROCK-2 becomes autophosphorylated and demonstrates stimulated kinase activity. The RA-stimulated interaction between RhoA and ROCK-2 is blocked by MDC and TGaseM, indicating a role for transglutaminase activity in the interaction. Biochemical effects of TGase activation, coupled with the formation of stress fibers and focal adhesion complexes, are proposed to have a significant role in cell differentiation.

Indexed as

CytoskeletonEnzyme ActivationFocal AdhesionsGTP-Binding ProteinsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsProtein Glutamine gamma Glutamyltransferase 2Protein Serine-Threonine KinasesrhoA GTP-Binding Proteinrho-Associated KinasesTransglutaminasesTretinoinGTP-Binding ProteinsIntracellular Signaling Peptides and ProteinsProtein Glutamine gamma Glutamyltransferase 2Protein Serine-Threonine KinasesrhoA GTP-Binding Proteinrho-Associated KinasesTransglutaminasesTretinoin

Identifiers

PMID11350930
PMCPMC125450
OpenAlexW2039339016

What OpenQuestion holds

Textmetadata
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.