Evidence map›Paper›PMID 22657737›Full record

ReviewAntioxidants & redox signaling2013

Redox regulation of Ras and Rho GTPases: mechanism and function.

Lauren Mitchell, G Aaron Hobbs, Amir Aghajanian, Sharon L Campbell

Abstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

53 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Redox-sensitive small GTPase H-Ras in murine astrocytes, anRedox report : communications in free radical research · 2022
    Article
  10. Article
  11. Post-translational modification of RAS proteins.Current opinion in structural biology · 2021
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

4 authors at 1 institution in 1 country.

Lauren MitchellDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.
G Aaron Hobbs
Amir Aghajanian
Sharon L Campbell
University of North Carolina at Chapel Hill · US

Funding

MOLECULAR AND CELLULAR BIOPHYSICS TRAINING PROGRAMT32GM008570 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KUHLMAN, BRIAN A, SLEP, KEVIN C · 1995 to 2022
$5.1M
Redox Regulation of Ras and Ras-Related GTPasesR01GM075431 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CAMPBELL, SHARON L · 2005 to 2008
$1.1M
Redox Regulation of RhoA and Modulation of Vascular PermeabilityF30HL094063 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI AGHAJANIAN, AMIR · 2009 to 2012
$123k
NHLBI NIH HHS F30 HL094063NIGMS NIH HHS GM075431NIGMS NIH HHS T32 GM008570PHS HHS RCA089614B
6 · The paper itself

Abstract

significanceOxidation and reduction events are critical to physiological and pathological processes and are highly regulated. Herein, we present evidence for the role of Ras and Rho GTPases in controlling these events and the unique underlying mechanisms. Evidence for redox regulation of Ras GTPases that contain a redox-sensitive cysteine (X) in the conserved NKXD motif is presented, and a growing consensus supports regulation by a thiyl radical-mediated oxidation mechanism. We also discuss the debate within the literature regarding whether 2e(-) oxidation mechanisms also regulate Ras GTPase activity. RECENT ADVANCES: We examine the increasing in vitro and cell-based data supporting oxidant-mediated activation of Rho GTPases that contain a redox-sensitive cysteine at the end of the conserved phosphoryl-binding loop (p-loop) motif (GXXXXG[S/T]C). While this motif is distinct from Ras, these data suggest a similar 1e(-) oxidation-mediated activation mechanism. CRITICAL ISSUES: We also review the data showing that the unique p-loop placement of the redox-sensitive cysteine in Rho GTPases supports activation by 2e(-) cysteine oxidation. Finally, we examine the role that Ras and Rho GTPases play in controlling key oxidant-regulating enzymes in the cell, and we speculate on a feedback mechanism. FUTURE DIRECTIONS: Given that these GTPases and redox-regulating enzymes are involved in multiple physiological and pathological processes, we discuss future experiments that may clarify the interplay between them.

Indexed as

Amino Acid MotifsAnimalsCatalytic DomainFree RadicalsGene Expression Regulation, EnzymologicGuanosine TriphosphateHumansModels, MolecularNADPH OxidasesNitric Oxide SynthaseOxidation-ReductionProtein Bindingras Proteinsrho GTP-Binding ProteinsSuperoxide DismutaseFree RadicalsGuanosine TriphosphateNADPH OxidasesNitric Oxide Synthaseras Proteinsrho GTP-Binding ProteinsSuperoxide Dismutase

Identifiers

PMID22657737
PMCPMC3518547
OpenAlexW2032040152

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.