Evidence map›Paper›PMID 22010840›Full record

ReviewAntioxidants & redox signaling2012

Regulation of cell physiology and pathology by protein S-glutathionylation: lessons learned from the cardiovascular system.

David Pimentel, Dagmar Johanna Haeussler, Reiko Matsui, Joseph Robert Burgoyne, Richard Alan Cohen, Markus Michael Bachschmid

Abstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

41 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Nitric Oxide: Physiological Functions, Delivery, and Biomedical Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  5. Review
  6. Review
  7. Article
  8. Increased ProteinInternational journal of molecular sciences · 2020
    Article
  9. Redox RegulationAntioxidants & redox signaling · 2020
    Review
  10. Review
  11. Endothelial cell-specific redox gene modulation inhibits angiogenesis but promotes B16F0 tumor growth in mice.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  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

6 authors at 1 institution in 1 country.

David PimentelMyocardial Biology Unit, Whitaker Cardiovascular Institute, Boston University School of Medicine, Massachusetts, USA.
Dagmar Johanna Haeussler
Reiko Matsui
Joseph Robert Burgoyne
Richard Alan Cohen
Markus Michael Bachschmid
Boston University · US

Funding

SIRT1, Polyphenols, and Endothelial OxidantsP01HL068758 · NHLBI · BOSTON MEDICAL CENTER · PI WALSH, KENNETH · 2003 to 2013
$14.1M
Redox Regulation of SERCA by Nitric OxideR01HL031607 · NHLBI · BOSTON UNIVERSITY MEDICAL CENTER HOSP · PI COHEN, RICHARD A · 1985 to 2013
$4.8M
Redox Regulation of p21ras in AngiogenesisR37HL104017 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COHEN, RICHARD A · 2010 to 2014
$2.2M
Ventricular Remodeling from H202 in Mechanical OverloadK08HL071563 · NHLBI · BOSTON MEDICAL CENTER · PI PIMENTEL, DAVID R · 2005 to 2009
$634k
NHLBI NIH HHS HHSN268201000031CNHLBI NIH HHS K08 HL71563NHLBI NIH HHS P01 HL 068758NHLBI NIH HHS R01 HL031607NHLBI NIH HHS R37 HL104017Wellcome Trust 085483/Z/08/Z
6 · The paper itself

Abstract

significanceReactive oxygen and nitrogen species contributing to homeostatic regulation and the pathogenesis of various cardiovascular diseases, including atherosclerosis, hypertension, endothelial dysfunction, and cardiac hypertrophy, is well established. The ability of oxidant species to mediate such effects is in part dependent on their ability to induce specific modifications on particular amino acids, which alter protein function leading to changes in cell signaling and function. The thiol containing amino acids, methionine and cysteine, are the only oxidized amino acids that undergo reduction by cellular enzymes and are, therefore, prime candidates in regulating physiological signaling. Various reports illustrate the significance of reversible oxidative modifications on cysteine thiols and their importance in modulating cardiovascular function and physiology. RECENT ADVANCES: The use of mass spectrometry, novel labeling techniques, and live cell imaging illustrate the emerging importance of reversible thiol modifications in cellular redox signaling and have advanced our analytical abilities. CRITICAL ISSUES: Distinguishing redox signaling from oxidative stress remains unclear. S-nitrosylation as a precursor of S-glutathionylation is controversial and needs further clarification. Subcellular distribution of glutathione (GSH) may play an important role in local regulation, and targeted tools need to be developed. Furthermore, cellular redundancies of thiol metabolism complicate analysis and interpretation. FUTURE DIRECTIONS: The development of novel pharmacological analogs that specifically target subcellular compartments of GSH to promote or prevent local protein S-glutathionylation as well as the establishment of conditional gene ablation and transgenic animal models are needed.

Indexed as

AnimalsCardiovascular SystemCellsGlutathioneHumansProteinsSulfhydryl CompoundsGlutathioneProteinsSulfhydryl Compounds

Identifiers

PMID22010840
PMCPMC3270052
OpenAlexW2003639259

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.