Evidence map›Paper›PMID 22732184›Full record

ReviewFree radical biology & medicine2012

Exploring the electrostatic repulsion model in the role of Sirt3 in directing MnSOD acetylation status and enzymatic activity.

Yueming Zhu, Seong-Hoon Park, Ozkan Ozden, Hyun-Seok Kim, Haiyan Jiang, Athanassios Vassilopoulos, Douglas R Spitz, David Gius

Open access · greenAbstract readReview
In one paragraph

Review in Free radical biology & medicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

38 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Mitochondrial Management of Reactive Oxygen Species.Antioxidants (Basel, Switzerland) · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. 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

8 authors at 3 institutions in 2 countries.

Yueming ZhuDepartment of Cancer Biology, and Vanderbilt University Medical Center, Vanderbilt University, Nashville, TN 37232, USA.
Seong-Hoon Park
Ozkan Ozden
Hyun-Seok Kim
Haiyan Jiang
Athanassios Vassilopoulos
Douglas R Spitz
David Gius
Vanderbilt University Medical Center · USEwha Womans University · KRUniversity of Iowa · US

Funding

Viral VectorP30CA086862 · NCI · UNIVERSITY OF IOWA · PI Mark E Burkard · 2000 to 2026
$70.0M
Loss of mtSIRT3, Decreased MnSOD Activity, and IR Induced Genomic InstabilityR01CA152601 · NCI · VANDERBILT UNIVERSITY · PI BONINI, MARCELO G. · 2010 to 2019
$3.5M
ROS and HIFa as molecular targets for chemoprevention in Sirt3 -/- breast cancersR01CA168292 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GIUS, DAVID · 2012 to 2016
$1.9M
SIRT3 is a Mitochondrial Tumor Suppressor in ER/PR Positive Mammary TumorsR01CA152799 · NCI · VANDERBILT UNIVERSITY · PI GIUS, DAVID · 2011 to 2015
$1.6M
The Use of 2-Deoxyglucose in Head and Neck Cancer TherapyR01CA133114 · NCI · UNIVERSITY OF IOWA · PI SPITZ, DOUGLAS ROBERT · 2009 to 2013
$1.5M
NCI NIH HHS 1R01CA152601-01NCI NIH HHS 1R01CA152799-01A1NCI NIH HHS P30 CA086862NCI NIH HHS P30CA086862NCI NIH HHS R01 CA133114NCI NIH HHS R01CA133114NCI NIH HHS R01 CA152601NCI NIH HHS R01 CA152799NCI NIH HHS R01 CA168292
6 · The paper itself

Abstract

Mitochondrial oxidative metabolism is the major site of ATP production as well as a significant source of reactive oxygen species (ROS) that can cause damage to critical biomolecules. It is well known that mitochondrial enzymes that scavenge ROS are targeted by stress responsive proteins to maintain the fidelity of mitochondrial function. Manganese superoxide dismutase (MnSOD) is a primary mitochondrial ROS scavenging enzyme, and in 1983 Irwin Fridovich proposed an elegant chemical mechanism/model whereby acetylation directs MnSOD enzymatic activity. He christened it the "electrostatic repulsion model." However, the biochemical and genetic mechanism(s) determining how acetylation directs activity and the reasons behind the evolutionarily conserved need for several layers of transcriptional and posttranslational MnSOD regulation remain unknown. In this regard, we and others have shown that MnSOD is regulated, at least in part, by the deacetylation of specific conserved lysines in a reaction catalyzed by the mitochondrial sirtuin, Sirt3. We speculate that the regulation of MnSOD activity by lysine acetylation via an electrostatic repulsion mechanism is a conserved and critical aspect of MnSOD regulation necessary to maintain mitochondrial homeostasis.

Indexed as

AcetylationAnimalsElectrochemistryHomeostasisHumansMitochondriaProtein BindingProtein Processing, Post-TranslationalReactive Oxygen SpeciesSignal TransductionSirtuin 3Superoxide DismutaseReactive Oxygen SpeciesSIRT3 protein, humanSirtuin 3Superoxide Dismutase

Identifiers

PMID22732184
PMCPMC3418453
OpenAlexW2066375771

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.