Evidence map›Paper›PMID 22148750›Full record

ArticleBiochemistry2012

Post-translational modification of Cu/Zn superoxide dismutase under anaerobic conditions.

Jeffry M Leitch, Cissy X Li, J Allen Baron, Lauren M Matthews, Xiaohang Cao, P John Hart, Valeria C Culotta

Abstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

14 citing papers in PubMed, 33 citations in OpenAlex.

  1. Sod1 integrates oxygen availability to redox regulate NADPH production and the thiol redoxome.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Nitration of MnSOD in the Carotid Body and Adrenal Gland Induced by Chronic Intermittent Hypoxia.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2018
    Article
  8. A role for Candida albicans superoxide dismutase enzymes in glucose signaling.Biochemical and biophysical research communications · 2018
    Article
  9. Riboflavin transport and metabolism in humans.Journal of inherited metabolic disease · 2016
    Review
  10. Cu/Zn superoxide dismutase and the proton ATPase Pma1p of Saccharomyces cerevisiae.Biochemical and biophysical research communications · 2015
    Article
  11. Species-specific activation of Cu/Zn SOD by its CCS copper chaperone in the pathogenic yeast Candida albicans.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014
    Article
  12. Review
  13. Yeast copper-zinc superoxide dismutase can be activated in the absence of its copper chaperone.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013
    Article
  14. 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

7 authors at 2 institutions in 1 country.

Jeffry M LeitchDepartment of Biochemistry and Molecular Biology, Johns Hopkins University Bloomberg School of Public Health, Baltimore, Maryland 21205, United States.
Cissy X Li
J Allen Baron
Lauren M Matthews
Xiaohang Cao
P John Hart
Valeria C Culotta
Johns Hopkins University · USThe University of Texas Health Science Center at Houston · US

Funding

PILOT STUDY--ACID FOG, AN EXPERIMENTAL MODELP30ES003819 · NIEHS · JOHNS HOPKINS UNIVERSITY · PI GROOPMAN, JOHN D · 1985 to 2012
$22.6M
Traning Program in Environmental Health SciencesT32ES007141 · NIEHS · JOHNS HOPKINS UNIVERSITY · PI Marsha Wills-Karp · 1985 to 2026
$22.2M
TRAINING IN AREAS FUNDAMENTAL TO CANCER RESEARCHT32CA009110 · NCI · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J., WEERARATNA, ASHANI T · 1985 to 2025
$13.1M
Genetic Determinants of Oxygen ToxicityR37GM050016 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CULOTTA, VALERIA C · 2005 to 2014
$3.6M
GENETIC DETERMINANTS OF OXYGEN TOXICITYR01GM050016 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CULOTTA, VALERIA C · 1993 to 2018
$3.0M
X-RAY STUDIES OF SOD IN AMYOTROPHIC LATERAL SCLEROSISR01NS039112 · NINDS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI HART, PETER JOHN · 2000 to 2010
$2.7M
Activation Mechanism of Cu/Zn Superoxide DimutaseF32GM087904 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI LEITCH, JEFFREY · 2009 to 2010
$70k
NCI NIH HHS T32 CA009110NIEHS NIH HHS ES 07141NIEHS NIH HHS P30 ES003819NIEHS NIH HHS T32 ES007141NIGMS NIH HHS F32 GM 087904NIGMS NIH HHS F32 GM087904NIGMS NIH HHS GM 50016NIGMS NIH HHS R01 GM050016NIGMS NIH HHS R37 GM050016NINDS NIH HHS NS 39112NINDS NIH HHS R01 NS039112
6 · The paper itself

Abstract

In eukaryotic organisms, the largely cytosolic copper- and zinc-containing superoxide dismutase (Cu/Zn SOD) enzyme represents a key defense against reactive oxygen toxicity. Although much is known about the biology of this enzyme under aerobic conditions, less is understood regarding the effects of low oxygen levels on Cu/Zn SOD enzymes from diverse organisms. We show here that like bakers' yeast (Saccharomyces cerevisiae), adaptation of the multicellular Caenorhabditis elegans to growth at low oxygen levels involves strong downregulation of its Cu/Zn SOD. Much of this regulation occurs at the post-translational level where CCS-independent activation of Cu/Zn SOD is inhibited. Hypoxia inactivates the endogenous Cu/Zn SOD of C. elegans Cu/Zn SOD as well as a P144 mutant of S. cerevisiae Cu/Zn SOD (herein denoted Sod1p) that is independent of CCS. In our studies of S. cerevisiae Sod1p, we noted a post-translational modification to the inactive enzyme during hypoxia. Analysis of this modification by mass spectrometry revealed phosphorylation at serine 38. Serine 38 represents a putative proline-directed kinase target site located on a solvent-exposed loop that is positioned at one end of the Sod1p β-barrel, a region immediately adjacent to residues previously shown to influence CCS-dependent activation. Although phosphorylation of serine 38 is minimal when the Sod1p is abundantly active (e.g., high oxygen level), up to 50% of Sod1p can be phosphorylated when CCS activation of the enzyme is blocked, e.g., by hypoxia or low-copper conditions. Serine 38 phosphorylation can be a marker for inactive pools of Sod1p.

Indexed as

Protein Processing, Post-TranslationalAnaerobiosisAnimalsCaenorhabditis elegansCopperEnzyme ActivationModels, MolecularMolecular ChaperonesOxygenPhosphorylationProtein ConformationSaccharomyces cerevisiaeSerineSuperoxide DismutaseSuperoxide Dismutase-1ZincCopperMolecular ChaperonesOxygenSerineSuperoxide DismutaseSuperoxide Dismutase-1Zinc

Identifiers

PMID22148750
PMCPMC3264780
OpenAlexW1990184725

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.