Evidence map›Paper›PMID 28533431›Full record

ArticleThe Journal of biological chemistry2017

Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site.

Morgan M Fetherolf, Stefanie D Boyd, Alexander B Taylor, Hee Jong Kim, James A Wohlschlegel, Ninian J Blackburn, P John Hart, Dennis R Winge, Duane D Winkler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
5.8field-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

41 citing papers in PubMed, 1 synthesis or guideline pooled it, 63 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. From hemocuprein to CSRP: the many faces of Cu/Zn superoxide dismutase.Metallomics : integrated biometal science · 2026
    Review
  5. Article
  6. Article
  7. Pathogenic RBiochemistry · 2024
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Evaluation of ZnMolecules (Basel, Switzerland) · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Copper metabolism in Saccharomyces cerevisiae: an update.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2021
    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

9 authors at 5 institutions in 1 country.

Morgan M FetherolfDepartment of Medicine, University of Utah Health Sciences Center School of Medicine, Salt Lake City, Utah 84132-2408; Department of Biochemistry, University of Utah, Salt Lake City, Utah 84112-5650.
Stefanie D BoydDepartment of Biological Sciences, University of Texas at Dallas, Richardson, Texas 75080.
Alexander B TaylorDepartment of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78229; X-ray Crystallography Core Laboratory, University of Texas Health Science Center, San Antonio, Texas 78229.
Hee Jong KimDepartment of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095.
James A WohlschlegelDepartment of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095.
Ninian J BlackburnInstitute of Environmental Health, Oregon Health and Science University, Portland, Oregon 97239.
P John HartDepartment of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78229; X-ray Crystallography Core Laboratory, University of Texas Health Science Center, San Antonio, Texas 78229; Geriatric Research, Education, and Clinical Center, Department of Veterans Affairs, South Texas Veterans Health Care System, University of Texas Health Science Center, San Antonio, Texas 78229.
Dennis R WingeDepartment of Medicine, University of Utah Health Sciences Center School of Medicine, Salt Lake City, Utah 84132-2408; Department of Biochemistry, University of Utah, Salt Lake City, Utah 84112-5650.
Duane D WinklerDepartment of Biological Sciences, University of Texas at Dallas, Richardson, Texas 75080. Electronic address: duane.winkler@utdallas.edu.
The University of Texas at Dallas · USThe University of Texas Health Science Center at San Antonio · USUniversity of California, Los Angeles · USUniversity of Utah · USOregon Health & Science University · US

Funding

TISSUE CULTURE---COREP30CA054174 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Lei Zheng · 1991 to 2026
$59.1M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Proteolytic Control of Iron Metabolism by the Ubiquitin Ligase FBXL5R01GM089778 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WOHLSCHLEGEL, JAMES AKIRA · 2010 to 2023
$4.0M
X-RAY SPECTROSCOPIC STUDIES ON HEME-COPPER OXIDASESR01GM054803 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI BLACKBURN, NINIAN J · 1997 to 2015
$3.2M
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
Succinate Dehydrogenase: Biogenesis and Role in DiseaseR01GM110755 · NIGMS · UNIVERSITY OF UTAH · PI WINGE, DENNIS R. · 2014 to 2021
$2.3M
Tracking Metal Flux Through a Pathogenic Export ComplexR01GM123725 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI BLACKBURN, NINIAN J · 2017 to 2020
$1.5M
Molecular Mechanisms of Sod1 Maturation ProcessesR01GM120252 · NIGMS · UNIVERSITY OF TEXAS DALLAS · PI WINKLER, DUANE DAVID · 2016 to 2020
$1.3M
Biogenesis of Extramitochondrial Iron-Sulfur Proteins in EukaryotesR01GM112763 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WOHLSCHLEGEL, JAMES AKIRA · 2015 to 2018
$982k
The Intron Debranching Enzyme (Dbr1) in Amyotrophic Lateral SclerosisI01BX002580 · VA · SOUTH TEXAS VETERANS HEALTH CARE SYSTEM · PI HART, PETER JOHN · 2015 to 2018
–
BLRD VA I01 BX002580NCI NIH HHS P30 CA054174NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM054803NIGMS NIH HHS R01 GM089778NIGMS NIH HHS R01 GM110755NIGMS NIH HHS R01 GM112763NIGMS NIH HHS R01 GM120252NIGMS NIH HHS R01 GM123725NINDS NIH HHS R01 NS039112
6 · The paper itself

Abstract

Metallochaperones are a diverse family of trafficking molecules that provide metal ions to protein targets for use as cofactors. The copper chaperone for superoxide dismutase (Ccs1) activates immature copper-zinc superoxide dismutase (Sod1) by delivering copper and facilitating the oxidation of the Sod1 intramolecular disulfide bond. Here, we present structural, spectroscopic, and cell-based data supporting a novel copper-induced mechanism for Sod1 activation. Ccs1 binding exposes an electropositive cavity and proposed "entry site" for copper ion delivery on immature Sod1. Copper-mediated sulfenylation leads to a sulfenic acid intermediate that eventually resolves to form the Sod1 disulfide bond with concomitant release of copper into the Sod1 active site. Sod1 is the predominant disulfide bond-requiring enzyme in the cytoplasm, and this copper-induced mechanism of disulfide bond formation obviates the need for a thiol/disulfide oxidoreductase in that compartment.

Indexed as

Models, MolecularProtein Processing, Post-TranslationalAmino Acid SubstitutionApoenzymesBinding SitesCopperCrystallography, X-RayCysteineCystineEnzyme ActivationEnzyme StabilityHumansLigandsMolecular ChaperonesMutagenesis, Site-DirectedMutationApoenzymesCCS1 protein, S cerevisiaeCopperCysteineCystineLigandsLYS7 protein, S cerevisiaeMolecular ChaperonesRecombinant ProteinsSaccharomyces cerevisiae ProteinsSuperoxide Dismutasechaperonecopperenzyme activationmetalloenzymesuperoxide dismutase (SOD)X-ray crystallography

Identifiers

PMID28533431
PMCPMC5519355
OpenAlexW2617570220

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.