Evidence map›Paper›PMID 24297923›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Cellular distribution of copper to superoxide dismutase involves scaffolding by membranes.

Christopher R Pope, Christopher J De Feo, Vinzenz M Unger

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

34 citing papers in PubMed, 58 citations in OpenAlex.

  1. Balancing cellular copper levels via the post-translational regulation of copper transport.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Review
  2. Review
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  5. Article
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  10. Copper metabolism in Saccharomyces cerevisiae: an update.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2021
    Review
  11. Copper Sources for Sod1 Activation.Antioxidants (Basel, Switzerland) · 2020
    Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Reconstitution of a thermophilic CuThe Journal of biological chemistry · 2018
    Article
  18. Article
  19. Article
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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

3 authors at 2 institutions in 1 country.

Christopher R PopeDepartment of Molecular Biosciences and Chemistry of Life Processes Institute, Northwestern University, Evanston, IL 60208.
Christopher J De Feo
Vinzenz M Unger
Northwestern University · USCenter for Biologics Evaluation and Research · US

Funding

The role of transferrin receptor 2 in iron homeostasisP01GM067166 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI HUBBARD, ANN L · 2003 to 2013
$14.6M
Structural Biology of Membrane ScaffoldsR01GM094479 · NIGMS · NORTHWESTERN UNIVERSITY · PI UNGER, VINZENZ · 2010 to 2013
$1.6M
Putting the pieces together: The role of CCS in intracellular copper distributionF31NS076213 · NINDS · NORTHWESTERN UNIVERSITY · PI POPE, CHRISTOPHER RYAN · 2011 to 2012
$64k
Structure and Function of the Human Copper TransporterF31NS056825 · NINDS · YALE UNIVERSITY · PI DEFEO, CHRISTOPHER J · 2006 to 2007
$58k
NIGMS NIH HHS GM094479NIGMS NIH HHS P01 GM067166NIGMS NIH HHS R01 GM094479NINDS NIH HHS F31 NS056825NINDS NIH HHS F31 NS076213NINDS NIH HHS F31 NS56825
6 · The paper itself

Abstract

Efficient delivery of copper ions to specific intracellular targets requires copper chaperones that acquire metal cargo through unknown mechanisms. Here we demonstrate that the human and yeast copper chaperones (CCS) for superoxide dismutase 1 (SOD1), long thought to exclusively reside in the cytosol and mitochondrial intermembrane space, can engage negatively charged bilayers through a positively charged lipid-binding interface. The significance of this membrane-binding interface is established through SOD1 activity and genetic complementation studies in Saccharomyces cerevisiae, showing that recruitment of CCS to the membrane is required for activation of SOD1. Moreover, we show that a CCS:SOD1 complex binds to bilayers in vitro and that CCS can interact with human high affinity copper transporter 1. Shifting current paradigms, we propose that CCS-dependent copper acquisition and distribution largely occur at membrane interfaces and that this emerging role of the bilayer may reflect a general mechanistic aspect of cellular transition metal ion acquisition.

Indexed as

Biological Transport, ActiveCopperCytosolEnzyme ActivationGenetic Complementation TestHumansIntracellular MembranesLipid BilayersMolecular ChaperonesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSuperoxide DismutaseSuperoxide Dismutase-1CCS1 protein, S cerevisiaeCCS protein, humanCopperLipid BilayersMolecular ChaperonesSaccharomyces cerevisiae ProteinsSOD1 protein, humanSuperoxide DismutaseSuperoxide Dismutase-1copper homeostasiscopper transfercopper uptakemembrane scaffold

Identifiers

PMID24297923
PMCPMC3870662
OpenAlexW1990323568

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.