Evidence map›Paper›PMID 24567322›Full record

ArticleThe Journal of biological chemistry2014

DJ-1 is a copper chaperone acting on SOD1 activation.

Stefania Girotto, Laura Cendron, Marco Bisaglia, Isabella Tessari, Stefano Mammi, Giuseppe Zanotti, Luigi Bubacco

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
7.0field-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

44 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Article
  3. Cuproptosis-associated genesFrontiers in immunology · 2026
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  15. Copper Metabolism inFrontiers in cell and developmental biology · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Review
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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

7 authors at 1 institution in 1 country.

Stefania GirottoDepartment of Chemical Sciences, University of Padova, via Marzolo, 1 35131 Padova, Italy; Department of Drug Discovery and Development, Istituto Italiano di Tecnologia, Via Morego, 30 16163 Genoa, Italy.
Laura CendronDepartment of Biomedical Sciences, University of Padova, Via Ugo Bassi, 58b 35121 Padova, Italy; Department of Biology, University of Padova, Via Ugo Bassi, 58b 35121 Padova, Italy.
Marco BisagliaDepartment of Biology, University of Padova, Via Ugo Bassi, 58b 35121 Padova, Italy.
Isabella TessariDepartment of Biology, University of Padova, Via Ugo Bassi, 58b 35121 Padova, Italy.
Stefano MammiDepartment of Chemical Sciences, University of Padova, via Marzolo, 1 35131 Padova, Italy.
Giuseppe ZanottiDepartment of Biomedical Sciences, University of Padova, Via Ugo Bassi, 58b 35121 Padova, Italy.
Luigi BubaccoDepartment of Biology, University of Padova, Via Ugo Bassi, 58b 35121 Padova, Italy. Electronic address: luigi.bubacco@unipd.it.
University of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lack of oxidative stress control is a common and often prime feature observed in many neurodegenerative diseases. Both DJ-1 and SOD1, proteins involved in familial Parkinson disease and amyotrophic lateral sclerosis, respectively, play a protective role against oxidative stress. Impaired activity and modified expression of both proteins have been observed in different neurodegenerative diseases. A potential cooperative action of DJ-1 and SOD1 in the same oxidative stress response pathway may be suggested based on a copper-mediated interaction between the two proteins reported here. To investigate the mechanisms underlying the antioxidative function of DJ-1 in relation to SOD1 activity, we investigated the ability of DJ-1 to bind copper ions. We structurally characterized a novel copper binding site involving Cys-106, and we investigated, using different techniques, the kinetics of DJ-1 binding to copper ions. The copper transfer between the two proteins was also examined using both fluorescence spectroscopy and specific biochemical assays for SOD1 activity. The structural and functional analysis of the novel DJ-1 copper binding site led us to identify a putative role for DJ-1 as a copper chaperone. Alteration of the coordination geometry of the copper ion in DJ-1 may be correlated to the physiological role of the protein, to a potential failure in metal transfer to SOD1, and to successive implications in neurodegenerative etiopathogenesis.

Indexed as

Gene Expression Regulation, EnzymologicAmyotrophic Lateral SclerosisBinding SitesCopperCrystallography, X-RayCysteineDNA, ComplementaryHumansIntracellular Signaling Peptides and ProteinsModels, MolecularMolecular ChaperonesOncogene ProteinsOxidative StressParkinson DiseasePeroxiredoxinsProtein BindingCopperCysteineDNA, ComplementaryIntracellular Signaling Peptides and ProteinsMolecular ChaperonesOncogene ProteinsPARK7 protein, humanPeroxiredoxinsProtein Deglycase DJ-1SOD1 protein, humanSuperoxide DismutaseSuperoxide Dismutase-1Amyotrophic Lateral Sclerosis (Lou Gehrig's Disease)CopperCys-106DJ-1MetalloproteinsParkinson DiseaseSuperoxide Dismutase (SOD)

Identifiers

PMID24567322
PMCPMC4036200
OpenAlexW1991362023

What OpenQuestion holds

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Registered trials

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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.