Evidence map›Paper›PMID 30389497›Full record

ArticleFree radical biology & medicine2019

Oxidation resistance 1 regulates post-translational modifications of peroxiredoxin 2 in the cerebellum.

Daria M Svistunova, Jillian N Simon, Elzbieta Rembeza, Mark Crabtree, Wyatt W Yue, Peter L Oliver, Mattéa J Finelli

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Article in Free radical biology & medicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

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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 2 institutions in 1 country.

Daria M SvistunovaDepartment of Physiology, Anatomy and Genetics, University of Oxford, Oxford OX1 3PT, UK.
Jillian N SimonDivision of Cardiovascular Medicine, Radcliffe Department of Medicine, John Radcliffe Hospital, University of Oxford, Oxford OX3 9DU, UK.
Elzbieta RembezaStructural Genomics Consortium, Nuffield Department of Clinical Medicine, University of Oxford, OX3 7DQ, UK.
Mark CrabtreeDivision of Cardiovascular Medicine, Radcliffe Department of Medicine, John Radcliffe Hospital, University of Oxford, Oxford OX3 9DU, UK.
Wyatt W YueStructural Genomics Consortium, Nuffield Department of Clinical Medicine, University of Oxford, OX3 7DQ, UK.
Peter L OliverDepartment of Physiology, Anatomy and Genetics, University of Oxford, Oxford OX1 3PT, UK; MRC Harwell Institute, Harwell Campus, Oxfordshire OX11 0RD, UK. Electronic address: p.oliver@har.mrc.ac.uk.
Mattéa J FinelliDepartment of Physiology, Anatomy and Genetics, University of Oxford, Oxford OX1 3PT, UK. Electronic address: mattea.finelli@ndcn.ox.ac.uk.
University of Oxford · GBJohn Radcliffe Hospital · GB

Funding

British Heart Foundation FS/14/56/31049Medical Research Council MC_EX_MR/P502005/1
6 · The paper itself

Abstract

Protein aggregation, oxidative and nitrosative stress are etiological factors common to all major neurodegenerative disorders. Therefore, identifying proteins that function at the crossroads of these essential pathways may provide novel targets for therapy. Oxidation resistance 1 (Oxr1) is a protein proven to be neuroprotective against oxidative stress, although the molecular mechanisms involved remain unclear. Here, we demonstrate that Oxr1 interacts with the multifunctional protein, peroxiredoxin 2 (Prdx2), a potent antioxidant enzyme highly expressed in the brain that can also act as a molecular chaperone. Using a combination of in vitro assays and two animal models, we discovered that expression levels of Oxr1 regulate the degree of oligomerization of Prdx2 and also its post-translational modifications (PTMs), specifically suggesting that Oxr1 acts as a functional switch between the antioxidant and chaperone functions of Prdx2. Furthermore, we showed in the Oxr1 knockout mouse that Prdx2 is aberrantly modified by overoxidation and S-nitrosylation in the cerebellum at the presymptomatic stage; this in-turn affected the oligomerization of Prdx2, potentially impeding its normal functions and contributing to the specific cerebellar neurodegeneration in this mouse model.

Indexed as

AnimalsCells, CulturedCerebellumDisease Models, AnimalHumansHydrogen PeroxideMiceMice, Inbred C57BLMice, KnockoutMitochondrial ProteinsNeurodegenerative DiseasesOxidation-ReductionOxidative StressPeroxiredoxinsProtein Aggregation, PathologicalProtein Processing, Post-TranslationalHydrogen PeroxideMitochondrial ProteinsOxr1 protein, mousePeroxiredoxinsAntioxidantChaperoneMouseNeurodegenerationOxidative stressPeroxiredoxin

Identifiers

PMID30389497
PMCPMC6339520
OpenAlexW2899412518

What OpenQuestion holds

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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.