Evidence map›Paper›PMID 29905912›Full record

ArticleMolecular neurobiology2019

Oxidation Resistance 1 Modulates Glycolytic Pathways in the Cerebellum via an Interaction with Glucose-6-Phosphate Isomerase.

Mattéa J Finelli, Teresa Paramo, Elisabete Pires, Brent J Ryan, Richard Wade-Martins, Philip C Biggin, James McCullagh, Peter L Oliver

Open access · hybridAbstract read
In one paragraph

Article in Molecular neurobiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 27 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

8 authors at 1 institution in 1 country.

Mattéa J FinelliDepartment of Physiology, Anatomy and Genetics, University of Oxford, Parks Road, Oxford, OX1 3PT, UK.
Teresa ParamoDepartment of Biochemistry, University of Oxford, Parks Road, Oxford, OX1 3QU, UK.
Elisabete PiresChemistry Research Laboratory, Department of Chemistry, University of Oxford, Mansfield Road, Oxford, OX1 3TA, UK.
Brent J RyanOxford Parkinson's Disease Centre, University of Oxford, South Parks Road, Oxford, OX1 3QX, UK.
Richard Wade-MartinsDepartment of Biochemistry, University of Oxford, Parks Road, Oxford, OX1 3QU, UK.
Philip C BigginDepartment of Biochemistry, University of Oxford, Parks Road, Oxford, OX1 3QU, UK.
James McCullaghChemistry Research Laboratory, Department of Chemistry, University of Oxford, Mansfield Road, Oxford, OX1 3TA, UK.
Peter L OliverDepartment of Physiology, Anatomy and Genetics, University of Oxford, Parks Road, Oxford, OX1 3PT, UK. peter.oliver@dpag.ox.ac.uk.ORCID http://orcid.org/0000-0003-3347-2461
University of Oxford · GB

Funding

European Research Council 311394European Research Council 311394 / PAROSINMedical Research Council MC_EX_MR/P502005/1Parkinson's UK G-1003Parkinson's UK J-0901Parkinson's UK J-1403 / Monument Trust Discovery Award
6 · The paper itself

Abstract

Glucose metabolism is essential for the brain: it not only provides the required energy for cellular function and communication but also participates in balancing the levels of oxidative stress in neurons. Defects in glucose metabolism have been described in neurodegenerative disease; however, it remains unclear how this fundamental process contributes to neuronal cell death in these disorders. Here, we investigated the molecular mechanisms driving the selective neurodegeneration in an ataxic mouse model lacking oxidation resistance 1 (Oxr1) and discovered an unexpected function for this protein as a regulator of the glycolytic enzyme, glucose-6-phosphate isomerase (GPI/Gpi1). Initially, we present a dysregulation of metabolites of glucose metabolism at the pre-symptomatic stage in the Oxr1 knockout cerebellum. We then demonstrate that Oxr1 and Gpi1 physically and functionally interact and that the level of Gpi1 oligomerisation is disrupted when Oxr1 is deleted in vivo. Furthermore, we show that Oxr1 modulates the additional and less well-understood roles of Gpi1 as a cytokine and neuroprotective factor. Overall, our data identify a new molecular function for Oxr1, establishing this protein as important player in neuronal survival, regulating both oxidative stress and glucose metabolism in the brain.

Indexed as

AnimalsCell MovementCerebellumGlucoseGlucose-6-Phosphate IsomeraseGlycolysisHeLa CellsHumansMiceMice, KnockoutMitochondrial ProteinsNeuronsNuclear ProteinsOxidative StressGlucoseGlucose-6-Phosphate IsomeraseMitochondrial ProteinsNuclear ProteinsOxr1 protein, mouseCerebellumGlucose metabolismMouseNeurodegenerationOxidative stress

Identifiers

PMID29905912
PMCPMC6368252
OpenAlexW2807711907

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.