Evidence map›Paper›PMID 31931282›Full record

ArticleRedox biology2020

Methylglyoxal interaction with superoxide dismutase 1.

Panagis Polykretis, Enrico Luchinat, Francesca Boscaro, Lucia Banci

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

20 citing papers in PubMed, 45 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

4 authors at 2 institutions in 1 country.

Panagis PolykretisInteruniversity Consortium for Magnetic Resonance of Metallo Proteins (CIRMMP), via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.
Enrico LuchinatMagnetic Resonance Center - CERM, University of Florence, via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy; Department of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Florence, viale Morgagni 50, 50134, Florence, Italy.
Francesca BoscaroMass Spectrometry Center (CISM), University of Florence, via U. Schiff 6, 50019, Sesto Fiorentino, Florence, Italy.
Lucia BanciMagnetic Resonance Center - CERM, University of Florence, via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy; Department of Chemistry, University of Florence, via della Lastruccia 3, 50019, Sesto Fiorentino, Florence, Italy. Electronic address: banci@cerm.unifi.it.
Interuniversity Consortium for Magnetic Resonance · ITUniversity of Florence · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methylglyoxal (MG) is a highly reactive aldehyde spontaneously formed in human cells mainly as a by-product of glycolysis. Such endogenous metabolite reacts with proteins, nucleotides and lipids forming advanced glycation end-products (AGEs). MG binds to arginine, lysine and cysteine residues of proteins causing the formation of stable adducts that can interfere with protein function. Among the proteins affected by glycation, MG has been found to react with superoxide dismutase 1 (SOD1), a fundamental anti-oxidant enzyme that is abundantly expressed in neurons. Considering the high neuronal susceptibility to MG-induced oxidative stress, we sought to investigate by mass spectrometry and NMR spectroscopy which are the structural modifications induced on SOD1 by the reaction with MG. We show that MG reacts preferentially with the disulfide-reduced, demetallated form of SOD1, gradually causing its unfolding, and to a lesser extent, with the intermediate state of maturation - the reduced, zinc-bound homodimer - causing its gradual monomerization. These results suggest that MG could impair the correct maturation of SOD1 in vivo, thus both increasing cellular oxidative stress and promoting the cytotoxic misfolding and aggregation process of SOD1.

Indexed as

Binding SitesGlycolysisHumansMagnetic Resonance SpectroscopyMass SpectrometryModels, MolecularOxidative StressProtein BindingProtein Structure, SecondaryProtein UnfoldingPyruvaldehydeSuperoxide Dismutase-1PyruvaldehydeSOD1 protein, humanSuperoxide Dismutase-1AGEsGlycationMethylglyoxalOxidative stressSuperoxide dismutase 1

Identifiers

PMID31931282
PMCPMC6957824
OpenAlexW3000349486

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.