Evidence map›Paper›PMID 36143193›Full record

ArticleJournal of personalized medicine2022

Protein Succinylation and Malonylation as Potential Biomarkers in Schizophrenia.

Bradley Joseph Smith, Caroline Brandão-Teles, Giuliana S Zuccoli, Guilherme Reis-de-Oliveira, Mariana Fioramonte, Verônica M Saia-Cereda, Daniel Martins-de-Souza

Abstract read
In one paragraph

Article in Journal of personalized medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Systematic analysis of lysine malonylation inFrontiers in cellular and infection microbiology · 2022
    Article
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.

Bradley Joseph SmithLaboratory of Neuroproteomics, Institute of Biology, Department of Biochemistry and Tissue Biology, University of Campinas, Campinas 13083-862, Brazil.ORCID 0000-0003-1383-5851
Caroline Brandão-TelesLaboratory of Neuroproteomics, Institute of Biology, Department of Biochemistry and Tissue Biology, University of Campinas, Campinas 13083-862, Brazil.ORCID 0000-0002-0408-8965
Giuliana S ZuccoliLaboratory of Neuroproteomics, Institute of Biology, Department of Biochemistry and Tissue Biology, University of Campinas, Campinas 13083-862, Brazil.ORCID 0000-0002-7604-9279
Guilherme Reis-de-OliveiraLaboratory of Neuroproteomics, Institute of Biology, Department of Biochemistry and Tissue Biology, University of Campinas, Campinas 13083-862, Brazil.
Mariana FioramonteLaboratory of Neuroproteomics, Institute of Biology, Department of Biochemistry and Tissue Biology, University of Campinas, Campinas 13083-862, Brazil.
Verônica M Saia-CeredaLaboratory of Neuroproteomics, Institute of Biology, Department of Biochemistry and Tissue Biology, University of Campinas, Campinas 13083-862, Brazil.
Daniel Martins-de-SouzaLaboratory of Neuroproteomics, Institute of Biology, Department of Biochemistry and Tissue Biology, University of Campinas, Campinas 13083-862, Brazil.ORCID 0000-0003-3595-5846

Funding

Coordenação de Aperfeicoamento de Pessoal de Nível Superior 88887.495565/2020-00National Council for Scientific and Technological Development 302453/2017-2São Paulo Research Foundation 2013/08711-3São Paulo Research Foundation 2014/10068-4São Paulo Research Foundation 2015/23049-0São Paulo Research Foundation 2016/07332-7São Paulo Research Foundation 2016/07948-8São Paulo Research Foundation 2017/18715-4São Paulo Research Foundation 2017/25055-3São Paulo Research Foundation 2017/25588-1São Paulo Research Foundation 2018/01410-1São Paulo Research Foundation 2018/14666-4São Paulo Research Foundation 2019/05747-3
6 · The paper itself

Abstract

Two protein post-translational modifications, lysine succinylation and malonylation, are implicated in protein regulation, glycolysis, and energy metabolism. The precursors of these modifications, succinyl-CoA and malonyl-CoA, are key players in central metabolic processes. Both modification profiles have been proven to be responsive to metabolic stimuli, such as hypoxia. As mitochondrial dysfunction and metabolic dysregulation are implicated in schizophrenia and other psychiatric illnesses, these modification profiles have the potential to reveal yet another layer of protein regulation and can furthermore represent targets for biomarkers that are indicative of disease as well as its progression and treatment. In this work, data from shotgun mass spectrometry-based quantitative proteomics were compiled and analyzed to probe the succinylome and malonylome of postmortem brain tissue from patients with schizophrenia against controls and the human oligodendrocyte precursor cell line MO3.13 with the dizocilpine chemical model for schizophrenia, three antipsychotics, and co-treatments. Several changes in the succinylome and malonylome were seen in these comparisons, revealing these modifications to be a largely under-studied yet important form of protein regulation with broad potential applications.

Indexed as

antipsychoticsbiomarkersmalonylationpost-translational modificationsschizophreniashotgun proteomicssuccinylation

Identifiers

PMID36143193
PMCPMC9500613

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.