Evidence map›Paper›PMID 30913880›Full record

ReviewJournal of proteome research2019

Mitochondrial Function, Metabolic Regulation, and Human Disease Viewed through the Prism of Sirtuin 4 (SIRT4) Functions.

Cora N Betsinger, Ileana M Cristea

Abstract readReview
In one paragraph

Review in Journal of proteome research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

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  13. Acetylation in Cardiac Aging: Molecular Mechanism and Therapeutic Approaches.Results and problems in cell differentiation · 2025
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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

2 authors.

Cora N BetsingerDepartment of Molecular Biology , Princeton University , Princeton , New Jersey 08544 , United States.
Ileana M CristeaDepartment of Molecular Biology , Princeton University , Princeton , New Jersey 08544 , United States.ORCID 0000-0002-6533-2458

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007388 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 1985 to 2022
$27.4M
Mechanisms mediating immune response upon sensing of nuclear viral DNAR01GM114141 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 2015 to 2023
$2.6M
NIGMS NIH HHS R01 GM114141NIGMS NIH HHS T32 GM007388
6 · The paper itself

Abstract

As cellular metabolic hubs, mitochondria are the main energy producers for the cell. These organelles host essential energy producing biochemical processes, including the TCA cycle, fatty acid oxidation, and oxidative phosphorylation. An accumulating body of literature has demonstrated that a majority of mitochondrial proteins are decorated with diverse posttranslational modifications (PTMs). Given the critical roles of these proteins in cellular metabolic pathways and response to environmental stress or pathogens, understanding the role of PTMs in regulating their functions has become an area of intense investigation. A major family of enzymes that regulate PTMs within the mitochondria are sirtuins (SIRTs). Albeit until recently the least understood sirtuin, SIRT4 has emerged as an enzyme capable of removing diverse PTMs from its substrates, thereby modulating their functions. SIRT4 was shown to have ADP-ribosyltransferase, deacetylase, lipoamidase, and deacylase enzymatic activities. As metabolic dysfunction is linked to human disease, SIRT4 levels and activities have been implicated in modulating susceptibility to hyperinsulinemia and diabetes, liver disease, cancer, neurodegeneration, heart disease, aging, and pathogenic infections. Therefore, SIRT4 has emerged as a possible candidate for targeted therapeutics. Here, we discuss the diverse enzymatic activities and substrates of SIRT4 and its roles in human health and disease.

Indexed as

Protein Processing, Post-TranslationalAgingCommunicable DiseasesDiabetes MellitusGene ExpressionHeart DiseasesHumansHyperinsulinismLiver DiseasesMitochondriaMitochondrial ProteinsMolecular Targeted TherapyNeoplasmsNeurodegenerative DiseasesProtein ConformationSirtuinsMitochondrial ProteinsSIRT4 protein, humanSirtuinsagingcancercardiovascular diseasediabetesliver diseasemetabolic regulationmitochondrianeurodegenerationPTMsSIRT4

Identifiers

PMID30913880
PMCPMC6889813

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.