Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

NAD+ and Sirt5 restore mitochondrial bioenergetics failure and improve locomotor defects caused by sucla2 mutations.

JCI insight - 23 Jan 2026

Richard Joy, Lizzo Giulia, Rochat Noélie, Jouary Adrien, Silva Pedro Tm, Parisi Alice, Christen Stefan, Moco Sofia, Orger Michael B, Gut Philipp

Abstract excerpt

Mitochondria-derived acyl-coenzyme A (acyl-CoA) species chemically modify proteins, causing damage when acylation reactions are not adequately detoxified by enzymatic removal or protein turnover. Defects in genes encoding the mitochondrial respiratory complex and TCA cycle enzymes have been shown to increase acyl-CoA levels due to reduced enzymatic flux and result in proteome-wide hyperacylation. How...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acyl Coenzyme A
Share to Energy Metabolism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Locomotion

Share to Mitochondria

Share to Mitochondrial Diseases

Share to Sirtuins

Share to Zebrafish

Source

Open in PubMed Open full text

Identifiers

PMID: 41574612
DOI: 10.1172/jci.insight.181812
PMCID: PMC12892911

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

NAD+ and Sirt5 restore mitochondrial bioenergetics failure and improve locomotor defects caused by sucla2 mutations.PMID 41574612Read ↗

SUCLA2 mutations cause global protein succinylation contributing to the pathomechanism of a hereditary mitochondrial disease.Semantic proximity Read ↗

SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks.Semantic proximity Read ↗

Defective Function of α-Ketoglutarate Dehydrogenase Exacerbates Mitochondrial ATP Deficits during Complex I DeficiencySemantic proximity Read ↗

Sucla2 Knock-Out in Skeletal Muscle Yields Mouse Model of Mitochondrial Myopathy With Muscle Type-Specific Phenotypes.Semantic proximity Read ↗

Protein hypoacylation induced by Sirt5 overexpression has minimal metabolic effect in mice.Semantic proximity Read ↗

Succinyl-CoA synthetase (SUCLA2) deficiency in two siblings with impaired activity of other mitochondrial oxidative enzymes in skeletal muscle without mitochondrial DNA depletion.Semantic proximity Read ↗

Metabolic Effects of Succinate Dehydrogenase Loss in CancerSemantic proximity Read ↗

Expanding the phenotypic spectrum of Succinyl-CoA ligase deficiency through functional validation of a new SUCLG1 variant.Semantic proximity Read ↗

Lysine desuccinylase SIRT5 binds to cardiolipin and regulates the electron transport chain.Semantic proximity Read ↗

Dysregulation of protein succinylation and disease developmentSemantic proximity Read ↗

Combinatorial glucose, nicotinic acid and N-acetylcysteine therapy has synergistic effect in preclinical C. elegans and zebrafish models of mitochondrial complex I disease.Semantic proximity Read ↗

The SIRT5-SUCLG2 desuccinylation axis delays ovarian aging via a mitochondrial-epigenetic regulatory mechanismSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.