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Article

Impact of mutations within the [Fe-S] cluster or the lipoic acid biosynthesis pathways on mitochondrial protein expression profiles in fibroblasts from patients.

Molecular genetics and metabolism - 1 Nov 2017

Lebigot E, Gaignard P, Dorboz I, Slama A, Rio M, de Lonlay P, Héron B, Sabourdy F, Boespflug-Tanguy O, Cardoso A, Habarou F, Ottolenghi C, Thérond P, Bouton C, Golinelli-Cohen M P, Boutron A

Abstract excerpt

Lipoic acid (LA) is the cofactor of the E2 subunit of mitochondrial ketoacid dehydrogenases and plays a major role in oxidative decarboxylation. De novo LA biosynthesis is dependent on LIAS activity together with LIPT1 and LIPT2. LIAS is an iron‑sulfur (Fe-S) cluster-containing mitochondrial protein, like mitochondrial aconitase (mt-aco) and some subunits of respiratory chain (RC) complexes I, II and III. All of...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 28803783
DOI: 10.1016/j.ymgme.2017.08.001

Genes

BOLA3
IBA57
NFU1
ISCA2
LIPT1
LIPT2
LIAS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

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