Article

Biogenesis of NDUFS3-less complex I indicates TMEM126A/OPA7 as an assembly factor of the ND4-module

2020-10-22

Abstract excerpt

<h4>ABSTRACT</h4> Complex I (CI) is the largest enzyme of the mitochondrial respiratory chain and its defects are the main cause of mitochondrial disease. To understand the mechanisms regulating the extremely intricate biogenesis of this fundamental bioenergetic machine, we analyzed the structural and functional consequences of the ablation of NDUFS3, a non-catalytic core subunit. We prove that in diverse mammali...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 378fa22b-75b9-5cb8-9ead-d8002fd23712
DOI: 10.1101/2020.10.22.350587

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Biogenesis of NDUFS3-less complex I indicates TMEM126A/OPA7 as an assembly factor of the ND4-moduleDOI 10.1101/2020.10.22.350587Read

Systematic analysis of NDUFAF6 in complex I assembly and mitochondrial diseaseSemantic proximity Read

Systematic analysis of NDUFAF6 in complex I assembly and mitochondrial disease.Semantic proximity Read

RTN4IP1 is essential for the final stages of mitochondrial complex I assembly and coenzyme Q biosynthesisSemantic proximity Read

Respiratory complex III <sub>2</sub> assembles complex I via toxic intermediate in mitochondrial diseaseSemantic proximity Read

Structural insights into complex I deficiency and assembly from the disease-related <i>ndufs4</i> <sup>-/-</sup> mouseSemantic proximity Read

Mitochondrial Proteome of Affected Neurons in a Mouse Model of Leigh SyndromeSemantic proximity Read

Optic atrophy-associated TMEM126A is an assembly factor for the ND4-module of mitochondrial complex I.Semantic proximity Read

Optic Atrophy-associated TMEM126A is an assembly factor for the ND4-module of Mitochondrial Complex ISemantic proximity Read

<i>OPA1</i> and disease-causing mutants perturb mitochondrial nucleoid distributionSemantic proximity Read

Sideroflexin 4 is a complex I assembly factor that interacts with the MCIA complex and is required for the assembly of the ND2 module.Semantic proximity Read

Expanding the phenotypic and biochemical spectrum of NDUFAF3-related mitochondrial disease.Semantic proximity Read

C6orf203 controls OXPHOS function through modulation of mitochondrial protein biosynthesisSemantic proximity Read