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Article

Understanding the molecular basis for multiple mitochondrial dysfunctions syndrome 1 (MMDS1): impact of a disease-causing Gly189Arg substitution on NFU1.

The FEBS journal - 1 Nov 2017

Wesley Nathaniel A, Wachnowsky Christine, Fidai Insiya, Cowan J A

Abstract excerpt

Iron-sulfur (Fe/S) cluster-containing proteins constitute one of the largest protein classes, with highly varied function. Consequently, the biosynthesis of Fe/S clusters is evolutionarily conserved and mutations in intermediate Fe/S cluster scaffold proteins can cause disease, including multiple mitochondrial dysfunctions syndrome (MMDS). Herein, we have characterized the impact of defects occurring in the MMDS1...

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Identifiers

PMID: 28906594
DOI: 10.1111/febs.14271
PMCID: PMC5696030

Genes

NFU1

Variants

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Understanding the molecular basis for multiple mitochondrial dysfunctions syndrome 1 (MMDS1): impact of a disease-causing Gly189Arg substitution on NFU1.PMID 28906594Read ↗

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