The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Cytochrome c oxidase deficiency
Abstract
Cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain, catalyzing the transfer of electrons from reduced cytochrome c to molecular oxygen. It is composed of 13 structural subunits, three of which are encoded in mtDNA and form the catalytic core of the enzyme. In addition to these structural subunits, a large number of accessory factors are necessary for the assembly and maintenance of the active holoenzyme complex. Most isolated COX deficiencies are inherited as autosomal recessive disorders; mutations in the mtDNA‐encoded COX subunit genes are relatively rare. These mutations are associated with a wide spectrum of clinical phenotypes ranging from isolated myopathy to multisystem disease, with onset from late childhood to adulthood. Autosomal recessive COX deficiencies generally have a very early age of onset and a fatal outcome. Several clinical presentations have been described including Leigh Syndrome, hypertrophic cardiomyopathy and myopathy, and fatal infantile lactic acidosis. Surprisingly, mutations in the nuclear‐encoded structural COX subunits have not been found in association with any of these phenotypes. Mutations have, however, been identified in several COX assembly factors: SURF1 (Leigh Syndrome), SCO2 (hypertrophic cardiomyopathy), SCO1 (hepatic failure, ketoacidotic coma), and COX10 (encephalopathy, tubulopathy). As all of these assembly factors are ubiquitously expressed, the molecular basis for the different clinical presentations remains unexplained. Although the genetic defects in the majority of patients with COX deficiency are unknown, it is likely that most will be solved in the near future using functional complementation techniques. © 2001 Wiley‐Liss, Inc.
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Metadata
- Authors
- Shoubridge, E. A.
- Venue
- American Journal of Medical Genetics
- Publisher
- Wiley
- Published
- 2001-03
- Volume
- 106
- Issue
- 1
- Pages
- 46-52
- ISSN
- 0148-7299 (ISSN-L)
- 1096-8628
- OpenAlex
- W2151271025
- Cited by
- 323
- References
- 50
- FWCI
- 5.65
- Type
- journal article
- Language
- en
- Open access
- closed
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