The human molybdenum hydroxylase gene family: co-conspirators in metabolic free-radical generation and disease
- PMID: 9388549
- DOI: 10.1042/bst0250799
The human molybdenum hydroxylase gene family: co-conspirators in metabolic free-radical generation and disease
Similar articles
-
Analysis of aldehyde oxidase and xanthine dehydrogenase/oxidase as possible candidate genes for autosomal recessive familial amyotrophic lateral sclerosis.Somat Cell Mol Genet. 1995 Mar;21(2):121-31. doi: 10.1007/BF02255787. Somat Cell Mol Genet. 1995. PMID: 7570184
-
Recent studies on xanthine oxidase and related enzymes.Biochem Soc Trans. 1996 Feb;24(1):99-105. doi: 10.1042/bst0240099. Biochem Soc Trans. 1996. PMID: 8674784 Review. No abstract available.
-
Properties of rabbit liver aldehyde oxidase and the relationship of the enzyme to xanthine oxidase and dehydrogenase.Eur J Biochem. 1995 Sep 1;232(2):646-57. Eur J Biochem. 1995. PMID: 7556219
-
Iron-sulphur systems in some isolated multi-component oxidative enzymes.Biochem Soc Trans. 1975;3(4):479-82. doi: 10.1042/bst0030479. Biochem Soc Trans. 1975. PMID: 1237425 No abstract available.
-
Molybdenum enzymes in reactions involving aldehydes and acids.Met Ions Biol Syst. 2002;39:539-70. Met Ions Biol Syst. 2002. PMID: 11913136 Review. No abstract available.
Cited by
-
Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases.J Biol Inorg Chem. 2015 Mar;20(2):403-33. doi: 10.1007/s00775-014-1234-2. Epub 2015 Jan 15. J Biol Inorg Chem. 2015. PMID: 25589250 Review.
-
Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes.Redox Biol. 2018 Oct;19:274-289. doi: 10.1016/j.redox.2018.08.020. Epub 2018 Aug 30. Redox Biol. 2018. PMID: 30196191 Free PMC article. Review.
-
NADH oxidase activity of rat and human liver xanthine oxidoreductase: potential role in superoxide production.J Biol Inorg Chem. 2007 Aug;12(6):777-87. doi: 10.1007/s00775-007-0229-7. Epub 2007 Apr 18. J Biol Inorg Chem. 2007. PMID: 17440754
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases