Role of human aldo–keto-reductase AKR1B10 in the protection against toxic aldehydes
- 16 March 2009
- journal article
- Published by Elsevier BV in Chemico-Biological Interactions
- Vol. 178 (1-3), 145-150
- https://doi.org/10.1016/j.cbi.2008.10.021
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Structural basis for the high all-trans -retinaldehyde reductase activity of the tumor marker AKR1B10Proceedings of the National Academy of Sciences of the United States of America, 2007
- Structure of a glutathione conjugate bound to the active site of aldose reductaseProteins-Structure Function and Bioinformatics, 2006
- Neuroprotective role for carbonyl reductase?Biochemical and Biophysical Research Communications, 2005
- PURIFICATION AND CHARACTERIZATION OF AKR1B10 FROM HUMAN LIVER: ROLE IN CARBONYL REDUCTION OF XENOBIOTICSDrug Metabolism and Disposition, 2005
- 4-Oxo-2-nonenal Is Both More Neurotoxic and More Protein Reactive than 4-Hydroxy-2-nonenalChemical Research in Toxicology, 2005
- Model Studies on Protein Side Chain Modification by 4-Oxo-2-nonenalChemical Research in Toxicology, 2003
- Molecular determinants of steroid recognition and catalysis in aldo-keto reductases. Lessons from 3α-hydroxysteroid dehydrogenaseThe Journal of Steroid Biochemistry and Molecular Biology, 1999
- New member of aldose reductase family proteins overexpressed in human hepatocellular carcinomaHepatology, 1998
- Substrate specificity of human aldose reductase: identification of 4-hydroxynonenal as an endogenous substrateBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976