The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily
Open accessAbstract
BACKGROUND: Aldehydes are highly reactive molecules. While several non-P450 enzyme systems participate in their metabolism, one of the most important is the aldehyde dehydrogenase (ALDH) superfamily, composed of NAD(P)+-dependent enzymes that catalyze aldehyde oxidation. OBJECTIVE: This article presents a review of what is currently known about each member of the human ALDH superfamily including the pathophysiological significance of these enzymes. METHODS: Relevant literature involving all members of the human ALDH family was extensively reviewed, with the primary focus on recent and novel findings. CONCLUSION: To date, 19 ALDH genes have been identified in the human genome and mutations in these genes and subsequent inborn errors in aldehyde metabolism are the molecular basis of several diseases, including Sjögren-Larsson syndrome, type II hyperprolinemia, gamma-hydroxybutyric aciduria and pyridoxine-dependent seizures. ALDH enzymes also play important roles in embryogenesis and development, neurotransmission, oxidative stress and cancer. Finally, ALDH enzymes display multiple catalytic and non-catalytic functions including ester hydrolysis, antioxidant properties, xenobiotic bioactivation and UV light absorption.
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Duester, G. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01497.x · Cited by 570
DNA adducts from acetaldehyde: implications for alcohol-related carcinogenesis
Brooks, P. J., & Theruvathu, J. A. (2005) · Alcohol · doi:10.1016/j.alcohol.2005.03.009 · Cited by 382
Sydow, K., Daiber, A., Oelze, M., Chen, Z., August, M., Wendt, M., Ullrich, V., Mülsch, A., Schulz, E., Keaney, J. F., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200419267 · Cited by 300
Niederreither, K., Fraulob, V., Garnier, J.-M., Chambon, P., & Dollé, P. (2002) · Mechanisms of Development · doi:10.1016/s0925-4773(01)00561-5 · Cited by 246
Kanski, J., Behring, A., Pelling, J., & Schöneich, C. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01030.2003 · Cited by 217
Klyosov, A. A., Rashkovetsky, L. G., Tahir, M. K., & Keung, W.-M. (1996) · Biochemistry · doi:10.1021/bi9521093 · Cited by 200
SAUER, S., KOLKER, S., HOFFMANN, G., TENBRINK, H., JAKOBS, C., GIBSON, K., & OKUN, J. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2006.12.009 · Cited by 50
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Hakim, M., Broza, Y. Y., Barash, O., Peled, N., Phillips, M., Amann, A., & Haick, H. (2012) · Chemical Reviews · doi:10.1021/cr300174a · Cited by 953
Vistoli, G., De Maddis, D., Cipak, A., Zarkovic, N., Carini, M., & Aldini, G. (2013) · Free Radical Research · doi:10.3109/10715762.2013.815348 · Cited by 823
Aldehyde dehydrogenases in cellular responses to oxidative/electrophilicstress
Singh, S., Brocker, C., Koppaka, V., Chen, Y., Jackson, B. C., Matsumoto, A., Thompson, D. C., & Vasiliou, V. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.11.010 · Cited by 601
Self-citationBiotransformation of Xenobiotics
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Metadata
- Authors
- Marchitti, S. A., Brocker, C., Stagos, D., & Vasiliou, V.
- Venue
- Expert Opinion on Drug Metabolism & Toxicology
- Publisher
- Informa UK Limited
- Published
- 2008-06
- Volume
- 4
- Issue
- 6
- Pages
- 697-720
- ISSN
- 1742-5255 (ISSN-L)
- 1744-7607
- OpenAlex
- W1968332094
- Cited by
- 805
- References
- 7
- FWCI
- 13.73
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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