The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Update on the aldehyde dehydrogenase gene (ALDH) superfamily
Open accessAbstract
Members of the aldehyde dehydrogenase gene (ALDH) superfamily play an important role in the enzymic detoxification of endogenous and exogenous aldehydes and in the formation of molecules that are important in cellular processes, like retinoic acid, betaine and gamma-aminobutyric acid. ALDHs exhibit additional, non-enzymic functions, including the capacity to bind to some hormones and other small molecules and to diminish the effects of ultraviolet irradiation in the cornea. Mutations in ALDH genes leading to defective aldehyde metabolism are the molecular basis of several diseases, including gamma-hydroxybutyric aciduria, pyridoxine-dependent seizures, Sjögren-Larsson syndrome and type II hyperprolinaemia. Interestingly, several ALDH enzymes appear to be markers for normal and cancer stem cells. The superfamily is evolutionarily ancient and is represented within Archaea, Eubacteria and Eukarya taxa. Recent improvements in DNA and protein sequencing have led to the identification of many new ALDH family members. To date, the human genome contains 19 known ALDH genes, as well as many pseudogenes. Whole-genome sequencing allows for comparison of the entire complement of ALDH family members among organisms. This paper provides an update of ALDH genes in several recently sequenced vertebrates and aims to clarify the associated records found in the National Center for Biotechnology Information (NCBI) gene database. It also highlights where and when likely gene-duplication and gene-loss events have occurred. This information should be useful to future studies that might wish to compare the role of ALDH members among species and how the gene superfamily as a whole has changed throughout evolution.
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The origin and evolution of model organisms
Hedges, S. B. (2002) · Nature Reviews Genetics · doi:10.1038/nrg929 · Cited by 806
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Cited by
Targeting Aldehyde Dehydrogenase 2: New Therapeutic Opportunities
Chen, C.-H., Ferreira, J. C. B., Gross, E. R., & Mochly-Rosen, D. (2014) · Physiological Reviews · doi:10.1152/physrev.00017.2013 · Cited by 614
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-citationNADPH-generating systems in bacteria and archaea
Spaans, S. K., Weusthuis, R. A., van der Oost, J., & Kengen, S. W. M. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00742 · Cited by 373
Aldehyde Dehydrogenases: Not Just Markers, but Functional Regulators of Stem Cells
Vassalli, G. (2019) · Stem Cells International · doi:10.1155/2019/3904645 · Cited by 300
Aldehyde dehydrogenases and cell proliferation
Muzio, G., Maggiora, M., Paiuzzi, E., Oraldi, M., & Canuto, R. A. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.033 · Cited by 297
Metadata
- Authors
- Jackson, B., Brocker, C., Thompson, D. C., Black, W., Vasiliou, K., Nebert, D. W., & Vasiliou, V.
- Venue
- Human Genomics
- Published
- 2011
- Volume
- 5
- Issue
- 4
- Pages
- 283
- ISSN
- 1473-9542 (ISSN-L)
- 1479-7364
- OpenAlex
- W2155091769
- Cited by
- 356
- References
- 4
- FWCI
- 8.00
- Type
- journal article
- Language
- en
- Open access
- gold
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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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