The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Alda-1 is an agonist and chemical chaperone for the common human aldehyde dehydrogenase 2 variant
Open accessAbstract
In approximately one billion people, a point mutation inactivates a key detoxifying enzyme, aldehyde dehydrogenase (ALDH2). This mitochondrial enzyme metabolizes toxic biogenic and environmental aldehydes, including the endogenously produced 4-hydroxynonenal (4HNE) and the environmental pollutant acrolein, and also bioactivates nitroglycerin. ALDH2 is best known, however, for its role in ethanol metabolism. The accumulation of acetaldehyde following the consumption of even a single alcoholic beverage leads to the Asian alcohol-induced flushing syndrome in ALDH2*2 homozygotes. The ALDH2*2 allele is semidominant, and heterozygotic individuals show a similar but less severe phenotype. We recently identified a small molecule, Alda-1, that activates wild-type ALDH2 and restores near-wild-type activity to ALDH2*2. The structures of Alda-1 bound to ALDH2 and ALDH2*2 reveal how Alda-1 activates the wild-type enzyme and how it restores the activity of ALDH2*2 by acting as a structural chaperone.
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PHENIX : building new software for automated crystallographic structure determination
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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
Self-citationImpaired dopamine metabolism in Parkinson’s disease pathogenesis
Masato, A., Plotegher, N., Boassa, D., & Bubacco, L. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0332-6 · Cited by 328
Post-translational modifications of mitochondrial aldehyde dehydrogenase and biomedical implications
Song, B.-J., Abdelmegeed, M. A., Yoo, S.-H., Kim, B.-J., Jo, S. A., Jo, I., & Moon, K.-H. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.05.013 · Cited by 73
Metadata
- Authors
- Perez-Miller, S., Younus, H., Vanam, R., Chen, C.-H., Mochly-Rosen, D., & Hurley, T. D.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2010-01-10
- Volume
- 17
- Issue
- 2
- Pages
- 159-164
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2146627313
- Cited by
- 236
- References
- 4
- FWCI
- 4.17
- Type
- journal article
- Language
- en
- Open access
- green
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