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Cited by 236

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 access
Perez-Miller, Samantha, Younus, Hina, Vanam, Ram, Chen, Che-Hong, Mochly-Rosen, Daria, Hurley, Thomas D·2010·Nature Structural & Molecular Biology

Abstract

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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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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CoChat. (2026). Citation check: Alda-1 is an agonist and chemical chaperone for the common human aldehyde dehydrogenase 2 variant. https://app.cochat.ai/papers/10.1038/nsmb.1737
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Perez-Miller, S., Younus, H., Vanam, R., Chen, C.-H., Mochly-Rosen, D., & Hurley, T. D. (2010). Alda-1 is an agonist and chemical chaperone for the common human aldehyde dehydrogenase 2 variant. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1737

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.