The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Human monoamine oxidase A and B genes exhibit identical exon-intron organization.
Open accessAbstract
Monoamine oxidases A and B [MAOA and MAOB; amine:oxygen oxidoreductase (deaminating) (flavin-containing), EC 1.4.3.4] play important roles in the metabolism of neuroactive, vasoactive amines and the Parkinsonism-producing neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Human MAOA and MAOB genes isolated from X chromosome-specific libraries span at least 60 kilobases, consist of 15 exons, and exhibit identical exon-intron organization. Exon 12 codes for the covalent FAD-binding-site and is the most conserved exon; the MAOA and MAOB exon 12 products share 93.9% peptide identity. These results suggest that MAOA and MAOB are derived from duplication of a common ancestral gene and provide insight on the structural/functional relationship of the enzyme products.
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Metadata
- Authors
- Grimsby, J., Chen, K., Wang, L. J., Lan, N. C., & Shih, J. C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1991-05
- Volume
- 88
- Issue
- 9
- Pages
- 3637-3641
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2024298846
- Cited by
- 271
- References
- 22
- FWCI
- 10.08
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Grimsby, J., Chen, K., Wang, L. J., Lan, N. C., & Shih, J. C. (1991). Human monoamine oxidase A and B genes exhibit identical exon-intron organization. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.88.9.3637
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.