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Cited by 271

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 access
Grimsby, J, Chen, K, Wang, L J, Lan, N C, Shih, J C·1991·Proceedings of the National Academy of Sciences

Abstract

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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CoChat. (2026). Citation check: Human monoamine oxidase A and B genes exhibit identical exon-intron organization. https://app.cochat.ai/papers/10.1073/pnas.88.9.3637
The paper
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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