ArticleProceedings of the National Academy of Sciences of the United States of America2005
Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 145 papers.
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Who cites it
145 citing papers in PubMed, 520 citations in OpenAlex.
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- Computational identification of quinoxaline-based 2-pyrazoline hybrids targeting monoamine oxidase A.Molecular diversity · 2026Article
- Computational Repurposing of Asparagus racemosus and Withania somnifera for Postpartum Depression: Insights into MAO-A and Inflammatory Signaling Modulation.Cell biochemistry and biophysics · 2026Article
- Structural Principles of Covalent Flavin Modification in Oxidoreductases.Biochemistry · 2026Review
- The discovery of monoamine oxidase inhibitors: virtual screening and in vitro inhibition potencies.Journal of computer-aided molecular design · 2026Article
- Probing the Inhibitory Potential of Halogenated Symmetrical Formamidine Against MAO-A and MAO-B: Structural Elucidation, Molecular Dynamic Simulation and DFT Computational Studies.Chemistry & biodiversity · 2025Article
- Qsarna: An Online Tool for Smart Chemical Space Navigation in Drug Design.Journal of chemical information and modeling · 2025Article
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- 1, 4-benzodioxan-substituted Thienyl chalcone derivatives as novel reversible inhibitors of human monoamine oxidase B with anti-neuroinflammatory activity.Scientific reports · 2025Article
- Evolutionary and Functional Analysis of Monoamine Oxidase F: A Novel Member of the Monoamine Oxidase Gene Family.Genome biology and evolution · 2025Article
- Theranostic Near-Infrared Monoamine Oxidase Inhibitor (NMI) Protein Binding Interactions with MAOA and Albumin.Pharmaceutical research · 2025Article
- Multi-target-directed therapeutic strategies for Alzheimer's disease: controlling amyloid-β aggregation, metal ion homeostasis, and enzyme inhibition.Chemical science · 2025Review
- Filtration of Natural Derivatives as MAO Inhibitors by Virtual Screening: A Potential Lead for Neurodegenerative Disorders.Central nervous system agents in medicinal chemistry · 2025Article
- Mechanisms involved in the antidepressant-like action of orally administered 5-((4-methoxyphenyl)thio)benzo[c][1,2,5]thiadiazole (MTDZ) in male and female mice.Psychopharmacology · 2024Article
- Prominent Neuroprotective Potential of Indole-2-Pharmaceuticals (Basel, Switzerland) · 2024Article
- Benzodioxane Carboxamide Derivatives As Novel Monoamine Oxidase B Inhibitors with Antineuroinflammatory Activity.ACS medicinal chemistry letters · 2024Article
- Design, Synthesis, and Biological Effect Studies of Novel Benzofuran-Thiazolylhydrazone Derivatives as Monoamine Oxidase Inhibitors.ACS omega · 2024Article
85 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
The three-dimensional structure of recombinant human monoamine oxidase A (hMAO A) as its clorgyline-inhibited adduct is described. Although the chain-fold of hMAO A is similar to that of rat MAO A and human MAO B (hMAO B), hMAO A is unique in that it crystallizes as a monomer and exhibits the solution hydrodynamic behavior of a monomeric form rather than the dimeric form of hMAO B and rat MAO A. hMAO A's active site consists of a single hydrophobic cavity of approximately 550 A3, which is smaller than that determined from the structure of deprenyl-inhibited hMAO B (approximately 700 A3) but larger than that of rat MAO A (approximately 450 A3). An important component of the active site structure of hMAO A is the loop conformation of residues 210-216, which differs from that of hMAO B and rat MAO A. The origin of this structural alteration is suggested to result from long-range interactions in the monomeric form of the enzyme. In addition to serving as a basis for the development of hMAO A specific inhibitors, these data support the proposal that hMAO A involves a change from the dimeric to the monomeric form through a Glu-151 --> Lys mutation that is specific of hMAO A [Andrès, A. M., Soldevila, M., Navarro, A., Kidd, K. K., Oliva, B. & Bertranpetit, J. (2004) Hum. Genet. 115, 377-386]. These considerations put into question the use of MAO A from nonhuman sources in drug development for use in humans.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.