ArticleProceedings of the National Academy of Sciences of the United States of America2008
Structure of human monoamine oxidase A at 2.2-A resolution: the control of opening the entry for substrates/inhibitors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 218 papers, 2 of them syntheses that pooled it.
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Who cites it
218 citing papers in PubMed, 2 syntheses or guidelines pooled it, 599 citations in OpenAlex.
- Meta-analysis examining the association between low platelet monoamine oxidase levels and Zuckerman's sensation seeking scale in a sex dependent manner.Frontiers in psychology · 2025Pooled it
- Marine natural products with monoamine oxidase (MAO) inhibitory activity.Pharmaceutical biology · 2020Pooled it
- Discovery of novel N-(prop-2-yn-1-yl)-1,2,3,4-tetrahydronaphthalen-1-amine derivatives as MAO-B inhibitors for the treatment of Parkinson's disease.Journal of enzyme inhibition and medicinal chemistry · 2026Article
- Exploring the Neuropharmacological Potential of Ligustrum sinense Relevant to Parkinson's Disease: In Vivo and In Silico Study.Chemistry & biodiversity · 2026Article
- Evaluation of Novel Isatin-Schiff Base Derivatives: Monoamine Oxidase Inhibition and Antimicrobial Assessment.ChemMedChem · 2026Article
- Phytochemical Characterization ofMolecules (Basel, Switzerland) · 2026Article
- Rational Design of Multifunctional Tacrine Derivatives as Candidates for the Treatment of Alzheimer and Parkinson Diseases.ChemMedChem · 2026Article
- In-depth multimodal validation ofExperimental & molecular medicine · 2026Article
- DYRK1A and Parkinson's disease, facts and hypotheses.Neurobiology of disease · 2026Review
- Development of 1-(substituted benzofuran-2-yl)-3-(halogen-substituted phenyl)prop-2-en-1-ones as potent, reversible, and selective MAO-B inhibitors for Parkinson's Disease.Scientific reports · 2026Article
- Monoamine Oxidase and Cholinesterase Inhibition Profiles of Semicarbazone and Thiosemicarbazone Derivatives.Chemistry & biodiversity · 2026Article
- Article
- Exploring the Biological Potency of Carotenoids Against Alzheimer's Disease: An Integrated Approach of Molecular Docking and Molecular Dynamics.Current issues in molecular biology · 2026Article
- Benzylisoquinoline Alkaloid Production in Yeast via Norlaudanosoline Improves Titer, Selectivity, and Yield.ACS synthetic biology · 2026Article
- A Single Flavoenzyme Forges the Pentacyclic Skeleton of α-Cyclopiazonic Acid.Journal of the American Chemical Society · 2026Article
- Behavioral, Biochemical, andPharmaceuticals (Basel, Switzerland) · 2026Article
- Novel Insights on Benzo[Antioxidants (Basel, Switzerland) · 2026Article
- The discovery of monoamine oxidase inhibitors: virtual screening and in vitro inhibition potencies.Journal of computer-aided molecular design · 2026Article
- Indole Scaffolds in Neurological Therapeutics: Synthesis, Structure- Activity Relationships and Drug-Receptor Interactions.Mini reviews in medicinal chemistry · 2026Review
- Potential of MAO-B Inhibitors with Multi-target Inhibition and Antioxidant Properties for the Treatment of Neurodegenerative Disorders.Mini reviews in medicinal chemistry · 2026Review
158 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mitochondrial outer membrane-anchored monoamine oxidase (MAO) is a biochemically important flavoenzyme that catalyzes the deamination of biogenic and xenobiotic amines. Its two subtypes, MAOA and MAOB, are linked to several psychiatric disorders and therefore are interesting targets for drug design. To understand the relationship between structure and function of this enzyme, we extended our previous low-resolution rat MAOA structure to the high-resolution wild-type and G110A mutant human MAOA structures at 2.2 and 2.17 A, respectively. The high-resolution MAOA structures are similar to those of rat MAOA and human MAOB, but different from the known structure of human MAOA [De Colibus L, et al. (2005) Proc Natl Acad Sci USA 102:12684-12689], specifically regarding residues 108-118 and 210-216, which surround the substrate/inhibitor cavity. The results confirm that the inhibitor selectivity of MAOA and MAOB is caused by the structural differences arising from Ile-335 in MAOA vs. Tyr-326 in MAOB. The structures exhibit a C-terminal transmembrane helix with clear electron density, as is also seen in rat MAOA. Mutations on one residue of loop 108-118, G110, which is far from the active center but close to the membrane surface, cause the solubilized enzyme to undergo a dramatic drop in activity, but have less effect when the enzyme is anchored in the membrane. These results suggest that the flexibility of loop 108-118, facilitated by anchoring the enzyme into the membrane, is essential for controlling substrate access to the active site. We report on the observation of the structure-function relationship between a transmembrane helical anchor and an extra-membrane domain.
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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.