ReviewJournal of neural transmission (Vienna, Austria : 1996)2018
The structure of monoamine oxidases: past, present, and future.
Review in Journal of neural transmission (Vienna, Austria : 1996), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 60 citations in OpenAlex.
- Discovery of potent and selective MAO-B inhibitors from a morpholine-substituted chalcone library for neurodegenerative disorders.Molecular diversity · 2026Article
- Genotype-Driven Diagnosis Enables Targeted Pharmacological Treatment in Brunner Syndrome: A Novel Splice-SiteInternational journal of molecular sciences · 2026Review
- A Renal Clearable Probe for In Vivo Monoamine Oxidase (MAO) Detection.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Novel Insights on Benzo[Antioxidants (Basel, Switzerland) · 2026Article
- Dehydrogenases in the Flavoprotein Amine Oxidoreductase Superfamily.Biochemistry · 2025Article
- Exploring neuropharmacokinetics: mechanisms, models, and clinical implications.Encephalitis (Seoul, Korea) · 2025Article
- Design of Benzyl-triazolopyrimidine-Based NADPH Oxidase Inhibitors Leads to the Discovery of a Potent Dual Covalent NOX2/MAOB Inhibitor.Journal of medicinal chemistry · 2025Article
- Theranostic Near-Infrared Monoamine Oxidase Inhibitor (NMI) Protein Binding Interactions with MAOA and Albumin.Pharmaceutical research · 2025Article
- Filtration of Natural Derivatives as MAO Inhibitors by Virtual Screening: A Potential Lead for Neurodegenerative Disorders.Central nervous system agents in medicinal chemistry · 2025Article
- Phenylstyrylpyrimidine derivatives as potential multipotent therapeutics for Alzheimer's disease.RSC medicinal chemistry · 2024Article
- Identification of high-affinity Monoamine oxidase B inhibitors for depression and Parkinson's disease treatment: bioinformatic approach of drug repurposing.Frontiers in pharmacology · 2024Article
- Evaluation of the combined activity of benzimidazole arylhydrazones as new anti-Parkinsonian agents: monoamine oxidase-B inhibition, neuroprotection and oxidative stress modulation.Neural regeneration research · 2021Article
- 4-Phenethyl-1-Propargylpiperidine-Derived Dual Inhibitors of Butyrylcholinesterase and Monoamine Oxidase B.Molecules (Basel, Switzerland) · 2021Article
- Monoamine Oxidase Inhibitors: A Review of Their Anti-Inflammatory Therapeutic Potential and Mechanisms of Action.Frontiers in pharmacology · 2021Review
- Rational Redesign of Monoamine Oxidase A into a Dehydrogenase to Probe ROS in Cardiac Aging.ACS chemical biology · 2020Article
- Synthesis, molecular modelling and biological activity of some pyridazinone derivatives as selective human monoamine oxidase-B inhibitors.Pharmacological reports : PR · 2020Article
- The Antiproliferative Effects of Flavonoid MAO Inhibitors on Prostate Cancer Cells.Molecules (Basel, Switzerland) · 2020Article
- Early Life Stress Induced DNA Methylation of Monoamine Oxidases Leads to Depressive-Like Behavior.Frontiers in cell and developmental biology · 2020Review
- Design, Synthesis, Docking Studies and Monoamine Oxidase Inhibition of a Small Library of 1-acetyl- and 1-thiocarbamoyl-3,5-diphenyl-4,5-dihydro-(1H)-pyrazoles.Molecules (Basel, Switzerland) · 2019Article
- Amphetamine Derivatives as Monoamine Oxidase Inhibitors.Frontiers in pharmacology · 2019Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The first crystal structure of mammalian monoamine oxidases (MAOs) was solved in 2002; almost 65 years after, these FAD-dependent enzymes were discovered and classified as responsible for the oxidation of aromatic neurotransmitters. Both MAO A and MAO B feature a two-domain topology characterized by the Rossmann fold, interacting with dinucleotide cofactors, which is intimately associated to a substrate-binding domain. This globular body is endowed with a C-terminal α-helix that anchors the protein to the outer mitochondrial phospholipid bilayer. As monotopic membrane proteins, the structural elucidation of MAOs was a challenging task that required the screening of different detergent conditions for their purification and crystallization. MAO A and MAO B structures differ both in their oligomerization architecture and in details of their active sites. Purified human MAO B and rat MAO A are dimeric, whereas human MAO A was found to be monomeric, which is believed to result from the detergent treatments used to extract the protein from the membrane. The active site of MAOs consists of a hydrophobic cavity located in front of the flavin cofactor and extending to the protein surface. Some structural features are highly conserved in the two isozymes, such as a Tyr-Tyr aromatic sandwich in front of the flavin ring and a Lys residue hydrogen-bonded to the cofactor N5 atom, whereas a pair of gating residues (Phe208/Ile335 in MAO A; Ile199/Tyr326 in MAO B) specifically determines the different substrate and inhibitor properties of the two enzymes.
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Registered trials
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.