ArticleJournal of neural transmission (Vienna, Austria : 1996)2007
New insights into the structures and functions of human monoamine oxidases A and B.
Article in Journal of neural transmission (Vienna, Austria : 1996), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
6 citing papers in PubMed, 37 citations in OpenAlex.
- Assay of MAO Inhibition by Chromatographic Techniques (HPLC/HPLC-MS).Methods in molecular biology (Clifton, N.J.) · 2023Article
- Study on the Neuroprotective, Radical-Scavenging and MAO-B Inhibiting Properties of New Benzimidazole Arylhydrazones as Potential Multi-Target Drugs for the Treatment of Parkinson's Disease.Antioxidants (Basel, Switzerland) · 2022Article
- Gene expression of serotonergic markers in peripheral blood mononuclear cells of patients with late-onset Alzheimer's disease.Heliyon · 2020Article
- Predicting monoamine oxidase inhibitory activity through ligand-based models.Current topics in medicinal chemistry · 2012Review
- Catalytic and inhibitor binding properties of zebrafish monoamine oxidase (zMAO): comparisons with human MAO A and MAO B.Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology · 2011Article
- Structure of human monoamine oxidase A at 2.2-A resolution: the control of opening the entry for substrates/inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural studies on recombinant human monoamine oxidase A (hMAO-A) provides interesting insights on comparison with that determined for human MAO-B (hMAO-B) as well as comparison with that previously published for rat MAO-A. The active site cavity of hMAO-A is monopartite (as with rat MAO-A) while hMAO-B is a bipartite cavity. hMAO-A crystallizes as a monomeric form, in contrast to the dimeric forms exhibited by hMAO-B and rat MAO-A. All of the known MAO structures show nearly identical geometries around the covalent FAD sites. Differences in active site cavity structures occur away from the FAD site through conformational alterations (MAO-A's) and by changes in amino acid residues (hMAO-A and hMAO-B). Differences observed between human and rat MAO-A's raise questions regarding the appropriateness of the rat model in the development of MAO-A specific inhibitors as drugs for eventual human use.
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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.