Evidence map›Paper›PMID 29516165›Full record

ReviewJournal of neural transmission (Vienna, Austria : 1996)2018

Kinetics, mechanism, and inhibition of monoamine oxidase.

Rona R Ramsay, Alen Albreht

Abstract readReview
PubMed Publisher
In one paragraph

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 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.6field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

40 citing papers in PubMed, 105 citations in OpenAlex.

  1. Review
  2. A Biomimetic Study of the Behavior ofThe Journal of organic chemistry · 2026
    Article
  3. BAM 15 Exerts Molluscicidal Effects onMolecules (Basel, Switzerland) · 2026
    Article
  4. Article
  5. Reaction of OThe journal of physical chemistry. A · 2025
    Article
  6. Review
  7. Anti-Stress Effects ofNutrients · 2025
    Article
  8. Type A monoamine oxidase; its unique role in mood, behavior and neurodegeneration.Journal of neural transmission (Vienna, Austria : 1996) · 2025
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Computational Chemistry and Molecular Modeling of Reversible MAO Inhibitors.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  18. Medicarpin and Homopterocarpin Isolated fromMolecules (Basel, Switzerland) · 2022
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 2 countries.

Rona R RamsayBiomedical Sciences Research Complex, University of St Andrews, North Haugh, St Andrews, KY16 8QP, UK. rrr@st-andrews.ac.uk.ORCID 0000-0003-1535-4904
Alen AlbrehtDepartment of Food Chemistry, National Institute of Chemistry, Hajdrihova 19, 1000, Ljubljana, Slovenia.ORCID 0000-0003-0594-8899
King's College London · GBUniversity of St Andrews · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Monoamine oxidases (MAOs) catalyse the oxidation of neurotransmitter amines and a wide variety of primary, secondary and tertiary amine xenobiotics, including therapeutic drugs. While inhibition of MAO activity in the periphery removes protection from biogenic amines and so is undesirable, inhibition in the brain gives vital antidepressant and behavioural advantages that make MAO a major pharmaceutical target for inhibitor design. In neurodegenerative diseases, MAO inhibitors can help to maintain neurotransmitter levels, making it a common feature in novel multi-target combinations designed to combat Alzheimer's disease, albeit not yet proven clinically. Vital information for inhibitor design comes from an understanding of the structure, mechanism, and kinetics of the catalyst. This review will summarize the kinetic behaviour of MAO A and B and the kinetic evaluation of reversible inhibitors that transiently decrease catalysis. Kinetic parameters and crystal structures have enabled computational approaches to ligand discovery and validation of hits by docking. Kinetics and a wide variety of substrates and inhibitors along with theoretical modelling have also contributed to proposed schemes for the still debated chemical mechanism of amine oxidation. However, most of the marketed MAO drugs are long-lasting irreversible inactivators. The mechanism of irreversible inhibition by hydrazine, cyclopropylamine, and propargylamine drugs will be discussed. The article finishes with some examples of the propargylamine moiety in multi-target ligand design to combat neurodegeneration.

Indexed as

Drug DesignHumansMonoamine OxidaseMonoamine Oxidase InhibitorsMonoamine OxidaseMonoamine Oxidase InhibitorsChemical mechanismComputation and modellingEnzyme kineticsIrreversible inhibitionMonoamine neurotransmittersMulti-target drug design

Identifiers

PMID29516165
OpenAlexW2790157639

What Socratic holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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 Socratic graph.