Evidence map›Paper›PMID 36169858›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Assay of MAO Inhibition by Chromatographic Techniques (HPLC/HPLC-MS).

Tomás Herraiz

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

1 author at 1 institution in 1 country.

Tomás HerraizInstituto de Ciencia y Tecnología de Alimentos y Nutrición (ICTAN), Spanish National Research Council (CSIC), Madrid, Spain. therraiz@ictan.csic.es.
Instituto de Ciencia y Tecnología de Alimentos y Nutrición · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Monoamine oxidase (MAO) enzymes (MAO A and B) catalyze the oxidative deamination of biogenic amines, neurotransmitters, and xenobiotic amines and contribute to the regulation of the content of these active substances in mammalian organisms. The oxidation of biogenic amines by MAO produces hydrogen peroxide (H

Indexed as

AlkaloidsNeuroprotective Agents1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridineAldehydesAnimalsCarbolinesCationsChromatography, High Pressure LiquidHydrogen PeroxideKynuramineMammalsMass SpectrometryMonoamine OxidaseMonoamine Oxidase InhibitorsNeurotoxinsXenobiotics1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridineAldehydesAlkaloidsCarbolinesCationsHydrogen PeroxideKynuramineMonoamine OxidaseMonoamine Oxidase InhibitorsNeuroprotective AgentsNeurotoxinsXenobiotics1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)1-Methyl-4-phenyl-2,3-dihydropyridinium (MPDP+)4-HydroxyquinolineHarmanHydrogen peroxide (H2O2)KynuramineMAO assayNorharmanRP-HPLCβ-Carbolines

Identifiers

PMID36169858
OpenAlexW4297463276

What OpenQuestion 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 OpenQuestion graph.