Evidence map›Paper›PMID 39459245›Full record

ArticleMolecules (Basel, Switzerland)2024

A New Activity Assay Method for Diamine Oxidase Based on Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry.

Jan Strnad, Miroslav Soural, Marek Šebela

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2024. 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
–field-weighted citation impact
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.

  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

3 authors.

Jan StrnadDepartment of Biochemistry, Faculty of Science, Palacký University, Šlechtitelů 27, CZ-779 00 Olomouc, Czech Republic.ORCID 0009-0009-3439-2771
Miroslav SouralDepartment of Organic Chemistry, Faculty of Science, Palacký University, 17. listopadu 12, CZ-771 46 Olomouc, Czech Republic.ORCID 0000-0001-7288-8617
Marek ŠebelaDepartment of Biochemistry, Faculty of Science, Palacký University, Šlechtitelů 27, CZ-779 00 Olomouc, Czech Republic.ORCID 0000-0001-9835-1375

Funding

Palacký University Olomouc IGA_PrF_2022_025
6 · The paper itself

Abstract

Copper-containing diamine oxidases are ubiquitous enzymes that participate in many important biological processes. These processes include the regulation of cell growth and division, programmed cell death, and responses to environmental stressors. Natural substrates include, for example, putrescine, spermidine, and histamine. Enzymatic activity is typically assayed using spectrophotometric, electrochemical, or fluorometric methods. The aim of this study was to develop a method for measuring activity using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry based on the intensity ratio of product to product-plus-substrate signals in the reaction mixtures. For this purpose, an enzyme purified to homogeneity from pea (

Indexed as

Amine Oxidase (Copper-Containing)Spectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationEnzyme AssaysKineticsPisum sativumSubstrate SpecificityAmine Oxidase (Copper-Containing)activity assayamine oxidaseenzyme kineticsMALDIpolyaminereaction rate

Identifiers

PMID39459245
PMCPMC11509957

What OpenQuestion holds

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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.