Evidence map›Paper›PMID 37138424›Full record

ArticleCurrent computer-aided drug design2024

Molecular Mechanism and Structure-activity Relationship of the Inhibition Effect between Monoamine Oxidase and Selegiline Analogues.

Chuanxi Yang, Xiaoning Wang, Chang Gao, Yunxiang Liu, Ziyi Ma, Jinqiu Zang, Haoce Wang, Lin Liu, Yonglin Liu, Haofen Sun and 1 more

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Article in Current computer-aided drug design, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
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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

11 authors.

Chuanxi YangSchool of Environmental and Municipal Engineering, Qingdao University of Technology, Qingdao, Shandong, 266520, China.
Xiaoning WangSchool of Mechanical Engineering and Automation, Northeastern University, Shenyang, Liaoning, 110819, China.
Chang GaoQingdao Jiaming Measurement and Control Technology Co., Ltd., Qingdao, Shandong, 266000, China.
Yunxiang LiuEnvironmental Monitoring Station of Yuncheng County Environmental Protection Bureau, Heze, Shandong, 274700, China.
Ziyi MaSchool of Environmental and Municipal Engineering, Qingdao University of Technology, Qingdao, Shandong, 266520, China.
Jinqiu ZangSchool of Environmental and Municipal Engineering, Qingdao University of Technology, Qingdao, Shandong, 266520, China.
Haoce WangSchool of Environmental and Municipal Engineering, Qingdao University of Technology, Qingdao, Shandong, 266520, China.
Lin LiuSchool of Environmental and Municipal Engineering, Qingdao University of Technology, Qingdao, Shandong, 266520, China.
Yonglin LiuSchool of Environmental and Municipal Engineering, Qingdao University of Technology, Qingdao, Shandong, 266520, China.
Haofen SunSchool of Environmental and Municipal Engineering, Qingdao University of Technology, Qingdao, Shandong, 266520, China.
Weiliang WangSchool of Environmental and Municipal Engineering, Qingdao University of Technology, Qingdao, Shandong, 266520, China.

Funding

National Natural Science Foundation of China Grant Nos: 41672340,42207019
6 · The paper itself

Abstract

introductionTo investigate the inhibition properties and structure-activity relationship between monoamine oxidase (MAO) and selected monoamine oxidase inhibitors (MAOIs, including selegiline, rasagiline and clorgiline).

methodsThe inhibition effect and molecular mechanism between MAO and MAOIs were identified via the half maximal inhibitory concentration (IC

resultsIt was indicated that selegiline and rasagiline were MAO B inhibitors, but clorgiline was MAO-A inhibitor based on the selectivity index (SI) of MAOIs (0.000264, 0.0197 and 14607.143 for selegiline, rasagiline and clorgiline, respectively). The high-frequency amino acid residues of the MAOIs and MAO were Ser24, Arg51, Tyr69 and Tyr407 for MAO-A and Arg42 and Tyr435 for MAO B. The MAOIs and MAO A/B pharmacophores included the aromatic core, hydrogen bond acceptor, hydrogen bond donor-acceptor and hydrophobic core.

conclusionThis study shows the inhibition effect and molecular mechanism between MAO and MAOIs and provides valuable findings on the design and treatment of Alzheimer's and Parkinson's diseases.

Indexed as

Molecular Docking SimulationMonoamine OxidaseMonoamine Oxidase InhibitorsSelegilineClorgylineHumansIndansStructure-Activity RelationshipClorgylineIndansMonoamine OxidaseMonoamine Oxidase InhibitorsrasagilineSelegilineAlzheimer'shydrophobicity.molecular dockingMonoamine oxidaseneurological disorderspharmacophore

Identifiers

PMID37138424

What OpenQuestion holds

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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.