ArticleToxins2022
Insight into the Molecular Mechanism for the Discrepant Inhibition of Microcystins (MCLR, LA, LF, LW, LY) on Protein Phosphatase 2A.
Article in Toxins, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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.
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.
Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Evaluating the Potential Inhibition of PP2A by Nodularin-R Disinfection By-Products: Effect and Mechanism.Toxins · 2025Article
- Global Occurrence of Cyanotoxins in Drinking Water Systems: Recent Advances, Human Health Risks, Mitigation, and Future Directions.Life (Basel, Switzerland) · 2025Review
- Regulation Effectiveness and Mechanism of Biotransformation Pathway on the Toxicity of Microcystin-LR Target to Protein Phosphatase 2A.International journal of environmental research and public health · 2023Article
- Mechanism for the Potential Inhibition Effect of Microcystin-LR Disinfectant By-Products on Protein Phosphatase 2A.Toxins · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microcystins (MCs) exhibit diversified inhibition effects on protein phosphatases (PPs) due to their structural differences. To fully evaluate the potential mechanism for the discrepant inhibition effects, the five most frequent MCs with varying residues at position Z4 were selected as the tested toxins. Their inhibition sequence on PP2A was detected as follows: MCLR > MCLW > MCLA > MCLF > MCLY. Combined with homology modeling and molecular docking technology, the major interaction parameters between the MCs and PP2A were obtained. The correlation analysis for the major interaction parameters and inhibition effects showed that the hydrophobicity of Z4 had an important influence on the interaction of the MCs to PP2A. The introduction of hydrophobic Z4 directly weakened hydrogen bonds Z4→Pro213 and Z4←Arg214, indirectly weakened hydrogen bonds Adda5←Asn117, Glu6←Arg89, and MeAsp3←Arg89, but indirectly enhanced ionic bonds Glu6←Arg89, Glu6-Mn12+, and Glu6-Mn22+. In this way, the combination of the MCs with PP2A was blocked, and thus, the interactions between PP2A and the Mn2+ ions (in the catalytic center) were further affected; metal bonds Asp85-Mn12+ and Asp85-Mn22+ were weakened, while metal bond His241-Mn12+ was enhanced. As a result, the interactions in the catalytic center were inhibited to varying degrees, resulting in the reduced toxicity of MCs.
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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.