Evidence map›Paper›PMID 39201616›Full record

ArticleInternational journal of molecular sciences2024

A Cationic Zn-Phthalocyanine Turns Alzheimer's Amyloid β Aggregates into Non-Toxic Oligomers and Inhibits Neurotoxicity in Culture.

Abdullah Md Sheikh, Shatera Tabassum, Shozo Yano, Fatema Binte Abdullah, Ruochen Wang, Takahisa Ikeue, Atsushi Nagai

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 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. Article
  2. Mechanism of Metal Complexes in Alzheimer's Disease.International journal of molecular sciences · 2024
    Review
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

7 authors.

Abdullah Md SheikhDepartment of Laboratory Medicine, Shimane University Faculty of Medicine, 89-1 Enya Cho, Izumo 693-8501, Japan.ORCID 0000-0003-1221-7787
Shatera TabassumDepartment of Laboratory Medicine, Shimane University Faculty of Medicine, 89-1 Enya Cho, Izumo 693-8501, Japan.
Shozo YanoDepartment of Laboratory Medicine, Shimane University Faculty of Medicine, 89-1 Enya Cho, Izumo 693-8501, Japan.ORCID 0000-0002-9210-2949
Fatema Binte AbdullahDepartment of Neurology, Shimane University Faculty of Medicine, 89-1 Enya Cho, Izumo 693-8501, Japan.
Ruochen WangDepartment of Neurology, Shimane University Faculty of Medicine, 89-1 Enya Cho, Izumo 693-8501, Japan.
Takahisa IkeueDepartment of Chemistry, Graduate School of Science and Engineering, Shimane University, 1060 Nishikawatsu, Matsue 690-8504, Japan.
Atsushi NagaiDepartment of Laboratory Medicine, Shimane University Faculty of Medicine, 89-1 Enya Cho, Izumo 693-8501, Japan.ORCID 0000-0002-9280-8044

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid β peptide (Aβ) aggregation and deposition are considered the main causes of Alzheimer's disease. In a previous study, we demonstrated that anionic Zn-phthalocyanine (ZnPc) can interact with the Aβ peptide and inhibit the fibril-formation process. However, due to the inability of anionic ZnPc to cross the intact blood-brain barrier, we decided to explore the interaction of cationic methylated Zn-phthalocyanine (cZnPc) with the peptide. Using a ThT fluorescence assay, we observed that cZnPc dose-dependently and time-dependently inhibited Aβ

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesIndolesIsoindolesOrganometallic CompoundsPeptide FragmentsZinc CompoundsAnimalsHumansMolecular Docking SimulationNeuronsProtein AggregatesAmyloid beta-Peptidesamyloid beta-protein (1-42)IndolesIsoindolesOrganometallic CompoundsPeptide FragmentsProtein AggregatesZinc CompoundsZn(II)-phthalocyanineAlzheimer’s diseaseamyloid βamyloid β bindingfibril formationneurodegenerationoligomers

Identifiers

PMID39201616
PMCPMC11354870

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.