Evidence map›Paper›PMID 36982505›Full record

ArticleInternational journal of molecular sciences2023

Effect of Ovocystatin on Amyloid β 1-42 Aggregation-In Vitro Studies.

Bartłomiej Stańczykiewicz, Tomasz M Goszczyński, Paweł Migdał, Marta Piksa, Krzysztof Pawlik, Jakub Gburek, Krzysztof Gołąb, Bogusława Konopska, Agnieszka Zabłocka

Open access · goldFull text read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

9 authors at 2 institutions in 1 country.

Bartłomiej StańczykiewiczDivision of Consultation Psychiatry and Neuroscience, Department of Psychiatry, Wroclaw Medical University, L. Pasteura 10, 50-367 Wroclaw, Poland.ORCID 0000-0001-9221-3502
Tomasz M GoszczyńskiDepartment of Experimental Oncology, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, R. Weigla 12, 53-114 Wroclaw, Poland.ORCID 0000-0002-9995-3260
Paweł MigdałDepartment of Microbiology, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, 53-114 Wroclaw, Poland.
Marta PiksaDepartment of Microbiology, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, 53-114 Wroclaw, Poland.
Krzysztof PawlikDepartment of Microbiology, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, 53-114 Wroclaw, Poland.ORCID 0000-0002-5881-9292
Jakub GburekDepartment of Pharmaceutical Biochemistry, Division of Pharmaceutical Biochemistry, Wroclaw Medical University, Borowska 211 A, 50-556 Wroclaw, Poland.
Krzysztof GołąbDepartment of Pharmaceutical Biochemistry, Division of Pharmaceutical Biochemistry, Wroclaw Medical University, Borowska 211 A, 50-556 Wroclaw, Poland.ORCID 0000-0002-9257-1497
Bogusława KonopskaDepartment of Pharmaceutical Biochemistry, Division of Pharmaceutical Biochemistry, Wroclaw Medical University, Borowska 211 A, 50-556 Wroclaw, Poland.ORCID 0000-0003-1388-1989
Agnieszka ZabłockaDepartment of Microbiology, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, 53-114 Wroclaw, Poland.ORCID 0000-0002-5707-9886
Ludwik Hirszfeld Institute of Immunology and Experimental Therapy · PLWroclaw Medical University · PL

Funding

Ministry of Education and Science in the "Regional Initiative of Excellence" program for the years 2019-2022 016/RID/2018/19
6 · The paper itself

Abstract

Amyloid β peptides (Aβ) aggregating in the brain have a potential neurotoxic effect and are believed to be a major cause of Alzheimer's disease (AD) development. Thus, inhibiting amyloid polypeptide aggregation seems to be a promising approach to the therapy and prevention of this neurodegenerative disease. The research presented here is directed at the determination of the inhibitory activity of ovocystatin, the cysteine protease inhibitor isolated from egg white, on Aβ42 fibril genesis in vitro. Thioflavin-T (ThT) assays, which determine the degree of aggregation of amyloid peptides based on fluorescence measurement, circular dichroism spectroscopy (CD), and transmission electron microscopy (TEM) have been used to assess the inhibition of amyloid fibril formation by ovocystatin. Amyloid beta 42 oligomer toxicity was measured using the MTT test. The results have shown that ovocystatin possesses Aβ42 anti-aggregation activity and inhibits Aβ42 oligomer toxicity in PC12 cells. The results of this work may help in the development of potential substances able to prevent or delay the process of beta-amyloid aggregation-one of the main reasons for Alzheimer's disease.

Indexed as

Alzheimer DiseaseNeurodegenerative DiseasesAmyloidAmyloid beta-PeptidesAnimalsHumansPeptide FragmentsPeptidesRatsAmyloidAmyloid beta-PeptidesovocystatinPeptide FragmentsPeptidesAlzheimer’s diseaseamyloid beta peptideCDovocystatinTEMThT

Identifiers

PMID36982505
PMCPMC10049317
OpenAlexW4324098253

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read77
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.