Evidence map›Paper›PMID 36430405›Full record

ArticleInternational journal of molecular sciences2022

Destruction of Lysozyme Amyloid Fibrils Induced by Magnetoferritin and Reconstructed Ferritin.

Jan Gombos, Lucia Balejcikova, Peter Kopcansky, Marianna Batkova, Katarina Siposova, Jozef Kovac, Kristina Zolochevska, Ivo Safarik, Alica Lokajova, Vasil M Garamus and 2 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. 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
0.8field-weighted citation impact, top 25% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. 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

12 authors at 4 institutions in 3 countries.

Jan GombosDepartment of Medical Biochemistry, Jessenius Faculty of Medicine, Comenius University, 036 01 Martin, Slovakia.
Lucia BalejcikovaInstitute of Hydrology, Slovak Academy of Sciences, 841 01 Bratislava, Slovakia.ORCID 0000-0003-2284-3482
Peter KopcanskyInstitute of Experimental Physics, Slovak Academy of Sciences, 040 01 Kosice, Slovakia.ORCID 0000-0002-5278-9504
Marianna BatkovaInstitute of Experimental Physics, Slovak Academy of Sciences, 040 01 Kosice, Slovakia.ORCID 0000-0003-4735-8942
Katarina SiposovaInstitute of Experimental Physics, Slovak Academy of Sciences, 040 01 Kosice, Slovakia.ORCID 0000-0003-2778-5023
Jozef KovacInstitute of Experimental Physics, Slovak Academy of Sciences, 040 01 Kosice, Slovakia.ORCID 0000-0002-7793-9564
Kristina ZolochevskaInstitute of Experimental Physics, Slovak Academy of Sciences, 040 01 Kosice, Slovakia.
Ivo SafarikDepartment of Nanobiotechnology, Biology Centre, ISBB, Czech Academy of Sciences, 370 05 Ceske Budejovice, Czech Republic.
Alica LokajovaDepartment of Medical Biochemistry, Jessenius Faculty of Medicine, Comenius University, 036 01 Martin, Slovakia.
Vasil M GaramusHelmholtz-Zentrum Hereon, Max-Planck-Str. 1, 21502 Geesthacht, Germany.ORCID 0000-0001-9315-4188
Dusan DobrotaDepartment of Medical Biochemistry, Jessenius Faculty of Medicine, Comenius University, 036 01 Martin, Slovakia.
Oliver StrbakBiomedical Center Martin, Jessenius Faculty of Medicine, Comenius University, 036 01 Martin, Slovakia.ORCID 0000-0002-0212-3392
Slovak Academy of Sciences · SKComenius University Bratislava · SKHelmholtz-Zentrum Hereon · DERegional Centre of Advanced Technologies and Materials · CZ

Funding

Competence Centre Martin ITMS code: 26220220153Ministry of Health of the Slovak Republic 2018/11-UKMT-7MVTS SKTW AMAZON SAS-MOST JRP 2021/2Scientific Grant Agency of the Ministry of Education, Science, Research and Sport of the Slovak Republic and the Slovak Academy of Sciences VEGA 2/0044/20Slovak Research and Development Agency APVV-19-0324Structural Funds of EU, Ministry of Education, Slovakia ITMS 313011T548 MODEX
6 · The paper itself

Abstract

Neurodegenerative disorders, including Alzheimer's disease (AD), Parkinson's disease (PD), or systemic amyloidosis, are characterized by the specific protein transformation from the native state to stable insoluble deposits, e.g., amyloid plaques. The design of potential therapeutic agents and drugs focuses on the destabilization of the bonds in their beta-rich structures. Surprisingly, ferritin derivatives have recently been proposed to destabilize fibril structures. Using atomic force microscopy (AFM) and fluorescence spectrophotometry, we confirmed the destructive effect of reconstructed ferritin (RF) and magnetoferritin (MF) on lysosome amyloid fibrils (LAF). The presence of iron was shown to be the main factor responsible for the destruction of LAF. Moreover, we found that the interaction of RF and MF with LAF caused a significant increase in the release of potentially harmful ferrous ions. Zeta potential and UV spectroscopic measurements of LAF and ferritin derivative mixtures revealed a considerable difference in RF compared to MF. Our results contribute to a better understanding of the mechanism of fibril destabilization by ferritin-like proteins. From this point of view, ferritin derivatives seem to have a dual effect: therapeutic (fibril destruction) and adverse (oxidative stress initiated by increased Fe

Indexed as

AmyloidMuramidaseApoferritinsFerritinsIronOxidesAmyloidApoferritinsFerritinsIronmagnetoferritinMuramidaseOxidesdestructionferritiniron releaselysozyme amyloid fibrilsmagnetoferritinreconstructed ferritin

Identifiers

PMID36430405
PMCPMC9696235
OpenAlexW4309009840

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.