Evidence map›Paper›PMID 34834056›Full record

ArticleMolecules (Basel, Switzerland)2021

The Impact of Redox, Hydrolysis and Dehydration Chemistry on the Structural and Magnetic Properties of Magnetoferritin Prepared in Variable Thermal Conditions.

Lucia Balejčíková, Karel Saksl, Jozef Kováč, Anne Martel, Vasil M Garamus, Mikhail V Avdeev, Viktor I Petrenko, László Almásy, Peter Kopčanský

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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 8 institutions in 6 countries.

Lucia BalejčíkováInstitute of Hydrology SAS, Dúbravská Cesta 9, 84104 Bratislava, Slovakia.ORCID 0000-0003-2284-3482
Karel SakslInstitute of Materials Research Slovak Academy of Sciences, Watsonova 47, 04001 Košice, Slovakia.ORCID 0000-0001-8133-5352
Jozef KováčInstitute of Experimental Physic SAS, Watsonova 47, 04001 Košice, Slovakia.ORCID 0000-0002-7793-9564
Anne MartelInstitut Laue-Langevin, 71 Avenue des Martyrs, 38042 Grenoble, France.ORCID 0000-0002-1232-8519
Vasil M GaramusHelmholtz-Zentrum Hereon, Max-Planck-Street 1, 21502 Geesthacht, Germany.ORCID 0000-0001-9315-4188
Mikhail V AvdeevJoint Institute for Nuclear Research, Joliot-Curie Str. 6, 141980 Dubna, Russia.ORCID 0000-0003-0721-4653
Viktor I PetrenkoBCMaterials, Basque Centre for Materials, Applications and Nanostructures, 48940 Leioa, Spain.ORCID 0000-0001-6532-8902
László AlmásyInstitute for Energy Security and Environmental Safety, Centre for Energy Research, Konkoly Thege Mi-klos ut 29-33, 1121 Budapest, Hungary.ORCID 0000-0001-5750-5788
Peter KopčanskýInstitute of Experimental Physic SAS, Watsonova 47, 04001 Košice, Slovakia.ORCID 0000-0002-5278-9504
Institute of Experimental Physics of the Slovak Academy of Sciences · SKHelmholtz-Zentrum Hereon · DEHUN-REN Centre for Energy Research · HUIkerbasque · ESInstitute of Hydrology of the Slovak Academy of Sciences · SKInstitut Laue-Langevin · FRJoint Institute for Nuclear Research · RUSlovak Academy of Sciences · SK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ferritin, a spherically shaped protein complex, is responsible for iron storage in bacteria, plants, animals, and humans. Various ferritin iron core compositions in organisms are associated with specific living requirements, health state, and different biochemical roles of ferritin isomers. Magnetoferritin, a synthetic ferritin derivative, serves as an artificial model system of unusual iron phase structures found in humans. We present the results of a complex structural study of magnetoferritins prepared by controlled in vitro synthesis. Using various complementary methods, it was observed that manipulation of the synthesis technology can improve the physicochemical parameters of the system, which is useful in applications. Thus, a higher synthesis temperature leads to an increase in magnetization due to the formation of the magnetite phase. An increase in the iron loading factor has a more pronounced impact on the protein shell structure in comparison with the pH of the aqueous medium. On the other hand, a higher loading factor at physiological temperature enhances the formation of an amorphous phase instead of magnetite crystallization. It was confirmed that the iron-overloading effect alone (observed during pathological events) cannot contribute to the formation of magnetite.

Indexed as

aqueous mediumloading factormagnetitemagnetoferritinprotein stability

Identifiers

PMID34834056
PMCPMC8619319
OpenAlexW3212079906

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.