Evidence map›Paper›PMID 34835893›Full record

ArticleNanomaterials (Basel, Switzerland)2021

Mechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides.

Oxana V Galzitskaya, Olga M Selivanova, Elena Y Gorbunova, Leila G Mustaeva, Viacheslav N Azev, Alexey K Surin

Abstract read
In one paragraph

Article in Nanomaterials (Basel, Switzerland), 2021. 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. Insights into Network of Hot Spots of Aggregation in Nucleophosmin 1.International journal of molecular sciences · 2022
    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

6 authors.

Oxana V GalzitskayaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0002-3962-1520
Olga M SelivanovaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Elena Y GorbunovaThe Branch of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Russia.
Leila G MustaevaThe Branch of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Russia.
Viacheslav N AzevThe Branch of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0003-3275-4811
Alexey K SurinInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.

Funding

RUSSIAN SCIENCE FOUNDATION 18-14-00321
6 · The paper itself

Abstract

Under certain conditions, many proteins/peptides are capable of self-assembly into various supramolecular formations: fibrils, films, amyloid gels. Such formations can be associated with pathological phenomena, for example, with various neurodegenerative diseases in humans (Alzheimer's, Parkinson's and others), or perform various functions in the body, both in humans and in representatives of other domains of life. Recently, more and more data have appeared confirming the ability of many known and, probably, not yet studied proteins/peptides, to self-assemble into quaternary structures. Fibrils, biofilms and amyloid gels are promising objects for the developing field of research of nanobiotechnology. To develop methods for obtaining nanobiomaterials with desired properties, it is necessary to study the mechanism of such structure formation, as well as the influence of various factors on this process. In this work, we present the results of a study of the structure of biogels formed by four 10-membered amyloidogenic peptides: the VDSWNVLVAG peptide (AspNB) and its analogue VESWNVLVAG (GluNB), which are amyloidogenic fragments of the glucantransferase Bgl2p protein from a yeast cell wall, and amyloidogenic peptides Aβ(31-40), Aβ(33-42) from the Aβ(1-42) peptide. Based on the analysis of the data, we propose a possible mechanism for the formation of amyloid gels with these peptides.

Indexed as

amyloid fibrilamyloidogenic regionsAβ peptidebiofilmoligomer

Identifiers

PMID34835893
PMCPMC8621528

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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.