Evidence map›Paper›PMID 32701952›Full record

ArticlePLoS biology2020

Accumulation of storage proteins in plant seeds is mediated by amyloid formation.

Kirill S Antonets, Mikhail V Belousov, Anna I Sulatskaya, Maria E Belousova, Anastasiia O Kosolapova, Maksim I Sulatsky, Elena A Andreeva, Pavel A Zykin, Yury V Malovichko, Oksana Y Shtark and 10 more

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
9.0field-weighted citation impact, top 2% 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

41 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Review
  3. Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  4. The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  5. Article
  6. Article
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  10. Article
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  14. Review
  15. Review
  16. Article
  17. Biochemistry · 2023
    Article
  18. Review
  19. OmpC and OmpF Outer Membrane Proteins ofInternational journal of molecular sciences · 2023
    Article
  20. Amyloid Fibrils ofInternational journal of molecular sciences · 2023
    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

20 authors at 6 institutions in 2 countries.

Kirill S AntonetsAll-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.ORCID 0000-0002-8575-2601
Mikhail V BelousovAll-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.ORCID 0000-0002-7856-9075
Anna I SulatskayaInstitute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia.
Maria E BelousovaAll-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.ORCID 0000-0002-2886-026X
Anastasiia O KosolapovaAll-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.
Maksim I SulatskyInstitute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia.ORCID 0000-0003-4665-3181
Elena A AndreevaSt. Petersburg State University, St. Petersburg, Russia.ORCID 0000-0002-9326-3170
Pavel A ZykinSt. Petersburg State University, St. Petersburg, Russia.ORCID 0000-0003-1624-6163
Yury V MalovichkoAll-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.ORCID 0000-0002-2963-7932
Oksana Y ShtarkAll-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.ORCID 0000-0002-3656-4559
Anna N LykholaySt. Petersburg State University, St. Petersburg, Russia.
Kirill V VolkovSt. Petersburg State University, St. Petersburg, Russia.ORCID 0000-0002-8027-5930
Irina M KuznetsovaInstitute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia.ORCID 0000-0002-3336-4834
Konstantin K TuroverovInstitute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia.ORCID 0000-0002-6977-1896
Elena Y KochetkovaInstitute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia.ORCID 0000-0002-6897-7171
Alexander G BobylevInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.ORCID 0000-0002-9477-1214
Konstantin S UsachevLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan, Russia.ORCID 0000-0002-6331-7764
Oleg N DemidovInstitute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia.ORCID 0000-0003-4323-7174
Igor A TikhonovichAll-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.ORCID 0000-0001-8968-854X
Anton A NizhnikovAll-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.ORCID 0000-0002-8338-3494
St Petersburg University · RUInstitute of Cytology · RUAll-Russian Research Institute of Agricultural Microbiology · RUInserm · FRInstitute of Theoretical and Experimental Biophysics · RUKazan Federal University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloids are protein aggregates with a highly ordered spatial structure giving them unique physicochemical properties. Different amyloids not only participate in the development of numerous incurable diseases but control vital functions in archaea, bacteria and eukarya. Plants are a poorly studied systematic group in the field of amyloid biology. Amyloid properties have not yet been demonstrated for plant proteins under native conditions in vivo. Here we show that seeds of garden pea Pisum sativum L. contain amyloid-like aggregates of storage proteins, the most abundant one, 7S globulin Vicilin, forms bona fide amyloids in vivo and in vitro. Full-length Vicilin contains 2 evolutionary conserved β-barrel domains, Cupin-1.1 and Cupin-1.2, that self-assemble in vitro into amyloid fibrils with similar physicochemical properties. However, Cupin-1.2 fibrils unlike Cupin-1.1 can seed Vicilin fibrillation. In vivo, Vicilin forms amyloids in the cotyledon cells that bind amyloid-specific dyes and possess resistance to detergents and proteases. The Vicilin amyloid accumulation increases during seed maturation and wanes at germination. Amyloids of Vicilin resist digestion by gastrointestinal enzymes, persist in canned peas, and exhibit toxicity for yeast and mammalian cells. Our finding for the first time reveals involvement of amyloid formation in the accumulation of storage proteins in plant seeds.

Indexed as

AmyloidDetergentsEscherichia coliIonsPancreatinPepsin APisum sativumProtein AggregatesProtein DomainsRecombinant ProteinsSaccharomyces cerevisiaeSeedsSeed Storage ProteinsAmyloidDetergentsIonsPancreatinPepsin AProtein AggregatesRecombinant ProteinsSeed Storage Proteinsvicilin protein, plant

Identifiers

PMID32701952
PMCPMC7377382
OpenAlexW3044190411

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.