Evidence map›Paper›PMID 33008049›Full record

ReviewInternational journal of molecular sciences2020

Biological Functions of Prokaryotic Amyloids in Interspecies Interactions: Facts and Assumptions.

Anastasiia O Kosolapova, Kirill S Antonets, Mikhail V Belousov, Anton A Nizhnikov

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. OmpC and OmpF Outer Membrane Proteins ofInternational journal of molecular sciences · 2023
    Article
  7. Amyloid Fibrils ofInternational journal of molecular sciences · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. RopB protein ofFrontiers in plant science · 2022
    Article
  13. Microbiome Impact on Amyloidogenesis.Frontiers in molecular biosciences · 2022
    Review
  14. Review
  15. Review
  16. Review
  17. 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

4 authors at 1 institution in 1 country.

Anastasiia O KosolapovaLaboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology (ARRIAM), 196608 St. Petersburg, Russia.ORCID 0000-0003-1674-8809
Kirill S AntonetsLaboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology (ARRIAM), 196608 St. Petersburg, Russia.ORCID 0000-0002-8575-2601
Mikhail V BelousovLaboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology (ARRIAM), 196608 St. Petersburg, Russia.ORCID 0000-0002-7856-9075
Anton A NizhnikovLaboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology (ARRIAM), 196608 St. Petersburg, Russia.ORCID 0000-0002-8338-3494
St Petersburg University · RU

Funding

Russian Science Foundation 17-16-01100Russian Science Foundation 19-76-00026
6 · The paper itself

Abstract

Amyloids are fibrillar protein aggregates with an ordered spatial structure called "cross-β". While some amyloids are associated with development of approximately 50 incurable diseases of humans and animals, the others perform various crucial physiological functions. The greatest diversity of amyloids functions is identified within prokaryotic species where they, being the components of the biofilm matrix, function as adhesins, regulate the activity of toxins and virulence factors, and compose extracellular protein layers. Amyloid state is widely used by different pathogenic bacterial species in their interactions with eukaryotic organisms. These amyloids, being functional for bacteria that produce them, are associated with various bacterial infections in humans and animals. Thus, the repertoire of the disease-associated amyloids includes not only dozens of pathological amyloids of mammalian origin but also numerous microbial amyloids. Although the ability of symbiotic microorganisms to produce amyloids has recently been demonstrated, functional roles of prokaryotic amyloids in host-symbiont interactions as well as in the interspecies interactions within the prokaryotic communities remain poorly studied. Here, we summarize the current findings in the field of prokaryotic amyloids, classify different interspecies interactions where these amyloids are involved, and hypothesize about their real occurrence in nature as well as their roles in pathogenesis and symbiosis.

Indexed as

AmyloidAmyloidosisBacteriaBacterial InfectionsBiofilmsHumansProkaryotic CellsToxins, BiologicalAmyloidToxins, Biologicalamyloidbacteriabiofilmhost–pathogenhost–symbiontinterspecies interactionsmicrobial communityOmpouter membrane proteintoxin

Identifiers

PMID33008049
PMCPMC7582709
OpenAlexW3090490957

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.