Evidence map›Paper›PMID 31690032›Full record

ArticleBiomolecules2019

Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule Bacterium

Anastasiia O Kosolapova, Mikhail V Belousov, Anna I Sulatskaya, Maria E Belousova, Maksim I Sulatsky, Kirill S Antonets, Kirill V Volkov, Anna N Lykholay, Oksana Y Shtark, Ekaterina N Vasileva and 7 more

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
4.7field-weighted citation impact, top 6% 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

13 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. OmpC and OmpF Outer Membrane Proteins ofInternational journal of molecular sciences · 2023
    Article
  5. Amyloid Fibrils ofInternational journal of molecular sciences · 2023
    Article
  6. Article
  7. RopB protein ofFrontiers in plant science · 2022
    Article
  8. Review
  9. Review
  10. Review
  11. Lifestyle adaptations ofProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Review
  13. 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

17 authors at 4 institutions in 1 country.

Anastasiia O KosolapovaLaboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology (ARRIAM), 196608 St. Petersburg, Russia. kosolapova97@mail.ru.
Mikhail V BelousovLaboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology (ARRIAM), 196608 St. Petersburg, Russia. belousovmix@gmail.com.
Anna I SulatskayaLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of Sciences, 194064 St. Petersburg, Russia. ansul@mail.ru.
Maria E BelousovaLaboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology (ARRIAM), 196608 St. Petersburg, Russia. coryphella@mail.ru.
Maksim I SulatskyLaboratory of Cell Morphology, Institute of Cytology of the Russian Academy of Sciences, 194064 St. Petersburg, Russia. m_sulatsky@mail.ru.
Kirill S AntonetsLaboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology (ARRIAM), 196608 St. Petersburg, Russia. k.antonets@arriam.ru.
Kirill V VolkovResearch Resource Center "Molecular and Cell Technologies", Research Park, St. Petersburg State University (SPbSU), 199034 St. Petersburg, Russia. kirill.volkov@spbu.ru.
Anna N LykholayResearch Resource Center "Molecular and Cell Technologies", Research Park, St. Petersburg State University (SPbSU), 199034 St. Petersburg, Russia. lankira@mail.ru.
Oksana Y ShtarkDepartment of Biotechnology, All-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, 196608, Russia. oshtark@yandex.ru.
Ekaterina N VasilevaFaculty of Biology, St. Petersburg State University (SPbSU), 199034 St. Petersburg, Russia. evasilieva@arriam.ru.
Vladimir A ZhukovDepartment of Biotechnology, All-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, 196608, Russia. vzhukov@arriam.ru.
Alexandra N IvanovaResearch Resource Center "Molecular and Cell Technologies", Research Park, St. Petersburg State University (SPbSU), 199034 St. Petersburg, Russia. alyx@bk.ru.
Pavel A ZykinFaculty of Biology, St. Petersburg State University (SPbSU), 199034 St. Petersburg, Russia. pavel.zykin@gmail.com.
Irina M KuznetsovaLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of Sciences, 194064 St. Petersburg, Russia. imk@incras.ru.
Konstantin K TuroverovLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of Sciences, 194064 St. Petersburg, Russia. kkt@incras.ru.
Igor A TikhonovichFaculty of Biology, St. Petersburg State University (SPbSU), 199034 St. Petersburg, Russia. i.tikhonovich@spbu.ru.
Anton A NizhnikovLaboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology (ARRIAM), 196608 St. Petersburg, Russia. a.nizhnikov@arriam.ru.
St Petersburg University · RUAll-Russian Research Institute of Agricultural Microbiology · RUInstitute of Cytology · RUPeter the Great St. Petersburg Polytechnic University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloids represent protein fibrils with a highly ordered spatial structure, which not only cause dozens of incurable human and animal diseases but also play vital biological roles in Archaea, Bacteria, and Eukarya. Despite the fact that association of bacterial amyloids with microbial pathogenesis and infectious diseases is well known, there is a lack of information concerning the amyloids of symbiotic bacteria. In this study, using the previously developed proteomic method for screening and identification of amyloids (PSIA), we identified amyloidogenic proteins in the proteome of the root nodule bacterium

Indexed as

Amyloidogenic ProteinsBacterial ProteinsGene Expression Regulation, BacterialPlantsRhizobium leguminosarumRoot Nodules, PlantAmyloidogenic ProteinsBacterial ProteinsRopA protein, bacteriaRopB protein, Rhizobium leguminosarumamyloidbacteriafibrilouter membrane proteinplant–microbial interactionporinRhizobium leguminosarumroot noduleRopARopB

Identifiers

PMID31690032
PMCPMC6920782
OpenAlexW2988239301

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.