Evidence map›Paper›PMID 32887478›Full record

ArticleInternational journal of molecular sciences2020

Antimicrobial and Amyloidogenic Activity of Peptides Synthesized on the Basis of the Ribosomal S1 Protein from Thermus Thermophilus.

Stanislav R Kurpe, Sergei Yu Grishin, Alexey K Surin, Olga M Selivanova, Roman S Fadeev, Ulyana F Dzhus, Elena Yu Gorbunova, Leila G Mustaeva, Vyacheslav N Azev, Oxana V Galzitskaya

Open access · goldAbstract read
In one paragraph

Article 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 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Isolation ofFrontiers in microbiology · 2024
    Article
  2. Article
  3. Creation of New Antimicrobial Peptides.International journal of molecular sciences · 2023
    Article
  4. Review
  5. Ribosomes: The New Role of Ribosomal Proteins as Natural Antimicrobials.International journal of molecular sciences · 2022
    Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Identification of Amyloidogenic Regions inInternational journal of molecular sciences · 2021
    Article
  14. Article
  15. 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

10 authors at 3 institutions in 1 country.

Stanislav R KurpeInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
Sergei Yu GrishinInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.ORCID 0000-0001-7373-9808
Alexey K SurinInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
Olga M SelivanovaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
Roman S FadeevInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russian.
Ulyana F DzhusInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
Elena Yu GorbunovaThe Branch of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
Leila G MustaevaThe Branch of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
Vyacheslav N AzevThe Branch of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
Oxana V GalzitskayaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.ORCID 0000-0002-3962-1520
Institute of Bioorganic Chemistry · RUInstitute of Protein Research · RUInstitute of Theoretical and Experimental Biophysics · RU

Funding

Russian Humanitarian Foundation 18-14-00321
6 · The paper itself

Abstract

Controlling the aggregation of vital bacterial proteins could be one of the new research directions and form the basis for the search and development of antibacterial drugs with targeted action. Such approach may be considered as an alternative one to antibiotics. Amyloidogenic regions can, like antibacterial peptides, interact with the "parent" protein, for example, ribosomal S1 protein (specific only for bacteria), and interfere with its functioning. The aim of the work was to search for peptides based on the ribosomal S1 protein from

Indexed as

Amino Acid SequenceAmyloidogenic ProteinsAnti-Bacterial AgentsBacterial ProteinsCell ProliferationCells, CulturedFibroblastsPeptide FragmentsRibosomal ProteinsSkinThermus thermophilusAmyloidogenic ProteinsAnti-Bacterial AgentsBacterial ProteinsPeptide FragmentsRibosomal Proteinsribosomal protein S1amyloidogenic regionsantibacterial peptidesmass spectrometryproteomeribosomal S1 proteinstoxicity

Identifiers

PMID32887478
PMCPMC7504387
OpenAlexW3082910240

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.