Evidence map›Paper›PMID 34200244›Full record

ArticleInternational journal of molecular sciences2021

RbfA Is Involved in Two Important Stages of 30S Subunit Assembly: Formation of the Central Pseudoknot and Docking of Helix 44 to the Decoding Center.

Elena M Maksimova, Alexey P Korepanov, Olesya V Kravchenko, Timur N Baymukhametov, Alexander G Myasnikov, Konstantin S Vassilenko, Zhanna A Afonina, Elena A Stolboushkina

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

  1. Inhibition of ascorbic acid on Pseudomonas bubulae under super-chilled storage.World journal of microbiology & biotechnology · 2026
    Article
  2. Mechanism of 30S subunit recognition and modification by the conserved bacterial ribosomal RNA methyltransferase RsmI.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. A general overview of the multifactorial adaptation to cold: biochemical mechanisms and strategies.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Review
  8. 30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtC.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. GTPase Era at the heart of ribosome assembly.Frontiers in molecular biosciences · 2023
    Review
  15. Article
  16. Increasing Complexity of Ribosomes and Their Biogenesis.International journal of molecular sciences · 2022
    Article
  17. Article
  18. 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

8 authors at 3 institutions in 2 countries.

Elena M MaksimovaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0001-8729-6526
Alexey P KorepanovInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Olesya V KravchenkoInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Timur N BaymukhametovNational Research Center, "Kurchatov Institute", Akademika Kurchatova pl. 1, 123182 Moscow, Russia.ORCID 0000-0001-8069-9998
Alexander G MyasnikovPetersburg Nuclear Physics Institute named by B.P. Konstantinov of NRC "Kurchatov Institute", 188300 Gatchina, Russia.
Konstantin S VassilenkoInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Zhanna A AfoninaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Elena A StolboushkinaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Institute of Protein Research · RUKurchatov Institute · RUSt. Jude Children's Research Hospital · US

Funding

Russian Science Foundation RSF 19-74-20186
6 · The paper itself

Abstract

Ribosome biogenesis is a highly coordinated and complex process that requires numerous assembly factors that ensure prompt and flawless maturation of ribosomal subunits. Despite the increasing amount of data collected, the exact role of most assembly factors and mechanistic details of their operation remain unclear, mainly due to the shortage of high-resolution structural information. Here, using cryo-electron microscopy, we characterized 30S ribosomal particles isolated from an

Indexed as

Binding SitesCryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsModels, MolecularProtein BindingRibosomal ProteinsRibosomesRibosome Subunits, Small, BacterialEscherichia coli ProteinsRbfA protein, E coliRibosomal Proteins30S subunit maturationcryo-EMRbfAribosome assemblytwo-dimensional gel electrophoresis

Identifiers

PMID34200244
PMCPMC8201178
OpenAlexW3172861586

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.