Evidence map›Paper›PMID 36316410›Full record

ArticleNature chemistry2023

Insights into the ribosome function from the structures of non-arrested ribosome-nascent chain complexes.

Egor A Syroegin, Elena V Aleksandrova, Yury S Polikanov

Open access · greenAbstract read
In one paragraph

Article in Nature chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.6field-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

38 citing papers in PubMed, 46 citations in OpenAlex.

  1. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
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  8. Molecular architecture and diversity of StopGo/2A translational recoding.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  9. Article
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  12. Capturing eukaryotic ribosome dynamics in situ at high resolution.Nature structural & molecular biology · 2025
    Article
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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

3 authors at 1 institution in 1 country.

Egor A SyroeginDepartment of Biological Sciences, University of Illinois at Chicago, Chicago, IL, USA.ORCID 0000-0003-2753-3950
Elena V AleksandrovaDepartment of Biological Sciences, University of Illinois at Chicago, Chicago, IL, USA.
Yury S PolikanovDepartment of Biological Sciences, University of Illinois at Chicago, Chicago, IL, USA. yuryp@uic.edu.ORCID 0000-0002-5064-0327
University of Illinois Chicago · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
Molecular mechanisms of action of ribosome-targeting antibiotics.R01GM132302 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI POLIKANOV, YURY · 2019 to 2022
$1.3M
Structural basis of Cfr-mediated resistance to antibiotics targeting the bacterial ribosomeR21AI163466 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI POLIKANOV, YURY · 2021 to 2022
$426k
NIAID NIH HHS R21 AI163466NIGMS NIH HHS P30 GM124165NIGMS NIH HHS R01 GM132302NIH HHS S10 OD021527
6 · The paper itself

Abstract

During protein synthesis, the growing polypeptide threads through the ribosomal exit tunnel and modulates ribosomal activity by itself or by sensing various small molecules, such as metabolites or antibiotics, appearing in the tunnel. While arrested ribosome-nascent chain complexes (RNCCs) have been extensively studied structurally, the lack of a simple procedure for the large-scale preparation of peptidyl-tRNAs, intermediates in polypeptide synthesis that carry the growing chain, means that little attention has been given to RNCCs representing functionally active states of the ribosome. Here we report the facile synthesis of stably linked peptidyl-tRNAs through a chemoenzymatic approach based on native chemical ligation and use them to determine several structures of RNCCs in the functional pre-attack state of the peptidyl transferase centre. These structures reveal that C-terminal parts of the growing peptides adopt the same uniform β-strand conformation stabilized by an intricate network of hydrogen bonds with the universally conserved 23S rRNA nucleotides, and explain how the ribosome synthesizes growing peptides containing various sequences with comparable efficiencies.

Indexed as

Anti-Bacterial AgentsRibosomesPeptidesProtein BiosynthesisRNA, Ribosomal, 23SAnti-Bacterial AgentsPeptidesRNA, Ribosomal, 23S

Identifiers

PMID36316410
PMCPMC9840698
OpenAlexW4307715805

What OpenQuestion holds

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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.