Evidence map›Paper›PMID 36358955›Full record

ArticleBiomolecules2022

Structural Consequences of Deproteinating the 50S Ribosome.

Daniel S D Larsson, Sandesh Kanchugal P, Maria Selmer

Abstract read
In one paragraph

Article in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Mechanistic insights into 50Science advances · 2025
    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

3 authors.

Daniel S D LarssonDepartment of Cell and Molecular Biology, Uppsala University, SE 751 24 Uppsala, Sweden.ORCID 0000-0001-7683-6419
Sandesh Kanchugal PDepartment of Cell and Molecular Biology, Uppsala University, SE 751 24 Uppsala, Sweden.
Maria SelmerDepartment of Cell and Molecular Biology, Uppsala University, SE 751 24 Uppsala, Sweden.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosomes are complex ribonucleoprotein particles. Purified 50S ribosomes subjected to high-salt wash, removing a subset of ribosomal proteins (r-proteins), were shown as competent for in vitro assembly into functional 50S subunits. Here, we used cryo-EM to determine the structures of such LiCl core particles derived from

Indexed as

Escherichia coliRibosomesRibosomal ProteinsRNA, Ribosomal, 23SRibosomal ProteinsRNA, Ribosomal, 23Sribosome assemblyRNA foldingRNA-protein interactionsRNA structuresingle-particle cryo-EM

Identifiers

PMID36358955
PMCPMC9687910

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.