Evidence map›Paper›PMID 36834797›Full record

ReviewInternational journal of molecular sciences2023

Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function.

Lijuan Qiu, Wen Chao, Shan Zhong, An-Jing Ren

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

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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

4 authors.

Lijuan QiuExperimental Teaching Center, College of Basic Medical Sciences, Naval Medical University, Shanghai 200433, China.
Wen ChaoExperimental Teaching Center, College of Basic Medical Sciences, Naval Medical University, Shanghai 200433, China.
Shan ZhongExperimental Teaching Center, College of Basic Medical Sciences, Naval Medical University, Shanghai 200433, China.
An-Jing RenExperimental Teaching Center, College of Basic Medical Sciences, Naval Medical University, Shanghai 200433, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ribosomal protein RPS5 is one of the prime proteins to combine with RNA and belongs to the conserved ribosomal protein family. It plays a substantial role in the process of translation and also has some non-ribosome functions. Despite the enormous studies on the relationship between the structure and function of prokaryotic RPS7, the structure and molecular details of the mechanism of eukaryotic RPS5 remain largely unexplored. This article focuses on the structure of RPS5 and its role in cells and diseases, especially the binding to 18S rRNA. The role of RPS5 in translation initiation and its potential use as targets for liver disease and cancer are discussed.

Indexed as

EukaryotaRibosomal ProteinsHumansRibosomesRNA, Ribosomal, 18SRibosomal Proteinsribosomal protein S5RNA, Ribosomal, 18Scancerfunctionliver diseaseribosomal protein S5translation

Identifiers

PMID36834797
PMCPMC9958902
OpenAlexW4319598276

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.