Evidence map›Paper›PMID 19362532›Full record

ReviewMolecular cell2009

How common are extraribosomal functions of ribosomal proteins?

Jonathan R Warner, Kerri B McIntosh

Abstract readReview
In one paragraph

Review in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 413 papers.

0numbers the graph read from it
0cells of the map it votes in
413citing 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

413 citing papers in PubMed.

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  10. International journal of molecular sciences · 2026
    Review
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353 more citing papers are in PubMed but not listed here.

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

2 authors.

Jonathan R WarnerDepartment of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. warner@aecom.yu.edu
Kerri B McIntosh

Funding

RIBOSOMAL PROTEIN GENES OF SACCHAROMYCES CEREVISIAER01GM025532 · NIGMS · YESHIVA UNIVERSITY · PI WARNER, JONATHAN R. · 1985 to 2010
$6.2M
NIGMS NIH HHS GM-25532NIGMS NIH HHS R01 GM025532PHS HHS CAI-3330
6 · The paper itself

Abstract

Ribosomal proteins are ubiquitous, abundant, and RNA binding: prime candidates for recruitment to extraribosomal functions. Indeed, they participate in balancing the synthesis of the RNA and protein components of the ribosome itself. An exciting new story is that ribosomal proteins are sentinels for the self-evaluation of cellular health. Perturbation of ribosome synthesis frees ribosomal proteins to interface with the p53 system, leading to cell-cycle arrest or to apoptosis. Yet in only a few cases can we clearly identify the recruitment of ribosomal proteins for other extraribosomal functions. Is this due to a lack of imaginative evolution by cells and viruses, or to a lack of imaginative experiments by molecular biologists?

Indexed as

ApoptosisNeoplasmsRibosomal ProteinsRibosomesSaccharomyces cerevisiaeRibosomal Proteins

Identifiers

PMID19362532
PMCPMC2679180

What OpenQuestion holds

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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.