Evidence map›Paper›PMID 21768774›Full record

ArticleCell cycle (Georgetown, Tex.)2011

Characterization of hibernating ribosomes in mammalian cells.

Dawid Krokowski, Francesca Gaccioli, Mithu Majumder, Michael R Mullins, Celvie L Yuan, Barbara Papadopoulou, William C Merrick, Anton A Komar, Derek Taylor, Maria Hatzoglou

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

27 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Detection and Characterization of the Eukaryotic Vacant Ribosome.International journal of molecular sciences · 2025
    Review
  3. Article
  4. Article
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  8. Article
  9. Exploring the molecular content of CHO exosomes during bioprocessing.Applied microbiology and biotechnology · 2021
    Article
  10. Review
  11. Article
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  15. Review
  16. Review
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  19. Review
  20. Capturing the Asc1p/Molecular & cellular proteomics : MCP · 2017
    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

10 authors at 6 institutions in 2 countries.

Dawid KrokowskiDepartment of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, OH, USA.
Francesca Gaccioli
Mithu Majumder
Michael R Mullins
Celvie L Yuan
Barbara Papadopoulou
William C Merrick
Anton A Komar
Derek Taylor
Maria Hatzoglou
Case Western Reserve University · USCarl Albert State College · USCase Comprehensive Cancer CenterCleveland State University · USThe University of Texas Health Science Center at San Antonio · USUniversité Laval · CA

Funding

Regulation of Gene Expression During StressR01DK053307 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI HATZOGLOU, MARIA · 1998 to 2021
$9.6M
Translational Control by NutrientsR01DK060596 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI MARIA HATZOGLOU · 2002 to 2026
$6.3M
Canadian Institutes of Health Research MOP-12182NIDDK NIH HHS R01 DK053307NIDDK NIH HHS R01 DK060596
6 · The paper itself

Abstract

Protein synthesis across kingdoms involves the assembly of 70S (prokaryotes) or 80S (eukaryotes) ribosomes on the mRNAs to be translated. 70S ribosomes are protected from degradation in bacteria during stationary growth or stress conditions by forming dimers that migrate in polysome profiles as 100S complexes. Formation of ribosome dimers in Escherichia coli is mediated by proteins, namely the ribosome modulation factor (RMF), which is induced in the stationary phase of cell growth. It is reported here a similar ribosomal complex of 110S in eukaryotic cells, which forms during nutrient starvation. The dynamic nature of the 110S ribosomal complex (mammalian equivalent of the bacterial 100S) was supported by the rapid conversion into polysomes upon nutrient-refeeding via a mechanism sensitive to inhibitors of translation initiation. Several experiments were used to show that the 110S complex is a dimer of nontranslating ribosomes. Cryo-electron microscopy visualization of the 110S complex revealed that two 80S ribosomes are connected by a flexible, albeit localized, interaction. We conclude that, similarly to bacteria, rat cells contain stress-induced ribosomal dimers. The identification of ribosomal dimers in rat cells will bring new insights in our thinking of the ribosome structure and its function during the cellular response to stress conditions.

Indexed as

AnimalsBinding SitesCell LineCricetinaeCryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsHumansMiceProtein BiosynthesisProtein MultimerizationRatsRibosomal ProteinsRibosomesStress, PhysiologicalEscherichia coli ProteinsRibosomal Proteinsribosome modulation factor, E coli

Identifiers

PMID21768774
PMCPMC3219539
OpenAlexW2057465205

What OpenQuestion holds

Textmetadata
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.