Evidence map›Paper›PMID 22099312›Full record

ArticleMolecular cell2011

rRNA pseudouridylation defects affect ribosomal ligand binding and translational fidelity from yeast to human cells.

Karen Jack, Cristian Bellodi, Dori M Landry, Rachel O Niederer, Arturas Meskauskas, Sharmishtha Musalgaonkar, Noam Kopmar, Olya Krasnykh, Alison M Dean, Sunnie R Thompson and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 225 papers.

0numbers the graph read from it
0cells of the map it votes in
225citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

225 citing papers in PubMed, 328 citations in OpenAlex.

  1. Article
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  12. Interprotomer communication and functional asymmetry in H/ACA snoRNPs.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Review
  14. Article
  15. Functions and therapeutic applications of pseudouridylation.Nature reviews. Molecular cell biology · 2025
    Review
  16. Article
  17. Epitranscriptomic alterations induced by environmental toxins: implications for RNA modifications and disease.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2025
    Review
  18. Article
  19. Review
  20. Article

165 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

12 authors at 4 institutions in 2 countries.

Karen JackDepartment of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742, USA.
Cristian Bellodi
Dori M Landry
Rachel O Niederer
Arturas Meskauskas
Sharmishtha Musalgaonkar
Noam Kopmar
Olya Krasnykh
Alison M Dean
Sunnie R Thompson
Davide Ruggero
Jonathan D Dinman
University of Maryland, College Park · USUniversity of Alabama at Birmingham · USUniversity of California, San Francisco · USUCSF Helen Diller Family Comprehensive Cancer Center · US

Funding

Translational Fidelity in EukaryotesR01GM058859 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI DINMAN, JONATHAN D · 1999 to 2011
$3.8M
Role of rRNA Modifications in Dyskeratosis Congenita and Translation ControlR01HL085572 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI RUGGERO, DAVIDE · 2006 to 2009
$1.8M
Mechanism of IRES-Mediated Translation InitiationR01GM084547 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI THOMPSON, SUNNIE R · 2009 to 2013
$1.4M
Role of ribosome impairments in X-linked Dyskeratosis Congenita pathogenesisR01DK098057 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI RUGGERO, DAVIDE · 2012 to 2015
$1.2M
NHLBI NIH HHS 3R01HL085572-05S1NHLBI NIH HHS R01 HL085572NHLBI NIH HHS R01HL085572NIDDK NIH HHS R01 DK098057NIGMS NIH HHS 3R01GM058859-10A1S1NIGMS NIH HHS 3R01GM084547-01A1S1NIGMS NIH HHS 5R01GM058859NIGMS NIH HHS R01 GM058859NIGMS NIH HHS R01 GM084547NIGMS NIH HHS R01GM084547
6 · The paper itself

Abstract

How pseudouridylation (Ψ), the most common and evolutionarily conserved modification of rRNA, regulates ribosome activity is poorly understood. Medically, Ψ is important because the rRNA Ψ synthase, DKC1, is mutated in X-linked dyskeratosis congenita (X-DC) and Hoyeraal-Hreidarsson (HH) syndrome. Here, we characterize ribosomes isolated from a yeast strain in which Cbf5p, the yeast homolog of DKC1, is catalytically impaired through a D95A mutation (cbf5-D95A). Ribosomes from cbf5-D95A cells display decreased affinities for tRNA binding to the A and P sites as well as the cricket paralysis virus internal ribosome entry site (IRES), which interacts with both the P and the E sites of the ribosome. This biochemical impairment in ribosome activity manifests as decreased translational fidelity and IRES-dependent translational initiation, which are also evident in mouse and human cells deficient for DKC1 activity. These findings uncover specific roles for Ψ modification in ribosome-ligand interactions that are conserved in yeast, mouse, and humans.

Indexed as

AnimalsBinding SitesCell Cycle ProteinsDyskeratosis CongenitaFetal Growth RetardationGenes, ReporterHumansHydro-LyasesIntellectual DisabilityLuciferasesMiceMicrocephalyMicrotubule-Associated ProteinsMutationNuclear ProteinsPlasmidsCBF5 protein, S cerevisiaeCell Cycle ProteinsDKC1 protein, humanHydro-LyasesLuciferasesMicrotubule-Associated ProteinsNuclear Proteinspseudouridylate synthetaseRibonucleoproteins, Small NuclearRNA, RibosomalRNA, TransferSaccharomyces cerevisiae Proteins

Identifiers

PMID22099312
PMCPMC3222873
OpenAlexW2008121312

What OpenQuestion holds

Textmetadata
LicenceTDM
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.