Evidence map›Paper›PMID 20368619›Full record

ArticleThe Journal of cell biology2010

A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis.

Véronique Albanèse, Stefanie Reissmann, Judith Frydman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

60 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. DNAJ protein gene expansion mechanism in Panicoideae and PgDNAJ functional identification in pearl millet.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2024
    Article
  5. Article
  6. Review
  7. Multimodal cotranslational interactions direct assembly of the human multi-tRNA synthetase complex.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Review
  9. The Relevance of G-Quadruplexes for DNA Repair.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Véronique AlbanèseDepartment of Biology, Stanford University, Palo Alto, CA 94305, USA.
Stefanie Reissmann
Judith Frydman
Palo Alto University · USStanford University · US

Funding

PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOLR01GM056433 · NIGMS · STANFORD UNIVERSITY · PI Judith Frydman · 1997 to 2026
$5.0M
Protein Folding in the Eukaryotic CytosolR37GM056433 · NIGMS · STANFORD UNIVERSITY · PI FRYDMAN, JUDITH · 2013 to 2022
$4.6M
NIGMS NIH HHS GM56433NIGMS NIH HHS R01 GM056433NIGMS NIH HHS R37 GM056433
6 · The paper itself

Abstract

Molecular chaperones assist cellular protein folding as well as oligomeric complex assembly. In eukaryotic cells, several chaperones termed chaperones linked to protein synthesis (CLIPS) are transcriptionally and physically linked to ribosomes and are implicated in protein biosynthesis. In this study, we show that a CLIPS network comprising two ribosome-anchored J-proteins, Jjj1 and Zuo1, function together with their partner Hsp70 proteins to mediate the biogenesis of ribosomes themselves. Jjj1 and Zuo1 have overlapping but distinct functions in this complex process involving the coordinated assembly and remodeling of dozens of proteins on the ribosomal RNA (rRNA). Both Jjj1 and Zuo1 associate with nuclear 60S ribosomal biogenesis intermediates and play an important role in nuclear rRNA processing, leading to mature 25S rRNA. In addition, Zuo1, acting together with its Hsp70 partner, SSB (stress 70 B), also participates in maturation of the 35S rRNA. Our results demonstrate that, in addition to their known cytoplasmic roles in de novo protein folding, some ribosome-anchored CLIPS chaperones play a critical role in nuclear steps of ribosome biogenesis.

Indexed as

CytosolEukaryotaHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesProtein FoldingRibosomesRNA, RibosomalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsJjj1 protein, S cerevisiaeMolecular ChaperonesRNA, RibosomalSaccharomyces cerevisiae ProteinsSSZ1 protein, S cerevisiaeZUO1 protein, S cerevisiae

Identifiers

PMID20368619
PMCPMC2854368
OpenAlexW2083621938

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.