Evidence map›Paper›PMID 22735702›Full record

ArticleNucleic acids research2012

Hierarchical recruitment into nascent ribosomes of assembly factors required for 27SB pre-rRNA processing in Saccharomyces cerevisiae.

Jason Talkish, Jingyu Zhang, Jelena Jakovljevic, Edward W Horsey, John L Woolford

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 9% 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

53 citing papers in PubMed, 1 synthesis or guideline pooled it, 72 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Archaea/eukaryote-specific ribosomal proteins - guardians of a complex structure.Computational and structural biotechnology journal · 2023
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019
    Review
  18. Article
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Jason TalkishDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213, USA.
Jingyu Zhang
Jelena Jakovljevic
Edward W Horsey
John L Woolford
Carnegie Mellon University · US

Funding

YEAST RIBOSOME BIOGENESISR01GM028301 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI WOOLFORD, JOHN L. · 1985 to 2025
$8.4M
NIGMS NIH HHS GM28301NIGMS NIH HHS R01 GM028301
6 · The paper itself

Abstract

To better define the roles of assembly factors required for eukaryotic ribosome biogenesis, we have focused on one specific step in maturation of yeast 60 S ribosomal subunits: processing of 27SB pre-ribosomal RNA. At least 14 assembly factors, the 'B-factor' proteins, are required for this step. These include most of the major functional classes of assembly factors: RNA-binding proteins, scaffolding protein, DEAD-box ATPases and GTPases. We have investigated the mechanisms by which these factors associate with assembling ribosomes. Our data establish a recruitment model in which assembly of the B-factors into nascent ribosomes ultimately leads to the recruitment of the GTPase Nog2. A more detailed analysis suggests that this occurs in a hierarchical manner via two largely independent recruiting pathways that converge on Nog2. Understanding recruitment has allowed us to better determine the order of association of all assembly factors functioning in one step of ribosome assembly. Furthermore, we have identified a novel subcomplex composed of the B-factors Nop2 and Nip7. Finally, we identified a means by which this step in ribosome biogenesis is regulated in concert with cell growth via the TOR protein kinase pathway. Inhibition of TOR kinase decreases association of Rpf2, Spb4, Nog1 and Nog2 with pre-ribosomes.

Indexed as

RNA Processing, Post-TranscriptionalDEAD-box RNA HelicasesGTP PhosphohydrolasesMethyltransferasesNuclear ProteinsRibosomal ProteinsRibosomesRibosome Subunits, Large, EukaryoticRNA-Binding ProteinsRNA PrecursorsRNA, RibosomalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTOR Serine-Threonine KinasesDBP10 protein, S cerevisiaeDEAD-box RNA HelicasesGTP PhosphohydrolasesMethyltransferasesNIP7 protein, S cerevisiaeNOG2 protein, S cerevisiaeNOP2 protein, S cerevisiaeNsa2 protein, S cerevisiaeNuclear ProteinsRibosomal ProteinsRNA-Binding ProteinsRNA PrecursorsRNA, RibosomalRPF2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSPB4 protein, S cerevisiaeTIF6 protein, S cerevisiaeTOR Serine-Threonine Kinases

Identifiers

PMID22735702
PMCPMC3458554
OpenAlexW2020068229

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.