Evidence map›Paper›PMID 15590835›Full record

ArticleEukaryotic cell2004

The small-subunit processome is a ribosome assembly intermediate.

Kara A Bernstein, Jennifer E G Gallagher, Brianna M Mitchell, Sander Granneman, Susan J Baserga

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

103 citing papers in PubMed, 177 citations in OpenAlex.

  1. Article
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  6. Review
  7. Article
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  11. Metacyclogenesis as the Starting Point of Chagas Disease.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Molecular mechanisms of resistance toFrontiers in plant science · 2022
    Article
  16. Review
  17. Genes · 2021
    Article
  18. Review
  19. Article
  20. Article

43 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

5 authors at 1 institution in 1 country.

Kara A BernsteinDepartment of Molecular Biophysics and Biochemistry, Yale School of Medicine, C114 SHM, 333 Cedar St., New Haven, CT 06520-8024, USA.
Jennifer E G Gallagher
Brianna M Mitchell
Sander Granneman
Susan J Baserga
Yale University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007499 · NIGMS · YALE UNIVERSITY · PI CARLSON, JOHN R, REINKE, VALERIE J · 1985 to 2022
$13.9M
The Architecture and Function of RNPs Required for Ribosome BiogenesisR01GM052581 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 2001 to 2013
$4.4M
Predoctoral Fellowship for Disabled StudentsF31GM067564 · NIGMS · YALE UNIVERSITY · PI BERNSTEIN, KARA A · 2002 to 2005
$136k
ASSEMBLY, LOCALIZATION AND FUNCTION OF THE U3 SNRNPR29GM052581 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1996 to 2000
$120k
MINORITY PREDOCTORAL FELLOWSHIP PROGRAMF31GM020905 · NIGMS · YALE UNIVERSITY · PI GALLAGHER, JENNIFER E · 2000 to 2003
$109k
NIGMS NIH HHS F31 GM020905NIGMS NIH HHS F31 GM067564NIGMS NIH HHS GM07499NIGMS NIH HHS GM20905NIGMS NIH HHS GM52581NIGMS NIH HHS GM67564NIGMS NIH HHS R01 GM052581NIGMS NIH HHS R29 GM052581NIGMS NIH HHS T32 GM007499
6 · The paper itself

Abstract

The small-subunit (SSU) processome is a large ribonucleoprotein required for the biogenesis of the 18S rRNA and likely corresponds to the terminal knobs visualized by electron microscopy on the 5' end of nascent rRNAs. The original purification of the SSU processome of Saccharomyces cerevisiae resulted in the identification of 28 proteins. Here, we characterize 12 additional protein components, including five small-ribosomal-subunit proteins (Rps4, Rps6, Rps7, Rps9, and Rps14) that had previously been copurified. Our multiple criteria for including a component as a bona fide SSU processome component included coimmunoprecipitation with Mpp10 (an SSU processome component), the U3 snoRNA, and the anticipated pre-rRNAs. Importantly, the association of specific ribosomal proteins with the SSU processome suggests that the SSU processome has roles in both pre-rRNA processing and ribosome assembly. These ribosomal proteins may be analogous to the primary or secondary RNA binding proteins first described in bacterial in vitro ribosome assembly maps. In addition to the ribosomal proteins and based on the same experimental approach, we found seven other proteins (Utp18, Noc4, Utp20, Utp21, Utp22, Emg1, and Krr1) to be bona fide SSU processome proteins.

Indexed as

Blotting, NorthernCell NucleolusImmunoprecipitationMacromolecular SubstancesMicroscopy, ElectronMicroscopy, FluorescenceModels, BiologicalNucleic Acid ConformationPhosphoproteinsPromoter Regions, GeneticRibonucleoproteinsRibosomal ProteinsRibosomesRNA PrecursorsRNA, Ribosomal, 18SRNA, Small NucleolarMacromolecular SubstancesMPP10 protein, S cerevisiaePhosphoproteinsRibonucleoproteinsRibosomal ProteinsRNA PrecursorsRNA, Ribosomal, 18SRNA, Small NucleolarRNA, U3 small nucleolarSaccharomyces cerevisiae Proteins

Identifiers

PMID15590835
PMCPMC539036
OpenAlexW2099308993

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.