Evidence map›Paper›PMID 12242301›Full record

ArticleMolecular and cellular biology2002

Components of an interdependent unit within the SSU processome regulate and mediate its activity.

Karen A Wehner, Jennifer E G Gallagher, Susan J Baserga

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

41 citing papers in PubMed, 60 citations in OpenAlex.

  1. Yeast pre-rRNA is processed at the A' site.microPublication biology · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. The SSU processome interactome inRNA (New York, N.Y.) · 2018
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
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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

3 authors at 1 institution in 1 country.

Karen A WehnerDepartments of Genetics. Therapeutic Radiology, Yale University School of Medicine, New Haven, Connecticut 06520-8040, USA.
Jennifer E G Gallagher
Susan J Baserga
Yale University · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
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
ASSEMBLY, LOCALIZATION AND FUNCTION OF THE U3 SNRNPR29GM052581 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1996 to 2000
$120k
NIGMS NIH HHS GM07223-25NIGMS NIH HHS GM07499-2NIGMS NIH HHS GM-52581NIGMS NIH HHS R01 GM052581NIGMS NIH HHS R29 GM052581NIGMS NIH HHS T32 GM007223NIGMS NIH HHS T32 GM007499PHS HHS F0001345
6 · The paper itself

Abstract

The SSU processome is required for production of the small ribosomal subunit RNA, the 18S rRNA. Specifically, the U3 small nucleolar RNA (snoRNA) component of the SSU processome is essential for the formation of the conserved central pseudoknot and for cleavages of the pre-rRNA, both of which are required for 18S maturation. To further elucidate how these events are mediated, we examined the regulatory and mechanistic roles of the U3 specific proteins: Imp3p, Imp4p, and Mpp10p. We found that these proteins demonstrated an interdependence with respect to their stability and to their association with the U3 snoRNA. Because mutations in the U3 snoRNA that disrupt pre-rRNA processing confer similar defects on growth and pre-rRNA processing as do carboxy-terminal truncations of Mpp10p, we hypothesized that Mpp10p may be involved in maintaining U3 snoRNA-pre-rRNA base pairing. However, combining the two mutations resulted in a more pronounced cleavage defect at site A(2), suggesting that Mpp10p is also required at an additional mechanistic step. Furthermore, heterologous complementation experiments demonstrate that the last 95 amino acids of yeast Mpp10p are specifically required for growth and pre-rRNA processing at low temperatures.

Indexed as

RNA Processing, Post-TranscriptionalSaccharomyces cerevisiae ProteinsAmino Acid SequenceAnimalsFungal ProteinsMolecular Sequence DataNucleic Acid ConformationPhosphoproteinsRibonucleoproteinsRibosomal ProteinsRibosomesRNA, FungalRNA PrecursorsRNA, Ribosomal, 18SRNA, Small NucleolarSaccharomyces cerevisiaeFungal ProteinsIMP3 protein, S cerevisiaeIMP4 protein, S cerevisiaeMPP10 protein, S cerevisiaePhosphoproteinsRibonucleoproteinsRibosomal ProteinsRNA, FungalRNA PrecursorsRNA, Ribosomal, 18SRNA, Small NucleolarRNA, U3 small nucleolarSaccharomyces cerevisiae Proteins

Identifiers

PMID12242301
PMCPMC139808
OpenAlexW2161794927

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.