Evidence map›Paper›PMID 9580698›Full record

ArticleNucleic acids research1998

Heterologous complementation reveals that mutant alleles of QSR1 render 60S ribosomal subunits unstable and translationally inactive.

F A Dick, B L Trumpower

Abstract read
In one paragraph

Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Trial
  2. Review
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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

2 authors.

F A DickDepartment of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
B L Trumpower

Funding

MECHANISM OF RESPIRATION AND ENERGY TRANSDUCTIONR37GM020379 · NIGMS · DARTMOUTH COLLEGE · PI TRUMPOWER, BERNARD L · 1995 to 2004
$2.7M
STRUCTURE AND FUNCTION OF HEART MEMBRANE PROTEINSR01GM020379 · NIGMS · DARTMOUTH COLLEGE · PI TRUMPOWER, BERNARD L · 1985 to 2009
$2.4M
NIGMS NIH HHS GM 20379
6 · The paper itself

Abstract

QSR1 is a highly conserved gene which encodes a 60S ribosomal subunit protein that is required for joining of large and small ribosomal subunits. In this report we demonstrate heterologous complementation of a yeast QSR1 deletion strain with both the human and corn homologs and show that the human and corn proteins are assembled into hybrid yeast/human and yeast/corn ribosomes. While the homologous genes complement lethality of the QSR1 deletion, they also result in a diminished growth rate. Analyses of the translation rates of ribosomes containing the human and corn proteins reveal a partial loss of function. Velocity gradient analyses of the hybrid ribosomes after exposure to high concentrations of salt indicate that the decreased activity is due to lability of the hybrid 60S subunits.

Indexed as

AllelesSaccharomyces cerevisiae ProteinsAmino Acid SequenceFungal ProteinsGenetic Complementation TestHumansMolecular Sequence DataMutationPeptide Chain Elongation, TranslationalPolyribosomesPotassium ChlorideProtein BiosynthesisRibosomal ProteinsRibosomesSaccharomyces cerevisiaeSequence Homology, Nucleic AcidFungal ProteinsPotassium ChlorideRibosomal ProteinsRPL10 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID9580698
PMCPMC147575

What OpenQuestion holds

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Registered trials

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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.