Evidence map›Paper›PMID 17443350›Full record

ArticleMolecular genetics and genomics : MGG2007

In vivo functional characterization of the Saccharomyces cerevisiae 60S biogenesis GTPase Nog1.

Jennifer L Fuentes, Kaustuv Datta, Susan M Sullivan, Angela Walker, Janine R Maddock

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular genetics and genomics : MGG, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Molecular biology of the cell · 2021
    Article
  7. Article
  8. Review
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  10. Review
  11. Article
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  16. Article
  17. A genome-scale protein interaction profile of Drosophila p53 uncovers additional nodes of the human p53 network.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  18. Article
  19. Article
  20. E. coli HflX interacts with 50S ribosomal subunits in presence of nucleotides.Biochemical and biophysical research communications · 2009
    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.

Jennifer L FuentesDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University Avenue, Ann Arbor, MI 48109, USA.
Kaustuv Datta
Susan M Sullivan
Angela Walker
Janine R Maddock
University of Michigan–Ann Arbor · US

Funding

BIOCHEMICAL AND GENETIC ANALYSIS OF CGTA IN CAULOBACTERR01GM055133 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MADDOCK, JANINE R. · 1998 to 2002
$559k
NIGMS NIH HHS GM-55133-S1
6 · The paper itself

Abstract

The Saccharomyces cerevisiae Nog1 GTPase is critical for assembly of the large ribosomal subunit. Mutations in conserved residues in the GTP-binding pocket cause defects in cell growth and 60S ribosome assembly but mutant proteins retain their ability to associate with the pre-60S. Association of Nog1 with the pre-60S is independent of guanine nucleotide added to cell extracts. Thus, it appears that nucleotide occupancy does not substantially affect Nog1 association with pre-60S particles. Somewhat surprisingly, neither of the conserved threonines in the G2 motif of the GTPase domain is essential for Nog1 function. Neither the steady-state rRNA levels nor the protein composition (as determined by isobaric labeling and identification by mass spectrometry of peptides) of the pre-60S particles in the nog1P176V mutant are grossly perturbed, although levels of four proteins (Nog1, Nop2, Nop15, and Tif6) are modestly reduced in pre-60S particles isolated from the mutant. Deletion analysis revealed that the C-terminal 168 amino acids are not required for function; however, the N-terminal 126 amino acids are required. Optimal association with pre-60S particles requires sequences between amino acids 347-456. Several conserved charge-to-alanine substitutions outside the GTPase domain display modest growth phenotypes indicating that these residues are not critical for function.

Indexed as

Gene Expression Regulation, FungalAmino Acid SequenceAnimalsGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine TriphosphateHumansMass SpectrometryMolecular Sequence DataNuclear ProteinsNucleotidesProtein Structure, TertiaryRibosomesRNA, RibosomalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine TriphosphateNOG1 protein, S cerevisiaeNuclear ProteinsNucleotidesRNA, RibosomalSaccharomyces cerevisiae Proteins

Identifiers

PMID17443350
OpenAlexW2029722980

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.