Evidence map›Paper›PMID 18263608›Full record

ArticleNucleic acids research2008

Structure/function analysis of yeast ribosomal protein L2.

Arturas Meskauskas, Johnathan R Russ, Jonathan D Dinman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021
    Review
  6. Nervous-Like Circuits in the Ribosome Facts, Hypotheses and Perspectives.International journal of molecular sciences · 2019
    Review
  7. Article
  8. Article
  9. Eukaryotic rpL10 drives ribosomal rotation.Nucleic acids research · 2014
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The eukaryotic ribosome: current status and challenges.The Journal of biological chemistry · 2009
    Review
  17. Article
  18. Article
  19. 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

3 authors at 1 institution in 1 country.

Arturas MeskauskasDepartment of Cell Biology and Molecular Genetics, Microbiology Building Rm. 2135, University of Maryland, College Park, MD, 20742, USA.
Johnathan R Russ
Jonathan D Dinman
University of Maryland, College Park · US

Funding

Translational Fidelity in EukaryotesR01GM058859 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI DINMAN, JONATHAN D · 1999 to 2011
$3.8M
Mechanisms of Virus Replication and Gene ExpressionT32AI051967 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI SIMON, ANNE ELIZABETH · 2002 to 2013
$1.8M
NIAID NIH HHS T32 AI051967NIAID NIH HHS T32 AI051967-05NIGMS NIH HHS R01 GM058859
6 · The paper itself

Abstract

Ribosomal protein L2 is a core element of the large subunit that is highly conserved among all three kingdoms. L2 contacts almost every domain of the large subunit rRNA and participates in an intersubunit bridge with the small subunit rRNA. It contains a solvent-accessible globular domain that interfaces with the solvent accessible side of the large subunit that is linked through a bridge to an extension domain that approaches the peptidyltransferase center. Here, screening of randomly generated library of yeast RPL2A alleles identified three translationally defective mutants, which could be grouped into two classes. The V48D and L125Q mutants map to the globular domain. They strongly affect ribosomal A-site associated functions, peptidyltransferase activity and subunit joining. H215Y, located at the tip of the extended domain interacts with Helix 93. This mutant specifically affects peptidyl-tRNA binding and peptidyltransferase activity. Both classes affect rRNA structure far away from the protein in the A-site of the peptidyltransferase center. These findings suggest that defective interactions with Helix 55 and with the Helix 65-66 structure may indicate a certain degree of flexibility in L2 in the neck region between the two other domains, and that this might help to coordinate tRNA-ribosome interactions.

Indexed as

AllelesAmino Acid SubstitutionBase SequenceModels, MolecularMolecular Sequence DataPeptidyl TransferasesPhenotypePolyribosomesProtein BiosynthesisRibosomal ProteinsRibosomesRibosome Subunits, Large, EukaryoticRNA, RibosomalSaccharomyces cerevisiae ProteinsPeptidyl Transferasesribosomal protein L2Ribosomal Proteinsribosomal protein YL6, S cerevisiaeRNA, RibosomalSaccharomyces cerevisiae Proteins

Identifiers

PMID18263608
PMCPMC2330241
OpenAlexW2165345282

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.