Evidence map›Paper›PMID 18832371›Full record

ArticleNucleic acids research2008

Ribosomal protein L3 functions as a 'rocker switch' to aid in coordinating of large subunit-associated functions in eukaryotes and Archaea.

Arturas Meskauskas, 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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed, 34 citations in OpenAlex.

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  13. Eukaryotic rpL10 drives ribosomal rotation.Nucleic acids research · 2014
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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 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.
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
NIGMS NIH HHS GM058859NIGMS NIH HHS R01 GM058859
6 · The paper itself

Abstract

Although ribosomal RNAs (rRNAs) comprise the bulk of the ribosome and carry out its main functions, ribosomal proteins also appear to play important structural and functional roles. Many ribosomal proteins contain long, nonglobular domains that extend deep into the rRNA cores. In eukaryotes and Archaea, ribosomal protein L3 contains two such extended domains tethered to a common globular hub, thus providing an excellent model to address basic questions relating to ribosomal protein structure/function relationships. Previous work in our laboratory identified the central 'W-finger' extension of yeast L3 in helping to coordinate ribosomal functions. New studies on the 'N-terminal' extension in yeast suggest that it works with the W-finger to coordinate opening and closing of the corridor through which the 3' end of aa-tRNA moves during the process of accommodation. Additionally, the effect of one of the L3 N-terminal extension mutants on the interaction between C75 of the aa-tRNA and G2921 (Escherichia coli G2553) of 25S rRNA provides the first evidence of the effect of a ribosomal protein on aa-tRNA positioning and peptidyltransfer, possibly through the induced fit model. A model is presented describing how all three domains of L3 may function together as a 'rocker switch' to coordinate the stepwise processes of translation elongation.

Indexed as

Peptide Chain Elongation, TranslationalArchaeal ProteinsBase SequenceDrug ResistanceEscherichia coliModels, MolecularMolecular Sequence DataMutationPeptide Elongation Factor 2Peptidyl TransferasesProtein SubunitsRibosomal Protein L3Ribosomal ProteinsRNA, Transfer, Amino AcylSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsArchaeal ProteinsPeptide Elongation Factor 2Peptidyl TransferasesProtein SubunitsRibosomal Protein L3Ribosomal ProteinsRNA, Transfer, Amino AcylSaccharomyces cerevisiae Proteins

Identifiers

PMID18832371
PMCPMC2577335
OpenAlexW2045608725

What OpenQuestion holds

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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.