Evidence map›Paper›PMID 10409717›Full record

ArticleMolecular and cellular biology1999

Mutations in elongation factor 1beta, a guanine nucleotide exchange factor, enhance translational fidelity.

A Carr-Schmid, L Valente, V I Loik, T Williams, L M Starita, T G Kinzy

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

33 citing papers in PubMed, 72 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

A Carr-SchmidDepartment of Molecular Genetics and Microbiology, UMDNJ Robert Wood Johnson Medical School, Piscataway, New Jersey, USA.
L Valente
V I Loik
T Williams
L M Starita
T G Kinzy
Johnson University · USRutgers Cancer Institute of New Jersey

Funding

UMDNJ-RUTGERS UNIVERSITY PIPELINE PROGRAMR25GM055145 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI HAIMOVICH, BEATRICE, LANGER, JEROME ALAN · 1996 to 2020
$8.7M
NIGMS NIH HHS 5R25GM55145NIGMS NIH HHS R25 GM055145
6 · The paper itself

Abstract

Translation elongation factor 1beta (EF-1beta) is a member of the family of guanine nucleotide exchange factors, proteins whose activities are important for the regulation of G proteins critical to many cellular processes. EF-1beta is a highly conserved protein that catalyzes the exchange of bound GDP for GTP on EF-1alpha, a required step to ensure continued protein synthesis. In this work, we demonstrate that the highly conserved C-terminal region of Saccharomyces cerevisiae EF-1beta is sufficient for normal cell growth. This region of yeast and metazoan EF-1beta and the metazoan EF-1beta-like protein EF-1delta is highly conserved. Human EF-1beta, but not human EF-1delta, is functional in place of yeast EF-1beta, even though both EF-1beta and EF-1delta have previously been shown to have guanine nucleotide exchange activity in vitro. Based on the sequence and functional homology, mutagenesis of two C-terminal residues identical in all EF-1beta protein sequences was performed, resulting in mutants with growth defects and sensitivity to translation inhibitors. These mutants also enhance translational fidelity at nonsense codons, which correlates with a reduction in total protein synthesis. These results indicate the critical function of EF-1beta in regulating EF-1alpha activity, cell growth, translation rates, and translational fidelity.

Indexed as

MutationProtein BiosynthesisAllelesAmino Acid SequenceCodonCodon, TerminatorFrameshift MutationFungal ProteinsGenetic Complementation TestGuanosine DiphosphateGuanosine TriphosphateHumansMolecular Sequence DataPeptide Chain Elongation, TranslationalPeptide Elongation Factor 1Peptide Elongation FactorsCodonCodon, TerminatorFungal ProteinsGuanosine DiphosphateGuanosine TriphosphatePeptide Elongation Factor 1Peptide Elongation FactorsRNA, Fungal

Identifiers

PMID10409717
PMCPMC84369
OpenAlexW2116433369

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.