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Hsp90 and cochaperones have two genetically distinct roles in regulating eEF2 function

PLoS Genetics(2024)10.1371/journal.pgen.1011508Source: DataRank Database

Hsp90 and cochaperones have two genetically distinct roles in regulating eEF2 function is a research paper published in PLoS Genetics (2024). On theSindex it has a DataRank of 0. It has been cited 4 times.

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0DataRank · unranked

Scored on demand from live citation data

Open Access4 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (4 grants)Impact (FWCI 0.62)OA: goldTopics (57)IDs (PubMed, PMC, OpenAlex)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (4)

Danielle Yama ORCID,Ella Dahl ORCID,Jill L. Johnson ORCID,Melody D. Fulton ORCID

Live enrichment

PubMed:39652595 PMC:PMC11651573 OpenAlex:https://openalex.org/W4405170962

Center for Scientific Review

Grant: R01 GM127675

Center for Scientific Review

Grant: P20GM104420

National Institutes of Health

Grant: 5R01GM127675-02

Determinants of the Hsp90-client interaction

National Institutes of Health

Grant: 2P20GM104420-06A1

Center for Modeling Complex Interactions

FWCI

0.62

Citation Percentile

0.7%

Citation Trend

2025

2026

goldLicense: cc-by

journalhttps://doi.org/10.1371/journal.pgen.1011508

publisherhttps://doi.org/10.1371/journal.pgen.1011508

publisherhttps://dx.plos.org/10.1371/journal.pgen.1011508

repositoryhttps://pubmed.ncbi.nlm.nih.gov/39652595

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/11651573

Fields of Study

Toxin Mechanisms and ImmunotoxinsHeat shock proteins researchRNA and protein synthesis mechanisms0301 basic medicine0303 health sciences03 medical and health sciencesHSP90 Heat-Shock ProteinsSaccharomyces cerevisiaePeptide Elongation Factor 2Saccharomyces cerevisiae ProteinsMutationMolecular ChaperonesHumansProtein FoldingCyclophilinsProtein BiosynthesisPeptidyl-Prolyl Isomerase FRibosomesPeptidyl-Prolyl Isomerase D

MeSH Terms

Peptidyl-Prolyl Isomerase FPeptidyl-Prolyl Isomerase DHumansMutationRibosomesSaccharomyces cerevisiaeProtein BiosynthesisProtein FoldingMolecular ChaperonesHSP90 Heat-Shock ProteinsPeptide Elongation Factor 2CyclophilinsSaccharomyces cerevisiae Proteins

Keywords

BiologySaccharomyces cerevisiaeMutantTranslation (biology)Hsp90GeneticsMutationProteostasisCell biologyProtein foldingHeat shock proteinGeneMessenger RNASaccharomyces cerevisiae ProteinsQH426-470CyclophilinsPeptide Elongation Factor 2Protein BiosynthesisHumansPeptidyl-Prolyl Isomerase FHSP90 Heat-Shock ProteinsPeptidyl-Prolyl Isomerase DRibosomesResearch ArticleMolecular Chaperones