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Mutations in the Hsp90 N Domain Identify a Site that Controls Dimer Opening and Expand Human Hsp90α Function in Yeast

Journal of Molecular Biology(2020)10.1016/j.jmb.2020.06.015Source: DataRank Database

Mutations in the Hsp90 N Domain Identify a Site that Controls Dimer Opening and Expand Human Hsp90α Function in Yeast is a research paper published in Journal of Molecular Biology (2020). On theSindex it has a DataRank of 0. It has been cited 14 times.

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Open Access14 citations

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Enrichment:Funding (2 grants)Impact (FWCI 0.22)OA: greenTopics (56)IDs (PubMed, PMC, OpenAlex)Annotations (2)

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 (2)

Daniel C. Masison ORCID,Michael Reidy ORCID

Live enrichment

PubMed:32565117 PMC:PMC7437358 OpenAlex:https://openalex.org/W3036300548

Intramural NIH HHS

Grant: Z01 DK024952

National Institute of Diabetes and Digestive and Kidney Diseases

FWCI

0.22

Citation Percentile

0.5%

Citation Trend

2022

2023

2024

2025

2026

greenLicense: cc-by-nc-nd

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/7437358

GREENhttps://www.ncbi.nlm.nih.gov/pmc/articles/7437358

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/7437358

publisherhttps://api.elsevier.com/content/article/PII:S0022283620304113?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0022283620304113?httpAccept=text/plain

Fields of Study

Heat shock proteins researchProtein Structure and DynamicsEnzyme Structure and FunctionMedicineChemistryBiologyAdenosine TriphosphateBinding SitesCloning, MolecularPeptidyl-Prolyl Isomerase FGene Expression RegulationHSP90 Heat-Shock ProteinsHumansModels, MolecularMolecular ChaperonesMutationProtein BindingProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPeptidyl-Prolyl Isomerase D

MeSH Terms

Protein DomainsPeptidyl-Prolyl Isomerase FPeptidyl-Prolyl Isomerase DAdenosine TriphosphateBinding SitesCloning, MolecularGene Expression RegulationHumansModels, MolecularMutationProtein BindingSaccharomyces cerevisiaeMolecular ChaperonesHSP90 Heat-Shock ProteinsSaccharomyces cerevisiae Proteins

Keywords

Hsp90YeastATP hydrolysisChaperone (clinical)Saccharomyces cerevisiaeFunction (biology)ATPaseBiologyBiochemistryCyclic nucleotide-binding domainCell biologyNucleotideChemistryHeat shock proteinEnzymeGeneSba1Hsp90 BetaHsp82Hsp90 Alpha

Mutations in the Hsp90 N Domain Identify a Site that Controls Dimer Opening and Expand Human Hsp90α Function in Yeast

FAIR Checklist

Authors (2)

Funding (2 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)