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Structural transitions modulate the chaperone activities of Grp94

Trends in Biochemical Sciences(2024)10.1016/j.tibs.2024.06.007Source: DataRank Database

Structural transitions modulate the chaperone activities of Grp94 is a research paper published in Trends in Biochemical Sciences (2024). On theSindex it has a DataRank of 0. It has been cited 5 times.

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0DataRank · unranked

Scored on demand from live citation data

Open Access5 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (3 grants)Impact (FWCI 0.78)OA: greenTopics (28)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 (3)

Yevheniia Bushman ORCID,Andrew W. Truman ORCID,Duhita A Mirikar ORCID

Live enrichment

PubMed:38906726 PMC:PMC11380588 OpenAlex:https://openalex.org/W4399857037

NIH

Grant: R01GM139885

NIH

Grant: R15 GM139059

NIH

Grant: R21NS133682

FWCI

0.78

Citation Percentile

0.7%

Citation Trend

2024

2025

greenLicense: http://www.elsevier.com/open-access/userlicense/1.0/

repositoryhttps://pmc.ncbi.nlm.nih.gov/articles/PMC11380588/pdf/nihms-2003731.pdf

publisherhttps://api.elsevier.com/content/article/PII:S0968000424001506?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0968000424001506?httpAccept=text/plain

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/11380588

Fields of Study

Heat shock proteins researchEndoplasmic Reticulum Stress and DiseaseEnzyme Structure and Function

MeSH Terms

Adenosine TriphosphateAnimalsEndoplasmic ReticulumHumansMembrane GlycoproteinsMolecular Chaperones

Keywords

Endoplasmic reticulumChaperone (clinical)Hsp90Co-chaperoneATP hydrolysisCell biologyChemistryBiochemistryBiologyHeat shock proteinEnzymeATPaseGeneMedicineProtein foldingDeerGRP94BipEndoplasmic Reticulum (Er)