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New insights into the structure and function of the complex between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE

Journal of Biological Chemistry(2023)10.1016/j.jbc.2023.105574Source: DataRank Database

New insights into the structure and function of the complex between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE is a research paper published in Journal of Biological Chemistry (2023). On theSindex it has a DataRank of 0.360. It has been cited 10 times.

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0.360DataRank · unranked

Scored on demand from live citation data

Open Access10 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 0.91)OA: goldTopics (56)IDs (PubMed, PMC, OpenAlex)Annotations (1)

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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DataRank Breakdown

Base Score 100%Citation Network 0%

Base Score Contribution

0.360

From this paper's citation signal

Citation Network Contribution

Citation network not refreshed for this result

This paper's DataRank is currently driven only by its base citation score. Citation network data was not refreshed for this result.

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Authors (5)

Alexandra Pozhidaeva ORCID,Eugenia M. Clérico ORCID,Constantine Petridis,Lila M. Gierasch ORCID,María-Agustina Rossi ORCID

Live enrichment

PubMed:38110031 PMC:PMC10825016 OpenAlex:https://openalex.org/W4389822888

NIGMS NIH HHS

Grant: R35 GM118161

NIGMS NIH HHS

Grant: F32 GM018161

National Institutes of Health

Grant: GM18161

National Institutes of Health

Grant: 1F32GM018161-01A1

INTERACTION OF PTO AND PTIL KINASES IN PLANT DISEASE RES

FWCI

0.91

Citation Percentile

0.7%

Citation Trend

2024

2025

2026

goldLicense: cc-by

journalhttp://www.jbc.org/article/S0021925823026029/pdf

journalhttps://doi.org/10.1016/j.jbc.2023.105574

repositoryhttps://pubmed.ncbi.nlm.nih.gov/38110031

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/10825016

Europe_PMChttps://europepmc.org/articles/PMC10825016

Fields of Study

Heat shock proteins researchProtein Structure and DynamicsInsect and Pesticide Research0301 basic medicine03 medical and health sciences

MeSH Terms

Protein DomainsAdenosine DiphosphateAdenosine TriphosphateAllosteric RegulationBacterial ProteinsEscherichia coliHeat-Shock ProteinsHumansProtein BindingRotationReproducibility of ResultsMutagenesisPoint MutationCrystallography, X-RayHSP70 Heat-Shock ProteinsEscherichia coli ProteinsHSP40 Heat-Shock Proteins

Keywords

Allosteric regulationNucleotideMutagenesisPoint mutationBinding siteBiologyCyclic nucleotide-binding domainHsp70Plasma protein bindingEscherichia coliProtein structureBiochemistryHeat shock proteinMutationBiophysicsChemistryReceptorNMRChaperoneDnakNucleotide Exchange FactorGrpe70 Kda Heat Shock ProteinRotationEscherichia coli ProteinsReproducibility of ResultsCrystallography, X-RayAdenosine DiphosphateAdenosine TriphosphateProtein DomainsHSP70 Heat-Shock ProteinsHeat-Shock ProteinsResearch ArticleProtein Binding

New insights into the structure and function of the complex between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE

FAIR Checklist

DataRank Breakdown

Authors (5)

Funding (4 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)