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Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding

Scientific Reports(2021)10.1038/s41598-021-85197-3Source: DataRank Database

Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding is a research paper published in Scientific Reports (2021). 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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Linked data & code

uniprot pdb

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (7 grants)Impact (FWCI 0.22)OA: goldTopics (54)IDs (PubMed, PMC, OpenAlex)Annotations (2)SDGs (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 (5)

Rui Ma ORCID,Wai Kwan Tang ORCID,Dashuang Shi ORCID,Niraj H. Tolia ORCID,Brian Nguyen ORCID

Live enrichment

PubMed:33723304 PMC:PMC7960994 OpenAlex:https://openalex.org/W3137563389

Division of Intramural Research, National Institute of Allergy and Infectious Diseases

Grant: 1ZIAAI001237

Division of Intramural Research, National Institute of Allergy and Infectious Diseases

Grant: 1ZIAAI001253

Intramural NIH HHS

Grant: ZIA AI001253

Intramural NIH HHS

Grant: ZIA AI001237

National Institutes of Health

Grant: 1ZIAAI001237-05

Structural characterization of host-pathogen interactions

National Institutes of Health

Grant: 1ZIAAI001253-01

Structural vaccinology for malaria

National Institute of Allergy and Infectious Diseases

FWCI

0.22

Citation Percentile

0.5%

Citation Trend

2022

2024

2025

goldLicense: cc-by

journalhttps://www.nature.com/articles/s41598-021-85197-3.pdf

publisherhttps://www.nature.com/articles/s41598-021-85197-3.pdf

publisherhttps://www.nature.com/articles/s41598-021-85197-3

journalhttps://doi.org/10.1038/s41598-021-85197-3

repositoryhttps://pubmed.ncbi.nlm.nih.gov/33723304

Fields of Study

Heat shock proteins researchProtein Structure and DynamicsEnzyme Structure and Function0301 basic medicine0303 health sciences03 medical and health sciencesAdenosine TriphosphateBinding SitesChaperonin 60Crystallography, X-RayMolecular ConformationMolecular Docking SimulationMolecular Dynamics SimulationPlasmodium falciparumProtein BindingProtein Interaction Domains and MotifsProtozoan ProteinsStructure-Activity Relationship

MeSH Terms

Adenosine TriphosphateBinding SitesMolecular ConformationPlasmodium falciparumProtein BindingStructure-Activity RelationshipProtozoan ProteinsCrystallography, X-RayChaperonin 60Protein Interaction Domains and MotifsMolecular Dynamics SimulationMolecular Docking Simulation

Keywords

ChaperoninProtein subunitProtein foldingPlasmodium falciparumBiologyBiophysicsProtein structureBiochemistryBinding SitesScienceQRMolecular ConformationProtozoan ProteinsChaperonin 60Molecular Dynamics SimulationCrystallography, X-RayArticleMolecular Docking SimulationStructure-Activity RelationshipAdenosine TriphosphateMedicineProtein Interaction Domains and MotifsProtein Binding

Sustainable Development Goals

SDG 3: 3. Good healthSDG 0: Life in Land