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Mutations in Hsp40 co-chaperone change the canonical interdomain interactions stimulating LGMDD1 myopathy

Journal of Biological Chemistry(2025)10.1016/j.jbc.2025.110945Source: DataRank Database

Mutations in Hsp40 co-chaperone change the canonical interdomain interactions stimulating LGMDD1 myopathy is a research paper published in Journal of Biological Chemistry (2025). On theSindex it has a DataRank of 0.

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Repositories this paper deposited data in (declared in PubMed).

figshare10.6084/m9.figshare.29133707

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Enrichment:Funding (7 grants)Impact (FWCI 0.00)OA: goldTopics (41)IDs (PubMed, PMC, OpenAlex)Annotations (1)

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Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (7)

Geetika Aggarwal ORCID,Mahapatra Anshuman Jaysingh ORCID,Daniel C. Chen,Jil Daw ORCID,Conrad C. Weihl ORCID

Live enrichment

PubMed:41241098 PMC:PMC12756002 OpenAlex:https://openalex.org/W4416335163

National Science Foundation

Grant: 2138259

Track 1: ACCESS Resource Allocations Marketplace and Platform Services (RAMPS)

National Science Foundation

Grant: 2138296

ACO: An Open CI Ecosystem to Advance Scientific Discovery (OpenCI)

National Science Foundation

Grant: 2138286

Track 2: Customized Multi-tier Assistance, Training, and Computational Help (MATCH) for End User ACCESS to CI

National Science Foundation

Grant: 2138307

Track 3: COre National Ecosystem for CyberinfrasTructure (CONECT)

National Science Foundation

Grant: 2137603

Track 4: Advanced CI Coordination Ecosystem: Monitoring and Measurement Services

National Institutes of Health

Grant: BIO240152

National Institute of Arthritis and Musculoskeletal and Skin Diseases

Grant: R01AR068797

FWCI

0.00

Citation Percentile

0.2%

goldLicense: cc-by

journalhttps://doi.org/10.1016/j.jbc.2025.110945

publisherhttps://doi.org/10.1016/j.jbc.2025.110945

publisherhttps://api.elsevier.com/content/article/PII:S0021925825027978?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0021925825027978?httpAccept=text/plain

repositoryhttps://pubmed.ncbi.nlm.nih.gov/41241098

Fields of Study

Heat shock proteins researchMuscle Physiology and DisordersGenetic Neurodegenerative Diseases0303 health sciences03 medical and health sciences

MeSH Terms

Protein DomainsHumansMutationNerve Tissue ProteinsMolecular ChaperonesHSP70 Heat-Shock ProteinsSaccharomyces cerevisiae ProteinsMuscular Dystrophies, Limb-GirdleHSP40 Heat-Shock ProteinsMolecular Dynamics Simulation

Keywords

Allosteric regulationMutantMutationChaperone (clinical)Muscular dystrophyMyopathyProtein–protein interactionYeastHomology modelingStructure function relationshipMolecular dynamicsPrionsMolecular Basis Of DiseaseChaperonopathyProtein Misfolding And AggregationChaperone Network And FunctionSaccharomyces cerevisiae ProteinsMuscular Dystrophies, Limb-GirdleProtein DomainsHumansNerve Tissue ProteinsHSP70 Heat-Shock ProteinsHSP40 Heat-Shock ProteinsMolecular Dynamics SimulationResearch ArticleMolecular Chaperones

Mutations in Hsp40 co-chaperone change the canonical interdomain interactions stimulating LGMDD1 myopathy

FAIR Checklist

Authors (7)

Funding (7 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)