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Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly

bioRxiv (Cold Spring Harbor Laboratory)(2023)10.1101/2023.05.15.540872Source: DataRank Database

Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2023). On theSindex it has a DataRank of 0. It has been cited 2 times.

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Open Access2 citations

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datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (6 grants)OA: greenTopics (36)IDs (PubMed, OpenAlex)

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Authors (5)

Hao Shao ORCID,Eric Tse ORCID,Jason E. Gestwicki ORCID,Daniel R. Southworth ORCID,Julian R. Braxton ORCID

Live enrichment

PubMed:37293102 OpenAlex:https://openalex.org/W4376646761

National Institutes of Health

Grant: 5F31GM142279-02

Structure and function of mitochondrial Hsp60

National Institutes of Health

Grant: 5R01NS059690-10

Molecular Chaperones and Small Molecules

National Institutes of Health

Grant: 3R01GM138690-04S1

Mechanisms of Protein Disaggregation and Turnover by AAA+ Chaperones

NIGMS NIH HHS

Grant: F31 GM142279

NIGMS NIH HHS

Grant: R01 GM138690

NINDS NIH HHS

Grant: R01 NS059690

greenLicense: cc-by-nc-nd

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2023/05/15/2023.05.15.540872.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2023.05.15.540872

repositoryhttps://doi.org/10.1101/2023.05.15.540872

repositoryhttps://pubmed.ncbi.nlm.nih.gov/37293102

Fields of Study

Heat shock proteins researchProtein Structure and DynamicsEnzyme Structure and Function0301 basic medicine03 medical and health sciences

Keywords

ChaperoninProteostasisChaperone (clinical)Protein foldingCell biologyBiologyBiophysicsMitochondrial matrixHSP60MutantChemistryCrystallographyBiochemistryHeat shock proteinCytosolHsp70Models, MolecularCryoelectron Microscopy150500610MolecularChaperonin 60Article620MitochondriaMitochondrial ProteinsAdenosine TriphosphateProtein DomainsModelsHumans