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Dynamic fibrillar assembly of αB-crystallin induced by perturbation of the conserved NT-IXI motif resolved by cryo-EM

bioRxiv (Cold Spring Harbor Laboratory)(2024)10.1101/2024.03.22.586355Source: DataRank Database

Dynamic fibrillar assembly of αB-crystallin induced by perturbation of the conserved NT-IXI motif resolved by cryo-EM is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2024). On theSindex it has a DataRank of 0.

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Enrichment:Funding (4 grants)OA: greenTopics (26)IDs (PubMed, OpenAlex)

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Authors (2)

Steve Reichow ORCID,Russell McFarland

Live enrichment

PubMed:38585788 OpenAlex:https://openalex.org/W4393235522

National Institutes of Health

Grant: 7R01EY030987-04

Structure, function and aggregation of lens α-crystallins by CryoEM

National Institutes of Health

Grant: 5U24GM129547-03

Pacific Northwest Center for Cryo-EM

National Institutes of Health

Grant: 7R35GM124779-07

Dynamic Mechanisms of Membrane Channel Gating by CryoEM

National Institutes of Health

Grant: 5F31EY033230-02

Mechanisms and functional effects of fibrillar aggregation in the lens alpha-crystallins

greenLicense: cc-by

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2024/03/27/2024.03.22.586355.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2024.03.22.586355

repositoryhttps://doi.org/10.1101/2024.03.22.586355

repositoryhttps://pubmed.ncbi.nlm.nih.gov/38585788

Fields of Study

Heat shock proteins researchConnexins and lens biologyEnzyme Structure and Function0301 basic medicine03 medical and health sciences

Keywords

ProteostasisOligomerCrystallinChaperone (clinical)Heat shock proteinBiophysicsFibrilBiologyStructural motifProtein foldingMotif (music)Cell biologyBiochemistryComputational biologyChemistryPhysicsGeneProteomicsMolecular biologyArticleProteins -- Metabolism