9 Result(s)
within
Lukasz A. Joachimiak
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Article
Open AccessHairpin trimer transition state of amyloid fibril
Protein fibril self-assembly is a universal transition implicated in neurodegenerative diseases. Although fibril structure/growth are well characterized, fibril nucleation is poorly understood. Here, we use a ...
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Article
Open AccessDual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin
The Papain-like protease (PLpro) is a domain of a multi-functional, non-structural protein 3 of coronaviruses. PLpro cleaves viral polyproteins and posttranslational conjugates with poly-ubiquitin and protecti...
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Article
Open AccessFTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregation
Amyloid deposition of the microtubule-associated protein tau is associated with neurodegenerative diseases. In frontotemporal dementia with abnormal tau (FTD-tau), missense mutations in tau enhance its aggrega...
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Open AccessNetwork of hotspot interactions cluster tau amyloid folds
Cryogenic electron microscopy has revealed unprecedented molecular insight into the conformations of β-sheet-rich protein amyloids linked to neurodegenerative diseases. It remains unknown how a protein can ado...
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Open AccessDnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation
Molecular chaperones, including Hsp70/J-domain protein (JDP) families, play central roles in binding substrates to prevent their aggregation. How JDPs select different conformations of substrates remains poorl...
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Open AccessTau strains shape disease
Tauopathies consist of over 25 different neurodegenerative diseases that include argyrophilic grain disease (AGD), progressive supranuclear palsy (PSP), corticobasal degeneration (CBD), and Pick’s disease (PiD...
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Open AccessBiophysical properties of a tau seed
Pathogenesis of tauopathies involves conversion of tau monomer into pathological tau conformers that serve as templates to recruit native tau into growing assemblies. Small soluble tau seeds have been proposed...
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Article
Open AccessRegulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone
The Hsp40/Hsp70 chaperone families combine versatile folding capacity with high substrate specificity, which is mainly facilitated by Hsp40s. The structure and function of many Hsp40s remain poorly understood,...
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Article
Open AccessTau local structure shields an amyloid-forming motif and controls aggregation propensity
Tauopathies are neurodegenerative diseases characterized by intracellular amyloid deposits of tau protein. Missense mutations in the tau gene (MAPT) correlate with aggregation propensity and cause dominantly inhe...
