Amyloid assembly and disassembly
E Chuang, AM Hori, CD Hesketh… - Journal of Cell …, 2018 - journals.biologists.com
Amyloid fibrils are protein homopolymers that adopt diverse cross-β conformations. Some
amyloid fibrils are associated with the pathogenesis of devastating neurodegenerative …
amyloid fibrils are associated with the pathogenesis of devastating neurodegenerative …
Spiraling in control: structures and mechanisms of the Hsp104 disaggregase
J Shorter, DR Southworth - Cold Spring Harbor …, 2019 - cshperspectives.cshlp.org
Hsp104 is a hexameric AAA+ ATPase and protein disaggregase found in yeast, which
couples ATP hydrolysis to the dissolution of diverse polypeptides trapped in toxic …
couples ATP hydrolysis to the dissolution of diverse polypeptides trapped in toxic …
Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase
Abstract Bacterial ClpB and yeast Hsp104 are homologous Hsp100 protein disaggregases
that serve critical functions in proteostasis by solubilizing protein aggregates. Two AAA+ …
that serve critical functions in proteostasis by solubilizing protein aggregates. Two AAA+ …
Functional mammalian amyloids and amyloid-like proteins
Amyloids are highly ordered fibrous cross-β protein aggregates that are notorious primarily
because of association with a variety of incurable human and animal diseases (termed …
because of association with a variety of incurable human and animal diseases (termed …
Mechanistic and structural insights into the prion-disaggregase activity of Hsp104
Hsp104 is a dynamic ring translocase and hexameric AAA+ protein found in yeast, which
couples ATP hydrolysis to disassembly and reactivation of proteins trapped in soluble …
couples ATP hydrolysis to disassembly and reactivation of proteins trapped in soluble …
AAA+ proteins: one motor, multiple ways to work
Numerous ATPases associated with diverse cellular activities (AAA+) proteins form
hexameric, ring-shaped complexes that function via ATPase-coupled translocation of …
hexameric, ring-shaped complexes that function via ATPase-coupled translocation of …
Designer protein disaggregases to counter neurodegenerative disease
J Shorter - Current Opinion in Genetics & Development, 2017 - Elsevier
Highlights•Showcases advances to define protein disaggregases to mitigate
neurodegenerative disease linked to protein misfolding.•Highlights therapeutic …
neurodegenerative disease linked to protein misfolding.•Highlights therapeutic …
Mining disaggregase sequence space to safely counter TDP-43, FUS, and α-synuclein proteotoxicity
Hsp104 is an AAA+ protein disaggregase, which can be potentiated via diverse mutations in
its autoregulatory middle domain (MD) to mitigate toxic misfolding of TDP-43, FUS, and α …
its autoregulatory middle domain (MD) to mitigate toxic misfolding of TDP-43, FUS, and α …
[HTML][HTML] Molecular mechanisms of amyloid disaggregation
KJY Low, A Venkatraman, JS Mehta… - Journal of Advanced …, 2022 - Elsevier
Introduction Protein aggregation and deposition of uniformly arranged amyloid fibrils in the
form of plaques or amorphous aggregates is characteristic of amyloid diseases. The …
form of plaques or amorphous aggregates is characteristic of amyloid diseases. The …
[HTML][HTML] Molecular determinants and modifiers of Matrin-3 toxicity, condensate dynamics, and droplet morphology
Summary Matrin-3 (MATR3) is a DNA-and RNA-binding protein implicated in amyotrophic
lateral sclerosis (ALS), frontotemporal dementia (FTD), and distal myopathy. Here, we report …
lateral sclerosis (ALS), frontotemporal dementia (FTD), and distal myopathy. Here, we report …