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Amyloid Cross-Seeding: Mechanism, Implication, and Inhibition [PDF]

open access: yesMolecules, 2022
Most neurodegenerative diseases such as Alzheimer’s disease, type 2 diabetes, Parkinson’s disease, etc. are caused by inclusions and plaques containing misfolded protein aggregates.
Sushma Subedi   +4 more
doaj   +4 more sources

Partial Prion Cross-Seeding between Fungal and Mammalian Amyloid Signaling Motifs [PDF]

open access: yesmBio, 2021
Amyloids are β-sheet-rich protein polymers that can be pathological or display a variety of biological roles. In filamentous fungi, specific immune receptors activate programmed cell death execution proteins through a process of amyloid templating akin ...
Thierry Bardin   +8 more
doaj   +5 more sources

Possible Role of Amyloid Cross-Seeding in Evolvability and Neurodegenerative Disease [PDF]

open access: yesJournal of Parkinson’s Disease, 2019
Aging-related neurodegenerative disorders are frequently associated with the aggregation of multiple amyloidogenic proteins (APs), although the reason why such detrimental phenomena have emerged in the post-reproductive human brain across evolution is ...
Makoto Hashimoto   +7 more
doaj   +5 more sources

Structural and molecular basis of cross-seeding barriers in amyloids. [PDF]

open access: yesProc Natl Acad Sci U S A, 2021
AbstractNeurodegenerative disorders are frequently associated with β-sheet-rich amyloid deposits. Amyloid-forming proteins can aggregate under different structural conformations known as strains, which can exhibit a prion-like behaviour and distinct patho-phenotypes.
Daskalov A   +14 more
europepmc   +6 more sources

A generic cross-seeding approach to protein crystallization. [PDF]

open access: yesJ Appl Crystallogr
Obtaining diffraction-quality crystals is often the rate-limiting step during structure determination of biological macromolecules by X-ray crystallography. To address this problem, we investigated a cross-seeding approach with a mixture integrating a heterogeneous set of protein crystal fragments to be used as generic seeds.
Caspy I, Tang S, Bellini D, Gorrec F.
europepmc   +4 more sources

Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots. [PDF]

open access: yesInt J Mol Sci
In classical amyloidoses, amyloid fibres form through the nucleation and accretion of protein monomers, with protofibrils and fibrils exhibiting a cross-β motif of parallel or antiparallel β-sheets oriented perpendicular to the fibre direction. These protofibrils and fibrils can intertwine to form mature amyloid fibres.
Kell DB, Pretorius E.
europepmc   +4 more sources

Amyloid particles facilitate surface-catalyzed cross-seeding by acting as promiscuous nanoparticles. [PDF]

open access: yesProc Natl Acad Sci U S A, 2021
Significance The formation of disease-associated fibrillar amyloid structures can be accelerated by preformed amyloid seeds. This seeding process is thought to occur solely through elongation at amyloid fibril ends, resulting in the templated propagation of the protein conformation encoded in the seeds.
Koloteva-Levine N   +6 more
europepmc   +5 more sources

Cross-seeding between Aβ and SEVI indicates a pathogenic link and gender difference between alzheimer diseases and AIDS [PDF]

open access: yesCommunications Biology, 2022
Cross-seeding of SEVI, a protein that enhances the infectivity of HIV virus, with Amyloid-β (Aβ) can prevent Aβ aggregation, disaggregate preformed Aβ fibrils, reduce Aβ-induced cell toxicity, and attenuate Aβ-accumulated paralysis in a transgenic C ...
Yijing Tang   +6 more
doaj   +2 more sources

Diverse Misfolded Conformational Strains and Cross-seeding of Misfolded Proteins Implicated in Neurodegenerative Diseases [PDF]

open access: yesFrontiers in Molecular Neuroscience, 2019
Numerous neurodegenerative diseases including prion, Alzheimer’s and Parkinson’s diseases are characterized by accumulation of protein aggregates in brain.
Kwang Hun Lim
doaj   +2 more sources

Cross-seeding of alpha-synuclein aggregation by amyloid fibrils of food proteins. [PDF]

open access: yesJ Biol Chem, 2021
The aggregation of the protein α-synuclein (aSyn) into amyloid fibrils in the human brain is associated with the development of several neurodegenerative diseases, including Parkinson's disease. The previously observed prion-like spreading of aSyn aggregation throughout the brain and the finding that heterologous cross-seeding of amyloid aggregation ...
Vaneyck J   +3 more
europepmc   +5 more sources

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