Antimicrobial Peptides as Cross-Seeding Modulators at the Neurodegenerative–Infectious Interface [PDF]
ResearchAntimicrobial peptides (AMPs), traditionally regarded as innate immune effectors, are increasingly recognized for their structural and functional convergence with pathogenic amyloids.
Yanxian Zhang +3 more
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Noncerebral Amyloidoses: Aspects on Seeding, Cross-Seeding, and Transmission. [PDF]
Cold Spring Harb Perspect Med, 2018 More than 30 proteins form amyloid in humans, most of them outside of the brain. Deposition of amyloid in extracerebral tissues is very common and seems inevitable for an aging person. Most deposits are localized, small, and probably without consequence, but in some instances, they are associated with diseases such as type 2 diabetes.
Westermark GT +3 more
europepmc +4 more sources
Cross-seeding between Aβ40 and Aβ42 in Alzheimer's disease. [PDF]
FEBS Lett, 2017 Aβ42 is the major component of parenchymal plaques in the brain of Alzheimer's patients, while Aβ40 is the major component of cerebrovascular plaques. Since Aβ40 and Aβ42 coexist in the brain, understanding the interaction between Aβ40 and Aβ42 during their aggregation is important to delineate the molecular mechanism underlying Alzheimer's disease ...
Tran J, Chang D, Hsu F, Wang H, Guo Z.
europepmc +6 more sources
Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy. [PDF]
PLoS Pathogens, 2017 Aggregation of misfolded proteins or peptides is a common feature of neurodegenerative diseases including Alzheimer's, Parkinson's, Huntington's, prion and other diseases.
Elizaveta Katorcha +6 more
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Heterologous cross-seeding mimics cross-species prion conversion in a yeast model [PDF]
BMC Biology, 2009 Background Prions are self-perpetuating, infectious, aggregated proteins that are associated with several neurodegenerative diseases in mammals and heritable traits in yeast.
Liebman Susan W, Vishveshwara Namitha
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Serine phosphorylation mimics of Aβ form distinct, non-cross-seeding fibril morphs. [PDF]
Chem SciLeft: One plane of an Aβ42 wt fibril with Ser8 and Ser26 marked. Right: Four aggregation time courses starting from a 1 : 1 mixture of Aβ42 wt and S26E, implying that the peptides fail to coaggregate and two separate types of fibrils are formed.
Sanagavarapu K +8 more
europepmc +3 more sources
Amyloidogenic cross-seeding of Tau protein: Transient emergence of structural variants of fibrils. [PDF]
PLoS ONE, 2018 Amyloid aggregates of Tau protein have been implicated in etiology of many neurodegenerative disorders including Alzheimer's disease (AD). When amyloid growth is induced by seeding with preformed fibrils assembled from the same protein, structural ...
Bartosz Nizynski +5 more
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Experimental and Computational Protocols for Studies of Cross-Seeding Amyloid Assemblies. [PDF]
Methods Mol Biol, 2018 Alzheimer's disease (AD) and type 2 diabetes (T2D) are two common protein aggregation diseases. Compelling evidence has shown a link between AD and T2D, which may derive from interspecies cross-sequence interactions between amyloid-β peptide (Aβ), associated with AD, and human islet amyloid polypeptide (hIAPP), associated with T2D.
Ren B +9 more
europepmc +4 more sources
Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae
Scientific Reports, 2017 The early stages of protein misfolding remain incompletely understood, as most mammalian proteinopathies are only detected after irreversible protein aggregates have formed.
Kathryn M. Keefer +2 more
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Inter-species cross-seeding: stability and assembly of rat-human amylin aggregates. [PDF]
PLoS ONE, 2014 Diseases such as type 2 diabetes, Alzheimer's and Parkinson's share as common feature the accumulation of mis-folded disease-specific protein aggregates into fibrillar structures, or plaques.
Workalemahu M Berhanu +1 more
doaj +4 more sources