Bacterial inclusion bodies contain amyloid-like structure. [PDF]
PLoS Biology, 2008 Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as amorphous, lacking any long-range order, or highly ordered fibrils. Protein fibrils can
Lei Wang +4 more
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Polymorphic Aβ42 fibrils adopt similar secondary structure but differ in cross-strand side chain stacking interactions within the same β-sheet. [PDF]
, 2020 Formation of polymorphic amyloid fibrils is a common feature in neurodegenerative diseases involving protein aggregation. In Alzheimer's disease, different fibril structures may be associated with different clinical sub-types.
Duo, Lan +5 more
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Molecular Dynamics Studies on 3D Structures of the Hydrophobic Region PrP(109-136) [PDF]
, 2013 Prion diseases caused by the conversion from a soluble normal cellular prion protein into insoluble abnormally folded infectious prions, are invariably fatal and highly infectious degenerative diseases that affect a wide variety of mammalian species. The
Zhang, Jiapu, Zhang, Yuanli
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Quercetin Disaggregates Prion Fibrils and Decreases Fibril-Induced Cytotoxicity and Oxidative Stress
Pharmaceutics, 2020 Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases caused by misfolding and aggregation of prion protein (PrP). Previous studies have demonstrated that quercetin can disaggregate some amyloid fibrils, such as amyloid β ...
Kun-Hua Yu, Cheng-I Lee
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Membrane-induced tau amyloid fibrils
Communications Biology, 2023 AbstractThe intrinsically disordered protein tau aggregates into β-sheet amyloid fibrils that spread in human brains afflicted with Alzheimer’s disease and other neurodegenerative diseases. Tau interaction with lipid membranes might play a role in the formation and spreading of these pathological aggregates.
Nadia El Mammeri +3 more
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2-arachidonoylglycerol metabolism is differently modulated by oligomeric and fibrillar conformations of amyloid beta in synaptic terminals [PDF]
, 2017 Alzheimer´s disease (AD) is the most prevalent disorder of senile dementia mainly characterized by amyloid-beta peptide (Aβ) deposits in the brain. Cannabinoids are relevant to AD as they exert several beneficial effects in many models of this disease ...
Gaveglio, Virginia Lucía +3 more
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Molecular Neurodegeneration, 2007 Background Amyloid-related degenerative diseases are associated with the accumulation of misfolded proteins as amyloid fibrils in tissue. In Alzheimer disease (AD), amyloid accumulates in several distinct types of insoluble plaque deposits, intracellular
Rasool Suhail +13 more
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Limited proteolysis in the investigation of beta2-microglobulin amyloidogenic and fibrillar states. [PDF]
, 2005 Amyloid fibrils of patients treated with regular haemodialysis essentially consists of β2-microglobulin (β2-m) and its truncated species ΔN6β2-m lacking six residues at the amino terminus.
AMORESANO, ANGELA +4 more
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Biology Open, 2015 Semen harbors amyloid fibrils formed by proteolytic fragments of prostatic acid phosphatase (PAP248-286 and PAP85-120) and semenogelins (SEM1 and SEM2) that potently enhance HIV infectivity.
Laura M. Castellano +4 more
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Modulation of β-Amyloid Fibril Formation in Alzheimer’s Disease by Microglia and Infection
Frontiers in Molecular Neuroscience, 2020 Amyloid plaques are a pathological hallmark of Alzheimer’s disease. The major component of these plaques are highly ordered amyloid fibrils formed by amyloid-β (Aβ) peptides.
Madeleine R. Brown +2 more
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