Results 21 to 30 of about 18,947 (293)
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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Molecules, 2020 The term “amyloid” refers to proteinaceous deposits of peptides that might be generated from larger precursor proteins e.g., by proteolysis.
Kristina Endres
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International Psychogeriatrics, 2011 Molecular neuroimaging techniques such as PET are proving valuable in the early and differential diagnosis of Alzheimer's disease (AD).With the advent of new therapeutic strategies aimed at reducing β-amyloid (Aβ) burden in the brain to potentially prevent or delay functional and irreversible cognitive loss, there is increased interest in developing ...
Victor L, Villemagne +1 more
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Biomedical Papers, 2017 Amyloidosis is a heterogeneous group of diseases characterized by the deposition of amyloid. It is caused by extracellular deposition of insoluble fibrils with beta-pleated sheet configuration. The protein misfolding abnormalities result in amyloid fibrils and may manifest as primary, secondary, or familial amyloidosis.
Lucie Karafiatova, Tomas Pika
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SynBio and the Boundaries between Functional and Pathogenic RepA-WH1 Bacterial Amyloids
mSystems, 2020 Amyloids are protein polymers that were initially linked to human diseases. Across the whole Tree of Life, many disease-unrelated proteins are now emerging for which amyloids represent distinct functional states.
Rafael Giraldo
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M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils. [PDF]
PLoS ONE, 2018 Amyloids are protein fibrils with a characteristic spatial structure. Amyloids were long perceived as the pathogens involved in a set of lethal diseases in humans and animals.
Mikhail V Belousov +9 more
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Gene Regulation of Biofilm-Associated Functional Amyloids
Pathogens, 2021 Biofilms are bacterial communities encased in a rigid yet dynamic extracellular matrix. The sociobiology of bacterial communities within a biofilm is astonishing, with environmental factors playing a crucial role in determining the switch from planktonic
Khushal Khambhati +4 more
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Hsp104 Gives Clients the Individual Attention They Need [PDF]
, 2010 Yeast heat shock protein 104 (Hsp104), the only known eukaryotic disaggregase, remodels both disordered protein aggregates and cross-β sheet amyloids. To handle this diverse clientele, DeSantis et al.
Murray, Amber N., Kelly, Jeffery W.
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Pharmacological Agents Targeting the Cellular Prion Protein
Pathogens, 2018 Prion diseases are associated with the conversion of the cellular prion protein (PrPC), a glycoprotein expressed at the surface of a wide variety of cell types, into a misfolded conformer (the scrapie form of PrP, or PrPSc) that accumulates in brain ...
Maria Letizia Barreca +4 more
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Catalytically Active Amyloids as Future Bionanomaterials
Nanomaterials, 2022 Peptides and proteins can aggregate into highly ordered and structured conformations called amyloids. These supramolecular structures generally have convergent features, such as the formation of intermolecular beta sheets, that lead to fibrillary ...
Rodrigo Diaz-Espinoza
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