Results 21 to 30 of about 18,838 (278)
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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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
doaj +1 more source
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
doaj +1 more source
Structure-function analysis of the curli accessory protein CsgE defines surfaces essential for coordinating amyloid fiber formation [PDF]
, 2018 Curli amyloid fibers are produced as part of the extracellular biofilm matrix and are composed primarily of the major structural subunit CsgA. The CsgE chaperone facilitates the secretion of CsgA through CsgG by forming a cap at the base of the nonameric
Amarasinghe, Gaya K +13 more
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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
doaj +1 more source
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
doaj +1 more source
STITCHER: Dynamic assembly of likely amyloid and prion β-structures from secondary structure predictions [PDF]
, 2011 The supersecondary structure of amyloids and prions, proteins of intense clinical and biological interest, are difficult to determine by standard experimental or computational means.
Berger, Bonnie +5 more
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Viruses, 2019 The mechanism of prion strain diversity remains unsolved. Investigation of inheritance and diversification of protein-based pathogenic information demands the identification of the detailed structures of abnormal isoforms of the prion protein (PrPSc ...
Yuzuru Taguchi +2 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.
core +4 more sources