Proline isomerization effects in the amyloidogenic protein β2-microglobulin [PDF]
Physical Chemistry Chemical Physics, 2021 The protein β2-microglobulin can aggregate in insoluble amyloid fibrils. By relying on extensive sampling simulations, we study the Pro32 isomerization as a possible triggering factor leading to structural modifications in β2-m.
Maria Celeste Maschio +3 more
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The amyloid interactome: Exploring protein aggregation. [PDF]
PLoS ONE, 2017 Protein-protein interactions are the quintessence of physiological activities, but also participate in pathological conditions. Amyloid formation, an abnormal protein-protein interaction process, is a widespread phenomenon in divergent proteins and ...
Konstantina V Biza +5 more
doaj +1 more source
RNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivity. [PDF]
, 2009 Aptamers are useful molecular recognition tools in research, diagnostics, and therapy. Despite promising results in other fields, aptamer use has remained scarce in amyloid research, including Alzheimer's disease (AD).
Bitan, Gal +4 more
core +5 more sources
Amyposomes, a nanotechnological chaperone with anti-amyloidogenic activity
Annals of Medicine, 2023 Aim The effect of liposomes bi-functionalized with phosphatidic acid and with a synthetic peptide derived from human apolipoprotein E has been evaluated on the aggregation features of different amyloidogenic proteins: human Amyloid β1–40 (Aβ1–40 ...
Francesca Re +13 more
doaj +1 more source
Prediction of peptide and protein propensity for amyloid formation [PDF]
, 2014 Understanding which peptides and proteins have the potential to undergo amyloid formation and what driving forces are responsible for amyloid-like fiber formation and stabilization remains limited.
A Quintas +80 more
core +5 more sources
AmyLoad: website dedicated to amyloidogenic protein fragments [PDF]
Bioinformatics, 2015 Abstract Analyses of amyloidogenic sequence fragments are essential in studies of neurodegenerative diseases. However, there is no one internet dataset that collects all the sequences that have been investigated for their amyloidogenicity.
Pawel P, Wozniak, Malgorzata, Kotulska
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Uncovering the Mechanism of Aggregation of Human Transthyretin. [PDF]
, 2015 The tetrameric thyroxine transport protein transthyretin (TTR) forms amyloid fibrils upon dissociation and monomer unfolding. The aggregation of transthyretin has been reported as the cause of the life-threatening transthyretin amyloidosis.
Cascio, Duilio +9 more
core +2 more sources
Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin [PDF]
Biophysical Chemistry, 2000 Familial amyloidotic polyneuropathy (FAP) is an autosomal dominant hereditary type of amyloidosis involving amino acid substitutions in transthyretin (TTR). V30M-TTR is the most frequent variant, and L55P-TTR is the variant associated with the most aggressive form of FAP.
Shnyrov, Valery L. +6 more
openaire +3 more sources
The proteome response to amyloid protein expression in vivo. [PDF]
PLoS ONE, 2012 Protein misfolding disorders such as Alzheimer, Parkinson and transthyretin amyloidosis are characterized by the formation of protein amyloid deposits.
Ricardo A Gomes +10 more
doaj +1 more source
Computational and Structural Biotechnology Journal, 2021 Alpha-synuclein (αSyn) is often described as a predominantly disordered protein that has a propensity to self-assemble into toxic oligomers that are found in patients with Parkinson's and Alzheimer's diseases.
Sarah R. Evans +2 more
doaj +1 more source