Results 81 to 90 of about 288,605 (343)
Thermodynamics of β-amyloid fibril formation [PDF]
The Journal of Chemical Physics, 2004 Amyloid fibers are aggregates of proteins. They are built out of a peptide called β-amyloid (Aβ) containing between 41 and 43 residues, produced by the action of an enzyme which cleaves a much larger protein known as the amyloid precursor protein (APP).
G. Tiana +3 more
openaire +5 more sources
Amyloid Fibrils Length Controls Shape and Structure of Nematic and Cholesteric Tactoids.
ACS Nano, 2018 Amyloid fibrils offer the possibility of controlling their contour length, aspect ratio, and length distribution, without affecting other structural parameters.
Massimo Bagnani +3 more
semanticscholar +1 more source
Exploring the sequence–structure relationship for amyloid peptides [PDF]
, 2012 Amyloid fibril formation is associated with misfolding diseases, as well as fulfilling a functional role. The cross-β molecular architecture has been reported in increasing numbers of amyloid-like fibrillar systems. The Waltz algorithm is able to predict
Morris, Kyle L. +14 more
core +1 more source
Advanced Science, EarlyView.The 10B‐enriched monocarbonyl analog of curcumin (BMAC) 10B‐9 enables site‐specific Boron Neutron Capture Therapy (BNCT) on amyloid‐β (Aβ) fibrils. Neutron irradiation induces histidine oxidation and fibril destabilization, as revealed by 1H‐NMR and FESEM analyses.
Sebastiano Micocci +13 more
wiley +1 more source
Angewandte Chemie, EarlyView.In this review, we discuss how biomolecular condensates can inhibit amyloid aggregation in their interior, while still facilitating fibril formation at the interface between the dense and dilute phases, where molecular and mesoscale properties are likely optimal to promote protein aggregation.
Marcell Papp +3 more
wiley +2 more sources
Nanomechanical Characterization of Apolipoprotein A-I Amyloid Fibrils
East European Journal of Physics, 2020 Amyloid fibrils represent a special type of protein aggregates that are currently receiving enormous attention due to their strong implication in molecular etiology of a wide range of human disorders.
Valeriya Trusova +5 more
doaj +1 more source
Food protein-derived amyloids do not accelerate amyloid β aggregation
Scientific Reports, 2023 The deposition of proteins in the form of amyloid fibrils is closely associated with several serious diseases. The events that trigger the conversion from soluble functional proteins into insoluble amyloid are not fully understood. Many proteins that are
M. Mahafuzur Rahman +6 more
doaj +1 more source
Biomolecules, 2022 The division of amyloid fibril particles through fragmentation is implicated in the progression of human neurodegenerative disorders such as Parkinson’s disease.
Sarina Sanami +4 more
doaj +1 more source
Crystallin proteins and amyloid fibrils
Cellular and Molecular Life Sciences, 2008 Improper protein folding (misfolding) can lead to the formation of disordered (amorphous) or ordered (amyloid fibril) aggregates. The major lens protein, alpha-crystallin, is a member of the small heat-shock protein (sHsp) family of intracellular molecular chaperone proteins that prevent protein aggregation.
Ecroyd, Heath, Carver, John
openaire +4 more sources
Scientific Reports, 2018 The formation of amyloid fibrils by human islet amyloid polypeptide protein (hIAPP) has been implicated in pancreas dysfunction and diabetes. However, efficient treatment options to reduce amyloid fibrils in vivo are still lacking.
Andras Franko +15 more
semanticscholar +1 more source