Results 11 to 20 of about 160,241 (252)
The association of lipids with amyloid fibrils [PDF]
Journal of Biological Chemistry, 2022 Amyloid formation continues to be a widely studied area because of its association with numerous diseases, such as Alzheimer's and Parkinson's diseases. Despite a large body of work on protein aggregation and fibril formation, there are still significant gaps in our understanding of the factors that differentiate toxic amyloid formation in vivo from ...
John M. Sanderson, Sanderson, John M.
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Structural Studies of Cystatin B Amyloid Fibre and Oligomer [PDF]
, 2013 Amyloid fibres are characteristic of over 25 degenerative human diseases including Alzheimer’s and Parkinson’s disease. Amyloid fibres are insoluble, highly stable, ordered cross-β sheet structures, which form as a result of conformational change and ...
Davis, Peter J.
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Branching in Amyloid Fibril Growth [PDF]
Biophysical Journal, 2009 Using the peptide hormone glucagon and Abeta(1-40) as model systems, we have sought to elucidate the mechanisms by which fibrils grow and multiply. We here present real-time observations of growing fibrils at a single-fibril level. Growing from preformed seeds, glucagon fibrils were able to generate new fibril ends by continuously branching into new ...
C B Andersen +8 more
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Role of sequence and structural polymorphism on the mechanical properties of amyloid fibrils. [PDF]
PLoS ONE, 2014 Amyloid fibrils playing a critical role in disease expression, have recently been found to exhibit the excellent mechanical properties such as elastic modulus in the order of 10 GPa, which is comparable to that of other mechanical proteins such as ...
Gwonchan Yoon +4 more
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Prion, 2008 Amyloid refers to the abnormal fibrous, extracellular, proteinaceous deposits found in organs and tissues. Amyloid is insoluble and is structurally dominated by beta-sheet structure. Unlike other fibrous proteins it does not commonly have a structural, supportive or motility role but is associated with the pathology seen in a range of diseases known as
Roma N, Rambaran, Louise C, Serpell
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Amyloidogenic cross-seeding of Tau protein: Transient emergence of structural variants of fibrils. [PDF]
PLoS ONE, 2018 Amyloid aggregates of Tau protein have been implicated in etiology of many neurodegenerative disorders including Alzheimer's disease (AD). When amyloid growth is induced by seeding with preformed fibrils assembled from the same protein, structural ...
Bartosz Nizynski +5 more
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Secondary Nucleation and the Conservation of Structural Characteristics of Amyloid Fibril Strains
Frontiers in Molecular Biosciences, 2021 Amyloid fibrils are ordered protein aggregates and a hallmark of many severe neurodegenerative diseases. Amyloid fibrils form through primary nucleation from monomeric protein, grow through monomer addition and proliferate through fragmentation or ...
Saeid Hadi Alijanvand +2 more
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Polymorphism of Amyloid Fibrils In Vivo [PDF]
Angewandte Chemie International Edition, 2016 AbstractPolymorphism is a wide‐spread feature of amyloid‐like fibrils formed in vitro, but it has so far remained unclear whether the fibrils formed within a patient are also affected by this phenomenon. In this study we show that the amyloid fibrils within a diseased individual can vary considerably in their three‐dimensional architecture.
Karthikeyan, Annamalai +10 more
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Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters [PDF]
, 2010 Amyloid assemblies are associated with several debilitating human disorders. Understanding the intra- and extracellular assembly of normally soluble proteins and peptides into amyloid aggregates and how they disrupt normal cellular functions is therefore
Xue, Wei-Feng +7 more
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International Journal of Immunopathology and Pharmacology, 2022 Introduction Dialysis-related amyloidosis (DRA) caused by β2-microgloblin (B2M) fibrils is a serious complication for patients with kidney failure on long-term dialysis.
Naoe Kaneko +5 more
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