Results 21 to 30 of about 288,605 (343)
Nucleation of amyloid fibrils [PDF]
The Journal of Chemical Physics, 2010 We consider nucleation of amyloid fibrils in the case when the process occurs by the mechanism of direct polymerization of practically fully extended protein segments, i.e., β-strands, into β-sheets. Applying the classical nucleation theory, we derive a general expression for the work to form a nanosized amyloid fibril (protofilament) constituted of ...
Kashchiev, Dimo, Auer, Stefan
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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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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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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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Do amyloid fibrils induce inflammation, or does inflammation generate amyloid fibrils?
Proceedings of the National Academy of Sciences of the United States of America, 2022 Even though inflammation has long been associated with neurodegenerative diseases, reducing microglial activation and cytokine induction has not been a common therapeutic strategy compared with efforts to reduce amyloid deposition. The limited success of
J. Rothbard
semanticscholar +1 more source
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
doaj +1 more source
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 +3 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
doaj +1 more source
Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry [PDF]
, 2015 There is an ongoing debate regarding the culprits of cytotoxicity associated with amyloid disorders. Although small pre-fibrillar amyloid oligomers have been implicated as the primary toxic species, the fibrillar amyloid material itself can also induce ...
Smith, Rachel A. S. +24 more
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