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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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Light Chain Amyloid Fibrils Cause Metabolic Dysfunction in Human Cardiomyocytes. [PDF]
PLoS ONE, 2015 Light chain (AL) amyloidosis is the most common form of systemic amyloid disease, and cardiomyopathy is a dire consequence, resulting in an extremely poor prognosis.
Helen P McWilliams-Koeppen +12 more
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Plasticity of Amyloid Fibrils [PDF]
Biochemistry, 2006 In experiments designed to characterize the basis of amyloid fibril stability through mutational analysis of the Abeta (1-40) molecule, fibrils exhibit consistent, significant structural malleability. In these results, and in other properties, amyloid fibrils appear to more resemble plastic materials generated from synthetic polymers than globular ...
Ronald, Wetzel +2 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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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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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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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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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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Zinc–dysprosium functionalized amyloid fibrils [PDF]
Dalton Transactions, 2019 The heterometallic Zn2Dy2 entity bearing partially saturated metal centres covalently decorates a highly ordered amyloid fibril core and the functionalised assembly exhibits catalytic Lewis acid behaviour.
Stavroula I. Sampani +4 more
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Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain. [PDF]
, 2015 Overproduction of immunoglobulin light chains leads to systemic amyloidosis, a lethal disease characterized by the formation of amyloid fibrils in patients' tissues. Excess light chains are in equilibrium between dimers and less stable monomers which can
Brumshtein, Boris +7 more
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