Results 21 to 30 of about 187,834 (297)
A common beta-sheet architecture underlies in vitro and in vivo beta(2)-microglobulin amyloid fibrils [PDF]
, 2008 Misfolding and aggregation of normally soluble proteins into amyloid fibrils and their deposition and accumulation underlies a variety of clinically significant diseases.
Jahn, T.R., Radford, S.E., Tennent, G.A.
core +2 more sources
The Role of Lipid Environment in Ganglioside GM1-Induced Amyloid β Aggregation
Membranes, 2020 Ganglioside GM1 is the most common brain ganglioside enriched in plasma membrane regions known as lipid rafts or membrane microdomains. GM1 participates in many modulatory and communication functions associated with the development, differentiation, and ...
Vladimir Rudajev, Jiri Novotny
doaj +1 more source
Nature Reviews Disease Primers, 2022 Atrial fibrillation (AF) is the most common cardiac arrhythmia despite substantial efforts to understand the pathophysiology of the condition and develop improved treatments. Identifying the underlying causative mechanisms of AF in individual patients is difficult and the efficacy of current therapies is suboptimal. Consequently, the incidence of AF is
Bianca J. J. M. Brundel +5 more
openaire +5 more sources
Biocatalysis of d,l-Peptide Nanofibrillar Hydrogel
Molecules, 2020 Self-assembling peptides are attracting wide interest as biodegradable building blocks to achieve functional nanomaterials that do not persist in the environment. Amongst the many applications, biocatalysis is gaining momentum, although a clear structure-
Tiziano Carlomagno +6 more
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Polymorphic Aβ42 fibrils adopt similar secondary structure but differ in cross-strand side chain stacking interactions within the same β-sheet. [PDF]
, 2020 Formation of polymorphic amyloid fibrils is a common feature in neurodegenerative diseases involving protein aggregation. In Alzheimer's disease, different fibril structures may be associated with different clinical sub-types.
Duo, Lan +5 more
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Entropy of water and the temperature-induced stiffening of amyloid networks [PDF]
, 2017 In water, networks of semi-flexible fibrils of the protein $\alpha$-synuclein stiffen significantly with increasing temperature. We make plausible that this reversible stiffening is a result of hydrophobic contacts between the fibrils that become more ...
Claessens, Mireille M. A. E. +5 more
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Revealing Accessibility of Cryptic Protein Binding Sites within the Functional Collagen Fibril
Biomolecules, 2017 Fibrillar collagens are the most abundant proteins in the extracellular matrix. Not only do they provide structural integrity to all of the connective tissues in the human body, but also their interactions with multiple cell receptors and other matrix ...
Cody L. Hoop +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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Brain Sciences, 2014 Huntington disease and other diseases of polyglutamine expansion are each caused by a different protein bearing an excessively long polyglutamine sequence and are associated with neuronal death.
Guylaine Hoffner, Philippe Djian
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The Cellular Prion Protein Increases the Uptake and Toxicity of TDP-43 Fibrils
Viruses, 2021 Cytoplasmic aggregation of the primarily nuclear TAR DNA-binding protein 43 (TDP-43) affects neurons in most amyotrophic lateral sclerosis (ALS) and approximately half of frontotemporal lobar degeneration (FTLD) cases.
Carlo Scialò +8 more
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