Results 41 to 50 of about 202,201 (346)
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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Structural Variation in Amyloid-β Fibrils from Alzheimer’s Disease Clinical Subtypes
Nature, 2017 Aggregation of amyloid-β peptides into fibrils or other self-assembled states is central to the pathogenesis of Alzheimer’s disease. Fibrils formed in vitro by 40- and 42-residue amyloid-β peptides (Aβ40 and Aβ42) are polymorphic, with variations in ...
W. Qiang +4 more
semanticscholar +1 more source
Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly [PDF]
, 2008 Self-assembly of misfolded proteins into ordered fibrillar aggregates known as amyloid results in numerous human diseases. Despite an increasing number of proteins and peptide fragments being recognised as amyloidogenic, how these amyloid aggregates ...
Xue, Wei-Feng +2 more
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The association of lipids with amyloid fibrils [PDF]
, 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
John M. Sanderson, Sanderson, John M.
core +1 more source
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
doaj +1 more source
Journal of Biological Chemistry, 2005 Alzheimer's disease (AD) involves amyloid β (Aβ) accumulation, oxidative damage, and inflammation, and risk is reduced with increased antioxidant and anti-inflammatory consumption.
Fu-Sheng Yang +10 more
semanticscholar +1 more source
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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MoleculesA recent analysis compared the proteome of (i) blood clots seen in two diseases—sepsis and long COVID—when blood was known to have clotted into an amyloid microclot form (as judged by staining with the fluorogenic amyloid stain thioflavin T) with (ii ...
Douglas B. Kell, Etheresia Pretorius
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Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils
Biochimica et Biophysica Acta, 2010 Intense efforts to detect, diagnose, and analyze the kinetic and structural properties of amyloid fibrils have generated a powerful toolkit of amyloid-specific molecular probes.
M. Biancalana, S. Koide
semanticscholar +1 more source