Results 131 to 140 of about 288,605 (343)
Formation and properties of whey protein fibrils
, 2011 Protein fibrils are threadlike aggregates that are about one molecule thick and more than thousand molecules long. Due to their threadlike structure they could potentially be used to form meat-like structures.
Kroes-Nijboer, A.
core
On the reversibility of amyloid fibril formation
Biophysics ReviewsAmyloids are elongated supramolecular protein self-assemblies. Their formation is a non-covalent assembly process and as such is fully reversible. Amyloid formation is associated with several neurodegenerative diseases, and the reversibility is key to maintaining the healthy state.
Tinna Pálmadóttir +7 more
openaire +2 more sources
Tafamidis Treatment for Patients with Transthyretin Amyloid Cardiomyopathy
New England Journal of Medicine, 2018 Background Transthyretin amyloid cardiomyopathy is caused by the deposition of transthyretin amyloid fibrils in the myocardium. The deposition occurs when wild‐type or variant transthyretin becomes unstable and misfolds. Tafamidis binds to transthyretin,
M. Maurer +21 more
semanticscholar +1 more source
Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43
Nature, 2022 Y. Jiang +10 more
semanticscholar +1 more source
Human Hsp70 Disaggregase Reverses Parkinson’s-Linked α-Synuclein Amyloid Fibrils
Molecules and Cells, 2015 Summary Intracellular amyloid fibrils linked to neurodegenerative disease typically accumulate in an age-related manner, suggesting inherent cellular capacity for counteracting amyloid formation in early life.
Xuechao Gao +9 more
semanticscholar +1 more source
Cyclic Peptides as Inhibitors of Amyloid Fibrillation
Chemistry – A European Journal, 2014 AbstractMany neurodegenerative diseases, like Parkinson’s, Alzheimer’s, or Huntington’s disease, occur as a result of amyloid protein fibril formation and cell death induced by this process. Cyclic peptides (CPs) and their derivatives form a new class of powerful inhibitors that prevent amyloid fibrillation and decrease the cytotoxicity of aggregates ...
Luo, J., Abrahams, J.P.
openaire +4 more sources
The Critical Aggregation Concentration of ß-Lactoglobulin-Based Fibril Formation
, 2009 The critical aggregation concentration (CAC) for fibril formation of ß-lactoglobulin (ß-lg) at pH 2 was determined at 343, 353, 358, 363, and 383 K using a Thioflavin T assay and was approximately 0.16 wt%.
Kroes-Nijboer, A. +3 more
core +1 more source
New nanomaterials: amyloid fibrils from waste proteins [PDF]
, 2012 The current landscape of nanotechnology has focussed attention on materials that self-assemble. The search for such materials has unsurprisingly led to the biological world, where functional nanoscale biomolecular assemblies are in abundance.
Domigan, Laura Joy
core +1 more source
A fluorescent amyloid sensor for quantitative super-resolution imaging of amyloid fibril assembly.
, 2021 Many soluble proteins can self-assemble into macromolecular structures called amyloids, a subset of which are implicated in a range of neurodegenerative disorders.
Liam D., Adair +4 more
core +1 more source
Food Chemistry, 2016 The structural properties of amyloid fibrils combined with their highly functional surface chemistry make them an attractive new food ingredient, for example as highly effective gelling agents.
Moritz Lassé +7 more
semanticscholar +1 more source