Results 31 to 40 of about 75,180 (286)
Membrane Anchored Polymers Modulate Amyloid Fibrillation [PDF]
Macromolecular Rapid Communications, 2021 AbstractThe nucleating role of cellular membrane components, such as lipid moieties on amyloid beta (Aβ1–40) fibrillation, has been reported in recent years. The influence of conjugates fabricated from lipid anchors (cholesterol, diacylglycerol) and hydrophilic polymers on Aβ1–40 fibrillation is reported here, aiming to understand the impact of ...
Sen, Newton +2 more
openaire +4 more sources
Interfacial Electrostatic Self‐Assembly of Amyloid Fibrils into Multifunctional Protein Films
Advanced Science, 2023 Amyloid fibrils have generated steadily increasing traction in the development of natural and artificial materials. However, it remains a challenge to construct bulk amyloid films directly from amyloid fibrils due to their intrinsic brittleness.
Yangyang Han +9 more
doaj +1 more source
Concentration-dependent polymorphism of insulin amyloid fibrils [PDF]
PeerJ, 2019 Protein aggregation into highly structured fibrils has long been associated with several neurodegenerative disorders, such as Alzheimer’s or Parkinson’s disease.
Andrius Sakalauskas +2 more
doaj +2 more sources
Apolipoprotein E Regulates Amyloid Formation within Endosomes of Pigment Cells
Cell Reports, 2015 Accumulation of toxic amyloid oligomers is a key feature in the pathogenesis of amyloid-related diseases. Formation of mature amyloid fibrils is one defense mechanism to neutralize toxic prefibrillar oligomers.
Guillaume van Niel +12 more
doaj +1 more source
Uncovering the Mechanism of Aggregation of Human Transthyretin. [PDF]
, 2015 The tetrameric thyroxine transport protein transthyretin (TTR) forms amyloid fibrils upon dissociation and monomer unfolding. The aggregation of transthyretin has been reported as the cause of the life-threatening transthyretin amyloidosis.
Cascio, Duilio +9 more
core +2 more sources
Molecules, 2021 Amyloidosis is a term referring to a group of various protein-misfolding diseases wherein normally soluble proteins form aggregates as insoluble amyloid fibrils.
Haruki Koike +3 more
doaj +1 more source
β-Cell failure in type 2 diabetes: a case of asking too much of too few? [PDF]
, 2013 The islet in type 2 diabetes (T2DM) is characterized by a deficit in β-cells, increased β-cell apoptosis, and extracellular amyloid deposits derived from islet amyloid polypeptide (IAPP). In the absence of longitudinal studies, it is unknown if the low β-
Butler, Peter C +4 more
core +1 more source
The relationship between amyloid structure and cytotoxicity [PDF]
, 2014 Self-assembly of proteins and peptides into amyloid structures has been the subject of intense and focused research due to their association with neurodegenerative, age-related human diseases and transmissible prion diseases in humans and mammals. Of the
Marchante, Ricardo +3 more
core +1 more source
Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches
Computational and Structural Biotechnology Journal, 2021 The aggregation of proteins into insoluble filamentous amyloid fibrils is a pathological hallmark of neurodegenerative diseases that include Parkinson’s disease and Alzheimer’s disease.
Lauren J. Rice +2 more
doaj +1 more source
Nucleation of Polymorphic Amyloid Fibrils [PDF]
Biophysical Journal, 2015 One and the same protein can self-assemble into amyloid fibrils with different morphologies. The phenomenon of fibril polymorphism is relevant biologically because different fibril polymorphs can have different toxicity, but there is no tool for predicting which polymorph forms and under what conditions.
openaire +4 more sources