Results 11 to 20 of about 3,689,678 (299)
Nucleation of protein fibrillation by nanoparticles [PDF]
Proceedings of the National Academy of Sciences, 2007 Nanoparticles present enormous surface areas and are found to enhance the rate of protein fibrillation by decreasing the lag time for nucleation. Protein fibrillation is involved in many human diseases, including Alzheimer's, Creutzfeld-Jacob disease, and dialysis-related amyloidosis. Fibril formation occurs by nucleation-dependent
Linse, Sara +7 more
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Toxic species in amyloid disorders: Oligomers or mature fibrils
Annals of Indian Academy of Neurology, 2015 Protein aggregation is the hallmark of several neurodegenerative disorders. These protein aggregation (fibrillization) disorders are also known as amyloid disorders. The mechanism of protein aggregation involves conformation switch of the native protein,
Meenakshi Verma +2 more
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Ca2+-Induced Cold-Set Gelation of Whey Protein Isolate Fibrils
Applied Rheology, 2006 In this paper we describe the rheological behaviour of Ca2+-induced cold-set gels of whey protein mixtures. Cold- set gels are important applications for products with a low thermal stability.
Bolder Suzanne G. +3 more
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Protein Fibrils Induce Emulsion Stabilization
Langmuir, 2016 The behavior of an oil-in-water emulsion was studied in the presence of protein fibrils for a wide range of fibril concentrations by using rheology, diffusing wave spectroscopy, and confocal laser scanning microscopy. Results showed that above a minimum fibril concentration depletion flocculation occurred, leading to oil droplet aggregation and ...
Peng, Jinfeng +3 more
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Research status and application of plant protein amyloid fibrils
Shipin yu jixieMost natural plant proteins have dense spherical structures, reducing their functionality and accessibility to proteases, which limits their application in the food industry to some extent.
WANG Pengwei +4 more
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Aggregation Condition-Structure Relationship of Mouse Prion Protein Fibrils. [PDF]
Int J Mol Sci, 2021 Prion diseases are associated with conformational conversion of cellular prion protein into a misfolded pathogenic form, which resembles many properties of amyloid fibrils.
Fridmanis J +6 more
europepmc +4 more sources
Formation of amyloid fibrils by the regulatory 14-3-3ζ protein [PDF]
Open BiologyThe 14-3-3 proteins are a highly conserved adaptor protein family with multi-layer functions, abundantly expressed in the brain. The 14-3-3 proteins modulate phosphorylation, regulate enzymatic activity and can act as chaperones.
Darius Šulskis +4 more
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Ligands for Protein Fibrils of Amyloid-β, α-Synuclein, and Tau. [PDF]
Chem RevAmyloid fibrils are characteristic features of many neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. The use of small molecule ligands that bind to amyloid fibrils underpins both fundamental research aiming to better ...
Chisholm TS, Hunter CA.
europepmc +9 more sources
SARS-CoV-2 N-protein induces the formation of composite α-synuclein/N-protein fibrils that transform into a strain of α-synuclein fibrils [PDF]
, 2023 The presence of deposits of alpha-synuclein (αS) fibrils in the cells of the brain is a hallmark of several α-synucleinopathies, including Parkinson's disease.
Semerdzhiev SA +4 more
europepmc +2 more sources
The Effect of Osmolytes on Protein Fibrillation [PDF]
International Journal of Molecular Sciences, 2012 Osmolytes are small molecules that are exploited by cells as a protective system against stress conditions. They favour compact protein states which makes them stabilize globular proteins in vitro and promote folding. Conversely, this preference for compact states promotes aggregation of unstructured proteins.
Macchi, Francesca +3 more
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