Results 21 to 30 of about 3,689,678 (299)
Physical determinants of the self-replication of protein fibrils. [PDF]
Nat Phys, 2016 The ability of biological molecules to replicate themselves is the foundation of life, requiring a complex cellular machinery. However, a range of aberrant processes involve the self-replication of pathological protein structures without any additional ...
Šarić A +7 more
europepmc +4 more sources
The role of protonation in protein fibrillation [PDF]
FEBS Letters, 2010 Many proteins fibrillate at low pH despite a high population of charged side chains. Therefore exchange of protons between the fibrillating peptide and its surroundings may play an important role in fibrillation. Here, we use isothermal titration calorimetry to measure exchange of protons between buffer and the peptide hormone glucagon during ...
Jeppesen, Martin D +2 more
openaire +4 more sources
Nanoparticles as catalysts for protein fibrillation [PDF]
Proceedings of the National Academy of Sciences, 2007 The study by Linse et al. (1) published in this issue of PNAS observes that nanoparticles (NPs) can significantly enhance the rate of protein fibrillation, or the formation of fibrils, potentially leading to novel mechanisms for amyloid diseases as well as therapeutic opportunities for their treatment.
Vicki L, Colvin, Kristen M, Kulinowski
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DNA-Guided Assembly for Fibril Proteins [PDF]
Mathematics, 2021 Current advances in computational modelling and simulation have led to the inclusion of computer scientists as partners in the process of engineering of new nanomaterials and nanodevices. This trend is now, more than ever, visible in the field of deoxyribonucleic acid (DNA)-based nanotechnology, as DNA’s intrinsic principle of self-assembly has been ...
Alexandru Amărioarei +11 more
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Quercetin Disaggregates Prion Fibrils and Decreases Fibril-Induced Cytotoxicity and Oxidative Stress
Pharmaceutics, 2020 Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases caused by misfolding and aggregation of prion protein (PrP). Previous studies have demonstrated that quercetin can disaggregate some amyloid fibrils, such as amyloid β ...
Kun-Hua Yu, Cheng-I Lee
doaj +1 more source
Instantaneous fibrillation of egg white proteome with ionic liquid and macromolecular crowding
Communications Materials, 2020 The applicability of protein fibrils as functional biomaterials is limited due to low scalability of production process, slow kinetics, and requirement of expensive purified proteins.
Pankaj Bharmoria +10 more
doaj +1 more source
Prion, 2008 Amyloid refers to the abnormal fibrous, extracellular, proteinaceous deposits found in organs and tissues. Amyloid is insoluble and is structurally dominated by beta-sheet structure. Unlike other fibrous proteins it does not commonly have a structural, supportive or motility role but is associated with the pathology seen in a range of diseases known as
Roma N, Rambaran, Louise C, Serpell
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Elevated temperatures accelerate the formation of toxic amyloid fibrils of hen egg‐white lysozyme
Veterinary Medicine and Science, 2021 The formation of amyloid fibrils is critical for neurodegenerative diseases. Some physiochemical conditions can promote the conversion of proteins from soluble globular shapes into insoluble well‐organized amyloid fibrils.
Zili Feng, Ying Li, Yu Bai
doaj +1 more source
Antiserum to scrapie-associated fibril protein cross-reacts with Spiroplasma mirum fibril proteins [PDF]
Journal of Clinical Microbiology, 1987 Protease-resistant fibril proteins purified from Spiroplasma mirum and from Creutzfeldt-Jakob disease-infected brain tissues reacted with antisera to scrapie-associated fibrils on Western immunoblot analysis. These data suggest that there are conformational similarities among spiroplasma proteins and infection-specific proteins of the transmissible ...
F O, Bastian +2 more
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Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry [PDF]
, 2015 There is an ongoing debate regarding the culprits of cytotoxicity associated with amyloid disorders. Although small pre-fibrillar amyloid oligomers have been implicated as the primary toxic species, the fibrillar amyloid material itself can also induce ...
Smith, Rachel A. S. +24 more
core +2 more sources