Results 11 to 20 of about 132,897 (299)

Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq

open access: yesAntibiotics, 2021
Hfq is a bacterial regulator with key roles in gene expression. The protein notably regulates translation efficiency and RNA decay in Gram-negative bacteria, thanks to its binding to small regulatory noncoding RNAs. This property is of primary importance
Florian Turbant   +6 more
doaj   +1 more source

Surface Properties of Aqueous Dispersions of Bovine Serum Albumin Fibrils

open access: yesColloids and Interfaces, 2023
The surface properties of aqueous dispersions of worm-like fibril aggregates of bovine serum albumin (BSA) differ from those of the adsorption layers of the native protein. The dispersions of BSA fibrils are characterized by slower changes of the surface
Alexander Akentiev   +4 more
doaj   +1 more source

Cryo-EM demonstrates the in vitro proliferation of an ex vivo amyloid fibril morphology by seeding

open access: yesNature Communications, 2022
Here, the authors present the cryo-EM structure of in vitro amyloid fibrils from recombinant SAA1.1 protein that were formed by seeding with fibrils purified from systemic AA amyloidosis tissue.
Thomas Heerde   +12 more
doaj   +1 more source

Antisera to scrapie-associated fibril protein and prion protein decorate scrapie-associated fibrils [PDF]

open access: yesJournal of Virology, 1987
Scrapie-associated fibrils (SAF) are an infection-specific structure observed in the unconventional-agent diseases. Polyclonal antisera raised to scrapie proteins were used to test the antigenic relationship between purified fibrils and SAF isolated from non-protease-treated synaptosomal-mitochondrial preparations.
P A, Merz   +4 more
openaire   +2 more sources

Antiserum to scrapie-associated fibril protein cross-reacts with Spiroplasma mirum fibril proteins [PDF]

open access: yesJournal 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
openaire   +2 more sources

Site-specific perturbations of alpha-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46K. [PDF]

open access: yes, 2013
PMCID: PMC3591419This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited ...
A Loquet   +50 more
core   +9 more sources

Quercetin Disaggregates Prion Fibrils and Decreases Fibril-Induced Cytotoxicity and Oxidative Stress

open access: yesPharmaceutics, 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

open access: yesCommunications 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

Elevated temperatures accelerate the formation of toxic amyloid fibrils of hen egg‐white lysozyme

open access: yesVeterinary 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

Nanoparticles as catalysts for protein fibrillation [PDF]

open access: yesProceedings 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
openaire   +2 more sources

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