The amyloid-β oligomer hypothesis: beginning of the third decade

EN Cline, MA Bicca, KL Viola… - Journal of Alzheimer's …, 2018 - content.iospress.com
The amyloid-β oligomer (AβO) hypothesis was introduced in 1998. It proposed that the brain
damage leading to Alzheimer's disease (AD) was instigated by soluble, ligand-like AβOs …

Post-translational modifications of tau protein: implications for Alzheimer's disease

L Martin, X Latypova, F Terro - Neurochemistry international, 2011 - Elsevier
Alzheimer's disease (AD) belongs to a group of neurodegenerative diseases collectively
designated as “tauopathies”, because they are characterized by the aggregation of …

Mesenchymal stem cells and cell-derived extracellular vesicles protect hippocampal neurons from oxidative stress and synapse damage induced by amyloid-β …

MA de Godoy, LM Saraiva, LRP de Carvalho… - Journal of Biological …, 2018 - ASBMB
Alzheimer's disease (AD) is a disabling and highly prevalent neurodegenerative condition,
for which there are no effective therapies. Soluble oligomers of the amyloid-β peptide (AβOs) …

Rationally designed peptides and peptidomimetics as inhibitors of amyloid-β (Aβ) aggregation: Potential therapeutics of Alzheimer's disease

D Goyal, S Shuaib, S Mann, B Goyal - ACS combinatorial science, 2017 - ACS Publications
Alzheimer's disease (AD) is a progressive neurodegenerative disease with no clinically
accepted treatment to cure or halt its progression. The worldwide effort to develop peptide …

Preparation and characterization of neurotoxic tau oligomers

CA Lasagna-Reeves, DL Castillo-Carranza… - Biochemistry, 2010 - ACS Publications
Tau aggregation is a pathological hallmark of Alzheimer's disease, Parkinson's disease, and
many other neurodegenerative disorders known as tauopathies. Tau aggregates take on …

Mutant p53 aggregates into prion-like amyloid oligomers and fibrils: implications for cancer

APDA Bom, LP Rangel, DCF Costa… - Journal of Biological …, 2012 - ASBMB
Over 50% of all human cancers lose p53 function. To evaluate the role of aggregation in
cancer, we asked whether wild-type (WT) p53 and the hot-spot mutant R248Q could …

Nanofibrils of food‐grade proteins: Formation mechanism, delivery systems, and application evaluation

D An, Q Ban, H Du, Q Wang, F Teng… - … Reviews in Food …, 2022 - Wiley Online Library
Due to the high aspect ratio, appealing mechanical characteristics, and various adjustable
functional groups on the surface proteins, food‐grade protein nanofibrils have attracted …

Lysozyme: a model protein for amyloid research

R Swaminathan, VK Ravi, S Kumar, MVS Kumar… - Advances in protein …, 2011 - Elsevier
Ever since lysozyme was discovered by Fleming in 1922, this protein has emerged as a
model for investigations on protein structure and function. Over the years, several high …

Rational design of amyloid‐like fibrillary structures for tailoring food protein techno‐functionality and their potential health implications

KJA Jansens, I Rombouts, C Grootaert… - … Reviews in Food …, 2019 - Wiley Online Library
To control and enhance protein functionality is a major challenge for food scientists. In this
context, research on food protein fibril formation, especially amyloid fibril formation, holds …

Extracellular vesicles derived from human Wharton's jelly mesenchymal stem cells protect hippocampal neurons from oxidative stress and synapse damage induced …

V Bodart-Santos, LRP de Carvalho… - Stem cell research & …, 2019 - Springer
Abstract Background Mesenchymal stem cells (MSCs) have been explored as promising
tools for treatment of several neurological and neurodegenerative diseases. MSCs release …