Results 111 to 120 of about 76,126 (160)

Electrochemistry of Alzheimer Disease Amyloid Beta Peptides

Current Medicinal Chemistry, 2018
Alzheimer’s disease (AD) is a widespread form of dementia that is estimated to affect 44.4 million people worldwide. AD pathology is closely related to the accumulation of amyloid beta (Aβ) peptides in fibrils and plagues, the small oligomeric intermediate species formed during the Aβ peptides aggregation presenting the highest neurotoxicity ...
Teodor Adrian Enache, Ana Maria Oliveira-Brett   +1 more
exaly   +3 more sources

Neprilysin and Amyloid Beta Peptide Degradation

Current Alzheimer Research, 2008
Neprilysin is a zinc metalloendopeptidase with relatively broad substrate specificity. The enzyme is localized to the plasma membrane of cells where it can function to degrade extracellular peptides. Structural studies show that neprilysin preferentially cleaves peptides on the amino side of hydrophobic amino acids.
Louis B, Hersh, David W, Rodgers
openaire   +2 more sources

Cholesterol Trafficking and Amyloid Beta Peptides

Pharmacopsychiatry, 2003
Currently, there is much interest in the association between cholesterol and Alzheimer's disease. An especially important aspect of this association is the relationship between amyloid beta-peptide (Abeta) and cholesterol that can be described as a reciprocal process.
W G, Wood, U, Igbavboa
openaire   +2 more sources

Alzheimer's Disease and the Amyloid-β Peptide [PDF]

Journal of Alzheimer's Disease, 2010
Alzheimer's disease (AD) pathogenesis is widely believed to be driven by the production and deposition of the amyloid-β peptide (Aβ). For many years, investigators have been puzzled by the weak to nonexistent correlation between the amount of neuritic plaque pathology in the human brain and the degree of clinical dementia.
Murphy M. Paul, LeVine, III Harry
openaire   +2 more sources

Amyloid beta peptide immunotherapy in Alzheimer disease

Revue Neurologique, 2014
Recent advances in the understanding of Alzheimer's disease pathogenesis have led to the development of numerous compounds that might modify the disease process. Amyloid β peptide represents an important molecular target for intervention in Alzheimer's disease.
J, Delrieu, P J, Ousset, T, Voisin, B, Vellas   +3 more
openaire   +2 more sources

Amyloid beta peptides electrochemistry: A review

Current Opinion in Electrochemistry, 2022
Abstract Alzheimer disease is a progressive age-related neurodegenerative disorder estimated to affect up to 107 million people by 2050, its pathology is associated with the dysfunction of the amyloid beta (Aβ) peptide mechanism, among others. Electrochemical methods were successfully applied for Aβ electrochemical characterisation and have received ...
Ana-Maria Chiorcea-Paquim, Ana Maria Oliveira-Brett   +1 more
openaire   +1 more source

Diversity of amyloid beta peptide actions

Reviews in the Neurosciences
Abstract Fibril formation by amyloidogenic proteins and peptides is considered the cause of a number of incurable diseases. One of the most known amyloid diseases is Alzheimer’s disease (AD). Traditionally, amyloidogenic beta peptides Aβ40 and Aβ42 (Aβs) are considered as main causes of AD and the foremost targets in AD fight.
Sona Mardanyan, Svetlana Sharoyan, Alvard Antonyan   +2 more
openaire   +2 more sources

In vitroOligomerization and Fibrillogenesis of Amyloid-beta Peptides

2012
The amyloid beta Ab(1-40) and Ab(1-42) peptides are the main components of the fibrillar plaques characteristically found in the brains affected by Alzheimer's disease. Fibril formation has been thoroughly studied in vitro using synthetic amyloid peptides and has been described to be a nucleation dependent polymerization process.
Núria, Benseny-Cases, Oksana, Klementieva, Josep, Cladera   +2 more
openaire   +2 more sources

Interfacial Effects on the Conformation of Amyloid-Beta Peptide

Protein & Peptide Letters, 2009
We examined the effects of air-water and water-sevoflurane interfaces on conformational properties of amyloid-beta peptide (ABP). Fractions were extracted from sub-interfacial (air-water) and supra-interfacial (water-sevoflurane) layers and compared with aqueous bulk layers using fluorescence properties of ABP provided by a single tyrosine.
Norbert W, Seidler, Joshua D, Eklund
openaire   +2 more sources

Amyloid Beta Peptide Folding in Reverse Micelles

Journal of the American Chemical Society, 2017
Previously published experimental studies have suggested that when the 40-residue amyloid beta peptide is encapsulated in a reverse micelle, it folds into a structure that may nucleate amyloid fibril formation (Yeung, P. S.-W.; Axelsen, P. H. J. Am. Chem. Soc. 2012, 134, 6061 ).
Gözde Eskici, Paul H Axelsen
openaire   +2 more sources