Results 21 to 30 of about 85,510 (321)

Decreased Deposition of Beta-Amyloid 1-38 and Increased Deposition of Beta-Amyloid 1-42 in Brain Tissue of Presenilin-1 E280A Familial Alzheimer’s Disease Patients

open access: yesFrontiers in Aging Neuroscience, 2020
Familial Alzheimer’s Disease (FAD) caused by Presenilin-1 (PS1) mutations is characterized by early onset, cognitive impairment, and dementia. Impaired gamma secretase function favors production of longer beta-amyloid species in PS1 FAD.
Felix Dinkel   +7 more
doaj   +1 more source

Insight into the structure of amyloid fibrils from the analysis of globular proteins. [PDF]

open access: yesPLoS Computational Biology, 2006
The conversion from soluble states into cross-beta fibrillar aggregates is a property shared by many different proteins and peptides and was hence conjectured to be a generic feature of polypeptide chains.
Antonio Trovato   +3 more
doaj   +1 more source

Oligomerization of amyloid Abeta peptides using hydrogen bonds and hydrophobicity forces [PDF]

open access: yes, 2004
The 16-22 amino acid fragment of the beta-amyloid peptide associated with the Alzheimer's disease, Abeta, is capable of forming amyloid fibrils. Here we study the aggregation mechanism of Abeta(16-22) peptides by unbiased thermodynamic simulations at the
Anders Irbäck   +48 more
core   +3 more sources

Contributions of Mass Spectrometry to the Identification of Low Molecular Weight Molecules Able to Reduce the Toxicity of Amyloid-β Peptide to Cell Cultures and Transgenic Mouse Models of Alzheimer’s Disease

open access: yesMolecules, 2019
Alzheimer’s Disease affects approximately 33 million people worldwide and is characterized by progressive loss of memory at the cognitive level. The formation of toxic amyloid oligomers, extracellular amyloid plaques and amyloid angiopathy in brain
Raluca Ştefănescu   +5 more
doaj   +1 more source

Fibrillisation of hydrophobically modified amyloid peptide fragments in an organic solvent [PDF]

open access: yes, 2007
The self-assembly of a hydrophobically modified fragment of the amyloid beta(A beta) peptide has been studied in methanol. The peptide FFKLVFF is based on A beta(16-20) extended at the N terminus by two phenylalanine residues.
Castelletto, Valeria   +2 more
core   +1 more source

Naturally occurring autoantibodies against beta-amyloid: investigating their role in transgenic animal and in vitro models of Alzheimer's disease [PDF]

open access: yes, 2011
Alzheimer's disease (AD) is a neurodegenerative disorder primarily affecting regions of the brain responsible for higher cognitive functions. Immunization against β-amyloid (Aβ) in animal models of AD has been shown to be effective on the molecular level
Al-Abed, Yousef   +13 more
core   +1 more source

Alzheimer’s Disease as a Membrane Disorder: Spatial Cross-Talk Among Beta-Amyloid Peptides, Nicotinic Acetylcholine Receptors and Lipid Rafts [PDF]

open access: yes, 2019
Biological membranes show lateral and transverse asymmetric lipid distribution. Cholesterol (Chol) localizes in both hemilayers, but in the external one it is mostly condensed in lipid-ordered microdomains (raft domains), together with saturated ...
Antollini, Silvia Susana   +1 more
core   +1 more source

Mechanisms of amyloid-β34 generation indicate a pivotal role for BACE1 in amyloid homeostasis

open access: yesScientific Reports, 2023
The beta‑site amyloid precursor protein (APP) cleaving enzyme (BACE1) was discovered due to its “amyloidogenic” activity which contributes to the production of amyloid-beta (Aβ) peptides. However, BACE1 also possesses an “amyloidolytic” activity, whereby
Irem Ulku   +10 more
doaj   +1 more source

Analyzing Amyloid Beta Aggregates with a Combinatorial Fluorescent Molecular Sensor

open access: yesProceedings, 2017
The self-assembly of amyloid beta (Aβ) peptides into insoluble aggregates is thought to play a [...]
Joydev Hatai   +2 more
doaj   +1 more source

A Condensation-Ordering Mechanism in Nanoparticle-Catalyzed Peptide Aggregation [PDF]

open access: yes, 2009
Nanoparticles introduced in living cells are capable of strongly promoting the aggregation of peptides and proteins. We use here molecular dynamics simulations to characterise in detail the process by which nanoparticle surfaces catalyse the self ...
A Aggeli   +62 more
core   +5 more sources

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