Results 51 to 60 of about 109,107 (305)

Investigation of low amyloid level toxicity effects on the function of hippocampal neurons

open access: yesOpen Life Sciences, 2015
Alzheimer disease (AD) is responsible for the majority of elderly dementia cases. There are multiple mouse models of AD, however, none of them completely recapitulate human pathology.
Popugaeva Elena   +4 more
doaj   +1 more source

Biomolecular studies in Alzheimer’s Disease models: investigations in vitro and in vivo

open access: yes, 2013
The Alzheimer’s disease (AD), the most prevalent form of age-related dementia, is a multifactorial and heterogeneous neurodegenerative disease. The molecular mechanisms underlying the pathogenesis of AD are yet largely unknown.
Lattanzio, Francesca <1982>
core   +1 more source

Characterization of amyloid-ß and other proteins related to Alzheimer's disease, their role in neurodegeneration and biomarker discovery [PDF]

open access: yes, 2006
Studies were performed to identify factors explaining the difference in the neurodegeneration seen in Alzheimer’s disease (AD) and in transgenic mice.
Güntert, Andreas
core   +1 more source

Estudo bioquímico e comportamental em camundongos submetidos à infusão intracerebroventricular dos peptídeos beta-amilóide AB1-40 E AB25-35 e o papel neuroprotetor da atorvastatina [PDF]

open access: yes, 2009
Dissertação (mestrado) - Universidade Federal de Santa Catarina. Centro de Ciências Biológicas. Programa de Pós-Graduação em Neurociências.The accumulation and aggregation of beta-amyloid peptide (Aâ) in brain of patients with Alzheimer's disease results
Piermartiri, Tetsade Camboim Bizerra
core  

Pro-domain removal in ASP-2 and the cleavage of the amyloid precursor are influenced by pH.

open access: yes, 2002
BACKGROUND: One of the signatures of Alzheimer's disease is the accumulation of aggregated amyloid protein, Abeta, in the brain. Abeta arises from cleavage of the Amyloid Precursor protein by beta and gamma secretases, which present attractive candidates
Brian Austen   +5 more
core   +1 more source

Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly [PDF]

open access: yes, 2008
Self-assembly of misfolded proteins into ordered fibrillar aggregates known as amyloid results in numerous human diseases. Despite an increasing number of proteins and peptide fragments being recognised as amyloidogenic, how these amyloid aggregates ...
Xue, Wei-Feng   +2 more
core   +1 more source

Multifunctional Gold Nanocluster‐Based PROTAC System for Targeted Degradation of Phosphorylated Tau and Modulation of Neuroinflammation in Alzheimer's Disease

open access: yesAdvanced Functional Materials, EarlyView.
We present a novel proteolysis‐targeting chimera (PROTAC) system conjugated to lipoic acid gold nanoclusters (PLANC), designed to degrade pTau, regulate inflammatory signaling, and effectively traverse the blood‐brain barrier (BBB). PLANC degraded pTau at various phosphorylation sites, with mechanistic studies confirming proteasome‐mediated degradation
Sarah Nevins   +9 more
wiley   +1 more source

Oxidative stress and the amyloid beta peptide in Alzheimer’s disease

open access: yesRedox Biology, 2018
Oxidative stress is known to play an important role in the pathogenesis of a number of diseases. In particular, it is linked to the etiology of Alzheimer's disease (AD), an age-related neurodegenerative disease and the most common cause of dementia in the elderly.
Cheignon, Clémence   +5 more
openaire   +4 more sources

Abeta(1-42) induces abnormal alternative splicing of tau exons 2/3 in NGF-induced PC12 cells

open access: yesAnais da Academia Brasileira de Ciências, 2014
Protein tau plays a pivotal role in the pathophysiology of Alzheimer's disease, where its hyperphos-phorylation promotes aggregation and microtubule destabilization.
TERESA LAGUNES   +3 more
doaj   +1 more source

The interaction of amyloid-β peptide with lipid membranes and glycosaminoglycans [PDF]

open access: yes, 2012
The aim of the thesis is a better understanding of the thermodynamics and structural aspects of the interaction of Aβ(1-40) with lipid membranes and glycosaminoglycans (GAGs).
Müller, Christian Thomas Benedikt
core   +1 more source

Home - About - Disclaimer - Privacy