Skip to search formSkip to main contentSkip to account menu
Alzheimer's disease.
  • D. Selkoe
  • Biology
    Cold Spring Harbor perspectives in biology
  • 2011
TLDR
It is discussed how elucidating the genotype-to-phenotype relationships of familial forms of Alzheimer's disease has highlighted the importance of the misfolding and altered proteostasis of two otherwise soluble proteins, amyloid β-protein and tau, suggesting mechanism-based therapeutic targets that have led to clinical trials.
View on PubMed
The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics
TLDR
It has been more than 10 years since it was first proposed that the neurodegeneration in Alzheimer's disease (AD) may be caused by deposition of amyloid β-peptide in plaques in brain tissue and the rest of the disease process is proposed to result from an imbalance between Aβ production and Aβ clearance.
View on Publisher
Alzheimer's disease: genes, proteins, and therapy.
  • D. Selkoe
  • Biology
    Physiological reviews
  • 1 April 2001
TLDR
Evidence that the presenilin proteins, mutations in which cause the most aggressive form of inherited AD, lead to altered intramembranous cleavage of the beta-amyloid precursor protein by the protease called gamma-secretase has spurred progress toward novel therapeutics and provided discrete biochemical targets for drug screening and development.
View on PubMed
Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
TLDR
It is reported that natural oligomers of human Aβ are formed soon after generation of the peptide within specific intracellular vesicles and are subsequently secreted from the cell, indicating that synaptotoxic Aβ oligomers can be targeted therapeutically.
View on Nature
Alzheimer's Disease Is a Synaptic Failure
  • D. Selkoe
  • Biology, Psychology
    Science
  • 25 October 2002
TLDR
Mounting evidence suggests that this syndrome begins with subtle alterations of hippocampal synaptic efficacy prior to frank neuronal degeneration, and that the synaptic dysfunction is caused by diffusible oligomeric assemblies of the amyloid β protein.
View on Publisher
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
TLDR
Findings in other neurodegenerative diseases indicate that a broadly similar process of neuronal dysfunction is induced by diffusible oligomers of misfolded proteins.
View on Nature
The amyloid hypothesis of Alzheimer's disease at 25 years
TLDR
Although many factors contribute to AD pathogenesis, Aβ dyshomeostasis has emerged as the most extensively validated and compelling therapeutic target.
View on Wiley
Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
TLDR
It is concluded that soluble Aβ oligomers extracted from Alzheimer's disease brains potently impair synapse structure and function and that dimers are the smallest synaptotoxic species.
View on Nature
Natural Oligomers of the Alzheimer Amyloid-β Protein Induce Reversible Synapse Loss by Modulating an NMDA-Type Glutamate Receptor-Dependent Signaling Pathway
TLDR
It is concluded that soluble, low-n oligomers of human Aβ trigger synapse loss that can be reversed by therapeutic agents and provides a quantitative cellular model for elucidating the molecular basis of Aβ-induced neuronal dysfunction.
View on Publisher
Advancing research diagnostic criteria for Alzheimer's disease: the IWG-2 criteria
View on Elsevier
...
...
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy, Terms of Service, and Dataset License