The coexistence of an equal amount of Alzheimer's amyloid-β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathway
Published 2014 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
The coexistence of an equal amount of Alzheimer's amyloid-β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathway
Authors
Keywords
-
Journal
FEBS Journal
Volume 281, Issue 11, Pages 2674-2687
Publisher
Wiley
Online
2014-04-11
DOI
10.1111/febs.12813
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Structural Basis for Increased Toxicity of Pathological Aβ42:Aβ40Ratios in Alzheimer Disease
- (2011) Kris Pauwels et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Two Distinct Amyloid β-Protein (Aβ) Assembly Pathways Leading to Oligomers and Fibrils Identified by Combined Fluorescence Correlation Spectroscopy, Morphology, and Toxicity Analyses
- (2011) Satoko Matsumura et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Soluble amyloid -protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration
- (2011) M. Jin et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Mass spectrometric characterization of brain amyloid beta isoform signatures in familial and sporadic Alzheimer’s disease
- (2010) Erik Portelius et al. ACTA NEUROPATHOLOGICA
- Amyloid β oligomers induce Ca2+ dysregulation and neuronal death through activation of ionotropic glutamate receptors
- (2010) Elena Alberdi et al. CELL CALCIUM
- Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio
- (2010) Inna Kuperstein et al. EMBO JOURNAL
- Amyloid -Protein Dimers Rapidly Form Stable Synaptotoxic Protofibrils
- (2010) B. O'Nuallain et al. JOURNAL OF NEUROSCIENCE
- Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
- (2010) Mahiuddin Ahmed et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Review: Sporadic cerebral amyloid angiopathy
- (2010) J. Attems et al. NEUROPATHOLOGY AND APPLIED NEUROBIOLOGY
- Alzheimer's Disease
- (2010) Henry W. Querfurth et al. NEW ENGLAND JOURNAL OF MEDICINE
- Structural Characterization of a Soluble Amyloid β-Peptide Oligomer
- (2009) Liping Yu et al. BIOCHEMISTRY
- Isolation and Characterization of Patient-derived, Toxic, High Mass Amyloid β-Protein (Aβ) Assembly from Alzheimer Disease Brains
- (2009) Akihiko Noguchi et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Fibrillar Oligomers Nucleate the Oligomerization of Monomeric Amyloid β but Do Not Seed Fibril Formation
- (2009) Jessica W. Wu et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Amyloid β Protein: Aβ40 Inhibits Aβ42 Oligomerization
- (2009) Megan M. Murray et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
- (2009) Summer L. Bernstein et al. Nature Chemistry
- Structure-neurotoxicity relationships of amyloid -protein oligomers
- (2009) K. Ono et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Quartz crystal microbalance analysis of growth kinetics for aggregation intermediates of the amyloid-β protein
- (2008) Joseph A. Kotarek et al. ANALYTICAL BIOCHEMISTRY
- Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior
- (2008) Dennis J. Selkoe BEHAVIOURAL BRAIN RESEARCH
- The Ratio of Monomeric to Aggregated Forms of Aβ40 and Aβ42 Is an Important Determinant of Amyloid-β Aggregation, Fibrillogenesis, and Toxicity
- (2008) Asad Jan et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Amyloid β-Protein Assembly and Alzheimer Disease
- (2008) Robin Roychaudhuri et al. JOURNAL OF BIOLOGICAL CHEMISTRY
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExploreBecome a Peeref-certified reviewer
The Peeref Institute provides free reviewer training that teaches the core competencies of the academic peer review process.
Get Started