Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

By Christian Haass, D. Selkoe. Nature reviews. Molecular cell biology, 2007

4,838 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/c7b9e9bbfb36934ec30641cabda76671b447ab9e

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Citations in the corpus

TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration (2009, background): “However, whether protein aggregates are themselves toxic, or instead play a protective role by helping to sequester smaller toxic protein species (such as soluble oligomers) continues to be a matter of intense investigation (29).”
Inflammation, Defective Insulin Signaling, and Mitochondrial Dysfunction as Common Molecular Denominators Connecting Type 2 Diabetes to Alzheimer Disease (2014, background): “Klein’s discovery, confirmed and expanded by several groups, led to a novel hypothesis on how AD progression leads to dementia: synapse failure and neuronal dysfunction are now considered to derive from the accumulation and impact of AbOs in AD brains (41,42,50).”
EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity (2010, background): “Recent studies indicate that small Aβ42 aggregates such as oligomers or protofibrils rather than long mature amyloid fibrils cause memory dysfunction in AD (24).”
Modeling Alzheimer's disease with iPSCs reveals stress phenotypes associated with intracellular Aβ and differential drug responsiveness. (2013, background): “Cognitive impairment observed in clinical AD is inversely well correlated with the amount of Aβ oligomers in the soluble fraction, rather than the amount of Aβ fibrils (amyloid plaques) constituting them Revised manuscript 4 (Haass and Selkoe, 2007; Krafft et al., 2010).”
Protection of synapses against Alzheimer's-linked toxins: Insulin signaling prevents the pathogenic binding of Aβ oligomers (2009, background): “This effect is particularly salient given the relevance of synaptotoxic A oligomers to AD memory impairment (7, 8).”
An anti-diabetes agent protects the mouse brain from defective insulin signaling caused by Alzheimer's disease- associated Aβ oligomers. (2012, neutral): “A β oligomers (A β Os) are small, diffus-ible aggregates that accumulate in AD brain and are recognized as potent synaptotoxins (10–12).”
The amyloid state and its association with protein misfolding diseases (2014, background): “Paired betasheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy.”
Aβ Oligomers Cause Localized Ca2+ Elevation, Missorting of Endogenous Tau into Dendrites, Tau Phosphorylation, and Destruction of Microtubules and Spines (2010, background): “Despite numerous studies on the pathway of APP misprocessing and its consequences for neurons the modes of A toxicity have remained enigmatic (Haass and Selkoe, 2007; Small and Duff, 2008).”
apoE isoform-specific disruption of amyloid beta peptide clearance from mouse brain. (2008, background): “Clearance of Alzheimer’s amyloid β(1-40)-peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier.”