Intraneuronal Aβ42 Accumulation in Human Brain

By Gunnar K. Gouras, J. Tsai, J. Näslund, B. Vincent, M. Edgar, F. Checler, J. Greenfield, V. Haroutunian, Joseph D. Buxbaum, Huaxi Xu and 2 more. 2000

907 citations recorded by the source corpus.

Subfields: Cell Biology, Cellular and Molecular Neuroscience, Physiology

View Paper: https://www.semanticscholar.org/paper/03a83b99a0eb1f384bfdb5f49c84e51b2317fcb6

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Citations in the corpus

Protein aggregation diseases: pathogenicity and therapeutic perspectives (2010, background): “Also, intracellular Aβ occurs most frequently in the hippocampus and entorhinal cortex (ERC), which are the brain regions to be affected first in Alzheimer's diseas”
Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease (2005, background): “predominately Aβ(1-42) (2–3), have been demonstrated to include the ER, multivesicular bodies, and the endosomal/lysosomal system (4, 7–10).”
Amyloid Precursor Protein Processing and Alzheimer’s Disease (2011, background): “…had suggested that significant amounts of APP were processed to Aβ intracellularly (Greenfield et al. 1999), and evidence provides support for BACE1 in the TGN (Huse et al. 2002) and for intracellular Aβ accumulation in neurons from patients with early AD (Gouras et al 2000; LaFerla et al 2007).”
Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases (2004, background): “It has been postulated that a portion of any Aβ peptides generated early in the secretory pathway (particularly Aβ42) remains inside the cell, and these could contribute to intracellular Aβ accumulation, which has been documented in neurons in culture and in the Alzheimer brai”
Autophagy, amyloidogenesis and Alzheimer disease (2007, background): “MVBs and late endosomes are relatively rich in APP and APP secretases, and those in AD brain and mouse models of AD contain A peptide (Gouras et al., 2000; Takahashi et al., 2002).”
Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation (2006, background): “, 2004), Down’s syndrome (DS) (Gouras et al., 2000; Gyure et al., 2001; Busciglio et al., 2002; Mori et al., 2002; Cataldo et al., 2004), and AD mouse models (Takahashi et al.”
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation (2001, background): “Interaction between Aβ(1-42) and Aβ(1-40) in Alzheimer’s β-amyloid fibril formation in vitro.”
Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers (2004, background): “Although A 1– 42 has been reported to accumulate intracellularly in AD and in transgenic mouse models of AD (Gouras et al., 2000; Oddo et al., 2003), ADDL immunoreactivity on neurons was exclusively at cell surfaces, even after permeabilization.”
Intraneuronal Aβ Causes the Onset of Early Alzheimer’s Disease-Related Cognitive Deficits in Transgenic Mice (2005, positive): “found Aβ42 staining within hippocampal pyramidal neurons of individuals with clinical diagnoses ranging from MCI to severe cognitive impairment as determined by the Clinical Dementia Rating Scale (Gouras et al., 2000), indicating that intraneuronal Aβ accumulation is an early event in humans with AD”