The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation

By C. Nilsberth, A. Westlind‐Danielsson, C. Eckman, M. Condron, K. Axelman, C. Forsell, C. Stenh, J. Luthman, David B. Teplow, S. Younkin and 2 more. Nature Neuroscience, 2001

1,244 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/f3ee07fdb5ac9b57c94b61abfc8c3f7769bf7197

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Citations in the corpus

Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. (2011, background): “The latter was included because it is known to populate higher levels of prefibrillar aggregates and toxic oligomers exposing hydrophobic surfaces (Bolognesi et al., 2010; Nilsberth et al., 2001).”
Alzheimer’s Disease: The Challenge of the Second Century (2011, background): “These mutations are C-terminal to the a-secretase cleavage site in APP and change the sequence of Ab such that it increases the propensity of Ab to oligomerize, fibrillize, or be cleared less effectively (66, 67, 76).”
Genetics of Alzheimer's Disease (2013, background): “Here we review the known genetics of early- and late-onset Alzheimer’s disease.”
Trafficking and proteolytic processing of APP. (2012, background): “Mutations in the mid region, such as the Arctic (Nilsberth et al. 2001) and Dutch mutations (Levy et al.”
Aβ Oligomers – a decade of discovery (2007, background): “…clustered around the central hydrophobic core of Ab and cause an increase in steady state levels of Ab and/or an increased propensity of the mutant peptide to aggregate (Wisniewski et al. 1991; De Jonghe et al. 1998; Nilsberth et al. 2001; Van Nostrand et al. 2001; Betts et al. unpublished data).”
Neurovascular mechanisms and blood–brain barrier disorder in Alzheimer’s disease (2009, background): “Alternatively, mutations in the Ab portion of APP, such as the Dutch (E693Q) [88], Iowa (D694N) [34], Flemish (A692G) [39], Arctic (E693G) [62] and Italian (E693K) [82], all lead to vasculotropic Ab peptides that may cause cerebral hemorrhage without any evidence of increased APP processing.”
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, neutral): “Nevertheless, all nine mutations are expected on theoretical grounds to increase the aggregation rate of the intrinsically disordered Aβ peptides, and for a number of them the predictions have been verified experimentally (54, 58, 59).”