2020
DOI: 10.1021/scimeetings.0c05922
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Use solid state nmr to characterize the structure of aβ1-42 150-kDa oligomers: Anti-parallel β-sheet and a special parallel β-sheet

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“…Aβ and αS oligomers of biological or synthetic origins range from dimers to ~200 mers (Breydo and Uversky, 2015) and display different morphologies, such as globular and protofibrillar shapes (Chen et al, 2015). While many Aβ and αS oligomers possess well-defined secondary structures, usually β-sheets, others are structurally disordered (Breydo and Uversky, 2015;Gao et al, 2020). Moreover, amyloid oligomers can be either on-pathway intermediates of fibrillization or off-pathway end products (Breydo and Uversky, 2015), differing in seeding ability.…”
Section: Additional Complexitymentioning
confidence: 99%
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“…Aβ and αS oligomers of biological or synthetic origins range from dimers to ~200 mers (Breydo and Uversky, 2015) and display different morphologies, such as globular and protofibrillar shapes (Chen et al, 2015). While many Aβ and αS oligomers possess well-defined secondary structures, usually β-sheets, others are structurally disordered (Breydo and Uversky, 2015;Gao et al, 2020). Moreover, amyloid oligomers can be either on-pathway intermediates of fibrillization or off-pathway end products (Breydo and Uversky, 2015), differing in seeding ability.…”
Section: Additional Complexitymentioning
confidence: 99%
“…The hydrophobic sequences of Aβ (e.g., Aβ17-21 and the C-terminus; Figure 1A) promote Aβ aggregation (Bolognesi et al, 2010;Hu et al, 2012). Aβ aggregation involves three distinct conformers (Figure 1B): monomeric Aβ spontaneously self-assembles into soluble oligomeric Aβ (Gao et al, 2020;Xiao et al, 2020), which then aggregates further to form insoluble fibrillar Aβ (Petkova et al, 2002; Luhrs et al, 2005). The primary toxic agents in AD are oligomeric rather than monomeric or fibrillar Aβ (Kayed et al, 2003;Aguzzi and O'Connor, 2010).…”
mentioning
confidence: 99%