2006
DOI: 10.1016/j.bpc.2005.09.015
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Quantitative determination of the topological propensities of amyloidogenic peptides

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Cited by 7 publications
(6 citation statements)
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“…More sophisticated and accurate schemes could be formulated by including structural effects or energetics derived from other experimental techniques (80). The approaches described above do not take into account interactions between b-sheet layers, which have been elucidated experimentally in Ab 1-40 fibrils (81) and GNNQQNY fibrils (30), but not in the fibrils discussed above.…”
Section: Theoretical Predictionsmentioning
confidence: 99%
“…More sophisticated and accurate schemes could be formulated by including structural effects or energetics derived from other experimental techniques (80). The approaches described above do not take into account interactions between b-sheet layers, which have been elucidated experimentally in Ab 1-40 fibrils (81) and GNNQQNY fibrils (30), but not in the fibrils discussed above.…”
Section: Theoretical Predictionsmentioning
confidence: 99%
“…(i) According to NMR studies, Aβ 14−23 fragment assumes parallel β-sheet topology when incorporated in the polymerizing Aβ [8], although inherently anti-parallel β sheet topology is preferred for this fragment. In a study reported by Shi et al [120], the FRET method was used in exploration of the mentioned topology shift that occurs on the Aβ 14−23 fragment when incorporated in longer fragments. Aβ 14−23 fragment is referring to a fragment of Aβ between amino acids 14 and 23.…”
Section: Single Molecule Fluorescence Microscopymentioning
confidence: 99%
“…In the studies of Shi et al FRET was also used to reveal the role of specific amino acids in the aggregation of Aβ. This knowledge could help with the Aβ anti-aggregation drug discoveries [120]. (ii) The FRET technique, in combination with a double immunofluorescence approach, was used by Kinoshita et al in order to investigate the subcellular localization of AβPP and its interactions with human AβPP cleaving enzyme (known as β-secretase, or BACE) [60].…”
Section: Single Molecule Fluorescence Microscopymentioning
confidence: 99%
“…
Nanofibers and nanorods have been encountered in natural biological systems, primarily amyloid peptides and proteins, [1][2][3][4][5][6] but have been also produced through diverse synthetic routes employing metals and semiconductors, [7,8] organic [9,10] and inorganic substances. [11] In general, two fundamental aspects govern nanostructure formation and morphology.
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mentioning
confidence: 99%