2006
DOI: 10.1016/j.jmb.2006.05.033
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Interpreting the Aggregation Kinetics of Amyloid Peptides

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Cited by 242 publications
(295 citation statements)
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“…3). A similar heterogeneity has been described previously for in vitro fibrillation reactions as well (24,25), or molecular dynamics simulations (26). Such heterogeneity may arise from the stochastic nature of the nucleation reaction or from the formation of differently structured nuclei.…”
Section: Resultssupporting
confidence: 66%
“…3). A similar heterogeneity has been described previously for in vitro fibrillation reactions as well (24,25), or molecular dynamics simulations (26). Such heterogeneity may arise from the stochastic nature of the nucleation reaction or from the formation of differently structured nuclei.…”
Section: Resultssupporting
confidence: 66%
“…The driving forces and the mechanistic details of aggregation of blobsized peptides are similar to those of small molecules. This distinction is important in light of several experimental and computational studies, which focus on the aggregation of short peptides [34][35][36][37][38][39]. Here, we discuss the physical principles of polymer aggregation that are relevant to proteins with multiple segments of length g T .…”
Section: Distinction Between Aggregation Of Short Peptides and Full-lmentioning
confidence: 99%
“…So far, the results we presented only involve the singlefibril case, which tries to mimic heterogeneous nucleation on a specific number of preset heterogeneous seeds ͑e.g., heterogeneous nucleation of A␤ [26][27][28][29][30][31][32][33][34][35][36][37][38][39][40] on A␤ [26][27][28][29][30][31][32][33][34][35][36][37][38][39][40][41][42][43] , 17 where homogeneous nucleation of A␤ [26][27][28][29][30][31][32][33][34][35][36][37][38][39][40] is unable to occur under the same conditions͒. When homogeneous nucleation occurs and an unspecific number of multiple...…”
Section: B Multiple Fibrilsmentioning
confidence: 99%
“…In a more recent off-lattice Langevin dynamics simulation, 41 self-assembly and chirality of the fibrillar aggregates from ␤ sheet forming short peptides were studied based on a coarse-grained united atom model. The influence 42 of intermediate states and reversibility of the polymerization process were addressed and it was shown 43 that the propensity of intermediates depends on the relative stability of ␤ prone conformational state. In contrast to these simulation models, our attempt here is to probe the later stages of nucleation of fibrils and their competitive growth.…”
Section: Introductionmentioning
confidence: 99%