Aggregation of amyloid-β (Aβ) peptides is fundamental to Alzheimer's disease. It has now been shown that nucleated proliferation of Aβ fibrils utilizes a secondary mechanism with existing fibrils catalyzing the formation of new ones. Here it is shown that the data for Aβ40 and Aβ42 require that the nuclei be monomeric; that is, an initial, unfavorable conformational change is rate limiting for the processes that appear to be nucleation. Following the conformational change, the assembly process is "downhill" despite clear lag times and significant concentration dependence. The similarity to polyglutamine nucleation suggests that monomeric nuclei may be widespread in amyloid formation.
This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 20 March 2015.
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#22,759,452
of 25,374,647 outputs
Outputs from Journal of Molecular Biology
#11,577
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#230,017
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Outputs of similar age from Journal of Molecular Biology
#46
of 56 outputs
Altmetric has tracked 25,374,647 research outputs across all sources so far. This one is in the 1st percentile – i.e., 1% of other outputs scored the same or lower than it.
So far Altmetric has tracked 11,921 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 5.6. This one is in the 1st percentile – i.e., 1% of its peers scored the same or lower than it.
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