@article{
 title = {Direct Observations of Amyloid β Self-Assembly in Live Cells Provide Insights into Differences in the Kinetics of Aβ(1-40) and Aβ(1-42) Aggregation},
 type = {article},
 year = {2014},
 identifiers = {[object Object]},
 pages = {732-742},
 volume = {21},
 websites = {http://dx.doi.org/10.1016/j.chembiol.2014.03.014},
 id = {820252d5-898d-3b5f-915e-06e1dd2f9236},
 created = {2016-04-27T11:42:58.000Z},
 accessed = {2016-04-18},
 file_attached = {true},
 profile_id = {9b1c14de-b75a-3e23-a406-ef006d6fed26},
 last_modified = {2017-03-25T02:42:51.878Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {false},
 hidden = {false},
 folder_uuids = {6e034f54-5623-437a-811f-80d304e37fd9},
 abstract = {SUMMARY Insight into how amyloid b (Ab) aggregation occurs in vivo is vital for understanding the molecular path-ways that underlie Alzheimer's disease and requires new techniques that provide detailed kinetic and mechanistic information. Using noninvasive fluores-cence lifetime recordings, we imaged the formation of Ab(1–40) and Ab(1–42) aggregates in live cells. For both peptides, the cellular uptake via endocy-tosis is rapid and spontaneous. They are then re-tained in lysosomes, where their accumulation leads to aggregation. The kinetics of Ab(1–42) aggregation are considerably faster than those of Ab(1–40) and, unlike those of the latter peptide, show no detectable lag phase. We used superresolution fluorescence im-aging to examine the resulting aggregates and could observe compact amyloid structures, likely because of spatial confinement within cellular compartments. Taken together, these findings provide clues as to how Ab aggregation may occur within neurons.},
 bibtype = {article},
 author = {Esbjörner, Elin K and Chan, Fiona and Rees, Eric and Erdelyi, Miklos and Luheshi, Leila M and Bertoncini, Carlos W and Kaminski, Clemens F and Dobson, Christopher M and Kaminski Schierle, Gabriele S},
 journal = {Chemistry & Biology}
}

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