@article{
 title = {Probing amyloid protein aggregation with optical superresolution methods : from the test tube to models of disease},
 type = {article},
 year = {2016},
 identifiers = {[object Object]},
 keywords = {amyloids,neurodegeneration,review,superresolution},
 pages = {041807},
 volume = {3},
 id = {221e63df-a106-32b8-a73c-14b2a93d6a19},
 created = {2016-06-29T09:31:24.000Z},
 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 = {true},
 hidden = {false},
 abstract = {The misfolding and self-assembly of intrinsically disordered proteins into insoluble amyloid structures are central to many neurodegenerative diseases such as Alzheimer’s and Parkinson’s diseases. Optical imaging of this self-assembly process in vitro and in cells is revolutionizing our understanding of the molecular mech- anisms behind these devastating conditions. In contrast to conventional biophysical methods, optical imaging and, in particular, optical superresolution imaging, permits the dynamic investigation of the molecular self- assembly process in vitro and in cells, at molecular-level resolution. In this article, current state-of-the-art imaging methods are reviewed and discussed in the context of research into neurodegeneration.},
 bibtype = {article},
 author = {Kaminski, Clemens F and Schierle, Gabriele S Kaminski},
 journal = {Neurophotonics},
 number = {4}
}

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