Probing amyloid protein aggregation with optical superresolution methods: from the test tube to models of disease

Clemens F. Kaminski; Gabriele S. Kaminski Schierle

doi:10.1117/1.NPh.3.4.041807

29 June 2016 Probing amyloid protein aggregation with optical superresolution methods: from the test tube to models of disease

Clemens F. Kaminski, Gabriele S. Kaminski Schierle

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Neurophotonics, Vol. 3, Issue 4, 041807 (June 2016). https://doi.org/10.1117/1.NPh.3.4.041807

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 mechanisms 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.

CC BY: © The Authors. Published by SPIE under a Creative Commons Attribution 4.0 Unported License. Distribution or reproduction of this work in whole or in part requires full attribution of the original publication, including its DOI.

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Clemens F. Kaminski and Gabriele S. Kaminski Schierle "Probing amyloid protein aggregation with optical superresolution methods: from the test tube to models of disease," Neurophotonics 3(4), 041807 (29 June 2016). https://doi.org/10.1117/1.NPh.3.4.041807

Published: 29 June 2016

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