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Phys Biol. 2020 Jan 8. doi: 10.1088/1478-3975/ab694e. [Epub ahead of print]

Advanced fluorescence imaging of in situ protein aggregation.

Author information

1
University of Cambridge, Cambridge, CB3 0AS, UNITED KINGDOM OF GREAT BRITAIN AND NORTHERN IRELAND.
2
Department of Chemical Engineering and Biotechnology, University of Cambridge, Pembroke Street, Cambridge, CB2 3RA, Cambridge, UNITED KINGDOM OF GREAT BRITAIN AND NORTHERN IRELAND.
3
University of Cambridge, Cambridge, Cambridgeshire, UNITED KINGDOM OF GREAT BRITAIN AND NORTHERN IRELAND.

Abstract

The aggregation of intrinsically disordered proteins is a hallmark of neurodegenerative diseases, such as Alzheimer's, Parkinson's and Huntington's disease. Although we currently have a good molecular level understanding on how protein aggregation occurs in vitro, the details of its self-assembly in live cells are still mainly unknown. During the last ten years, we have witnessed the rapid development of advanced imaging techniques, especially super-resolution and fluorescence lifetime-based microscopy, in different areas of cell biology. These methods have been revolutionising our understanding on how proteins aggregate, providing unprecedented high spatial-temporal resolution which permit to capture the kinetics of aggregate seeding and expansion, the motion and distribution of individual aggregates within the cells, and its structural change. In this article, we will review the study of in situ protein aggregation using advanced imaging techniques, with the focus on protein aggregate structure and its assembly dynamics.

KEYWORDS:

advanced imaging; neurodegenerative diseases; protein aggregation; structural progression; super-resolution microscopy

PMID:
31914432
DOI:
10.1088/1478-3975/ab694e

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