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Nano-scale Infrared Imaging of β-sheet Structures in Synaptic Junctions of Primary Neurons Isolated from Transgenic Mice

Klementieva, O. LU orcid ; Mathurin, J. ; Engdahl, A. LU ; Freitas, R. ; Willen, K. LU ; Uvdal, P. LU ; Miller, L. M. and Gouras, G. LU orcid (2018) 43rd International Conference on Infrared Millimeter and Terahertz Waves, IRMMW-THz 2018 2018-September.
Abstract

Aβ is a class of aggregation-prone proteins, which may misfold into stable, β-sheet rich fibrils. Aβ is linked to the development of synaptic pathology in Alzheimer's disease (AD). However, a main question in the AD field is how Aβ contributes to AD neuropathology? Up to now there is little evidence for protein structural changes in diseased neuron. Our aim is to study the distribution of β-sheet structures in AD transgenic neurons in order to uncover sub-cellular mechanism(s) by which amyloid β-sheet structures are involved in AD pathology.

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author
; ; ; ; ; ; and
organization
publishing date
type
Chapter in Book/Report/Conference proceeding
publication status
published
subject
host publication
2018 43rd International Conference on Infrared Millimeter and Terahertz Waves, IRMMW-THz 2018
volume
2018-September
article number
8510376
publisher
IEEE Computer Society
conference name
43rd International Conference on Infrared Millimeter and Terahertz Waves, IRMMW-THz 2018
conference location
Nagoya, Japan
conference dates
2018-09-09 - 2018-09-14
external identifiers
  • scopus:85056832774
ISBN
9781538638095
DOI
10.1109/IRMMW-THz.2018.8510376
language
English
LU publication?
yes
id
ea7ecf85-7628-4f44-96ce-81a765c24107
date added to LUP
2018-11-29 14:19:41
date last changed
2022-05-03 08:24:51
@inproceedings{ea7ecf85-7628-4f44-96ce-81a765c24107,
  abstract     = {{<p>Aβ is a class of aggregation-prone proteins, which may misfold into stable, β-sheet rich fibrils. Aβ is linked to the development of synaptic pathology in Alzheimer's disease (AD). However, a main question in the AD field is how Aβ contributes to AD neuropathology? Up to now there is little evidence for protein structural changes in diseased neuron. Our aim is to study the distribution of β-sheet structures in AD transgenic neurons in order to uncover sub-cellular mechanism(s) by which amyloid β-sheet structures are involved in AD pathology.</p>}},
  author       = {{Klementieva, O. and Mathurin, J. and Engdahl, A. and Freitas, R. and Willen, K. and Uvdal, P. and Miller, L. M. and Gouras, G.}},
  booktitle    = {{2018 43rd International Conference on Infrared Millimeter and Terahertz Waves, IRMMW-THz 2018}},
  isbn         = {{9781538638095}},
  language     = {{eng}},
  month        = {{10}},
  publisher    = {{IEEE Computer Society}},
  title        = {{Nano-scale Infrared Imaging of β-sheet Structures in Synaptic Junctions of Primary Neurons Isolated from Transgenic Mice}},
  url          = {{http://dx.doi.org/10.1109/IRMMW-THz.2018.8510376}},
  doi          = {{10.1109/IRMMW-THz.2018.8510376}},
  volume       = {{2018-September}},
  year         = {{2018}},
}