Single-molecule imaging of individual amyloid protein aggregates in human biofluids

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Single-molecule imaging of individual amyloid protein aggregates in human biofluids. / Horrocks, Mathew Harry; Lee, Steven F; Gandhi, Sonia; Magdalinou, Nadia K; Chen, Serene W; Devine, Michael J; Tosatto, Laura; Kjaergaard, Magnus; Beckwith, Joseph S; Zetterberg, Henrik; Iljina, Marija; Cremades, Nunilo; Dobson, Christopher M; Wood, Nicholas W; Klenerman, David.

I: A C S Chemical Neuroscience, Bind 7, Nr. 3, 22.01.2016, s. 399–406.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Horrocks, MH, Lee, SF, Gandhi, S, Magdalinou, NK, Chen, SW, Devine, MJ, Tosatto, L, Kjaergaard, M, Beckwith, JS, Zetterberg, H, Iljina, M, Cremades, N, Dobson, CM, Wood, NW & Klenerman, D 2016, 'Single-molecule imaging of individual amyloid protein aggregates in human biofluids', A C S Chemical Neuroscience, bind 7, nr. 3, s. 399–406. https://doi.org/10.1021/acschemneuro.5b00324

APA

Horrocks, M. H., Lee, S. F., Gandhi, S., Magdalinou, N. K., Chen, S. W., Devine, M. J., Tosatto, L., Kjaergaard, M., Beckwith, J. S., Zetterberg, H., Iljina, M., Cremades, N., Dobson, C. M., Wood, N. W., & Klenerman, D. (2016). Single-molecule imaging of individual amyloid protein aggregates in human biofluids. A C S Chemical Neuroscience, 7(3), 399–406. https://doi.org/10.1021/acschemneuro.5b00324

CBE

Horrocks MH, Lee SF, Gandhi S, Magdalinou NK, Chen SW, Devine MJ, Tosatto L, Kjaergaard M, Beckwith JS, Zetterberg H, Iljina M, Cremades N, Dobson CM, Wood NW, Klenerman D. 2016. Single-molecule imaging of individual amyloid protein aggregates in human biofluids. A C S Chemical Neuroscience. 7(3):399–406. https://doi.org/10.1021/acschemneuro.5b00324

MLA

Vancouver

Horrocks MH, Lee SF, Gandhi S, Magdalinou NK, Chen SW, Devine MJ o.a. Single-molecule imaging of individual amyloid protein aggregates in human biofluids. A C S Chemical Neuroscience. 2016 jan 22;7(3):399–406. https://doi.org/10.1021/acschemneuro.5b00324

Author

Horrocks, Mathew Harry ; Lee, Steven F ; Gandhi, Sonia ; Magdalinou, Nadia K ; Chen, Serene W ; Devine, Michael J ; Tosatto, Laura ; Kjaergaard, Magnus ; Beckwith, Joseph S ; Zetterberg, Henrik ; Iljina, Marija ; Cremades, Nunilo ; Dobson, Christopher M ; Wood, Nicholas W ; Klenerman, David. / Single-molecule imaging of individual amyloid protein aggregates in human biofluids. I: A C S Chemical Neuroscience. 2016 ; Bind 7, Nr. 3. s. 399–406.

Bibtex

@article{affc35ba6e474b6e88403cb880b51933,
title = "Single-molecule imaging of individual amyloid protein aggregates in human biofluids",
abstract = "The misfolding and aggregation of proteins into amyloid fibrils characterizes many neurodegenerative disorders such as Parkinson's and Alzheimer's diseases. We report here a method, termed SAVE (single aggregate visualization by enhancement) imaging, for the ultra-sensitive detection of individual amyloid fibrils and oligomers using single-molecule fluorescence microscopy. We demonstrate that this method is able to detect the presence of amyloid aggregates of alpha-synuclein, tau and amyloid-β. In addition, we show that aggregates can also be identified in human cerebrospinal fluid (CSF). Significantly, we see a two-fold increase in the average aggregate concentration in CSF from PD patients compared to age-matched controls. Taken together, we conclude that this method provides an opportunity to characterize the structural nature of amyloid aggregates in a key biofluid, and therefore has the potential to study disease progression in both animal models and humans to enhance our understanding of neurodegenerative disorders.",
author = "Horrocks, {Mathew Harry} and Lee, {Steven F} and Sonia Gandhi and Magdalinou, {Nadia K} and Chen, {Serene W} and Devine, {Michael J} and Laura Tosatto and Magnus Kjaergaard and Beckwith, {Joseph S} and Henrik Zetterberg and Marija Iljina and Nunilo Cremades and Dobson, {Christopher M} and Wood, {Nicholas W} and David Klenerman",
year = "2016",
month = jan,
day = "22",
doi = "10.1021/acschemneuro.5b00324",
language = "English",
volume = "7",
pages = "399–406",
journal = "A C S Chemical Neuroscience",
issn = "1948-7193",
publisher = "American Chemical Society",
number = "3",

}

RIS

TY - JOUR

T1 - Single-molecule imaging of individual amyloid protein aggregates in human biofluids

AU - Horrocks, Mathew Harry

AU - Lee, Steven F

AU - Gandhi, Sonia

AU - Magdalinou, Nadia K

AU - Chen, Serene W

AU - Devine, Michael J

AU - Tosatto, Laura

AU - Kjaergaard, Magnus

AU - Beckwith, Joseph S

AU - Zetterberg, Henrik

AU - Iljina, Marija

AU - Cremades, Nunilo

AU - Dobson, Christopher M

AU - Wood, Nicholas W

AU - Klenerman, David

PY - 2016/1/22

Y1 - 2016/1/22

N2 - The misfolding and aggregation of proteins into amyloid fibrils characterizes many neurodegenerative disorders such as Parkinson's and Alzheimer's diseases. We report here a method, termed SAVE (single aggregate visualization by enhancement) imaging, for the ultra-sensitive detection of individual amyloid fibrils and oligomers using single-molecule fluorescence microscopy. We demonstrate that this method is able to detect the presence of amyloid aggregates of alpha-synuclein, tau and amyloid-β. In addition, we show that aggregates can also be identified in human cerebrospinal fluid (CSF). Significantly, we see a two-fold increase in the average aggregate concentration in CSF from PD patients compared to age-matched controls. Taken together, we conclude that this method provides an opportunity to characterize the structural nature of amyloid aggregates in a key biofluid, and therefore has the potential to study disease progression in both animal models and humans to enhance our understanding of neurodegenerative disorders.

AB - The misfolding and aggregation of proteins into amyloid fibrils characterizes many neurodegenerative disorders such as Parkinson's and Alzheimer's diseases. We report here a method, termed SAVE (single aggregate visualization by enhancement) imaging, for the ultra-sensitive detection of individual amyloid fibrils and oligomers using single-molecule fluorescence microscopy. We demonstrate that this method is able to detect the presence of amyloid aggregates of alpha-synuclein, tau and amyloid-β. In addition, we show that aggregates can also be identified in human cerebrospinal fluid (CSF). Significantly, we see a two-fold increase in the average aggregate concentration in CSF from PD patients compared to age-matched controls. Taken together, we conclude that this method provides an opportunity to characterize the structural nature of amyloid aggregates in a key biofluid, and therefore has the potential to study disease progression in both animal models and humans to enhance our understanding of neurodegenerative disorders.

U2 - 10.1021/acschemneuro.5b00324

DO - 10.1021/acschemneuro.5b00324

M3 - Journal article

C2 - 26800462

VL - 7

SP - 399

EP - 406

JO - A C S Chemical Neuroscience

JF - A C S Chemical Neuroscience

SN - 1948-7193

IS - 3

ER -