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Daniel Otzen

ThT 101: a primer on the use of thioflavin T to investigate amyloid formation

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ThT 101 : a primer on the use of thioflavin T to investigate amyloid formation. / Malmos, Kirsten; Blancas-Mejia, Luis M; Weber, Benedikt et al.

In: Amyloid: the Journal of Protein Folding Disorders, Vol. 24, No. 1, 04.2017, p. 1-16.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Malmos, K, Blancas-Mejia, LM, Weber, B, Buchner, J, Ramirez-Alvarado, M, Naiki, H & Otzen, D 2017, 'ThT 101: a primer on the use of thioflavin T to investigate amyloid formation', Amyloid: the Journal of Protein Folding Disorders, vol. 24, no. 1, pp. 1-16. https://doi.org/10.1080/13506129.2017.1304905

APA

Malmos, K., Blancas-Mejia, L. M., Weber, B., Buchner, J., Ramirez-Alvarado, M., Naiki, H., & Otzen, D. (2017). ThT 101: a primer on the use of thioflavin T to investigate amyloid formation. Amyloid: the Journal of Protein Folding Disorders, 24(1), 1-16. https://doi.org/10.1080/13506129.2017.1304905

CBE

Malmos K, Blancas-Mejia LM, Weber B, Buchner J, Ramirez-Alvarado M, Naiki H, Otzen D. 2017. ThT 101: a primer on the use of thioflavin T to investigate amyloid formation. Amyloid: the Journal of Protein Folding Disorders. 24(1):1-16. https://doi.org/10.1080/13506129.2017.1304905

MLA

Malmos, Kirsten et al. "ThT 101: a primer on the use of thioflavin T to investigate amyloid formation". Amyloid: the Journal of Protein Folding Disorders. 2017, 24(1). 1-16. https://doi.org/10.1080/13506129.2017.1304905

Vancouver

Malmos K, Blancas-Mejia LM, Weber B, Buchner J, Ramirez-Alvarado M, Naiki H et al. ThT 101: a primer on the use of thioflavin T to investigate amyloid formation. Amyloid: the Journal of Protein Folding Disorders. 2017 Apr;24(1):1-16. doi: 10.1080/13506129.2017.1304905

Author

Malmos, Kirsten ; Blancas-Mejia, Luis M ; Weber, Benedikt et al. / ThT 101 : a primer on the use of thioflavin T to investigate amyloid formation. In: Amyloid: the Journal of Protein Folding Disorders. 2017 ; Vol. 24, No. 1. pp. 1-16.

Bibtex

@article{05eb4b5ded7743f29617da5cb1840e4c,
title = "ThT 101: a primer on the use of thioflavin T to investigate amyloid formation",
abstract = "Thioflavin T (ThT) has been widely used to investigate amyloid formation since 1989. While concerns have recently been raised about its use as a probe specific for amyloid, ThT still continues to be a very valuable tool for studying kinetic aspects of fibrillation and associated inhibition mechanisms. This review aims to provide a conceptual instruction manual, covering appropriate considerations and pitfalls related to the use of ThT. We start by giving a brief introduction to amyloid formation with focus on the morphology of different aggregate species, followed by a discussion of the quality of protein needed to obtain reliable fibrillation data. After an overview of the photochemical basis for ThT's amyloid binding properties and artifacts that may arise from this, we describe how to plan and analyze ThT assays. We conclude with recommendations for complementary techniques to address shortcomings in the ThT assay.",
keywords = "Journal Article",
author = "Kirsten Malmos and Blancas-Mejia, {Luis M} and Benedikt Weber and Johannes Buchner and Marina Ramirez-Alvarado and Hironobu Naiki and Daniel Otzen",
year = "2017",
month = apr,
doi = "10.1080/13506129.2017.1304905",
language = "English",
volume = "24",
pages = "1--16",
journal = "Amyloid: the Journal of Protein Folding Disorders",
issn = "1350-6129",
publisher = "Taylor & Francis Online",
number = "1",

}

RIS

TY - JOUR

T1 - ThT 101

T2 - a primer on the use of thioflavin T to investigate amyloid formation

AU - Malmos, Kirsten

AU - Blancas-Mejia, Luis M

AU - Weber, Benedikt

AU - Buchner, Johannes

AU - Ramirez-Alvarado, Marina

AU - Naiki, Hironobu

AU - Otzen, Daniel

PY - 2017/4

Y1 - 2017/4

N2 - Thioflavin T (ThT) has been widely used to investigate amyloid formation since 1989. While concerns have recently been raised about its use as a probe specific for amyloid, ThT still continues to be a very valuable tool for studying kinetic aspects of fibrillation and associated inhibition mechanisms. This review aims to provide a conceptual instruction manual, covering appropriate considerations and pitfalls related to the use of ThT. We start by giving a brief introduction to amyloid formation with focus on the morphology of different aggregate species, followed by a discussion of the quality of protein needed to obtain reliable fibrillation data. After an overview of the photochemical basis for ThT's amyloid binding properties and artifacts that may arise from this, we describe how to plan and analyze ThT assays. We conclude with recommendations for complementary techniques to address shortcomings in the ThT assay.

AB - Thioflavin T (ThT) has been widely used to investigate amyloid formation since 1989. While concerns have recently been raised about its use as a probe specific for amyloid, ThT still continues to be a very valuable tool for studying kinetic aspects of fibrillation and associated inhibition mechanisms. This review aims to provide a conceptual instruction manual, covering appropriate considerations and pitfalls related to the use of ThT. We start by giving a brief introduction to amyloid formation with focus on the morphology of different aggregate species, followed by a discussion of the quality of protein needed to obtain reliable fibrillation data. After an overview of the photochemical basis for ThT's amyloid binding properties and artifacts that may arise from this, we describe how to plan and analyze ThT assays. We conclude with recommendations for complementary techniques to address shortcomings in the ThT assay.

KW - Journal Article

U2 - 10.1080/13506129.2017.1304905

DO - 10.1080/13506129.2017.1304905

M3 - Journal article

C2 - 28393556

VL - 24

SP - 1

EP - 16

JO - Amyloid: the Journal of Protein Folding Disorders

JF - Amyloid: the Journal of Protein Folding Disorders

SN - 1350-6129

IS - 1

ER -