The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Protein amyloids develop an intrinsic fluorescence signature during aggregation
Open accessAbstract
We report observations of an intrinsic fluorescence in the visible range, which develops during the aggregation of a range of polypeptides, including the disease-related human peptides amyloid-β(1-40) and (1-42), lysozyme and tau. Characteristic fluorescence properties such as the emission lifetime and spectra were determined experimentally. This intrinsic fluorescence is independent of the presence of aromatic side-chain residues within the polypeptide structure. Rather, it appears to result from electronic levels that become available when the polypeptide chain folds into a cross-β sheet scaffold similar to what has been reported to take place in crystals. We use these findings to quantify protein aggregation in vitro by fluorescence imaging in a label-free manner.
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Propagation of Tau Pathology in a Model of Early Alzheimer's Disease
de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427
Neurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000
Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice
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Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
Barghorn, S., & Mandelkow, E. (2002) · Biochemistry · doi:10.1021/bi026469j · Cited by 341
Structural Principles of Tau and the Paired Helical Filaments of Alzheimer's Disease
Mandelkow, E., Von Bergen, M., Biernat, J., & Mandelkow, E. (2007) · Brain Pathology · doi:10.1111/j.1750-3639.2007.00053.x · Cited by 243
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Clusterization-triggered emission: Uncommon luminescence from common materials
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Self-assembling peptide semiconductors
Tao, K., Makam, P., Aizen, R., & Gazit, E. (2017) · Science · doi:10.1126/science.aam9756 · Cited by 490
Nonconventional luminophores: characteristics, advancements and perspectives
Tang, S., Yang, T., Zhao, Z., Zhu, T., Zhang, Q., Hou, W., & Yuan, W. Z. (2021) · Chemical Society Reviews · doi:10.1039/d0cs01087a · Cited by 462
Fan, Z., Sun, L., Huang, Y., Wang, Y., & Zhang, M. (2016) · Nature Nanotechnology · doi:10.1038/nnano.2015.312 · Cited by 369
Prevalent intrinsic emission from nonaromatic amino acids and poly(amino acids)
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Metadata
- Authors
- Chan, F. T. S., Kaminski Schierle, G. S., Kumita, J. R., Bertoncini, C. W., Dobson, C. M., & Kaminski, C. F.
- Venue
- The Analyst
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2013
- Volume
- 138
- Issue
- 7
- Pages
- 2156
- ISSN
- 0003-2654 (ISSN-L)
- 1364-5528
- OpenAlex
- W1998730965
- Cited by
- 230
- References
- 6
- FWCI
- 7.55
- Type
- journal article
- Language
- en
- Open access
- green
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- Chan, F. T. S., Kaminski Schierle, G. S., Kumita, J. R., Bertoncini, C. W., Dobson, C. M., & Kaminski, C. F. (2013). Protein amyloids develop an intrinsic fluorescence signature during aggregation. The Analyst. https://doi.org/10.1039/c3an36798c
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