The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Template-assisted filament growth by parallel stacking of tau
Open accessAbstract
Tau Filaments are found in >20 neurodegenerative diseases. Yet, because of their enormous molecular weights and poor tendency to form highly ordered 3D crystal lattices, they have evaded high-resolution structure determination. Here, we studied 25 derivatized tau mutants by using electron paramagnetic resonance and fluorescence spectroscopy to report structural details of tau filaments. Based on strong spin exchange and pyrene excimer formation of core residues, we find that individual tau proteins form single molecule layers along the fiber axis that perfectly stack on top of each other by in-register, parallel alignment of β-strands. We suggest a model of filament growth wherein the existing filament serves as a template for the incoming, unfolded tau molecule, resulting in a new structured layer with maximized hydrogen-bonded contact surface and side-chain stacking.
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Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480
Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., & Crowther, R. A. (1996) · Nature · doi:10.1038/383550a0 · Cited by 1,036
Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929
Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein
Giasson, B. I., Forman, M. S., Higuchi, M., Golbe, L. I., Graves, C. L., Kotzbauer, P. T., Trojanowski, J. Q., & Lee, V. M.-Y. (2003) · Science · doi:10.1126/science.1082324 · Cited by 879
Novak, M., Kabat, J., & Wischik, C. M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05665.x · Cited by 398
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
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Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development
Chen, G.-F., Xu, T.-H., Yan, Y., Zhou, Y.-R., Jiang, Y., Melcher, K., & Xu, H. E. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.28 · Cited by 1,965
Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils
Petkova, A. T., Yau, W.-M., & Tycko, R. (2006) · Biochemistry · doi:10.1021/bi051952q · Cited by 1,044
Structural Classification of Toxic Amyloid Oligomers
Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800016200 · Cited by 783
Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice
Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Clos, A. L., Jackson, G. R., & Kayed, R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-39 · Cited by 633
Metadata
- Authors
- Margittai, M., & Langen, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2004-07-06
- Volume
- 101
- Issue
- 28
- Pages
- 10278-10283
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2091441518
- Cited by
- 274
- References
- 6
- FWCI
- 9.12
- Type
- journal article
- Language
- en
- Open access
- green
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
