In vitro 0N4R tau fibrils contain a monomorphic β-sheet core enclosed by dynamically heterogeneous fuzzy coat segments
Misfolding of the microtubule-binding protein tau into filamentous aggregates is characteristic of many neurodegenerative diseases such as Alzheimer’s disease and progressive supranuclear palsy. Determining the structures and dynamics of these tau fibrils is important for designing inhibitors agains...
Main Authors: | Dregni, Aurelio J., Mandala, Venkata Shiva, Wu, Haifan, Elkins, Matthew Ryan, Wang, Harrison K., Hung, Ivan, DeGrado, William F., Hong, Mei |
---|---|
Other Authors: | Massachusetts Institute of Technology. Department of Chemistry |
Format: | Article |
Language: | English |
Published: |
Proceedings of the National Academy of Sciences
2020
|
Online Access: | https://hdl.handle.net/1721.1/125945 |
Similar Items
-
Inclusion of the C-Terminal Domain in the β-Sheet Core of Heparin-Fibrillized Three-Repeat Tau Protein Revealed by Solid-State Nuclear Magnetic Resonance Spectroscopy
by: Dregni, Aurelio J, et al.
Published: (2022) -
Inclusion of the C-Terminal Domain in the β-Sheet Core of Heparin-Fibrillized Three-Repeat Tau Protein Revealed by Solid-State Nuclear Magnetic Resonance Spectroscopy
by: Dregni, Aurelio J., et al.
Published: (2022) -
The peptide hormone glucagon forms amyloid fibrils with two coexisting β-strand conformations
by: Gelenter, Martin David, et al.
Published: (2020) -
Atomic Resolution Structure of Monomorphic Aβ₄₂ Amyloid Fibrils
by: Sergeyev, Ivan, et al.
Published: (2018) -
Hydration and Dynamics of Full-Length Tau Amyloid Fibrils Investigated by Solid-State Nuclear Magnetic Resonance
by: Dregni, Aurelio J, et al.
Published: (2022)