Propagation of tau aggregates and neurodegeneration
M Goedert, DS Eisenberg… - Annual review of …, 2017 - annualreviews.org
A pathway from the natively unfolded microtubule-associated protein Tau to a highly
structured amyloid fibril underlies human Tauopathies. This ordered assembly causes …
structured amyloid fibril underlies human Tauopathies. This ordered assembly causes …
[HTML][HTML] Amyloid polymorphism: structural basis and neurobiological relevance
R Tycko - Neuron, 2015 - cell.com
Our understanding of the molecular structures of amyloid fibrils that are associated with
neurodegenerative diseases, of mechanisms by which disease-associated peptides and …
neurodegenerative diseases, of mechanisms by which disease-associated peptides and …
Disease-specific tau filaments assemble via polymorphic intermediates
Intermediate species in the assembly of amyloid filaments are believed to play a central role
in neurodegenerative diseases and may constitute important targets for therapeutic …
in neurodegenerative diseases and may constitute important targets for therapeutic …
Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer's and Pick's diseases
W Zhang, B Falcon, AG Murzin, J Fan, RA Crowther… - elife, 2019 - elifesciences.org
Assembly of microtubule-associated protein tau into filamentous inclusions underlies a
range of neurodegenerative diseases. Tau filaments adopt different conformations in …
range of neurodegenerative diseases. Tau filaments adopt different conformations in …
Solid-state NMR studies of amyloid fibril structure
R Tycko - Annual review of physical chemistry, 2011 - annualreviews.org
Current interest in amyloid fibrils stems from their involvement in neurodegenerative and
other diseases and from their role as an alternative structural state for many peptides and …
other diseases and from their role as an alternative structural state for many peptides and …
Structural polymorphism of 441-residue tau at single residue resolution
MD Mukrasch, S Bibow, J Korukottu, S Jeganathan… - PLoS …, 2009 - journals.plos.org
Alzheimer disease is characterized by abnormal protein deposits in the brain, such as
extracellular amyloid plaques and intracellular neurofibrillary tangles. The tangles are made …
extracellular amyloid plaques and intracellular neurofibrillary tangles. The tangles are made …
Physical and structural basis for polymorphism in amyloid fibrils
R Tycko - Protein Science, 2014 - Wiley Online Library
As our understanding of the molecular structures of amyloid fibrils has matured over the past
15 years, it has become clear that, while amyloid fibrils do have well‐defined molecular …
15 years, it has become clear that, while amyloid fibrils do have well‐defined molecular …
Amyloid fibril structures of tau: Conformational plasticity of the second microtubule-binding repeat
The intrinsically disordered protein tau associates with microtubules in neurons but
aggregates into cross–β amyloid fibrils that propagate in neurodegenerative brains. Different …
aggregates into cross–β amyloid fibrils that propagate in neurodegenerative brains. Different …
Applications of high-resolution 1H solid-state NMR
SP Brown - Solid State Nuclear Magnetic Resonance, 2012 - Elsevier
This article reviews the large increase in applications of high-resolution 1H magic-angle
spinning (MAS) solid-state NMR, in particular two-dimensional heteronuclear and …
spinning (MAS) solid-state NMR, in particular two-dimensional heteronuclear and …
The natively unfolded character of tau and its aggregation to Alzheimer-like paired helical filaments
S Jeganathan, M Von Bergen, EM Mandelkow… - Biochemistry, 2008 - ACS Publications
The abnormal aggregation of the microtubule-associated protein Tau into paired helical
filaments (PHFs) is one of the hallmarks of Alzheimer disease (AD). Tau in solution behaves …
filaments (PHFs) is one of the hallmarks of Alzheimer disease (AD). Tau in solution behaves …