The authors present a method for the conversion of full-length tau protein into seeding-competent amyloid fibrils without heparin or other negatively charged co-factors, which could be useful for studying the effects of post-translational modifications on Tau aggregation as well as to identify potential inhibitors of tau aggregation. Biochemical experiments and solid-state NMR spectroscopy measurements show that these co-factor-free tau fibrils have similar properties as amyloid fibrils isolated from brain tissue but differ from those of commonly used heparin-induced tau fibrils
Background: The misfolding of amyloidogenic proteins including human Tau protein, human prion protei...
The mechanism of amyloid fibril formation by proteins has been classically described by the nucleati...
Tau protein aggregates represent a type of amyloid that are the pathological hallmark of over 20 neu...
Pathological aggregation of the protein tau into insoluble aggregates is a hallmark of neurodegenera...
Amyloid fibrils are cross-β-rich aggregates that are exceptionally stable forms of protein assembly....
Amyloid aggregates of Tau protein have been implicated in etiology of many neurodegenerative disorde...
<div><p>Amyloid aggregates of Tau protein have been implicated in etiology of many neurodegenerative...
Fibrils composed of tau protein are a pathological hallmark of several neurodegenerative disorders i...
In the Tauopathy subfamily of neurodegenerative diseases, the intrinsically disordered protein (IDP)...
Self-assembly of the microtubule-associated protein tau into neurotoxic oligomers, fibrils, and pair...
ABSTRACT: The propagation of Tau pathology in Alz-heimer’s disease (AD) is thought to proceed throug...
The aggregation of the natively disordered protein, Tau, to form lesions called neurofibrillary tang...
Colby, David W.Fibrils composed of tau protein are a pathological hallmark of several neurodegenerat...
Self-assembly of the microtubule-associated protein tau into neurotoxic oligomers, fibrils, and pair...
Tau fibrils are the main proteinacious components of neurofibrillary lesions in Alzheimer disease. A...
Background: The misfolding of amyloidogenic proteins including human Tau protein, human prion protei...
The mechanism of amyloid fibril formation by proteins has been classically described by the nucleati...
Tau protein aggregates represent a type of amyloid that are the pathological hallmark of over 20 neu...
Pathological aggregation of the protein tau into insoluble aggregates is a hallmark of neurodegenera...
Amyloid fibrils are cross-β-rich aggregates that are exceptionally stable forms of protein assembly....
Amyloid aggregates of Tau protein have been implicated in etiology of many neurodegenerative disorde...
<div><p>Amyloid aggregates of Tau protein have been implicated in etiology of many neurodegenerative...
Fibrils composed of tau protein are a pathological hallmark of several neurodegenerative disorders i...
In the Tauopathy subfamily of neurodegenerative diseases, the intrinsically disordered protein (IDP)...
Self-assembly of the microtubule-associated protein tau into neurotoxic oligomers, fibrils, and pair...
ABSTRACT: The propagation of Tau pathology in Alz-heimer’s disease (AD) is thought to proceed throug...
The aggregation of the natively disordered protein, Tau, to form lesions called neurofibrillary tang...
Colby, David W.Fibrils composed of tau protein are a pathological hallmark of several neurodegenerat...
Self-assembly of the microtubule-associated protein tau into neurotoxic oligomers, fibrils, and pair...
Tau fibrils are the main proteinacious components of neurofibrillary lesions in Alzheimer disease. A...
Background: The misfolding of amyloidogenic proteins including human Tau protein, human prion protei...
The mechanism of amyloid fibril formation by proteins has been classically described by the nucleati...
Tau protein aggregates represent a type of amyloid that are the pathological hallmark of over 20 neu...