Cofactors are essential constituents of stable and seeding-active tau fibrils (Q90411704)

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13 April 2020

title

Cofactors are essential constituents of stable and seeding-active tau fibrils (English)

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1

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Yanxian Lin

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Kenneth S Kosik

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Jack H Freed

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author name string

Jennifer N Rauch

3

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Michael Vigers

4

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Zhikai Zeng

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Madhur Srivastava

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Timothy J Keller

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Songi Han

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publication date

11 December 2018

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Proceedings of the National Academy of Sciences of the United States of America

13 April 2020

published in

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volume

115

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issue

52

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page(s)

13234-13239

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Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans.

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cites work

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12 December 2020

RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments

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12 December 2020

Free fatty acids stimulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease.

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12 December 2020

RNA sequestration to pathological lesions of neurodegenerative diseases.

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12 December 2020

Tau pathology in a family with dementia and a P301L mutation in tau.

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12 December 2020

The Yin and Yang of protein folding

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12 December 2020

The core of tau-paired helical filaments studied by scanning transmission electron microscopy and limited proteolysis.

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12 December 2020

Structural impact of heparin binding to full-length Tau as studied by NMR spectroscopy

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12 December 2020

A complex mechanism for inducer mediated tau polymerization

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12 December 2020

Role of intermolecular forces in defining material properties of protein nanofibrils

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12 December 2020

Biology of amyloid: structure, function, and regulation

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12 December 2020

Nuclear tau, a key player in neuronal DNA protection

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12 December 2020

Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau protein

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12 December 2020

Biochemistry and cell biology of tau protein in neurofibrillary degeneration

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12 December 2020

Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein

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12 December 2020

Distinct tau prion strains propagate in cells and mice and define different tauopathies

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12 December 2020

Amplification of Tau fibrils from minute quantities of seeds

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12 December 2020

Proteopathic tau seeding predicts tauopathy in vivo.

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12 December 2020

Conformation determines the seeding potencies of native and recombinant Tau aggregates

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12 December 2020

RNA Binds to Tau Fibrils and Sustains Template-Assisted Growth

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12 December 2020

Protein structural and surface water rearrangement constitute major events in the earliest aggregation stages of tau.

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12 December 2020

Mobility and subcellular localization of endogenous, gene-edited Tau differs from that of over-expressed human wild-type and P301L mutant Tau

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12 December 2020

Unique pathological tau conformers from Alzheimer's brains transmit tau pathology in nontransgenic mice

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12 December 2020

Tau prions from Alzheimer's disease and chronic traumatic encephalopathy patients propagate in cultured cells

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12 December 2020

Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo.

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12 December 2020

A New Wavelet Denoising Method for Experimental Time-Domain Signals: Pulsed Dipolar Electron Spin Resonance.

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12 December 2020

Signature of an aggregation-prone conformation of tau.

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12 December 2020

Cryo-EM structures of tau filaments from Alzheimer's disease.

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12 December 2020

RNA stores tau reversibly in complex coacervates

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12 December 2020

Singular Value Decomposition Method to Determine Distance Distributions in Pulsed Dipolar Electron Spin Resonance

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12 December 2020

Extracellular Tau and Its Potential Role in the Propagation of Tau Pathology

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12 December 2020

Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer's disease filaments

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12 December 2020

Tau Internalization is Regulated by 6-O Sulfation on Heparan Sulfate Proteoglycans (HSPGs).

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12 December 2020

The role of heparan sulfates in protein aggregation and their potential impact on neurodegeneration

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12 December 2020

Inert and seed-competent tau monomers suggest structural origins of aggregation.

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12 December 2020

Structures of filaments from Pick's disease reveal a novel tau protein fold

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12 December 2020

Identifiers

DOI

10.1073/PNAS.1810058115

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PubMed publication ID

30538196

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