(Q57840222)

6

0 references

Ruth Nussinov

5

object named as

Ruth Nussinov

0 references

Buyong Ma

4

object named as

Buyong Ma

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author name string

Hilary A. Weismiller

1

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Rachel Murphy

Journal of Biological Chemistry

2

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language of work or name

English

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publication date

21 September 2018

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published in

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page(s)

jbc.RA118.005316

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describes a project that uses

ImageJ

1 reference

Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC6231118/fullTextXML

inferred from PubMed Central ID database lookup

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Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure

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Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this work

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Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure

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Side chain-dependent stacking modulates tau filament structure

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Pathological tau burden and distribution distinguishes progressive supranuclear palsy-parkinsonism from Richardson's syndrome

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Fibrillogenic nuclei composed of P301L mutant tau induce elongation of P301L tau but not wild-type tau

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Investigation of alpha-synuclein fibril structure by site-directed spin labeling

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A general model of prion strains and their pathogenicity

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Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy

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Three- and four-repeat Tau coassemble into heterogeneous filaments: an implication for Alzheimer disease

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Variations in filament conformation dictate seeding barrier between three- and four-repeat tau

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Electron paramagnetic resonance spectroscopy measures the distance between the external β-strands of folded α-synuclein in amyloid fibrils

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The dynamic structure of filamentous tau

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Fibril structure of human islet amyloid polypeptide

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

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Amplification of Tau fibrils from minute quantities of seeds

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Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease.

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Conformation determines the seeding potencies of native and recombinant Tau aggregates

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Invited review: Frontotemporal dementia caused by microtubule-associated protein tau gene (MAPT) mutations: a chameleon for neuropathology and neuroimaging

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RNA Binds to Tau Fibrils and Sustains Template-Assisted Growth

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Fracture and Growth Are Competing Forces Determining the Fate of Conformers in Tau Fibril Populations

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

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Pathological Tau Strains from Human Brains Recapitulate the Diversity of Tauopathies in Nontransgenic Mouse Brain

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Distinct differences in prion-like seeding and aggregation between tau protein variants provide mechanistic insights into tauopathies

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Tau Proteolysis in the Pathogenesis of Tauopathies: Neurotoxic Fragments and Novel Biomarkers.

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

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12 December 2020

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

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