Characterization of tau prion seeding activity and strains from formaldehyde-fixed tissue

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2051-5960

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Characterization of tau prion seeding activity and strains from formaldehyde-fixed tissue ; volume:5 ; number:1 ; day:7 ; month:6 ; year:2017 ; pages:1-12 ; date:12.2017
Acta Neuropathologica Communications ; 5, Heft 1 (7.6.2017), 1-12, 12.2017

Keyword: Hirnkrankheit
Neuropsychiatrie
Nervenkrankheit

Creator: Kaufman, Sarah K.

Contributor: Thomas, Talitha L.
Del Tredici, Kelly
Braak, Heiko
Diamond, Marc I.
SpringerLink (Online service)

DOI: 10.1186/s40478-017-0442-8

URN: urn:nbn:de:1111-201707132267

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:33 AM CEST

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Kaufman, Sarah K.
Thomas, Talitha L.
Del Tredici, Kelly
Braak, Heiko
Diamond, Marc I.
SpringerLink (Online service)

Other Objects (12)

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Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo

Tau seeding in cases of multiple sclerosis

Detection limitations of prion seeding activities in blood samples from patients with sporadic prion disease

Aβ43 aggregates exhibit enhanced prion-like seeding activity in mice

$The cellular prion protein does not affect tau seeding and spreading of sarkosyl-insoluble fractions from Alzheimer’s disease$

The cellular prion protein does not affect tau seeding and spreading of sarkosyl-insoluble fractions from Alzheimer’s disease

Decrease in Skin Prion-Seeding Activity of Prion-Infected Mice Treated with a Compound Against Human and Animal Prions: a First Possible Biomarker for Prion Therapeutics

Tau exhibits unique seeding properties in globular glial tauopathy

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Structure of Tau filaments in Prion protein amyloidoses

Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates

FRET-based Tau seeding assay does not represent prion-like templated assembly of Tau filaments

Detecting Alpha Synuclein Seeding Activity in Formaldehyde-Fixed MSA Patient Tissue by PMCA

Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo

Tau seeding in cases of multiple sclerosis

Detection limitations of prion seeding activities in blood samples from patients with sporadic prion disease

Aβ43 aggregates exhibit enhanced prion-like seeding activity in mice

$The cellular prion protein does not affect tau seeding and spreading of sarkosyl-insoluble fractions from Alzheimer’s disease$

The cellular prion protein does not affect tau seeding and spreading of sarkosyl-insoluble fractions from Alzheimer’s disease

Decrease in Skin Prion-Seeding Activity of Prion-Infected Mice Treated with a Compound Against Human and Animal Prions: a First Possible Biomarker for Prion Therapeutics

Tau exhibits unique seeding properties in globular glial tauopathy

Heterologous cross-seeding mimics cross-species prion conversion in a yeast model

Structure of Tau filaments in Prion protein amyloidoses

Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates

FRET-based Tau seeding assay does not represent prion-like templated assembly of Tau filaments

Detecting Alpha Synuclein Seeding Activity in Formaldehyde-Fixed MSA Patient Tissue by PMCA

Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo

Tau seeding in cases of multiple sclerosis

Detection limitations of prion seeding activities in blood samples from patients with sporadic prion disease

Aβ43 aggregates exhibit enhanced prion-like seeding activity in mice

$The cellular prion protein does not affect tau seeding and spreading of sarkosyl-insoluble fractions from Alzheimer’s disease$

The cellular prion protein does not affect tau seeding and spreading of sarkosyl-insoluble fractions from Alzheimer’s disease

Decrease in Skin Prion-Seeding Activity of Prion-Infected Mice Treated with a Compound Against Human and Animal Prions: a First Possible Biomarker for Prion Therapeutics

Tau exhibits unique seeding properties in globular glial tauopathy

Heterologous cross-seeding mimics cross-species prion conversion in a yeast model

Structure of Tau filaments in Prion protein amyloidoses

Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates

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Characterization of tau prion seeding activity and strains from formaldehyde-fixed tissue

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Other Objects (12)

FRET-based Tau seeding assay does not represent prion-like templated assembly of Tau filaments

Detecting Alpha Synuclein Seeding Activity in Formaldehyde-Fixed MSA Patient Tissue by PMCA

Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo

Tau seeding in cases of multiple sclerosis

Detection limitations of prion seeding activities in blood samples from patients with sporadic prion disease

Aβ43 aggregates exhibit enhanced prion-like seeding activity in mice

The cellular prion protein does not affect tau seeding and spreading of sarkosyl-insoluble fractions from Alzheimer’s disease

Decrease in Skin Prion-Seeding Activity of Prion-Infected Mice Treated with a Compound Against Human and Animal Prions: a First Possible Biomarker for Prion Therapeutics

Tau exhibits unique seeding properties in globular glial tauopathy

Heterologous cross-seeding mimics cross-species prion conversion in a yeast model

Structure of Tau filaments in Prion protein amyloidoses

Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates

FRET-based Tau seeding assay does not represent prion-like templated assembly of Tau filaments

Detecting Alpha Synuclein Seeding Activity in Formaldehyde-Fixed MSA Patient Tissue by PMCA

Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo

Tau seeding in cases of multiple sclerosis

Detection limitations of prion seeding activities in blood samples from patients with sporadic prion disease

Aβ43 aggregates exhibit enhanced prion-like seeding activity in mice

The cellular prion protein does not affect tau seeding and spreading of sarkosyl-insoluble fractions from Alzheimer’s disease

Decrease in Skin Prion-Seeding Activity of Prion-Infected Mice Treated with a Compound Against Human and Animal Prions: a First Possible Biomarker for Prion Therapeutics

Tau exhibits unique seeding properties in globular glial tauopathy

Heterologous cross-seeding mimics cross-species prion conversion in a yeast model

Structure of Tau filaments in Prion protein amyloidoses

Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates

FRET-based Tau seeding assay does not represent prion-like templated assembly of Tau filaments

Detecting Alpha Synuclein Seeding Activity in Formaldehyde-Fixed MSA Patient Tissue by PMCA

Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo

Tau seeding in cases of multiple sclerosis

Detection limitations of prion seeding activities in blood samples from patients with sporadic prion disease

Aβ43 aggregates exhibit enhanced prion-like seeding activity in mice

The cellular prion protein does not affect tau seeding and spreading of sarkosyl-insoluble fractions from Alzheimer’s disease

Decrease in Skin Prion-Seeding Activity of Prion-Infected Mice Treated with a Compound Against Human and Animal Prions: a First Possible Biomarker for Prion Therapeutics

Tau exhibits unique seeding properties in globular glial tauopathy

Heterologous cross-seeding mimics cross-species prion conversion in a yeast model

Structure of Tau filaments in Prion protein amyloidoses

Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates

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