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Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau

Nature communications, 2017-08, Vol.8 (1), p.275-13, Article 275

2017

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Tau stabilizes microtubules by binding at the interface between tubulin heterodimers

Proceedings of the National Academy of Sciences - PNAS, 2015-06, Vol.112 (24), p.7501-7506

2015

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Lysine/RNA-interactions drive and regulate biomolecular condensation

Nature communications, 2019-07, Vol.10 (1), p.2909-15, Article 2909

2019

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Residue-specific identification of phase separation hot spots of Alzheimer's-related protein tau

Chemical science (Cambridge), 2019-07, Vol.1 (26), p.653-657

2019

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Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau

Nature communications, 2017-12, Vol.8 (1), p.1981-12, Article 1981

2017

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Lipid membrane templated misfolding and self-assembly of intrinsically disordered tau protein

Scientific reports, 2020-08, Vol.10 (1), p.13324-13324, Article 13324

2020

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Folding of the Tau Protein on Microtubules

Angewandte Chemie International Edition, 2015-08, Vol.54 (35), p.10347-10351

International ed. in English, 2015

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Mechanistic Basis of Phenothiazine-Driven Inhibition of Tau Aggregation

Angewandte Chemie International Edition, 2013-03, Vol.52 (12), p.3511-3515

International ed. in English, 2013

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Structural Impact of Tau Phosphorylation at Threonine 231

Structure (London), 2015-08, Vol.23 (8), p.1448-1458

2015

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Novel diffusion barrier for axonal retention of Tau in neurons and its failure in neurodegeneration

The EMBO journal, 2011-11, Vol.30 (23), p.4825-4837

2011

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FLEXITau: Quantifying Post-translational Modifications of Tau Protein in Vitro and in Human Disease

Analytical chemistry (Washington), 2016-04, Vol.88 (7), p.3704-3714

2016

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Structural polymorphism of 441-residue tau at single residue resolution

PLoS biology, 2009-02, Vol.7 (2), p.e34-e1000034

2009

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Oligomer Formation of Tau Protein Hyperphosphorylated in Cells

The Journal of biological chemistry, 2014-12, Vol.289 (49), p.34389-34407

2014

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Inhibition of tau aggregation in a novel Caenorhabditis elegans model of tauopathy mitigates proteotoxicity

Human molecular genetics, 2012-08, Vol.21 (16), p.3587-3603

2012

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Backbone assignment for minimal protein amounts of low structural homogeneity in the absence of deuteration

Chemical communications (Cambridge, England), 2016-03, Vol.52 (21), p.4002-4005

2016

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Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex

Nature communications, 2018-10, Vol.9 (1), p.4532-13, Article 4532

2018

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Structural Impact of Proline-Directed Pseudophosphorylation at AT8, AT100, and PHF1 Epitopes on 441-Residue Tau

Journal of the American Chemical Society, 2011-10, Vol.133 (40), p.15842-15845

2011

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Proline-directed Pseudo-phosphorylation at AT8 and PHF1 Epitopes Induces a Compaction of the Paperclip Folding of Tau and Generates a Pathological (MC-1) Conformation

The Journal of biological chemistry, 2008-11, Vol.283 (46), p.32066-32076

2008

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A current view on Tau protein phosphorylation in Alzheimer's disease

Current opinion in neurobiology, 2021-08, Vol.69, p.131-138

2021

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

Molecular neurodegeneration, 2020-07, Vol.15 (1), p.1-39, Article 39

2020

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Stages and Conformations of the Tau Repeat Domain during Aggregation and Its Effect on Neuronal Toxicity

The Journal of biological chemistry, 2014-07, Vol.289 (29), p.20318-20332

2014

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MARK/PAR1 Kinase Is a Regulator of Microtubule-Dependent Transport in Axons

The Journal of cell biology, 2004-10, Vol.167 (1), p.99-110

2004

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Conformational Changes Specific for Pseudophosphorylation at Serine 262 Selectively Impair Binding of Tau to Microtubules

Biochemistry (Easton), 2009-10, Vol.48 (42), p.10047-10055

2009

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Anthraquinones Inhibit Tau Aggregation and Dissolve Alzheimer's Paired Helical Filaments in Vitro and in Cells

The Journal of biological chemistry, 2005-02, Vol.280 (5), p.3628-3635

2005

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Phosphorylation of Human Tau Protein by Microtubule Affinity-Regulating Kinase 2

Biochemistry (Easton), 2013-12, Vol.52 (50), p.9068-9079

2013

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Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers

Lysine/RNA-interactions drive and regulate biomolecular condensation

Residue-specific identification of phase separation hot spots of Alzheimer's-related protein tau

Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau

Lipid membrane templated misfolding and self-assembly of intrinsically disordered tau protein

Folding of the Tau Protein on Microtubules

Mechanistic Basis of Phenothiazine-Driven Inhibition of Tau Aggregation

Structural Impact of Tau Phosphorylation at Threonine 231

Novel diffusion barrier for axonal retention of Tau in neurons and its failure in neurodegeneration

FLEXITau: Quantifying Post-translational Modifications of Tau Protein in Vitro and in Human Disease

Structural polymorphism of 441-residue tau at single residue resolution

Oligomer Formation of Tau Protein Hyperphosphorylated in Cells

Inhibition of tau aggregation in a novel Caenorhabditis elegans model of tauopathy mitigates proteotoxicity

Backbone assignment for minimal protein amounts of low structural homogeneity in the absence of deuteration

Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex

Structural Impact of Proline-Directed Pseudophosphorylation at AT8, AT100, and PHF1 Epitopes on 441-Residue Tau

Proline-directed Pseudo-phosphorylation at AT8 and PHF1 Epitopes Induces a Compaction of the Paperclip Folding of Tau and Generates a Pathological (MC-1) Conformation

A current view on Tau protein phosphorylation in Alzheimer's disease

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

Stages and Conformations of the Tau Repeat Domain during Aggregation and Its Effect on Neuronal Toxicity

MARK/PAR1 Kinase Is a Regulator of Microtubule-Dependent Transport in Axons

Conformational Changes Specific for Pseudophosphorylation at Serine 262 Selectively Impair Binding of Tau to Microtubules

Anthraquinones Inhibit Tau Aggregation and Dissolve Alzheimer's Paired Helical Filaments in Vitro and in Cells

Phosphorylation of Human Tau Protein by Microtubule Affinity-Regulating Kinase 2

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