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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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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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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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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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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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Transport and diffusion of Tau protein in neurons

Cellular and molecular life sciences : CMLS, 2014-08, Vol.71 (16), p.3139-3150

2014

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The Core of Tau-Paired Helical Filaments Studied by Scanning Transmission Electron Microscopy and Limited Proteolysis

Biochemistry (Easton), 2006-05, Vol.45 (20), p.6446-6457

2006

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PAK5 kinase is an inhibitor of MARK/Par-1, which leads to stable microtubules and dynamic actin

Molecular biology of the cell, 2005-09, Vol.16 (9), p.4410-4422

2005

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The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease

Molecular biology of the cell, 1998-06, Vol.9 (6), p.1495-1512

1998

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Nonsaturable Binding Indicates Clustering of Tau on the Microtubule Surface in a Paired Helical Filament-like Conformation

The Journal of biological chemistry, 2000-09, Vol.275 (39), p.30335-30343

2000

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Structural and Microtubule Binding Properties of Tau Mutants of Frontotemporal Dementias

Biochemistry (Easton), 2007-03, Vol.46 (10), p.2574-2582

2007

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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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Axodendritic sorting and pathological missorting of Tau are isoform-specific and determined by axon initial segment architecture

The Journal of biological chemistry, 2017-07, Vol.292 (29), p.12192-12207

2017

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Modulation of kinesin binding by the C-termini of tubulin

The EMBO journal, 2004-03, Vol.23 (5), p.989-999

2004

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Screening for inhibitors of tau polymerization

Current Alzheimer research, 2005-04, Vol.2 (2), p.219-226

2005

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Structural Principles of Tau and the Paired Helical Filaments of Alzheimer's Disease

Brain pathology (Zurich, Switzerland), 2007-01, Vol.17 (1), p.83-90

2007

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Tau Protein Diffuses along the Microtubule Lattice

The Journal of biological chemistry, 2012-11, Vol.287 (46), p.38559-38568

2012

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Molecular crowding and RNA synergize to promote phase separation, microtubule interaction, and seeding of Tau condensates

The EMBO journal, 2022-06, Vol.41 (11), p.e108882-n/a

2022

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The “Jaws” of the Tau-Microtubule Interaction

The Journal of biological chemistry, 2007-04, Vol.282 (16), p.12230-12239

2007

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Microtubule affinity regulating kinase activity in living neurons was examined by a genetically encoded fluorescence resonance energy transfer/fluorescence lifetime imaging-based biosensor: inhibitors with therapeutic potential

The Journal of biological chemistry, 2011-12, Vol.286 (48), p.41711-41722

2011

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Single-molecule investigation of the interference between kinesin, tau and MAP2c

The EMBO journal, 2002-09, Vol.21 (18), p.4896-4905

2002

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Kinesin motors and disease

Trends in cell biology, 2002-12, Vol.12 (12), p.585-591

2002

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MARK, a Novel Family of Protein Kinases That Phosphorylate Microtubule-Associated Proteins and Trigger Microtubule Disruption

Cell, 1997-04, Vol.89 (2), p.297-308

1997

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Spatial Patterns from Oscillating Microtubules

Science (American Association for the Advancement of Science), 1989-12, Vol.246 (4935), p.1291-1293

1989

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Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262

The Journal of biological chemistry, 1995-03, Vol.270 (13), p.7679-7688

1995

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

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

Structural polymorphism of 441-residue tau at single residue resolution

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

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

Transport and diffusion of Tau protein in neurons

The Core of Tau-Paired Helical Filaments Studied by Scanning Transmission Electron Microscopy and Limited Proteolysis

PAK5 kinase is an inhibitor of MARK/Par-1, which leads to stable microtubules and dynamic actin

The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease

Nonsaturable Binding Indicates Clustering of Tau on the Microtubule Surface in a Paired Helical Filament-like Conformation

Structural and Microtubule Binding Properties of Tau Mutants of Frontotemporal Dementias

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

Axodendritic sorting and pathological missorting of Tau are isoform-specific and determined by axon initial segment architecture

Modulation of kinesin binding by the C-termini of tubulin

Screening for inhibitors of tau polymerization

Structural Principles of Tau and the Paired Helical Filaments of Alzheimer's Disease

Tau Protein Diffuses along the Microtubule Lattice

Molecular crowding and RNA synergize to promote phase separation, microtubule interaction, and seeding of Tau condensates

The “Jaws” of the Tau-Microtubule Interaction

Microtubule affinity regulating kinase activity in living neurons was examined by a genetically encoded fluorescence resonance energy transfer/fluorescence lifetime imaging-based biosensor: inhibitors with therapeutic potential

Single-molecule investigation of the interference between kinesin, tau and MAP2c

Kinesin motors and disease

MARK, a Novel Family of Protein Kinases That Phosphorylate Microtubule-Associated Proteins and Trigger Microtubule Disruption

Spatial Patterns from Oscillating Microtubules

Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262

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