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Susanne Wegmann et al.
EMBO JOURNAL (2018)
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Liquid-liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau
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Amayra Hernandez-Vega et al.
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Xuemei Zhang et al.
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Marina Feric et al.
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Amandine Molliex et al.
CELL (2015)
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Avinash Patel et al.
CELL (2015)
Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins
Yuan Lin et al.
MOLECULAR CELL (2015)
Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits
Sang-Won Min et al.
NATURE MEDICINE (2015)
Frontotemporal dementia caused by microtubule-associated protein tau gene (MAPT) mutations: a chameleon for neuropathology and neuroimaging
B. Ghetti et al.
NEUROPATHOLOGY AND APPLIED NEUROBIOLOGY (2015)
Nuclear Magnetic Resonance Analysis of the Acetylation Pattern of the Neuronal Tau Protein
Amina Kamah et al.
BIOCHEMISTRY (2014)
Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance
Casey Cook et al.
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Oligomer Formation of Tau Protein Hyperphosphorylated in Cells
Katharina Tepper et al.
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Mechanistic Studies Unravel the Complexity Inherent in Tau Aggregation Leading to Alzheimer's Disease and the Tauopathies
Gayathri Ramachandran et al.
BIOCHEMISTRY (2013)
Phase transitions and size scaling of membrane-less organelles
Clifford P. Brangwynne
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Stress granules as crucibles of ALS pathogenesis
Yun R. Li et al.
JOURNAL OF CELL BIOLOGY (2013)
Modulation of allostery by protein intrinsic disorder
Allan Chris M. Ferreon et al.
NATURE (2013)
The microtubule-associated tau protein has intrinsic acetyltransferase activity
Todd J. Cohen et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2013)
Tau degradation: The ubiquitin-proteasome system versus the autophagy-lysosome system
Min Jae Lee et al.
PROGRESS IN NEUROBIOLOGY (2013)
The Synaptic Accumulation of Hyperphosphorylated Tau Oligomers in Alzheimer Disease Is Associated With Dysfunction of the Ubiquitin-Proteasome System
Hwan-Ching Tai et al.
AMERICAN JOURNAL OF PATHOLOGY (2012)
Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels
Masato Kato et al.
CELL (2012)
Phase transitions in the assembly of multivalent signalling proteins
Pilong Li et al.
NATURE (2012)
Post-translational modifications of tau protein: Implications for Alzheimer's disease
Ludovic Martin et al.
NEUROCHEMISTRY INTERNATIONAL (2011)
Alzheimer's Disease: The Challenge of the Second Century
David M. Holtzman et al.
SCIENCE TRANSLATIONAL MEDICINE (2011)
The acetylation of tau inhibits its function and promotes pathological tau aggregation
Todd J. Cohen et al.
NATURE COMMUNICATIONS (2011)
Alteration of the alpha-Synuclein Folding Landscape by a Mutation Related to Parkinson's Disease
Allan Chris M. Ferreon et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2010)
Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy
Sang-Won Min et al.
NEURON (2010)
Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2
Josephine C. Ferreon et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)
Structural Polymorphism of 441-Residue Tau at Single Residue Resolution
Marco D. Mukrasch et al.
PLOS BIOLOGY (2009)
SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis
Dohoon Kim et al.
EMBO JOURNAL (2007)
Characterization of two VQIXXK motifs for tau fibrillization in vitro
Wenkai Li et al.
BIOCHEMISTRY (2006)
Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation
D Cripps et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Sites of tau important for aggregation populate β-structure and bind to microtubules and polyanions
MD Mukrasch et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Inability of tau to properly regulate neuronal microtubule dynamics: a loss-of-function mechanism by which tau might mediate neuronal cell death
SC Feinstein et al.
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE (2005)
Tau pathology in Alzheimer disease and other tauopathies
K Iqbal et al.
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE (2005)
Regulation of the p300 HAT domain via a novel activation loop
PR Thompson et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2004)
Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on β-structure in the core domain
S Barghorn et al.
BIOCHEMISTRY (2004)
Tau protein isoforms, phosphorylation and role in neurodegenerative disorders
L Buée et al.
BRAIN RESEARCH REVIEWS (2000)
Assembly of τ protein into Alzheimer paired helical filaments depends on a local sequence motif (306VQIVYK311) forming β structure
M von Bergen et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2000)
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