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

Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

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Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

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A protein factor essential for microtubule assembly

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Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

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Uber eine eigenartige Erkrankung der Hirnrinde

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Mutation in the tau gene in familial multiple system tauopathy with presenile dementia

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Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease.

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A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau

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Tau is a candidate gene for chromosome 17 frontotemporal dementia

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Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein

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Microtubule Formation in vitro in Solutions Containing Low Calcium Concentrations

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Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau

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THE MECHANISM OF ACTION OF COLCHICINE

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Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans

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

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Paired Helical Filaments in Electron Microscopy of Alzheimer's Disease

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Mutation-Specific Functional Impairments in Distinct Tau Isoforms of Hereditary FTDP-17

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Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau.

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Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.

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Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.

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Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding

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Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress

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Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly

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

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Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease

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Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding

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Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)

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Tau protein function in living cells.

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Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms

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Age-dependent neurofibrillary tangle formation, neuron loss, and memory impairment in a mouse model of human tauopathy (P301L)

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The Primary Structure and Heterogeneity of Tau Protein from Mouse Brain

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Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons

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Developmentally regulated expression of specific tau sequences

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Mutations of Tau Protein in Frontotemporal Dementia Promote Aggregation of Paired Helical Filaments by Enhancing Local β-Structure

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Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure.

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Phosphorylation that Detaches Tau Protein from Microtubules (Ser262, Ser214) Also Protects It against Aggregation into Alzheimer Paired Helical Filaments

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Tau protein binds to microtubules through a flexible array of distributed weak sites.

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RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments

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Cyclic AMP-dependent endogenous phosphorylation of a microtubule-associated protein.

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Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology

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Inhibition of Heparin-induced Tau Filament Formation by Phenothiazines, Polyphenols, and Porphyrins

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Tau Consists of a Set of Proteins with Repeated C-Terminal Microtubule-Binding Domains and Variable N-Terminal Domains

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X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.

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Microtubule-Associated Protein MAP2 Shares a Microtubule Binding Motif with Tau Protein

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Tau proteins with FTDP‐17 mutations have a reduced ability to promote microtubule assembly

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Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro.

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Tau phosphorylation: physiological and pathological consequences

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Global Hairpin Folding of Tau in Solution

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Phosphorylation of Tau by Fyn: Implications for Alzheimer's Disease

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THE FINE STRUCTURE OF NEUROFIBRILLARY TANGLES IN ALZHEIMERʼS DISEASE

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The Structural Basis of Monoclonal Antibody Alz50's Selectivity for Alzheimer's Disease Pathology

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Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau

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Recent atomic models of amyloid fibril structure

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Tau proteins: the molecular structure and mode of binding on microtubules.

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Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments.

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Progress towards a molecular-level structural understanding of amyloid fibrils

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Polymerization of τ into Filaments in the Presence of Heparin: The Minimal Sequence Required for τ ‐ τ Interaction

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Free fatty acids stimulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease.

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Straight and paired helical filaments in Alzheimer disease have a common structural unit.

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Structure, Microtubule Interactions, and Paired Helical Filament Aggregation by Tau Mutants of Frontotemporal Dementias

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Inducible Expression of Tau Repeat Domain in Cell Models of Tauopathy

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Mammalian SAD Kinases Are Required for Neuronal Polarization

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One of the Antigenic Determinants of Paired Helical Filaments Is Related to Tau Protein1

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

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MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments

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Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments

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Sites of Tau Important for Aggregation Populate β-Structure and Bind to Microtubules and Polyanions

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Tau gene alternative splicing: expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases

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Phosphorylation of microtubule‐associated protein tau: identification of the site for Ca2(+)‐calmodulin dependent kinase and relationship with tau phosphorylation in Alzheimer tangles.

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The Endogenous and Cell Cycle-dependent Phosphorylation of tau Protein in Living Cells: Implications for Alzheimer’s Disease

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

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A decade of modeling Alzheimer's disease in transgenic mice

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Accelerated filament formation from tau protein with specific FTDP‐17 missense mutations

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Template-assisted filament growth by parallel stacking of tau

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The Generation of a 17 kDa Neurotoxic Fragment: An Alternative Mechanism by which Tau Mediates β-Amyloid-Induced Neurodegeneration

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Effects of frontotemporal dementia FTDP‐17 mutations on heparin‐induced assembly of tau filaments

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

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Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system.

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Antibodies to paired helical filaments in Alzheimer's disease do not recognize normal brain proteins

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Going new places using an old MAP: tau, microtubules and human neurodegenerative disease

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The Formation of Straight and Twisted Filaments from Short Tau Peptides

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Regulation of microtubule-associated proteins

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Tau Paired Helical Filaments from Alzheimer's Disease Brain and Assembled in Vitro Are Based on β-Structure in the Core Domain

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Mise en évidence immunologique de la protéine tau au niveau des lésions de dégénérescence neurofibrillaire de la maladie d'Alzheimer

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The Neuronal Microtubule‐Associated Protein Tau Is a Substrate for Caspase‐3 and an Effector of Apoptosis

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Inability of tau to properly regulate neuronal microtubule dynamics: a loss-of-function mechanism by which tau might mediate neuronal cell death

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