Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain

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

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

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Cloning and sequencing of the cDNA encoding an isoform of microtubule‐associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain.

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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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Ubiquitin Is a Component of Paired Helical Filaments in Alzheimer's Disease

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A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis.

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The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein

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Developmentally regulated expression of specific tau sequences

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A Neuronal Antigen in the Brains of Alzheimer Patients

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Phosphorylated Tau Protein Is Integrated into Paired Helical Filaments in Alzheimer's Disease1

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Epitopes that span the tau molecule are shared with paired helical filaments

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Substrates for p34cdc2: In vivo veritas?

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Alzheimer's Disease: Insolubility of Partially Purified Paired Helical Filaments in Sodium Dodecyl Sulfate and Urea

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Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA.

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Neuritic pathology and dementia in alzheimer's disease

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The car☐yl third of tau is tightly bound to paired helical filaments

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Massive somatodendritic sprouting of cortical neurons in Alzheimer's disease

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

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Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51.

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Fetal‐Type Phosphorylation of the τ in Paired Helical Filaments

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Abnormal phosphorylation of tau precedes ubiquitination in neurofibrillary pathology of Alzheimer disease

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Identification of a Novel Proline-directed Serine/Threonine Protein Kinase in Rat Pheochromocytoma

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Identification of 3‐ and 4‐repeat tau isoforms within the PHF in Alzheimer's disease.

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Structural stability of paired helical filaments requires microtubule-binding domains of Tau: A model for self-association

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Alzheimer disease tangles share immunological similarities with multiphosphorylation repeats in the two large neurofilament proteins.

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Alzheimer disease proteins (A68) share epitopes with tau but show distinct biochemical properties

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Self assembly of microtubule associated protein tau into filaments resembling those found in alzheimer disease

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A68 proteins in Alzheimer's disease are composed of several tau isoforms in a phosphorylated state which affects their electrophoretic mobilities

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Immunochemical evidence that fragments of phosphorylated MAP5 (MAP1B) are bound to neurofibrillary tangles in Alzheimer's disease

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A serine/threonine proline kinase activity is included in the tau protein kinase fraction forming a paired helical filament epitope.

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Characterization of two pathological Tau protein variants in Alzheimer brain cortices

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Localization of the Alz-50 epitope in recombinant human microtubule-associated protein tau

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A Novel Tubulin-Dependent Protein Kinase Forming a Paired Helical Filament Epitope on Tau

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A distinct form of tau is selectively incorporated into Alzheimer's paired helical filaments

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Characterization of Antisera to Paired Helical Filaments and Tau

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Proteolytic Fragments of Alzheimer's Paired Helical Filaments1

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Neuroscience Year–Supplement 1 to the Encyclopedia of Neuroscience

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TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

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α-Synuclein is phosphorylated in synucleinopathy lesions

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Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this work.

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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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Targeted disruption of the cyclin-dependent kinase 5 gene results in abnormal corticogenesis, neuronal pathology and perinatal death.

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Abnormal tau proteins from Alzheimer's disease brains. Purification and amino acid analysis.

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New Phosphorylation Sites Identified in Hyperphosphorylated Tau (Paired Helical Filament‐Tau) from Alzheimer's Disease Brain Using Nanoelectrospray Mass Spectrometry

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Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.

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Phosphate analysis and dephosphorylation of modified tau associated with paired helical filaments

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Alzheimer's Disease Abnormally Phosphorylated τ Is Dephosphorylated by Protein Phosphatase‐2B (Calcineurin)

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