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Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments

Data up to Jan 2025

Published1992
Citations146
References27

Total Citations Per Year

Abstract

References (27)

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

1986 • 3,430 citations

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

1989 • 2,308 citations

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

1991 • 1,397 citations

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.

1988 • 1,073 citations

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

1988 • 920 citations

Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state.

1992 • 563 citations

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

1991 • 540 citations

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

1986 • 504 citations

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

1988 • 494 citations

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

1989 • 478 citations

The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region.

1992 • 468 citations

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

1992 • 415 citations

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

1987 • 393 citations

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

1988 • 342 citations

Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains.

1989 • 321 citations

Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments.

1992 • 246 citations

Fetal‐Type Phosphorylation of the τ in Paired Helical Filaments

1992 • 217 citations

The Alzheimer‐like phosphorylation of tau protein reduces microtubule binding and involves Ser‐Pro and Thr‐Pro motifs

1992 • 210 citations

Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's disease

1992 • 190 citations

Two novel kinases phosphorylate tau and the KSP site of heavy neurofilament subunits in high stoichiometric ratios

1991 • 134 citations

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

1991 • 109 citations

τ Protein Kinase II Is Involved in the Regulation of the Normal Phosphorylation State of τ Protein

1993 • 85 citations

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

1988 • 80 citations

Microtubule-binding domain of tau proteins.

1988 • 66 citations

A protein kinase associated with paired helical filaments in Alzheimer disease.

1992 • 65 citations

Improved protective groups for phosphate of o-phosphoserine useful for the solid-phase peptide synthesis

1991 • 25 citations

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Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating… (1992) – Neuroscience Letters | Metascience Observatory Explorer