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Biochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration

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Mandelkow, E.-M., Mandelkow, E.·2012·Cold Spring Harbor Perspectives in Medicine

Abstract

Tau represents the subunit protein of one of the major hallmarks of Alzheimer disease (AD), the neurofibrillary tangles, and is therefore of major interest as an indicator of disease mechanisms. Many of the unusual properties of Tau can be explained by its nature as a natively unfolded protein. Examples are the large number of structural conformations and biochemical modifications (phosphorylation, proteolysis, glycosylation, and others), the multitude of interaction partners (mainly microtubules, but also other cytoskeletal proteins, kinases, and phosphatases, motor proteins, chaperones, and membrane proteins). The pathological aggregation of Tau is counterintuitive, given its high solubility, but can be rationalized by short hydrophobic motifs forming β structures. The aggregation of Tau is toxic in cell and animal models, but can be reversed by suppressing expression or by aggregation inhibitors. This review summarizes some of the structural, biochemical, and cell biological properties of Tau and Tau fibers. Further aspects of Tau as a diagnostic marker and therapeutic target, its involvement in other Tau-based diseases, and its histopathology are covered by other chapters in this volume.

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Metadata

Authors
Mandelkow, E.-M., & Mandelkow, E.
Venue
Cold Spring Harbor Perspectives in Medicine
Published
2012-03-20
Volume
2
Issue
7
Pages
a006247-a006247
ISSN
2157-1422 (ISSN-L)
OpenAlex
W2099795098
Cited by
847
References
253
Type
posted content
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Biochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration. https://app.cochat.ai/papers/10.1101/cshperspect.a006247
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Mandelkow, E.-M., & Mandelkow, E. (2012). Biochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration. Cold Spring Harbor Perspectives in Medicine. https://doi.org/10.1101/cshperspect.a006247

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