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Tau is a microtubule-associated protein that plays an important role in axonal stabilization, neuronal development, and neuronal polarity. In this review, we focus on the primary, secondary, tertiary, and quaternary tau structures. We describe the structure of tau from its specific residues until its conformation in dimers, oligomers, and larger polymers in physiological and pathological situations.
posttranslational modification, Tubulin binding, Motifs, microtubule-associated proteins, aggregation, motifs, Neurosciences. Biological psychiatry. Neuropsychiatry, tau residues, tubuling binding, Aggregation, Posttranslational modifications, Tubuling binding, posttranslational modifications, PHFs, Tau residues, Microtubule-Associated Proteins, RC321-571, Neuroscience
posttranslational modification, Tubulin binding, Motifs, microtubule-associated proteins, aggregation, motifs, Neurosciences. Biological psychiatry. Neuropsychiatry, tau residues, tubuling binding, Aggregation, Posttranslational modifications, Tubuling binding, posttranslational modifications, PHFs, Tau residues, Microtubule-Associated Proteins, RC321-571, Neuroscience
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