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Jacek Biernat

Researcher at Max Planck Society

Publications -  96
Citations -  19528

Jacek Biernat is an academic researcher from Max Planck Society. The author has contributed to research in topics: Tau protein & Phosphorylation. The author has an hindex of 65, co-authored 93 publications receiving 17925 citations. Previous affiliations of Jacek Biernat include Ruhr University Bochum & Center of Advanced European Studies and Research.

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

TL;DR: The data indicate that PHF assembly is initiated by a short fragment containing the minimal interaction motif forming a local beta structure embedded in a largely random-coil protein.
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Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding

TL;DR: Although MAP kinase efficiently phosphorylates many Ser/Thr-Pro motifs of tau, its effect on microtubule binding is only moderate, and phosphorylation of a single residue, Ser262, has a major effect on binding.
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Domains of tau protein and interactions with microtubules.

TL;DR: The role of the neuronal microtubule-associated protein tau has been studied by generating a series of tau constructs differing in one or several of its subdomains: length and composition of the repeat domains, extensions of the repeats in the N- or C-terminal direction, constructs without repeats, assembly vs projection domain, and number of N- terminal inserts.
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Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state.

TL;DR: It is proposed that MAP kinase is abnormally active in Alzheimer brain tissue, or that the corresponding phosphatases are abnormally passive, due to a breakdown of the normal regulatory mechanisms.