J
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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Journal ArticleDOI
Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure.
M. von Bergen,Peter Friedhoff,Jacek Biernat,Joachim Heberle,Eva Maria Mandelkow,E. Mandelkow +5 more
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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Indirubins Inhibit Glycogen Synthase Kinase-3β and CDK5/P25, Two Protein Kinases Involved in Abnormal Tau Phosphorylation in Alzheimer's Disease A PROPERTY COMMON TO MOST CYCLIN-DEPENDENT KINASE INHIBITORS?
Sophie Leclerc,Matthieu Garnier,Ralph Hoessel,Doris Marko,James A. Bibb,Gretchen L. Snyder,Paul Greengard,Jacek Biernat,Yong-Zhong Wu,Eva-Maria Mandelkow,Gerhard Eisenbrand,Laurent Meijer +11 more
TL;DR: It is reported here that indirubins are also powerful inhibitors (IC(50): 5-50 nm) of an evolutionarily related kinase, glycogen synthase kinase-3beta (GSK-3 beta), and it is shown that many, but not all, reported CDK inhibitors are powerful inhibitors of GSK-3 Beta.
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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.
Gerard Drewes,Birgit Lichtenberg-Kraag,Frank Döring,Eva Maria Mandelkow,Jacek Biernat,Jozef Goris,M Dorée,E. Mandelkow +7 more
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.