J. Biernat

Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias.

E. Mandelkow, Q. Zheng-Fischhöfer, J. Biernat, 2000, Biochemistry.

Abnormal Alzheimer‐like phosphorylation of tau‐protein by cyclin‐dependent kinases cdk2 and cdk5

E. Mandelkow, E. Mandelkow, H. Piwnica-Worms, 1993, FEBS letters.

A Two-Component Adhesive: Tau Fibrils Arise from a Combination of a Well-Defined Motif and Conformationally Flexible Interactions.

E. Mandelkow, C. Griesinger, Katharina Tepper, 2017, Journal of the American Chemical Society.

Phosphorylation of microtubule‐associated protein tau: identification of the site for Ca2(+)‐calmodulin dependent kinase and relationship with tau phosphorylation in Alzheimer tangles.

M. Kirschner, E. Mandelkow, E. Mandelkow, 1990, The EMBO journal.

The development of cell processes induced by tau protein requires phosphorylation of serine 262 and 356 in the repeat domain and is inhibited by phosphorylation in the proline-rich domains.

E. Mandelkow, J. Biernat, J. Biernat, 1999, Molecular biology of the cell.

Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules.

E. Mandelkow, E. Mandelkow, K. Baumann, 1995, Molecular biology of the cell.

Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro

G. Drewes, E. Mandelkow, E. Mandelkow, 1992, The Journal of cell biology.

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

E. Mandelkow, E. Mandelkow, M. Mercken, 1992, The EMBO journal.