E M Mandelkow|E Mandelkow - JoVE Visualize

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European Journal of Cell Biology|June 1, 1994

Phosphorylation of microtubule-associated proteins MAP2a,b and MAP2c at Ser136 by proline-directed kinases in vivo and in vitroB Berling, H Wille, B Röll, et al.

European Biophysics Journal : EBJ|October 7, 1998

Conformations of kinesin: solution vs. crystal structures and interactions with microtubulesA Marx, M Thormählen, J Müller, et al.

FEBS Letters|December 28, 1993

Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcineurin and phosphatase-2AG Drewes, E M Mandelkow, K Baumann, et al.

Neurobiology of Aging|May 1, 1995

Tau domains, phosphorylation, and interactions with microtubulesE M Mandelkow, J Biernat, G Drewes, et al.

European Journal of Biochemistry|April 18, 1998

Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformationQ Zheng-Fischhöfer, J Biernat, E M Mandelkow, et al.

Proceedings of the National Academy of Sciences of the United States of America|May 11, 2000

Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structureM von Bergen, P Friedhoff, J Biernat, et al.

Journal of Structural Biology|January 1, 1992

Domain structure and antiparallel dimers of microtubule-associated protein 2 (MAP2)H Wille, E M Mandelkow, J Dingus, et al.

Journal of Structural Biology|December 22, 1999

Crystallization of a macromolecular ring assembly of tubulin liganded with the anti-mitotic drug podophyllotoxinE Schönbrunn, W Phlippen, B Trinczek, et al.

Annals of the New York Academy of Sciences|January 17, 1996

Structure, microtubule interactions, and phosphorylation of tau proteinE M Mandelkow, O Schweers, G Drewes, et al.

FEBS Letters|July 28, 1992

The Alzheimer-like phosphorylation of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifsN Gustke, B Steiner, E M Mandelkow, et al.

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Showing results (51-60 of 134) with videos related to

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European Journal of Cell Biology|June 1, 1994

Phosphorylation of microtubule-associated proteins MAP2a,b and MAP2c at Ser136 by proline-directed kinases in vivo and in vitroB Berling, H Wille, B Röll, et al.

European Biophysics Journal : EBJ|October 7, 1998

Conformations of kinesin: solution vs. crystal structures and interactions with microtubulesA Marx, M Thormählen, J Müller, et al.

FEBS Letters|December 28, 1993

Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcineurin and phosphatase-2AG Drewes, E M Mandelkow, K Baumann, et al.

Neurobiology of Aging|May 1, 1995

Tau domains, phosphorylation, and interactions with microtubulesE M Mandelkow, J Biernat, G Drewes, et al.

European Journal of Biochemistry|April 18, 1998

Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformationQ Zheng-Fischhöfer, J Biernat, E M Mandelkow, et al.

Proceedings of the National Academy of Sciences of the United States of America|May 11, 2000

Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structureM von Bergen, P Friedhoff, J Biernat, et al.

Journal of Structural Biology|January 1, 1992

Domain structure and antiparallel dimers of microtubule-associated protein 2 (MAP2)H Wille, E M Mandelkow, J Dingus, et al.

Journal of Structural Biology|December 22, 1999

Crystallization of a macromolecular ring assembly of tubulin liganded with the anti-mitotic drug podophyllotoxinE Schönbrunn, W Phlippen, B Trinczek, et al.

Annals of the New York Academy of Sciences|January 17, 1996

Structure, microtubule interactions, and phosphorylation of tau proteinE M Mandelkow, O Schweers, G Drewes, et al.

FEBS Letters|July 28, 1992

The Alzheimer-like phosphorylation of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifsN Gustke, B Steiner, E M Mandelkow, et al.

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