A Ebneth

Summary

Affiliation: Max-Planck-Unit for Structural Molecular Biology
Country: Germany

Publications

  1. pmc Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease
    A Ebneth
    Max Planck Unit for Structural Molecular Biology, D 22607 Hamburg, Germany
    J Cell Biol 143:777-94. 1998
  2. ncbi request reprint Tau regulates the attachment/detachment but not the speed of motors in microtubule-dependent transport of single vesicles and organelles
    B Trinczek
    Max Planck Unit for Structural Molecular Biology, Notkestrasse 85, D 22607 Hamburg, Germany
    J Cell Sci 112:2355-67. 1999
  3. ncbi request reprint Phosphorylation of MAP2c and MAP4 by MARK kinases leads to the destabilization of microtubules in cells
    A Ebneth
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    Cell Motil Cytoskeleton 44:209-24. 1999
  4. ncbi request reprint MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    G Drewes
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    Cell 89:297-308. 1997

Collaborators

Detail Information

Publications4

  1. pmc Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease
    A Ebneth
    Max Planck Unit for Structural Molecular Biology, D 22607 Hamburg, Germany
    J Cell Biol 143:777-94. 1998
    ..Since in Alzheimer's disease tau protein is elevated and mislocalized, these observations point to a possible cause for the gradual degeneration of neurons...
  2. ncbi request reprint Tau regulates the attachment/detachment but not the speed of motors in microtubule-dependent transport of single vesicles and organelles
    B Trinczek
    Max Planck Unit for Structural Molecular Biology, Notkestrasse 85, D 22607 Hamburg, Germany
    J Cell Sci 112:2355-67. 1999
    ....
  3. ncbi request reprint Phosphorylation of MAP2c and MAP4 by MARK kinases leads to the destabilization of microtubules in cells
    A Ebneth
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    Cell Motil Cytoskeleton 44:209-24. 1999
    ..Concomitant with microtubule disruption, we also observed a breakdown of the vimentin network, whereas actin fibers remained unaffected. Thus, MARK seems to play an important role in controlling cytoskeletal dynamics...
  4. ncbi request reprint MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    G Drewes
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    Cell 89:297-308. 1997
    ..Overexpression of MARK in cells leads to hyperphosphorylation of MAPs on KXGS motifs and to disruption of the microtubule array, resulting in morphological changes and cell death...