B Trinczek

Summary

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

Publications

  1. 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
  2. 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
  3. pmc The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease
    S Illenberger
    Max Planck Unit for Structural Molecular Biology, D 22603 Hamburg, Germany
    Mol Biol Cell 9:1495-512. 1998
  4. ncbi request reprint Structure, microtubule interactions, and phosphorylation of tau protein
    E M Mandelkow
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    Ann N Y Acad Sci 777:96-106. 1996
  5. ncbi request reprint Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics
    S Illenberger
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    J Biol Chem 271:10834-43. 1996
  6. ncbi request reprint Crystallization of a macromolecular ring assembly of tubulin liganded with the anti-mitotic drug podophyllotoxin
    E Schonbrunn
    Max Planck Unit for Structural Molecular Biology, c o DESY, Hamburg, 22603, Germany
    J Struct Biol 128:211-5. 1999

Collaborators

  • A Ebneth
  • U Preuss
  • E Schonbrunn
  • S Illenberger
  • E M Mandelkow
  • E Mandelkow
  • J Biernat
  • G Drewes
  • K Stamer
  • K Baumann
  • R Godemann
  • Q Zheng-Fischhöfer
  • N Gustke
  • J B Olmsted
  • O Schweers
  • H E Meyer

Detail Information

Publications6

  1. 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
    ....
  2. 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...
  3. pmc The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease
    S Illenberger
    Max Planck Unit for Structural Molecular Biology, D 22603 Hamburg, Germany
    Mol Biol Cell 9:1495-512. 1998
    ..Since S214 is also phosphorylated in Alzheimer's disease tau, our results support the view that reactivation of the cell cycle machinery is involved in tau hyperphosphorylation...
  4. ncbi request reprint Structure, microtubule interactions, and phosphorylation of tau protein
    E M Mandelkow
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    Ann N Y Acad Sci 777:96-106. 1996
    ..This site can be phosphorylated by kinases present in brain tissue, and it is uniquely phosphorylated in Alzheimer brain...
  5. ncbi request reprint Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics
    S Illenberger
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    J Biol Chem 271:10834-43. 1996
    ..Thus, the phosphorylation of the repeated motifs in the microtubule binding domains of MAPs by p110mark might provide a mechanism for the regulation of microtubule dynamics in cells...
  6. ncbi request reprint Crystallization of a macromolecular ring assembly of tubulin liganded with the anti-mitotic drug podophyllotoxin
    E Schonbrunn
    Max Planck Unit for Structural Molecular Biology, c o DESY, Hamburg, 22603, Germany
    J Struct Biol 128:211-5. 1999
    ..Thus, the use of highly homogeneous tubulin preparations should improve the diffraction quality of these crystals...