Dirk Gorlich

Summary

Affiliation: University of Heidelberg
Country: Germany

Publications

  1. pmc Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm
    Markus T Bohnsack
    ZMBH, INF 282, D 69120 Heidelberg, Germany
    EMBO J 21:6205-15. 2002
  2. pmc NDC1: a crucial membrane-integral nucleoporin of metazoan nuclear pore complexes
    Fabrizia Stavru
    Zentrum fur Molekulare Biologie der Universitat Heidelberg, D 69120 Heidelberg, Germany
    J Cell Biol 173:509-19. 2006
  3. pmc Nuclear pore complex assembly and maintenance in POM121- and gp210-deficient cells
    Fabrizia Stavru
    Zentrum fur Molekulare Biologie der Universitat Heidelberg, D 69120 Heidelberg, Germany
    J Cell Biol 173:477-83. 2006
  4. pmc Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation
    Dirk Gorlich
    ZMBH, INF 282, 69120 Heidelberg, Germany
    EMBO J 22:1088-100. 2003
  5. pmc The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    Katharina Ribbeck
    ZMBH, INF 282, D 69120 Heidelberg, Germany
    EMBO J 21:2664-71. 2002
  6. pmc Exportin 7 defines a novel general nuclear export pathway
    José Manuel Mingot
    ZMBH, INF 282, Heidelberg, Germany
    EMBO J 23:3227-36. 2004
  7. pmc Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes
    Theis Stüven
    ZMBH, INF 282, D 69120 Heidelberg and Universität Lübeck, Ratzeburger Allee 160, D 23538 Lubeck, Germany
    EMBO J 22:5928-40. 2003
  8. ncbi FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
    Steffen Frey
    Zentrum für Molekulare Biologie der Universität Heidelberg ZMBH, INF 282, D 69120 Heidelberg, Germany
    Science 314:815-7. 2006
  9. ncbi A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes
    Markus T Bohnsack
    Zentrum für Molekulare Biologie der Universität Heidelberg ZMBH, INF 282, D 69120 Heidelberg, Germany
    Nat Cell Biol 8:257-63. 2006
  10. pmc Characterisation of the passive permeability barrier of nuclear pore complexes
    Dagmar Mohr
    ZMBH, Im Neuenheimer Feld 282, Heidelberg, Germany
    EMBO J 28:2541-53. 2009

Collaborators

Detail Information

Publications11

  1. pmc Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm
    Markus T Bohnsack
    ZMBH, INF 282, D 69120 Heidelberg, Germany
    EMBO J 21:6205-15. 2002
    ..Besides Exp5 and importin 13, CRM1 and as yet unidentified exportins also contribute to the depletion of translation factors from nuclei...
  2. pmc NDC1: a crucial membrane-integral nucleoporin of metazoan nuclear pore complexes
    Fabrizia Stavru
    Zentrum fur Molekulare Biologie der Universitat Heidelberg, D 69120 Heidelberg, Germany
    J Cell Biol 173:509-19. 2006
    ..Instead, homozygous NDC1-deficient worms can be propagated. This indicates that none of the membrane-integral Nups is universally essential for NPC assembly, and suggests that NPC biogenesis is an extremely fault-tolerant process...
  3. pmc Nuclear pore complex assembly and maintenance in POM121- and gp210-deficient cells
    Fabrizia Stavru
    Zentrum fur Molekulare Biologie der Universitat Heidelberg, D 69120 Heidelberg, Germany
    J Cell Biol 173:477-83. 2006
    ..In Stavru et al., we describe such an additional transmembrane nucleoporin as the metazoan orthologue of yeast Ndc1p...
  4. pmc Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation
    Dirk Gorlich
    ZMBH, INF 282, 69120 Heidelberg, Germany
    EMBO J 22:1088-100. 2003
    ..This indicates that RanGTP gradients can provide positional information for mitotic spindle and NE assembly in early embryonic cells, but hardly any in small somatic cells...
  5. pmc The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    Katharina Ribbeck
    ZMBH, INF 282, D 69120 Heidelberg, Germany
    EMBO J 21:2664-71. 2002
    ....
  6. pmc Exportin 7 defines a novel general nuclear export pathway
    José Manuel Mingot
    ZMBH, INF 282, Heidelberg, Germany
    EMBO J 23:3227-36. 2004
    ..Second, basic residues are critical for Exp7 recruitment...
  7. pmc Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes
    Theis Stüven
    ZMBH, INF 282, D 69120 Heidelberg and Universität Lübeck, Ratzeburger Allee 160, D 23538 Lubeck, Germany
    EMBO J 22:5928-40. 2003
    ..In contrast to a previous report, we found no indications of a major and direct role for CRM1 in actin export from mammalian or insect nuclei...
  8. ncbi FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
    Steffen Frey
    Zentrum für Molekulare Biologie der Universität Heidelberg ZMBH, INF 282, D 69120 Heidelberg, Germany
    Science 314:815-7. 2006
    ..Furthermore, we obtained evidence that such hydrogel formation is required for viability in yeast...
  9. ncbi A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes
    Markus T Bohnsack
    Zentrum für Molekulare Biologie der Universität Heidelberg ZMBH, INF 282, D 69120 Heidelberg, Germany
    Nat Cell Biol 8:257-63. 2006
    ..Apparently, their mechanical integrity cannot be maintained by chromatin and the associated nuclear matrix, but instead requires an intranuclear actin-scaffold...
  10. pmc Characterisation of the passive permeability barrier of nuclear pore complexes
    Dagmar Mohr
    ZMBH, Im Neuenheimer Feld 282, Heidelberg, Germany
    EMBO J 28:2541-53. 2009
    ..This suggests that passive and facilitated NPC passage proceed through one and the same permeability barrier...
  11. pmc Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains
    Stefan Jäkel
    ZMBH, INF 282, D 69120 Heidelberg, Germany
    EMBO J 21:377-86. 2002
    ..Thus, just as heat shock proteins function as chaperones for exposed hydrophobic patches, importins act as chaperones for exposed basic domains, and we suggest that this represents a major and general cellular function of importins...