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Kutay, U.; Izaurralde, E.; Bischoff, F. R.; Mattaj, I. W.; Görlich, D.: Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex. The EMBO Journal 16 (6), pp. 1153 - 1163 (1997)

Kutay, U.; Izaurralde, E.; Bischoff, F. R.; Mattaj, I. W.; Görlich, D.: Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex. The EMBO Journal 16 (6), pp. 1153 - 1163 (1997)

Görlich, D.; Pante, N.; Kutay, U.; Aebi, U.; Bischoff, F. R.: Identification of different roles for RanGDP and RanGTP in nuclear protein import. The EMBO Journal 15 (20), pp. 5584 - 5595 (1996)

Görlich, D.; Kraft, R.; Kostka, S.; Vogel, F.; Hartmann, E.; Laskey, R. A.; Mattaj, I. W.; Izaurralde, E.: Importin provides a link between nuclear protein import and U snRNA export. Cell 87, pp. 21 - 32 (1996)

Görlich, D.; Henklein, P.; Laskey, R. A.; Hartmann, E.: A 41 amino acid motif in importin-alpha confers binding to importin-beta and hence transit into the nucleus. The EMBO Journal 15 (8), pp. 1810 - 1817 (1996)

Görlich, D.; Mattaj, I. W.: Nucleocytoplasmic transport. Science 271 (5255), pp. 1513 - 1518 (1996)

Lewis, J. D.; Görlich, D.; Mattaj, I. W.: A yeast cap binding protein complex (yCBC) acts at an early step in pre-mRNA splicing. Nucleic Acids Research 24 (17), pp. 3332 - 03336 (1996)

Görlich, D.; Vogel, F.; Mills, A. D.; Hartmann, E.; Laskey, R. A.: Distinct functions for the two importin subunits in nuclear protein import. Nature 377 (6546), pp. 246 - 248 (1995)

Hartmann, E.; Görlich, D.: A ran-binding motif in nuclear pore proteins. Trends in Cell Biology 5 (5), pp. 192 - 193 (1995)

Oliver, J.; Jungnickel, B.; Görlich, D.; Rapoport, T. A.; High, S.: The Sec61 complex is essential for the insertion of proteins into the membrane of the endoplasmic reticulum. FEBS Letters 362 (2), pp. 126 - 130 (1995)

Görlich, D.; Kostka, S.; Kraft, R.; Dingwall, C.; Laskey, R. A.; Hartmann, E.; Prehn, S.: Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope. Current Biology 5 (4), pp. 383 - 392 (1995)

Görlich, D.; Prehn, S.; Laskey, R. A.; Hartmann, E.: Isolation of a protein that is essential for the first step of nuclear protein import. Cell 79 (5), pp. 767 - 778 (1994)

Kalies, K. U.; Görlich, D.; Rapoport, T. A.: Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex. The Journal of Cell Biology 126 (4), pp. 925 - 934 (1994)

Hartmann, E.; Sommer, T.; Prehn, S.; Görlich, D.; Jentsch, S.; Rapoport, T. A.: Evolutionary conservation of components of the protein translocation complex. Nature 367 (6464), pp. 654 - 657 (1994)

High, S.; Martoglio, B.; Görlich, D.; Andersen, S. S.; Ashford, A. J.; Giner, A.; Hartmann, E.; Prehn, S.; Rapoport, T. A.; Dobberstein, B.: Site-specific photocross-linking reveals that Sec61p and TRAM contact different regions of a membrane-inserted signal sequence. The Journal of Biological Chemistry 268 (35), pp. 26745 - 26751 (1993)

Görlich, D.; Rapoport, T. A.: Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75 (4), pp. 615 - 630 (1993)

Hartmann, E.; Görlich, D.; Kostka, S.; Otto, A.; Kraft, R.; Knespel, S.; Bürger, E.; Rapoport, T. A.; Prehn, S.: A tetrameric complex of membrane proteins in the endoplasmic reticulum. European Journal of Biochemistry 214 (2), pp. 375 - 381 (1993)

High, S.; Andersen, S. S.; Görlich, D.; Hartmann, E.; Prehn, S.; Rapoport, T. A.; Dobberstein, B.: Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion. The Journal of Cell Biology 121 (4), pp. 743 - 750 (1993)

Görlich, D.; Prehn, S.; Hartmann, E.; Kalies, K. U.; Rapoport, T. A.: A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation. Cell 71 (3), pp. 489 - 503 (1992)

Görlich, D.; Hartmann, E.; Prehn, S.; Rapoport, T. A.: A protein of the endoplasmic reticulum involved early in polypeptide translocation. Nature 357 (6373), pp. 47 - 52 (1992)