Publications of D. Görlich
All genres
Journal Article (76)
61.
Journal Article
39 (38), pp. 11629 - 11639 (2000)
Different structural and kinetic requirements for the interaction of Ran with the Ran-binding domains from RanBP2 and importin-β. Biochemistry 62.
Journal Article
10 (8), pp. 467 - 470 (2000)
Acetylation of importin-α nuclear import factors by CBP/p300. Current Biology 63.
Journal Article
6 (1), pp. 136 - 158 (2000)
The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates. RNA 64.
Journal Article
19 (11), pp. 7782 - 7791 (1999)
Evidence for distinct substrate specificities of importin α family members in nuclear protein import. Molecular and Cellular Biology 65.
Journal Article
17 (10), pp. 2721 - 2727 (1998)
Transport into and out of the cell nucleus. The EMBO Journal 66.
Journal Article
16 (20), pp. 6237 - 6249 (1997)
Yrb4p, a yeast Ran–GTP‐binding protein involved in import of ribosomal protein L25 into the nucleus. The EMBO Journal 67.
Journal Article
17 (9), pp. 5087 - 5096 (1997)
Ran-binding protein 5 (RanBP5) is related to the nuclear transport factor importin-beta but interacts differently with RanBP1. Molecular and Cellular Biology 68.
Journal Article
24 (17), pp. 3332 - 03336 (1996)
A yeast cap binding protein complex (yCBC) acts at an early step in pre-mRNA splicing. Nucleic Acids Research 69.
Journal Article
362 (2), pp. 126 - 130 (1995)
The Sec61 complex is essential for the insertion of proteins into the membrane of the endoplasmic reticulum. FEBS Letters 70.
Journal Article
126 (4), pp. 925 - 934 (1994)
Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex. The Journal of Cell Biology 71.
Journal Article
268 (35), pp. 26745 - 26751 (1993)
Site-specific photocross-linking reveals that Sec61p and TRAM contact different regions of a membrane-inserted signal sequence. The Journal of Biological Chemistry 72.
Journal Article
214 (2), pp. 375 - 381 (1993)
A tetrameric complex of membrane proteins in the endoplasmic reticulum. European Journal of Biochemistry 73.
Journal Article
121 (4), pp. 743 - 750 (1993)
Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion. The Journal of Cell Biology 74.
Journal Article
113 (1), pp. 35 - 44 (1991)
The identification of proteins in the proximity of signal-anchor sequences during their targeting to and insertion into the membrane of the ER. The Journal of Cell Biology 75.
Journal Article
53 (2), pp. 197 - 202 (1990)
Segregation of the signal sequence receptor protein in the rough endoplasmic reticulum membrane. European Journal of Cell Biology 76.
Journal Article
257 (2), pp. 263 - 268 (1989)
Photocrosslinking demonstrates proximity of a 34 kDa membrane protein to different portions of preprolactin during translocation through the endoplasmic reticulum. FEBS Letters Book Chapter (1)
77.
Book Chapter
Nucleocytoplasmic transport. In: Protein targeting, transport, and translocation, pp. 293 - 321 (Ed. Dalbey, R. E.). Acad. Pr., Amsterdam (2002)
Conference Paper (7)
78.
Conference Paper
48 (Suppl 1), p. S228 - S228 (2019)
Mechanical characterization of phase separated nucleoporin droplets using Atomic Force Microscopy techniques. Joint 12th EBSA European Biophysics Congress / 10th IUPAP International Conference on Biological Physics (ICBP), Madrid, Spain, July 20, 2019 - July 24, 2019. European Biophysics Journal 79.
Conference Paper
48 (Suppl 1), p. S227 - S227 (2019)
Recapitulation of nucleocytoplasmic transport with phase-separation of engineered protein repeats. Joint 12th EBSA European Biophysics Congress / 10th IUPAP International Conference on Biological Physics (ICBP), Madrid, Spain, July 20, 2019 - July 24, 2019. European Biophysics Journal 80.
Conference Paper
46 (Suppl_1), p. S328 - S328 (2017)
Mechanical characterization of phase separated FG particles using Atomic Force Microscopy techniques. 19th IUPAB Congress / 11th EBSA Congress, Edinburgh, Scotland, July 16, 2017 - July 20, 2017. European Biophysics Journal