Distinct Regions Specify the Targeting of Otefin to the Nucleoplasmic Side of the Nuclear Envelope
Open Access
- 1 January 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (4) , 2493-2499
- https://doi.org/10.1074/jbc.272.4.2493
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane.The Journal of cell biology, 1995
- Analysis of nuclear lamin isoprenylation in Xenopus oocytes: isoprenylation of lamin B3 precedes its uptake into the nucleus.The Journal of cell biology, 1995
- The role of CaaX-dependent modifications in membrane association of Xenopus nuclear lamin B3 during meiosis and the fate of B3 in transfected mitotic cells.The Journal of cell biology, 1993
- The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal.The Journal of cell biology, 1993
- The first membrane spanning region of the lamin B receptor is sufficient for sorting to the inner nuclear membrane.The Journal of cell biology, 1993
- Targeting lamin proteins to the nuclear envelope: the role of CaaX box modificationsBiochemical Society Transactions, 1992
- The nuclear envelope and nuclear transportCurrent Opinion in Cell Biology, 1990
- The nuclear envelopeCurrent Opinion in Cell Biology, 1989
- Functional Organization of the Nuclear EnvelopeAnnual Review of Cell Biology, 1988
- Studies on the Cytoplasmic Organization of Early Drosophila EmbryosCold Spring Harbor Symposia on Quantitative Biology, 1985