In Vitro Assay and Characterization of the Farnesylation-dependent Prelamin A Endoprotease
Open Access
- 1 February 1997
- journal article
- Published by Elsevier
- Vol. 272 (8) , 5298-5304
- https://doi.org/10.1074/jbc.272.8.5298
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Solubilization, Partial Purification, and Affinity Labeling of the Membrane-Bound Isoprenylated Protein EndoproteaseBiochemistry, 1996
- Binding of prenylated and polybasic peptides to membranes: affinities and intervesicle exchangeBiochemistry, 1995
- Characterization of Prenylcysteines That Interact with P-glycoprotein and Inhibit Drug Transport in Tumor CellsPublished by Elsevier ,1995
- Substrate specificity of the isoprenylated protein endoproteaseBiochemistry, 1992
- Assembly-disassembly of the nuclear laminaCurrent Opinion in Cell Biology, 1992
- Isoprenylation is required for the processing of the lamin A precursor.The Journal of cell biology, 1990
- Maturation of nuclear lamin A involves a specific carboxy‐terminal trimming, which removes the polyisoprenylation site from the precursor; implications for the structure of the nuclear laminaFEBS Letters, 1989
- Incorporation of a product of mevalonic acid metabolism into proteins of Chinese hamster ovary cell nuclei.The Journal of cell biology, 1988
- Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteinsNature, 1986
- Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphenylglycolurilBiochemical and Biophysical Research Communications, 1978