The Hepatitis Delta Virus Large Antigen Is Farnesylated Both in Vitro and in Animal Cells
Open Access
- 1 March 1996
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 271 (9) , 4569-4572
- https://doi.org/10.1074/jbc.271.9.4569
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- THE MOLECULAR BIOLOGY OF HEPATITIS DELTA VIRUSAnnual Review of Biochemistry, 1995
- Role of Protein Modification Reactions in Programming Interactions Between Ras-Related GTPases and Cell MembranesAnnual Review of Cell Biology, 1994
- Inhibitors of ras farnesyltransferasesTrends in Biochemical Sciences, 1993
- Benzodiazepine Peptidomimetics: Potent Inhibitors of Ras Farnesylation In Animal CellsScience, 1993
- Identification of a Prenylation Site in Delta Virus Large AntigenScience, 1992
- Immunoblot analysis demonstrates that the large and small forms of hepatitis delta virus antigen have different C-terminal amino acid sequencesJournal of General Virology, 1992
- Structural characterization of prenyl groups attached to proteinsMethods, 1990
- A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membraneCell, 1990
- Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptidesCell, 1990
- The Delta AgentHepatology, 1983