J
Jackson B. Gibbs
Researcher at United States Military Academy
Publications - 117
Citations - 12704
Jackson B. Gibbs is an academic researcher from United States Military Academy. The author has contributed to research in topics: Farnesyl Protein Transferase & Farnesyltransferase. The author has an hindex of 55, co-authored 117 publications receiving 12547 citations. Previous affiliations of Jackson B. Gibbs include Merck & Co. & Duke University.
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Dominant inhibitory Ras mutants demonstrate the requirement for Ras activity in the action of tyrosine kinase oncogenes.
Dennis W. Stacey,Margaret Roudebush,Regina M. Day,Scott D. Mosser,Jackson B. Gibbs,Larry A. Feig +5 more
TL;DR: Results with all three reagents clearly indicate that cellular Ras activity is required in the late G1 phase of the cell cycle and is essential for the maintenance of the transformed phenotype induced by tyrosine but not serine kinase oncogenes.
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cDNA cloning and expression of rat and human protein geranylgeranyltransferase type-I.
Fang L. Zhang,R E Diehl,Nancy E. Kohl,Jackson B. Gibbs,Bruno Giros,Patrick J. Casey,C A Omer +6 more
TL;DR: Amo acid sequence comparison suggests that the protein encoded by the Saccharomyces cerevisiae gene CDC43 is the yeast counterpart of the mammalian GGTase-I beta subunit.
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Isolation and structure of chaetomellic acids A and B from Chaetomella acutiseta: farnesyl pyrophosphate mimic inhibitors of ras farnesyl-protein transferase
Suresh B. Singh,Deborah L. Zink,Jerrold M. Liesch,Michael A. Goetz,Rosalind G. Jenkins,Mary Nallin-Omstead,Keith C. Silverman,Gerald F. Bills,Ralph T. Mosley,Jackson B. Gibbs,Georg Albers-Schönberg,Russell B. Lingham +11 more
TL;DR: Two novel dicarboxylic acids, named chaetomellic acids from Chaetomella acutiseta, are isolated as potent and selective inhibitors which appear to be the first examples of nonphosphorous containing FPP mimics.
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Isoprenoid diphosphate utilization by recombinant human farnesyl:protein transferase: interactive binding between substrates and a preferred kinetic pathway.
David L. Pompliano,Michael D. Schaber,Scott D. Mosser,Charles A. Omer,Jules A. Shafer,Jackson B. Gibbs +5 more
TL;DR: Isotope partitioning studies showed that, at high concentrations of Ras-CVIM, more than 80% of the bound farnesyl diphosphate (FPP) can be trapped as product, suggesting that the binary complex is catalytically competent and that the ternary complex proceeds to product faster than it releases FPP.
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Farnesyltransferase inhibitors versus Ras inhibitors
Jackson B. Gibbs,Samuel L. Graham,George D. Hartman,Kenneth S. Koblan,Nancy E. Kohl,Charles A. Omer,Oliff Allen I +6 more
TL;DR: It now seems likely that the ability of FPTase inhibitors to reverse the malignant phenotype results, at least in part, from inhibiting the farnesylation of proteins other than Ras.