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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Journal ArticleDOI
Lung Cancer Cell Lines Harboring MET Gene Amplification Are Dependent on Met for Growth and Survival
Bart Lutterbach,Qinwen Zeng,Lenora Davis,Harold Hatch,Gaozhen Hang,Nancy E. Kohl,Jackson B. Gibbs,Bo-Sheng Pan +7 more
TL;DR: The results strongly suggest that Met amplification identifies a subset of NSCLC likely to respond to new molecular therapies targeting Met, which is implicated in growth, invasion, and metastasis of many tumors includingNSCLC.
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S. cerevisiae genes IRA1 and IRA2 encode proteins that may be functionally equivalent to mammalian ras GTPase activating protein
Kazuma Tanaka,Masato Nakafuku,Takaya Satoh,Mark S. Marshall,Jackson B. Gibbs,Kunihiro Matsumoto,Yoshito Kaziro,Akio Toh-e,Akio Toh-e +8 more
TL;DR: Overexpression of bovine GAP suppressed the phenotypes of ira mutants by reducing the level of RAS-GTP, suggesting that IRA proteins may be functionally analogous to mammalian GAP.
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Modulation of guanine nucleotides bound to Ras in NIH3T3 cells by oncogenes, growth factors, and the GTPase activating protein (GAP).
TL;DR: Results indicate that PDGF receptor activation and tyrosine kinase-encoding oncogene products can stimulate Ras into the GTP complex and that GAP in intact mammalian cells can decrease the amount of GTP complexes complexed to Ras.
Journal ArticleDOI
Selective inhibition of farnesyl-protein transferase blocks ras processing in vivo.
Jackson B. Gibbs,David L. Pompliano,Scott D. Mosser,Rands E,Russell B. Lingham,Sheo B. Singh,Edward M. Scolnick,Nancy E. Kohl,Oliff Allen I +8 more
TL;DR: These results are the first demonstration that a small organic chemical selected for inhibition of FPTase can inhibit Ras processing in vivo.
Journal ArticleDOI
Steady-state kinetic mechanism of Ras farnesyl:protein transferase.
David L. Pompliano,Elaine Rands,Michael D. Schaber,Scott D. Mosser,Neville J. Anthony,Jackson B. Gibbs +5 more
TL;DR: It is concluded that bovine brain FPTase proceeds through a random order sequential mechanism, and four nonsubstrate tetrapeptides were all shown to be noncompetitive inhibitors of farnesyl diphosphate and competitive inhibitors of Ras-CVLS, consistent with random order of substrate addition.