scispace - formally typeset
M

Michael D. Schaber

Researcher at GlaxoSmithKline

Publications -  37
Citations -  3981

Michael D. Schaber is an academic researcher from GlaxoSmithKline. The author has contributed to research in topics: Farnesyltransferase & GTPase-activating protein. The author has an hindex of 26, co-authored 37 publications receiving 3850 citations. Previous affiliations of Michael D. Schaber include University of Pennsylvania & Merck & Co..

Papers
More filters
Journal ArticleDOI

Cloning of bovine GAP and its interaction with oncogenic ras p21

TL;DR: It is shown that GAP interacts preferentially with the active GTP complexes of both normal and oncogenic Harvey (Ha) ras p21 compared with the inactive GDP complexes.
Journal ArticleDOI

Sequence dependence of protein isoprenylation

TL;DR: Three different isoprenyl-protein transferases are identified that are each selective for theirIsoprenoid and protein substrates, and a leucine residue at the C terminus influenced whether a CAAX protein was either farnesylated or geranylgeranylated preferentially.
Journal ArticleDOI

Demonstration of a Genetic Therapeutic Index for Tumors Expressing Oncogenic BRAF by the Kinase Inhibitor SB-590885

TL;DR: The characterization of SB-590885 is reported, a novel triarylimidazole that selectively inhibits Raf kinases with more potency towards B-Raf than c-Rafa, and provides the first evidence of a correlation between the expression of oncogenic BRAF alleles and a positive response to a selective B- Raf inhibitor.
Journal ArticleDOI

Steady-state kinetic mechanism of Ras farnesyl:protein transferase.

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.
Journal ArticleDOI

Purification of ras GTPase activating protein from bovine brain

TL;DR: In cytosolic extracts of bovine brain, ras GTPase activating protein (GAP) activity that stimulated the GTP hydrolytic activity of normal c-Ha-ras p21 but not that of the oncogenic [Val12]p21 variant.