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Mol. Cell. Biol. 27, 7735–7744. Restricting conformational flexibility of the switch II region creates a dominant-inhibitory phenotype in Obg GTPase Nog1. 2007

Lapik, Y.R., Misra, J.M., Lau, L.F. and Pestov, D.G.

Notes: The authors show that substitution of alanine for the conserved glycine 224 of Nog1, a eukaryotic GTPase, disrupts assembly of pre-60S ribosome subunits but does not significantly affect GTP binding. Amino acids 1–357 of Nog1 (Nog1NG) were expressed with an N-terminal biotinylated tag in E. coli, then purified using the SoftLink™ Soft Release Avidin Resin. The resin was incubated with the cleared lysate for 2 hours with mixing and washed with B300 buffer (25mM Tris-HCl [pH7.4], 10mM MgOAc2, 10% glycerol, 0.05% Brij 30, 1mM dithiothreitol, 300mM KOAc) and B1000 buffer (25mM Tris-HCl [pH7.4], 10mM MgOAc2, 10% glycerol, 0.05% Brij 30, 1mM dithiothreitol, 1M KOAc). Purified protein was eluted with B300 buffer containing 5mM biotin, and the protein was concentrated and biotin removed by ultracentrifugation. The protein was estimated to be 95% pure by SDS-PAGE. GTP-binding assays were performed by UV cross-linking purified Nog1NG and [α-32P]-GTP, recovering the protein by binding to SAM2 Biotin Capture Membrane and quantifying the amount of GTP bound using a Phosphorimager. (3804)

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Mol. Cell. Biol. 26, 6082-6093. Kinase domain mutants of Bcr-Abl exhibit altered transformation potency, kinase activity, and substrate utilization irrespective of sensitivity to imatinib. 2006

Griswold, I., MacPartlin, M., Bumm, T., Goss, V.L., O'Hare, T., Lee, K.A., Corbin, A.S., Stoffregen, E.P., Smith, C., Johnson, K., Moseson, E.M., Wood, L.J., Polakiewicz, R.D., Druker, B.J., and Deininger, M.W.

Notes: The authors compared the transformation potency of five Bcr-Abl kinase domain mutants. They found reproducible differences in the transformation potency of these five mutants, and they investigated whether these potencies could be explained by changes in kinase activity by performing in vitro kinase assays using a biotinylated peptide substrate. Assays were carried out using varying peptide substrate concentrations. The reactions were stopped, and aliquots of each reaction were transferred to the SAM Biotin Capture Membrane. Membranes were dried and phosphate incorporation was determined by scintillation counting. (3505)

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Cancer Res. 65, 4500-4505. In vitro activity of Bcr-Abl inhibitors AMN107 and BMS-354825 against clinically relevant Imatinib-resistant Abl kinase domain mutants. 2005

O'Hare, T., Walters, D.K., Stoffregen, E.P., Jia, T., Manley, P.W., Mestan, J., Cowan-Jacob, S.W., Lee, F.Y., Heinrich, M.C., Deininger, M.W.N. and Druker, B.J.

Notes: Ba/F3 cells were transfected with constructs encoding either wildtype or mutant (Imatinib-resistant) Bcr-Abl kinase. Src-family kinase activity was assayed using the SignaTECT® Protein Tyrosine Kinase Peptide 2 and SAM Biotin Capture Membranes. Cell viability was measured using the CellTiter 96® AQueous One Solution Cell Proliferation Assay. (3405)

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J. Biol. Chem. 280, 1521-1528. RGS12 Interacts with the SNARE-binding region of the Cav2.2 calcium channel. 2005

Richman, R.W., Strock, J., Hains, M.D., Cabanilla, N.J., Lau, K-K., Siderovski, D.P. and Diversé-Pierluissi, M.

Notes: Voltage-dependent and independent events regulate the activation of the Cav2.2 calcium channel in dorsal root ganglion neurons (DRG). The authors of this study synthesized a biotinylated tyrosine-containing peptide capable of crossing cell membranes. DRG neurons were treated in the presence of this peptide and then lysed. The lysates were applied to a SAM2 Biotin Capture Membrane to capture the biotinylated peptide, and tyrosine phosphorylation was measured. (3547)

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Biochemistry 37, 9827-9835. Implication of DNA-dependent protein kinase in an early, essential, local phosphorylation event during end-joining of DNA double-strand breaks in vitro. 1998

Gu, X.-Y., Weinfeld, M.A., Povirk, L.F.

Notes: The ability of wortmannin to inhibit DNA-dependent phosphorylation was determined with the SignaTECT® DNA-PK Assay System. Rather than counting the individual SAM Membrane squares, the authors exposed the membrane to film for a graphic display of the inhibition. (1081)

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