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Ph.D., UCLA, 1977

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Steussy, C. N., Robison, A. D., Tetrick, A. M., Knight, J. T., Rodwell, V. W., Stauffacher, C. V., Sutherlin, A. L. 2006. A structural limitation on enzyme activity: the case of HMG-CoA synthase. Biochemistry. 45: 14407-14414. Zabell, A. P., Schroff, A. D., Jr., Bain, B. E., Van Etten, R. L., Wiest, O., Stauffacher, C. V. 2006. Crystal structure of the human B-form low molecular weight phosphotyrosyl phosphatase at 1.6-A resolution. J Biol Chem. 281: 6520-6527. Zabell, K. M., Laurence, J. S., Kinch, M. S., Knapp, D. W., Stauffacher, C. V. 2006. Expression and purification of the intact cytoplasmic domain of the human ephrin receptor A2 tyrosine kinase in Escherichia coli. Protein Expr Purif. 47: 210-216. Gustafson, C. L., Stauffacher, C. V., Hallenga, K., Van Etten, R. L. 2005. Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop. Protein Sci. 14: 2515-2525. Steussy, C. N., Vartia, A. A., Burgner, J. W., 2nd, Sutherlin, A., Rodwell, V. W., Stauffacher, C. V. 2005. X-ray crystal structures of HMG-CoA synthase from Enterococcus faecalis and a complex with its second substrate/inhibitor acetoacetyl-CoA. Biochemistry. 44: 14256-14267. Hedl, M., Tabernero, L., Stauffacher, C. V., Rodwell, V. W. 2004. Class II 3-hydroxy-3-methylglutaryl coenzyme A reductases. J Bacteriol. 186: 1927-1932. Laurence, J. S., Hallenga, K., Stauffacher, C. V. 2004. 1H, 15N, 13C resonance assignments of the human protein tyrosine phosphatase PRL-1. J Biomol NMR. 29: 417-418. Zabell, A. P., Corden, S., Helquist, P., Stauffacher, C. V., Wiest, O. 2004. Inhibition studies with rationally designed inhibitors of the human low molecular weight protein tyrosine phosphatase. Bioorg Med Chem. 12: 1867-1880. Fujita, T., Maggio, A., Garcia-Rios, M., Stauffacher, C., Bressan, R. A., Csonka, L. N. 2003. Identification of regions of the tomato gamma-glutamyl kinase that are involved in allosteric regulation by proline. J Biol Chem. 278: 14203-14210. Tabernero, L., Rodwell, V. W., Stauffacher, C. V. 2003. Crystal structure of a statin bound to a class II hydroxymethylglutaryl-CoA reductase. J Biol Chem. 278: 19933-19938. Chi, Y. I., Sadler, I., Jablonski, L. M., Callantine, S. D., Deobald, C. F., Stauffacher, C. V., Bohach, G. A. 2002. Zinc-mediated dimerization and its effect on activity and conformation of staphylococcal enterotoxin type C. J Biol Chem. 277: 22839-22846. Hedl, M., Sutherlin, A., Wilding, E. I., Mazzulla, M., McDevitt, D., Lane, P., Burgner, J. W., 2nd, Lehnbeuter, K. R., Stauffacher, C. V., Gwynn, M. N., Rodwell, V. W. 2002. Enterococcus faecalis acetoacetyl-coenzyme A thiolase/3-hydroxy-3-methylglutaryl-coenzyme A reductase, a dual-function protein of isopentenyl diphosphate biosynthesis. J Bacteriol. 184: 2116-2122. Sutherlin, A., Hedl, M., Sanchez-Neri, B., Burgner, J. W., 2nd, Stauffacher, C. V., Rodwell, V. W. 2002. Enterococcus faecalis 3-hydroxy-3-methylglutaryl coenzyme A synthase, an enzyme of isopentenyl diphosphate biosynthesis. J Bacteriol. 184: 4065-4070. Kim, D. Y., Stauffacher, C. V., Rodwell, V. W. 2000. Dual coenzyme specificity of Archaeoglobus fulgidus HMG-CoA reductase. Protein Sci. 9: 1226-1234. Kim, D. Y., Stauffacher, C. V., Rodwell, V. W. 2000. Engineering of Sulfolobus solfataricus HMG-CoA reductase to a form whose activity is regulated by phosphorylation and dephosphorylation. Biochemistry. 39: 2269-2275. Wang, S., Stauffacher, C. V., Van Etten, R. L. 2000. Structural and mechanistic basis for the activation of a low-molecular weight protein tyrosine phosphatase by adenine. Biochemistry. 39: 1234-1242. Wang, S., Tabernero, L., Zhang, M., Harms, E., Van Etten, R. L., Stauffacher, C. V. 2000. Crystal structures of a low-molecular weight protein tyrosine phosphatase from Saccharomyces cerevisiae and its complex with the substrate p-nitrophenyl phosphate. Biochemistry. 39: 1903-1914. Wilding, E. I., Kim, D. Y., Bryant, A. P., Gwynn, M. N., Lunsford, R. D., McDevitt, D., Myers, J. E., Jr., Rosenberg, M., Sylvester, D., Stauffacher, C. V., Rodwell, V. W. 2000. Essentiality, expression, and characterization of the class II 3-hydroxy-3-methylglutaryl coenzyme A reductase of Staphylococcus aureus. J Bacteriol. 182: 5147-5152. Bochar, D. A., Stauffacher, C. V., Rodwell, V. W. 1999. Investigation of the conserved lysines of Syrian hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase. Biochemistry. 38: 15848-15852. Bochar, D. A., Stauffacher, C. V., Rodwell, V. W. 1999. Sequence comparisons reveal two classes of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mol Genet Metab. 66: 122-127. Bochar, D. A., Tabernero, L., Stauffacher, C. V., Rodwell, V. W. 1999. Aminoethylcysteine can replace the function of the essential active site lysine of Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase. Biochemistry. 38: 8879-8883. Kim, D. Y., Bochar, D. A., Stauffacher, C. V., Rodwell, V. W. 1999. Expression and characterization of the HMG-CoA reductase of the thermophilic archaeon Sulfolobus solfataricus. Protein Expr Purif. 17: 435-442. Lin, T., Chen, Z., Usha, R., Stauffacher, C. V., Dai, J. B., Schmidt, T., Johnson, J. E. 1999. The refined crystal structure of cowpea mosaic virus at 2.8 A resolution. Virology. 265: 20-34. Tabernero, L., Bochar, D. A., Rodwell, V. W., Stauffacher, C. V. 1999. Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase. Proc Natl Acad Sci U S A. 96: 7167-7171. Tabernero, L., Evans, B. N., Tishmack, P. A., Van Etten, R. L., Stauffacher, C. V. 1999. The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism. Biochemistry. 38: 11651-11658.

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