Cynthia Stauffacher Publications

Journal

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.

Zhang, M., Stauffacher, C. V., Lin, D., Van Etten, R. L. 1998. Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. Implications for substrate specificity. J Biol Chem. 273: 21714-21720.

Bochar, D. A., Brown, J. R., Doolittle, W. F., Klenk, H. P., Lam, W., Schenk, M. E., Stauffacher, C. V., Rodwell, V. W. 1997. 3-hydroxy-3-methylglutaryl coenzyme A reductase of Sulfolobus solfataricus: DNA sequence, phylogeny, expression in Escherichia coli of the hmgA gene, and purification and kinetic characterization of the gene product. J Bacteriol. 179: 3632-3638.

Deringer, J. R., Ely, R. J., Monday, S. R., Stauffacher, C. V., Bohach, G. A. 1997. Vbeta-dependent stimulation of bovine and human T cells by host-specific staphylococcal enterotoxins. Infect Immun. 65: 4048-4054.

Edwards, V. M., Deringer, J. R., Callantine, S. D., Deobald, C. F., Berger, P. H., Kapur, V., Stauffacher, C. V., Bohach, G. A. 1997. Characterization of the canine type C enterotoxin produced by Staphylococcus intermedius pyoderma isolates. Infect Immun. 65: 2346-2352.

Elkins, P., Bunker, A., Cramer, W. A., Stauffacher, C. V. 1997. A mechanism for toxin insertion into membranes is suggested by the crystal structure of the channel-forming domain of colicin E1. Structure. 5: 443-458.

Zhang, M., Zhou, M., Van Etten, R. L., Stauffacher, C. V. 1997. Crystal structure of bovine low molecular weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate. Biochemistry. 36: 15-23.

Bohach, G. A., Stauffacher, C. V., Ohlendorf, D. H., Chi, Y. I., Vath, G. M., Schlievert, P. M. 1996. The staphylococcal and streptococcal pyrogenic toxin family. Adv Exp Med Biol. 391: 131-154.

Deringer, J. R., Ely, R. J., Stauffacher, C. V., Bohach, G. A. 1996. Subtype-specific interactions of type C staphylococcal enterotoxins with the T-cell receptor. Mol Microbiol. 22: 523-534.

Fields, B. A., Malchiodi, E. L., Li, H., Ysern, X., Stauffacher, C. V., Schlievert, P. M., Karjalainen, K., Mariuzza, R. A. 1996. Crystal structure of a T-cell receptor beta-chain complexed with a superantigen. Nature. 384: 188-192.

Friesen, J. A., Lawrence, C. M., Stauffacher, C. V., Rodwell, V. W. 1996. Structural determinants of nucleotide coenzyme specificity in the distinctive dinucleotide binding fold of HMG-CoA reductase from Pseudomonas mevalonii. Biochemistry. 35: 11945-11950.

Cramer, W. A., Heymann, J. B., Schendel, S. L., Deriy, B. N., Cohen, F. S., Elkins, P. A., Stauffacher, C. V. 1995. Structure-function of the channel-forming colicins. Annu Rev Biophys Biomol Struct. 24: 611-641.

Lawrence, C. M., Chi, Y. I., Rodwell, V. W., Stauffacher, C. V. 1995. Crystallization of HMG-CoA reductase from Pseudomonas mevalonii. Acta Crystallogr D Biol Crystallogr. 51: 386-389.

Lawrence, C. M., Rodwell, V. W., Stauffacher, C. V. 1995. Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at 3.0 angstrom resolution. Science. 268: 1758-1762.

Schlievert, P. M., Bohach, G. A., Ohlendorf, D. H., Stauffacher, C. V., Leung, D. Y., Murray, D. L., Prasad, G. S., Earhart, C. A., Jablonski, L. M., Hoffmann, M. L., Chi, Y. I. 1995. Molecular structure of staphylococcus and streptococcus superantigens. J Clin Immunol. 15: 4S-10S.

Elkins, P. A., Song, H. Y., Cramer, W. A., Stauffacher, C. V. 1994. Crystallization and characterization of colicin E1 channel-forming polypeptides. Proteins. 19: 150-157.

Hoffmann, M. L., Jablonski, L. M., Crum, K. K., Hackett, S. P., Chi, Y. I., Stauffacher, C. V., Stevens, D. L., Bohach, G. A. 1994. Predictions of T-cell receptor- and major histocompatibility complex-binding sites on staphylococcal enterotoxin C1. Infect Immun. 62: 3396-3407.

Hovde, C. J., Marr, J. C., Hoffmann, M. L., Hackett, S. P., Chi, Y. I., Crum, K. K., Stevens, D. L., Stauffacher, C. V., Bohach, G. A. 1994. Investigation of the role of the disulphide bond in the activity and structure of staphylococcal enterotoxin C1. Mol Microbiol. 13: 897-909.

Jardetzky, T. S., Brown, J. H., Gorga, J. C., Stern, L. J., Urban, R. G., Chi, Y. I., Stauffacher, C., Strominger, J. L., Wiley, D. C. 1994. Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen. Nature. 368: 711-718.

Zhang, M., Van Etten, R. L., Lawrence, C. M., Stauffacher, C. V. 1994. Crystallization and preliminary X-ray analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart. J Mol Biol. 238: 281-283.

Zhang, M., Van Etten, R. L., Stauffacher, C. V. 1994. Crystal structure of bovine heart phosphotyrosyl phosphatase at 2.2-A resolution. Biochemistry. 33: 11097-11105.

Bohach, G. A., Chi, Y. I., Stauffacher, C. V. 1992. Crystallization and preliminary X-ray diffraction analysis of staphylococcal enterotoxin type C. Proteins. 13: 152-157.

Cramer, W. A., Zhang, Y. L., Schendel, S., Merrill, A. R., Song, H. Y., Stauffacher, C. V., Cohen, F. S. 1992. Dynamic properties of the colicin E1 ion channel. FEMS Microbiol Immunol. 5: 71-81.

Chen, Z, Stauffacher, C. V., Johnson, J. E. 1990. Capsid structure and RNA packaging in comoviruses. Seminars in Virology. 1: 453-466.

Chen, Z. G., Stauffacher, C., Li, Y., Schmidt, T., Bomu, W., Kamer, G., Shanks, M., Lomonossoff, G., Johnson, J. E. 1989. Protein-RNA interactions in an icosahedral virus at 3.0 A resolution. Science. 245: 154-159.

Weisel, J. W., Stauffacher, C. V., Bullitt, E., Cohen, C. 1985. A model for fibrinogen: domains and sequence. Science. 230: 1388-1391.

Cohen, C., Weisel, J. W., Phillips, G. N., Jr., Stauffacher, C. V., Fillers, J. P., Daub, E. 1983. The structure of fibrinogen and fibrin: I. Electron microscopy and X-ray crystallography of fibrinogen. Ann N Y Acad Sci. 408: 194-213.

Stubbs, G., Stauffacher, C. 1981. Structure of the RNA in tobacco mosaic virus. J Mol Biol. 152: 387-396.

 



Purdue University Biological Sciences, 915 W. State Street, West Lafayette, IN 47907

Main Office: (765) 494-4408   Business Office: (765) 494-4764  Contact Us

© 2015 Purdue University | An equal access/equal opportunity university | Copyright Complaints

Trouble with this page? Disability-related accessibility issue? Please contact the College of Science Webmaster.

Maintained by Science IT