Carlson College of Veterinary Medicine

R. J. Suchland, Rockey, D. D., Bannantine, J. P., and Stamm, W. E., “Isolates of Chlamydia trachomatis that occupy nonfusogenic inclusions lack IncA, a protein localized to the inclusion membrane.”, Infect Immun, vol. 68, no. 1, pp. 360-7, 2000.

R. J. Suchland, Rockey, D. D., Bannantine, J. P., and Stamm, W. E., “Isolates of Chlamydia trachomatis that occupy nonfusogenic inclusions lack IncA, a protein localized to the inclusion membrane.”, Infection and immunity, vol. 68, no. 1, pp. 360-7, 2000.

T. Hackstadt, Scidmore, M. A., and Rockey, D. D., “Lipid metabolism in Chlamydia trachomatis-infected cells: directed trafficking of Golgi-derived sphingolipids to the chlamydial inclusion.”, Proc Natl Acad Sci U S A, vol. 92, no. 11, pp. 4877-81, 1995.

T. Hackstadt, Scidmore, M. A., and Rockey, D. D., “Lipid metabolism in Chlamydia trachomatis-infected cells: directed trafficking of Golgi-derived sphingolipids to the chlamydial inclusion.”, Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 11, pp. 4877-81, 1995.

X. Wang, Rockey, D. D., and Dolan, B. P., “Lipooligosaccharide Has Varied Direct and Indirect Roles in Evading both Innate and Adaptive Host Immune Responses.”, Infect Immun, vol. 88, no. 8, 2020.

Y. Yuan, Lyng, K., Zhang, Y. X., Rockey, D. D., and Morrison, R. P., “Monoclonal antibodies define genus-specific, species-specific, and cross-reactive epitopes of the chlamydial 60-kilodalton heat shock protein (hsp60): specific immunodetection and purification of chlamydial hsp60.”, Infect Immun, vol. 60, no. 6, pp. 2288-96, 1992.

Y. Yuan, Lyng, K., Zhang, Y. X., Rockey, D. D., and Morrison, R. P., “Monoclonal antibodies define genus-specific, species-specific, and cross-reactive epitopes of the chlamydial 60-kilodalton heat shock protein (hsp60): specific immunodetection and purification of chlamydial hsp60.”, Infection and immunity, vol. 60, no. 6, pp. 2288-96, 1992.

T. Hackstadt, Fischer, E. R., Scidmore, M. A., Rockey, D. D., and Heinzen, R. A., “Origins and functions of the chlamydial inclusion.”, Trends in microbiology, vol. 5, no. 7, pp. 288-93, 1997.

T. Hackstadt, Fischer, E. R., Scidmore, M. A., Rockey, D. D., and Heinzen, R. A., “Origins and functions of the chlamydial inclusion.”, Trends Microbiol, vol. 5, no. 7, pp. 288-93, 1997.

D. D. Rockey and Rosquist, J. L., “Protein antigens of Chlamydia psittaci present in infected cells but not detected in the infectious elementary body.”, Infect Immun, vol. 62, no. 1, pp. 106-12, 1994.

D. D. Rockey and Rosquist, J. L., “Protein antigens of Chlamydia psittaci present in infected cells but not detected in the infectious elementary body.”, Infection and immunity, vol. 62, no. 1, pp. 106-12, 1994.

D. D. Rockey, Scidmore, M. A., Bannantine, J. P., and Brown, W. J., “Proteins in the chlamydial inclusion membrane.”, Microbes and infection / Institut Pasteur, vol. 4, no. 3, pp. 333-40, 2002.

H. Su, Raymond, L., Rockey, D. D., Fischer, E., Hackstadt, T., and Caldwell, H. D., “A recombinant Chlamydia trachomatis major outer membrane protein binds to heparan sulfate receptors on epithelial cells.”, Proc Natl Acad Sci U S A, vol. 93, no. 20, pp. 11143-8, 1996.

H. Su, Raymond, L., Rockey, D. D., Fischer, E., Hackstadt, T., and Caldwell, H. D., “A recombinant Chlamydia trachomatis major outer membrane protein binds to heparan sulfate receptors on epithelial cells.”, Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 20, pp. 11143-8, 1996.

K. M. Sandoz, Eriksen, S. G., Jeffrey, B. M., Suchland, R. J., Putman, T. E., Hruby, D. E., Jordan, R., and Rockey, D. D., “Resistance to a novel antichlamydial compound is mediated through mutations in Chlamydia trachomatis secY.”, Antimicrobial agents and chemotherapy, 2012.

K. M. Sandoz, Eriksen, S. G., Jeffrey, B. M., Suchland, R. J., Putman, T. E., Hruby, D. E., Jordan, R., and Rockey, D. D., “Resistance to a Novel Antichlamydial Compound Is Mediated through Mutations in Chlamydia trachomatis secY.”, Antimicrobial agents and chemotherapy, vol. 56, no. 8, pp. 4296-302, 2012.

K. M. Sandoz, Eriksen, S. G., Jeffrey, B. M., Suchland, R. J., Putman, T. E., Hruby, D. E., Jordan, R., and Rockey, D. D., “Resistance to a novel antichlamydial compound is mediated through mutations in Chlamydia trachomatis secY.”, Antimicrob Agents Chemother, vol. 56, no. 8, pp. 4296-302, 2012.

S. J. Jouffroy, Schlueter, A. H., Bildfell, R. J., and Rockey, D. D., “Rhabdochlamydia spp. in an Oregon raptor.”, J Vet Diagn Invest, vol. 28, no. 4, pp. 473-6, 2016.

J. P. Bannantine, Griffiths, R. S., Viratyosin, W., Brown, W. J., and Rockey, D. D., “A secondary structure motif predictive of protein localization to the chlamydial inclusion membrane.”, Cellular microbiology, vol. 2, no. 1, pp. 35-47, 2000.

J. P. Bannantine, Griffiths, R. S., Viratyosin, W., Brown, W. J., and Rockey, D. D., “A secondary structure motif predictive of protein localization to the chlamydial inclusion membrane.”, Cell Microbiol, vol. 2, no. 1, pp. 35-47, 2000.

D. D. Rockey, Turaga, P. S., Wiens, G. D., Cook, B. A., and Kaattari, S. L., “Serine proteinase of Renibacterium salmoninarum digests a major autologous extracellular and cell-surface protein.”, Can J Microbiol, vol. 37, no. 10, pp. 758-63, 1991.

D. D. Rockey, Turaga, P. S., Wiens, G. D., Cook, B. A., and Kaattari, S. L., “Serine proteinase of Renibacterium salmoninarum digests a major autologous extracellular and cell-surface protein.”, Canadian journal of microbiology, vol. 37, no. 10, pp. 758-63, 1991.

J. P. Bannantine, Rockey, D. D., and Hackstadt, T., “Tandem genes of Chlamydia psittaci that encode proteins localized to the inclusion membrane.”, Molecular microbiology, vol. 28, no. 5, pp. 1017-26, 1998.

J. P. Bannantine, Rockey, D. D., and Hackstadt, T., “Tandem genes of Chlamydia psittaci that encode proteins localized to the inclusion membrane.”, Mol Microbiol, vol. 28, no. 5, pp. 1017-26, 1998.

D. D. Rockey, Fischer, E. R., and Hackstadt, T., “Temporal analysis of the developing Chlamydia psittaci inclusion by use of fluorescence and electron microscopy.”, Infect Immun, vol. 64, no. 10, pp. 4269-78, 1996.