| Publications List: |
| Marinova
Z, Yakovleva T, Melzig MF, Hallberg M, Nylander I, Ray K, Rodgers
DW, Hauser KF, Ekstrom TJ, Bakalkin G. A novel soluble protein factor
with non-opioid dynorphin A-binding activity. Biochem Biophys Res
Commun. 2004 Aug 13;321(1):202-9. HTML PDF Cai, Y., Cronin, C.N., Engel, A.G., Ohno, K., Hersh, L.B. and Rodgers, D.W. (2004) Choline acetyltransferase structure reveals distribution of mutations that cause motor disorders. EMBO J. 23, 2047-2058. ABSTRACT HTML PDF Ray, K., Hines, C.S., Coll-Rodriguez, J. and Rodgers, D.W. (2004) Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation and localization. J. Biol. Chem. 279, 20480-20489. ABSTRACT HTML PDF Ma, Z., Daquin, A., Yao, J., Rodgers, D., Thompson, M.W. and Hersh, L.B. (2003) Proteolytic cleavage of the puromycin-sensitive aminopeptidase generates a substrate binding domain. Arch Biochem Biophys. 415, 80-86. HTML PDF Ray, K., Hines, C.S., and Rodgers, D.W. (2002) Mapping sequence differences between thimet oligopeptidase and neurolysin implicates key residues in substrate recognition. Protein Science 11, 2237-2246. ABSTRACT HTML PDF Koder, R.L., Haynes, C., Rodgers, M.E., Rodgers, D.W. and Miller, A-F. (2002) Flavin thermodynamics explain the oxygen insensitivity of enteric nitroreductases. Biochemistry 41, 14197-14205. ABSTRACT HTML PDF Koder, R.L., Haynes, C., Rodgers, M.E., Rodgers, D.W. and Miller, A-F. Active site thermodynamics and structure explain the oxygen insensitivity of type I nitroreductases. (manuscript submitted). Haynes, C., Koder, R.L, Miller, A-F. and Rodgers, D.W. (2002) Structures of nitroreductase in three states: Effects of inhibitor binding and reduction. J. Biol. Chem. 277(13):11513-20 ABSTRACT HTML PDF Brown, C.K., Madauss, K., Lian, W., Tolbert, W.D., Beck, M.R. and Rodgers, D.W. (2001) Structure of neurolysin reveals a deep channel that limits substrate access. Proc. Natl. Acad. Sci. USA 98, 3127-3132. ABSTRACT HTML PDF Rodgers, D.W. (2001) Cryocrystallography techniques and devices. In “International Tables for Crystallography, Vol. F. Crystallography of Biological Macromolecules.” (Rossman, M. and Arnold, E., Eds.) Dordrecht: Kluwer Academic Publishers, The Netherlands. Lian, W., Chen, G., Wu, D., Brown, C.K., Madauss, K., Hersh, L.B. and Rodgers, D.W. (2000) Crystallization and preliminary analysis of neurolysin. Acta Crystallogr. D. Biol. Crystallogr. 56, 1644-1646. ABSTRACT HTML PDF Hong, Y., Lubert E.J., Rodgers, D.W. and Sarge, K.D. (2000) Molecular basis of competition between HSF2 and catalytic subunit for binding to the Pr65/A subunit of PP2A. Biochem. Biophys. Res. Commun. 272, 84-89. ABSTRACT PDF Rodgers, D.W. Practical Cryocrystallography. (1997) In "Methods in Enzymology” (Carter, C.W., Jr. and Sweet, R.M., eds.), Vol. 276 PartA, Academic Press, London. Rodgers, D.W. (1996) Cryocrystallography of macromolecules. Synch. Radiation News 9: 4-11. |
Department of Molecular and Cellular Biochemistry
University of Kentucky
Biomedical Biological Sciences Research Building, Rm 236
741 South Limestone
Lexington, Ky 40356
859.323.8183 lab
859.323.1037 fax