Selected Publications
Miller, M.A., Scott, E.E., and Limberg, J. (2008) Expression, purification, crystallization and preliminary X-ray studies of a proly-4-hydroxylase protein from Bacillus anthracis. Acta Crystallogr. F (accepted).
Reed, T.M., Hirakawa, H., Mure, M., Scott, E.E., and Limberg, J. (2008) Expression, purification and crystallization and preliminary X-ray studies of histamine dehydrogenase from Nocardiodes simplex. Acta Crystallogr. F (accepted).
Porubsky, P.R., Scott, E.E., and Williams, T.D. (2008)
p-Dimethylaminocinnamaldehyde derivatization for colorimetric detection and HPLC-UV/Vis-MS/MS identification of indoles. Arch. Biochem. Biophys. 475:14-17.
Schlicht, K.E., Michno, N., Smith, B.D., Scott, E.E., and Murphy, S.E. (2007)
Functional characterization of CYP2A13 polymorphisms. Xenobiotica. 37:1439-1349.
Smith B.D., Sanders J.L., Porubsky P.R., Lushington G.H., Stout C.D., and Scott, E.E. (2007)
Structure of the human lung cytochrome P450 2A13. J. Biol. Chem. 282:17306-17313.
Li W., Liu H., Scott E.E., Grater F., Halpert J.R., Luo X., Shen J., and Hiang H. (2005)
Possible pathway(s) of testosterone egress from the active site of cytochrome P450 2B1: A steered molecular dynamics simulation. Drug Metab Dispos. 33:910-919.
Scott E.E. and Halpert J.R. (2005)
Structures of cytochrome P450 3A4. Trends in Biochem. Sci. 30:5-7.
Honma W., Li W., Liu H., Scott, E.E., and Halpert, J.R. (2005)
Functional role of residues in the helix B' region of cytochrome P450 2B1. Arch. Biochem. Biophys. 435:157-165.
Scott, E.E., White, M.A., He, Y.A., Johnson, E.F., Stout, C.D., and Halpert, J.R. (2004)
Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-Å resolution: Insight into the range of P450 conformations and the coordination of redox partner binding, J. Biol. Chem. 279:27294-27301. Crystal structure:
1SUO
Scott, E. E., He, Y. A., Wester, M. R., White, M. A., Chin, C. C., Halpert, J. R., Johnson, E. F., and Stout, C. D. (2003)
An open conformation of mammalian cytochrome P450 2B4 at 1.6 Å resolution, Proc. Nat. Acad. Sci. U.S.A. 100:13196-13201. [
commentary Poulos, T.L. (2003), PNAS 100, 13121-13122.] Crystal structure:
1P05
Scott E.E., Liu H., He Y.Q, Li W., and Halpert J.R. (2004)
Mutagenesis and molecular dynamics suggest structural and functional roles for residues in the N-terminal portion of the cytochrome P450 2B1 I helix. Arch Biochem Biophys. 423:266-276.
Kumar, S., Scott, E.E., Liu, H., and Halpert, J.R. (2003)
A rational approach to re-engineer cytochrome P450 2B1 regioselectivity based on the crystal structure of P450 2C5. J. Biol. Chem. 278:17178-171784.
Scott, E.E., He, Y.Q., and Halpert, J.R. (2002)
Substrate routes to the buried active site may vary among cytochromes P450: Mutagenesis of the F-G region in P450 2B1. Chem. Res. Tox. 11:1407-1413.
Scott, E.E., Spatzenegger, M., and Halpert, J.R. (2001)
A truncation of 2B subfamily cytochromes P450 yields increased expression levels, increased solubility, and decreased aggregation while retaining function. Arch. Biochem. Biophys. 395:57-68.
Domanski, T.L., He, Y.Q., Scott, E.E., Wang, Q., and Halpert, J.R. (2001)
The role of cytochrome 2B1 substrate recognition site residues 115, 294, 297, 298, and 362 in the oxidation of steroids and 7-alkoxycoumarins. Arch. Biochem. Biophys. 394:21-28.
Scott, E.E., Paster, E.V., and Olson, J.S. (2000) The stabilities of mammalian apomyoglobins vary over a 600-fold range and can be enhanced by comparative mutagenesis. J. Biol. Chem. 35:27129-27136.
Liong, E.C., Dou, Y., Scott, E.E., Olson, J.S., and Phillips, Jr., G.N. (2000) Water-proofing the heme pocket: role of proximal amino acid side chains in preventing hemin loss from myoglobin. J. Biol. Chem. 276:9093-9100.
Scott, E.E., Gibson, Q.H., and Olson, J.S. (2000) Mapping pathways for ligand entry into and exit from myoglobin. J. Biol. Chem. 276:5177-5188.
Krzywda, S., Murshudov, G.N., Brzozowski, A.M., Jaskolski, M., Scott, E.E., Klizas, S.A., Gibson, Q.H., Olson, J.S., and Wilkinson, A.J. (1998) Stabilizing bound O2 in myoglobin by valine 68 (E11) to asparagine substitution. Biochemistry 37:15896-15907.
Scott, E.E. and Gibson, Q.H. (1997) Ligand migration in sperm whale myoglobin. Biochemistry 36:11909-11917.
For More Information, Please Contact:
Emily E. Scott, Ph.D.
Department of Medicinal Chemistry
4067 Malott Hall
Tel: 785-864-5559
FAX: 785-864-5326
Email:
eescott@ku.edu
