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Home | Contact |J. Kim Kemper Lab | University of Illinois
Publication
  • Doray, B., Chen, C., and Kemper, B.  Substitutions in the C-terminal portion of the catalytic domain partially reverse assembly defects introduced by mutations in the N-terminal linker sequence of cytochrome P450 2C2.  Biochemistry 37:12180-12186 (1999).
     
  • Szczesna-Skorupa, E., Chen, C., Rogers, S., and Kemper, B.  Mobility of cytochrome P450 in the endoplasmic reticulum membrane.  Proc. Natl. Acad. Sci. USA 95: 14793-14798 (1998).
     
  • Liu, S., Park, Y., Rivera-Rivera, I., Li, H., and Kemper, B.  A nuclear factor-1 motif and redundant regulatory elements comprise a phenobarbital responsive enhancer in CYP2B1/2.  DNA Cell Biol. 17: 461-470 (1998).
     
  • Chen, C., Doray, B., and Kemper, B.  A conserved proline-rich sequence between the N-terminal signal-anchor and catalytic domains is required for assembly of functional cytochrome P450 2C2. Arch. Biochem. Biophys. 350: 233-238 (1998).
     
  • Kim, J. and Kemper, B.  Phenobarbital alters protein binding to the CYP2B1/2 phenobarbital-responsive unit in native chromatin.  J. Biol. Chem. 272: 29423-2942(1997).
     
  • Chen, C., Doray, B., and Kemper, B.  Efficient assembly of functional cytochrome P450 2C2 requires a spacer sequence between the N-terminal signal-anchor and catalytic domain.  J. Biol.Chem. 272:22891-22897 (1997).
     
  • Chen, C. and Kemper, B. Different structural requirements at specific proline residue positions in the conserved proline-rich region of cytochrome P450 2C2.  J. Biol. Chem. 271:28697-28611(1996).
     
  • Park, Y., Li, H., and Kemper, B. Phenobarbital induction mediated by a distal CYP2B2 sequence in rat liver transiently transfected in situJ. Biol. Chem. 271:23725-23728 (1996).
     
  • Li, H., Liu, S., and Kemper, B. Sex- and tissue-specific expression of a cytochrome P450 2C2-luciferase transgene.  Mol. Cell. Endocrinol. 120:77-83 (1996).
     
  • Park,  Y. and Kemper, B. The CYP2B1 proximal promoter contains a functional C/EBP regulatory element.  DNA Cell Biol. 15:693-701 (1996).
     
  • Richardson, T. H., Jung, F. Griffin, K. J., Wester, M., Raucy, J. L., Kemper, B., Bornheim, L. M., Hassett, C., Omiecinski, C. J., and Johnson, E. F. A universal approach to the expression of human and rabbit cytochrome P450s of the 2C subfamily in Escherichia coliArch. Biochem. Biophys.
    323
    :87-96 (1995).
     
  • Szczesna-Skorupa, E., Ahn, K., Chen, C., Doray, B. and Kemper, B. The cytoplasmic and N-terminal transmembrane domains of cytochrome P450 contain independent signals for retention in the endoplasmic reticulum.  J. Biol. Chem. 270:24327-24333 (1995).
     
  • Ramarao, M. K. and Kemper, B. Substitution at residue 473 confers progesterone 21-hydroxylase activity to cytochrome P450 2C2.  Mol. Pharm. 48:417-424 (1995).
     
  • Ramarao, M. K., Straub, P., and Kemper, B.  Identification by in vitro mutagenesis of the interaction of two segments of C2MstC1, a chimera of cytochromes P450 2C2 and 2C1. J. Biol. Chem. 270:1873-1880 (1995).
     
  • Ahn, K., Chen, D., and Kemper, B.  Inverse relationship of cotranslational translocation with the hydrophobic moment of the bovine preproparathyroid hormone signal sequence. Biochim. Biophys. Acta 1224:459-462 (1994).
     
  • Straub, P., Lloyd, M., Johnson, E. F., and Kemper, B.  Differential effects of mutations in SRS1 of cytochrome P450 2C2 on lauric acid and progesterone hydroxylation.  Biochemistry,33:8029-8034 (1994).
     
  • Chen, D., Park, Y., and Kemper, B.  Differential protein binding and transcriptional activities of HNF-4 elements in three closely related CYP2C genes.  DNA Cell Biol., 7:771-779 (1994).
     
  • Chen, D., Lepar, G., and Kemper, B.  A transcriptional regulatory element common to a large family of hepatic cytochrome P450 genes is a functional binding site of the orphan receptor HNF-4.  J. Biol. Chem. 269:5420-5427 (1994).
     
  • Straub, P., Ramarao, M. K., and Kemper, B.  Preference for aromatic substitution at tryptophan-120, which is highly conserved and a potential mediator of electron transfer in cytochrome P450 2C2.  Biochem. Biophys. Res. Commun.  197:433-439 (1993).
     
  • Straub, P., Johnson, E. F., and Kemper, B.  Hydrophobic side chain requirements for lauric acid and progesterone hydroxylation at amino acid 113 in cytochrome P450 2C2, a potential determinant of substrate specificity.  Arch. Biochem. Biophy. 306: 521-527 (1993).
     
  • Straub, P., Lloyd, M., Johnson, E. F., and Kemper, B. Cassette-mutagenesis of a potential substrate recognition region of cytochrome P450 2C2.  J. Biol. Chem. 268:21997-22003 (1993).
     
  • Ahn, K., Szczesna-Skorupa, E., and Kemper, B. The amino-terminal 29 amino acids of cytochrome P450 2C1 are sufficient for retention in the endoplasmic reticulum.  J. Biol. Chem.268:18726-18733 (1993).
     
  • Szczesna-Skorupa, E., Straub, P., and Kemper, B. Deletion of a conserved tetrapeptide, PPGP, in P450 2C2 results in loss of enzymatic activity without a change in its cellular location.  Arch. Biochem. Biophy. 304:170-175 (1993).
  • Hsu, M-H, Griffin, K. J., Wang, Y., Kemper, B., and Johnson, E. F.,  A single amino acid substitution confers progesterone 6β-hydroxylase activity to rabbit P450 2C3.  J. Biol. Chem. 268:6939-6944 (1993).
     
  • Richardson, T. H., Hsu, M-H., Kronbach, T., Barnes, H. J., Chan, G., Waterman, M. R., Kemper, B., and Johnson, E. F. Purification and characterization of recombinant-expressed cytochrome P450 2C3 from Escherichia coli: 2C3 encodes the 6β-hydroxylase deficient form of P4503b.  Arch. Biochem. Biophy. 300:510-516 (1993).
     
  • Szczesna-Skorupa, E. and Kemper, B. An N-terminal glycosylation signal on cytochrome P450 is restricted to the endoplasmic reticulum in a luminal orientation.  J. Biol. Chem. 268:1757-1762 (1993).
     
  • Venepally, P., Chen, D., and Kemper, B. Transcriptional regulatory elements for basal expression of cytochrome P450IIC genes.  J. Biol. Chem.267:17333-17338 (1992).
     
  • Kim, J. and Kemper, B.  Differences in DNaseI hypersensitive sites in phenobarbital-inducible and constitutive rabbit P450IIC genes.  Biochemistry 30:10287-10294 (1991).
     
  • Kronbach, T., Kemper, B., and Johnson, E. F.  A hypervariable region of P450IIC5 confers progesterone 21-hydroxylase activity to P450IIC1.  Biochemistry 30:6097-6102 (1991).
     
  • Chan, G. and Kemper, B.  Structure of the rabbit cytochrome P450IIC3 gene, a constitutive member of the P450IIC subfamily.  Biochemistry 29:3743-3750 (1990).
     
  • Zhao, J., Chan, G., Govind, S., Bell, P., and Kemper, B.  Structure of 5' regions and expression of phenobarbital-inducible rabbit cytochrome P450IIC genes.  DNA Cell Biol. 9:37-48 (1990).

 
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