|
|
-
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 situ.
J. 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 coli. Arch. 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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