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Volumn 52, Issue 34, 2013, Pages 5821-5829

Structural basis for the functional roles of critical residues in human cytochrome P450 aromatase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE RESIDUES; ANALYTICAL ULTRACENTRIFUGATION; CATALYTIC RESIDUE; INTERMOLECULAR INTERACTIONS; INTERMOLECULAR INTERFACES; NATIVE GEL ELECTROPHORESIS; QUATERNARY STRUCTURE; STRUCTURE-FUNCTION RELATIONSHIP;

EID: 84883210549     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400669h     Document Type: Article
Times cited : (75)

References (33)
  • 1
    • 58149339806 scopus 로고    scopus 로고
    • Structural basis for androgen specificity and oestrogen synthesis in human aromatase
    • Ghosh, D., Griswold, J., Erman, M., and Pangborn, W. (2009) Structural basis for androgen specificity and oestrogen synthesis in human aromatase Nature 457, 219-223
    • (2009) Nature , vol.457 , pp. 219-223
    • Ghosh, D.1    Griswold, J.2    Erman, M.3    Pangborn, W.4
  • 2
    • 77950348123 scopus 로고    scopus 로고
    • X-ray structure of human aromatase reveals an androgen-specific active site
    • Ghosh, D., Griswold, J., Erman, M., and Pangborn, W. (2010) X-ray structure of human aromatase reveals an androgen-specific active site J. Steroid Biochem. Mol. Biol. 118, 197-202
    • (2010) J. Steroid Biochem. Mol. Biol. , vol.118 , pp. 197-202
    • Ghosh, D.1    Griswold, J.2    Erman, M.3    Pangborn, W.4
  • 3
    • 79958766162 scopus 로고    scopus 로고
    • Higher order organization of human placental aromatase
    • Ghosh, D., Jiang, W., Lo, J., and Egbuta, C. (2011) Higher order organization of human placental aromatase Steroids 76, 753-758
    • (2011) Steroids , vol.76 , pp. 753-758
    • Ghosh, D.1    Jiang, W.2    Lo, J.3    Egbuta, C.4
  • 4
    • 84857615120 scopus 로고    scopus 로고
    • Motion and Flexibility in Human Cytochrome P450 Aromatase
    • Jiang, W. and Ghosh, D. (2012) Motion and Flexibility in Human Cytochrome P450 Aromatase PLoS One 7, e32565
    • (2012) PLoS One , vol.7 , pp. 32565
    • Jiang, W.1    Ghosh, D.2
  • 5
    • 0036829928 scopus 로고    scopus 로고
    • Expression and purification of a recombinant form of human aromatase from Escherichia coli
    • Zhang, F., Zhou, D., Kao, Y. C., Ye, J., and Chen, S. (2002) Expression and purification of a recombinant form of human aromatase from Escherichia coli Biochem. Pharmacol. 64, 1317-1324
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 1317-1324
    • Zhang, F.1    Zhou, D.2    Kao, Y.C.3    Ye, J.4    Chen, S.5
  • 6
    • 84874042214 scopus 로고    scopus 로고
    • Human aromatase: Perspectives in biochemistry and biotechnology
    • Di Nardo, G. and Gilardi, G. (2013) Human aromatase: Perspectives in biochemistry and biotechnology Biotechnol. Appl. Biochem. 60, 92-101
    • (2013) Biotechnol. Appl. Biochem. , vol.60 , pp. 92-101
    • Di Nardo, G.1    Gilardi, G.2
  • 7
    • 67449136137 scopus 로고    scopus 로고
    • History of aromatase: Saga of an important biological mediator and therapeutic target
    • Santen, R. J., Brodie, H., Simpson, E. R., Siiteri, P. K., and Brodie, A. (2009) History of aromatase: Saga of an important biological mediator and therapeutic target Endocr. Rev. 30, 343-375
    • (2009) Endocr. Rev. , vol.30 , pp. 343-375
    • Santen, R.J.1    Brodie, H.2    Simpson, E.R.3    Siiteri, P.K.4    Brodie, A.5
  • 8
    • 0028100793 scopus 로고
    • Mutagenesis study at a postulated hydrophobic region near the active site of aromatase cytochrome P450
    • Zhou, D., Cam, L. L., Laughton, C. A., Korzekwa, K. R., and Chen, S. (1994) Mutagenesis study at a postulated hydrophobic region near the active site of aromatase cytochrome P450 J. Biol. Chem. 269, 19501-19508
    • (1994) J. Biol. Chem. , vol.269 , pp. 19501-19508
    • Zhou, D.1    Cam, L.L.2    Laughton, C.A.3    Korzekwa, K.R.4    Chen, S.5
  • 9
    • 2942595904 scopus 로고    scopus 로고
    • Characterization of stable human aromatase expressed in E. Coli
    • Kagawa, N., Hori, H., Waterman, M. R., and Yoshioka, S. (2004) Characterization of stable human aromatase expressed in E. coli Steroids 69, 235-243
    • (2004) Steroids , vol.69 , pp. 235-243
    • Kagawa, N.1    Hori, H.2    Waterman, M.R.3    Yoshioka, S.4
  • 10
    • 61649110467 scopus 로고    scopus 로고
    • Molecular characterization of aromatase
    • Hong, Y., Li, H., Yuan, Y. C., and Chen, S. (2009) Molecular characterization of aromatase Ann. N.Y. Acad. Sci. 1155, 112-120
    • (2009) Ann. N.Y. Acad. Sci. , vol.1155 , pp. 112-120
    • Hong, Y.1    Li, H.2    Yuan, Y.C.3    Chen, S.4
  • 11
    • 0028341176 scopus 로고
    • Baculovirus mediated high level expression of human placental aromatase (CYP19A1)
    • Sigle, R. O., Titus, M. A., Harada, N., and Nelson, S. D. (1994) Baculovirus mediated high level expression of human placental aromatase (CYP19A1) Biochem. Biophys. Res. Commun. 201, 694-700
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 694-700
    • Sigle, R.O.1    Titus, M.A.2    Harada, N.3    Nelson, S.D.4
  • 14
    • 0025089197 scopus 로고
    • Stable expression of human aromatase complementary DNA in mammalian cells: A useful system for aromatase inhibitor screening
    • Zhou, D. J., Pompon, D., and Chen, S. A. (1990) Stable expression of human aromatase complementary DNA in mammalian cells: A useful system for aromatase inhibitor screening Cancer Res. 50, 6949-6954
    • (1990) Cancer Res. , vol.50 , pp. 6949-6954
    • Zhou, D.J.1    Pompon, D.2    Chen, S.A.3
  • 15
    • 0025965047 scopus 로고
    • Structure-function studies of human aromatase by site-directed mutagenesis: Kinetic properties of mutants Pro-308 → Phe, Tyr-361 → Phe, Tyr-361 → Leu, and Phe-406 → Arg
    • Zhou, D. J., Pompon, D., and Chen, S. A. (1991) Structure-function studies of human aromatase by site-directed mutagenesis: Kinetic properties of mutants Pro-308 → Phe, Tyr-361 → Phe, Tyr-361 → Leu, and Phe-406 → Arg Proc. Natl. Acad. Sci. U.S.A. 88, 410-414
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 410-414
    • Zhou, D.J.1    Pompon, D.2    Chen, S.A.3
  • 16
    • 79952471723 scopus 로고    scopus 로고
    • Efficient expression of human aromatase (CYP19) in E. Coli
    • Kagawa, N. (2011) Efficient expression of human aromatase (CYP19) in E. coli Methods Mol. Biol. 705, 109-122
    • (2011) Methods Mol. Biol. , vol.705 , pp. 109-122
    • Kagawa, N.1
  • 17
    • 33846619697 scopus 로고    scopus 로고
    • Molecular basis for the aromatization reaction and exemestane-mediated irreversible inhibition of human aromatase
    • Hong, Y., Yu, B., Sherman, M., Yuan, Y. C., Zhou, D., and Chen, S. (2007) Molecular basis for the aromatization reaction and exemestane-mediated irreversible inhibition of human aromatase Mol. Endocrinol. 21, 401-414
    • (2007) Mol. Endocrinol. , vol.21 , pp. 401-414
    • Hong, Y.1    Yu, B.2    Sherman, M.3    Yuan, Y.C.4    Zhou, D.5    Chen, S.6
  • 18
    • 38949101404 scopus 로고    scopus 로고
    • Molecular basis for the interaction of four different classes of substrates and inhibitors with human aromatase
    • Hong, Y., Cho, M., Yuan, Y. C., and Chen, S. (2008) Molecular basis for the interaction of four different classes of substrates and inhibitors with human aromatase Biochem. Pharmacol. 75, 1161-1169
    • (2008) Biochem. Pharmacol. , vol.75 , pp. 1161-1169
    • Hong, Y.1    Cho, M.2    Yuan, Y.C.3    Chen, S.4
  • 19
    • 0034819384 scopus 로고    scopus 로고
    • Evaluation of the mechanism of aromatase cytochrome P450. A site-directed mutagenesis study
    • Kao, Y. C., Korzekwa, K. R., Laughton, C. A., and Chen, S. (2001) Evaluation of the mechanism of aromatase cytochrome P450. A site-directed mutagenesis study Eur. J. Biochem. 268, 243-251
    • (2001) Eur. J. Biochem. , vol.268 , pp. 243-251
    • Kao, Y.C.1    Korzekwa, K.R.2    Laughton, C.A.3    Chen, S.4
  • 20
    • 2342436397 scopus 로고    scopus 로고
    • Suppression of human cytochrome P450 aromatase activity by monoclonal and recombinant antibody fragments and identification of a stable antigenic complex
    • Lala, P., Higashiyama, T., Erman, M., Griswold, J., Wagner, T., Osawa, Y., and Ghosh, D. (2004) Suppression of human cytochrome P450 aromatase activity by monoclonal and recombinant antibody fragments and identification of a stable antigenic complex J. Steroid Biochem. Mol. Biol. 88, 235-245
    • (2004) J. Steroid Biochem. Mol. Biol. , vol.88 , pp. 235-245
    • Lala, P.1    Higashiyama, T.2    Erman, M.3    Griswold, J.4    Wagner, T.5    Osawa, Y.6    Ghosh, D.7
  • 21
    • 0004288248 scopus 로고    scopus 로고
    • version 5.0, GraphPad Software, San Diego
    • Motulsky, H. (2003) GraphPad Prism, version 5.0, GraphPad Software, San Diego.
    • (2003) GraphPad Prism
    • Motulsky, H.1
  • 22
    • 19544388796 scopus 로고    scopus 로고
    • P450 aromatase inhibition assay using a competitive ELISA
    • Matsui, K., Nishii, S., and Oka, M. (2005) P450 aromatase inhibition assay using a competitive ELISA J. Pharm. Biomed. Anal. 38, 307-312
    • (2005) J. Pharm. Biomed. Anal. , vol.38 , pp. 307-312
    • Matsui, K.1    Nishii, S.2    Oka, M.3
  • 23
    • 79952804747 scopus 로고    scopus 로고
    • A novel non-SET domain multi-subunit methyltransferase required for sequential nucleosomal histone H3 methylation by the mixed lineage leukemia protein-1 (MLL1) core complex
    • Patel, A., Vought, V. E., Dharmarajan, V., and Cosgrove, M. S. (2011) A novel non-SET domain multi-subunit methyltransferase required for sequential nucleosomal histone H3 methylation by the mixed lineage leukemia protein-1 (MLL1) core complex J. Biol. Chem. 286, 3359-3369
    • (2011) J. Biol. Chem. , vol.286 , pp. 3359-3369
    • Patel, A.1    Vought, V.E.2    Dharmarajan, V.3    Cosgrove, M.S.4
  • 24
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling Biophys. J. 78, 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 26
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr. D60, 2126-2132
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 27
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr. D53, 240-255
    • (1997) Acta Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 31
    • 84859608215 scopus 로고    scopus 로고
    • Coupled electron transfer and proton hopping in the final step of CYP19-catalyzed androgen aromatization
    • Sen, K. and Hackett, J. C. (2012) Coupled electron transfer and proton hopping in the final step of CYP19-catalyzed androgen aromatization Biochemistry (Moscow) 51, 3039-3049
    • (2012) Biochemistry (Moscow) , vol.51 , pp. 3039-3049
    • Sen, K.1    Hackett, J.C.2
  • 33
    • 0025343452 scopus 로고
    • Reversible inhibition of human placental microsomal aromatase by CGS 18320B and other non-steroidal compounds
    • Bullion, K. A., Osawa, Y., and Braun, D. G. (1990) Reversible inhibition of human placental microsomal aromatase by CGS 18320B and other non-steroidal compounds Endocr. Res. 16, 255-267
    • (1990) Endocr. Res. , vol.16 , pp. 255-267
    • Bullion, K.A.1    Osawa, Y.2    Braun, D.G.3


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