메뉴 건너뛰기




Volumn 301, Issue 1-2, 2009, Pages 235-244

The binding of lignans, flavonoids and coumestrol to CYP450 aromatase: A molecular modelling study

Author keywords

Aromatase; CYP450; Enterolactone; Flavone; Isoflavone; Lignan; Molecular modelling; Phytoestrogen

Indexed keywords

3 DEMETHOXY 3' O DEMETHYLMATAIRESINOL; 3 DEMETHOXYMATAIRESINOL; 3' DEMETHOXYSECOISOLARICIRESINOL; 3' DEMETHYLSECOISOLARICIRESINOL; 3,3,' DIDEMTHYLSECOISOLARICIRESINOL; 4,4' DIHYDROXYENTEROLACTONE; ALPHA NAPHTHOFLAVONE; APIGENIN; AROMATASE; BIOCHANIN A; CHRYSIN; COUMESTROL; CYTOCHROME P450; DIDEMETHOXYMATAIRESINOL; ENTERODIOL; ENTEROLACTONE; FLAVONOID; GALANGIN; GENISTEIN; ISOFLAVONE; LIGNAN DERIVATIVE; MATAIRESINOL; NORDIHYDROGUAIARETIC ACID; PHYTOESTROGEN; QUERCETIN; SECOISOLARICIRESINOL; UNCLASSIFIED DRUG;

EID: 60249092439     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2008.10.003     Document Type: Article
Times cited : (43)

References (58)
  • 1
    • 52649105178 scopus 로고    scopus 로고
    • Accelrys Inc, Insight II Version, Suite, San Diego, CA 92121, USA
    • Accelrys Inc., Insight II Version 2005, 10188 Telesis Court, Suite 100, San Diego, CA 92121, USA.
    • (2005) 10188 Telesis Court , pp. 100
  • 2
    • 0028849729 scopus 로고
    • Phytoestrogens: epidemiology and a possible role in cancer protection
    • Adlercreutz H. Phytoestrogens: epidemiology and a possible role in cancer protection. Environ. Health Perspect. 103 (1995) 103-112
    • (1995) Environ. Health Perspect. , vol.103 , pp. 103-112
    • Adlercreutz, H.1
  • 5
    • 18144386167 scopus 로고    scopus 로고
    • Mammalian lignans and genistein decrease the activities of aromatase and 17β-hydroxysteroid dehydrogenase in MCF-7 cells
    • Brooks J.D., and Thompson L.U. Mammalian lignans and genistein decrease the activities of aromatase and 17β-hydroxysteroid dehydrogenase in MCF-7 cells. J. Steroid Biochem. Mol. Biol. 94 (2005) 461-467
    • (2005) J. Steroid Biochem. Mol. Biol. , vol.94 , pp. 461-467
    • Brooks, J.D.1    Thompson, L.U.2
  • 6
    • 0035671735 scopus 로고    scopus 로고
    • Effects of phytoestrogens and synthetic combinatorial libraries on aromatase, estrogen biosynthesis, and metabolism
    • Brueggemeier R.W., and Whetstone J.L. Effects of phytoestrogens and synthetic combinatorial libraries on aromatase, estrogen biosynthesis, and metabolism. Ann. N. Y. Acad. Sci. 948 (2001) 51-66
    • (2001) Ann. N. Y. Acad. Sci. , vol.948 , pp. 51-66
    • Brueggemeier, R.W.1    Whetstone, J.L.2
  • 7
    • 0027365576 scopus 로고
    • Flavonoid inhibition of aromatase enzyme activity in human preadipocytes
    • Campbell D.R., and Kurzer M.S. Flavonoid inhibition of aromatase enzyme activity in human preadipocytes. J. Steroid Biochem. Mol. Biol. 46 (1993) 381-388
    • (1993) J. Steroid Biochem. Mol. Biol. , vol.46 , pp. 381-388
    • Campbell, D.R.1    Kurzer, M.S.2
  • 9
    • 0031124888 scopus 로고    scopus 로고
    • Binding characteristics of aromatase inhibitors and phytoestrogens to human aromatase
    • Chen S., Kao Y.C., and Laughton C.A. Binding characteristics of aromatase inhibitors and phytoestrogens to human aromatase. J. Steroid Biochem. Mol. Biol. 61 (1997) 107-115
    • (1997) J. Steroid Biochem. Mol. Biol. , vol.61 , pp. 107-115
    • Chen, S.1    Kao, Y.C.2    Laughton, C.A.3
  • 10
    • 33744814910 scopus 로고    scopus 로고
    • Occurrence and activity of human intestinal bacteria involved in the conversion of dietary lignans
    • Clavel T., Borrmann D., Braune A., and Blaut J.D.M. Occurrence and activity of human intestinal bacteria involved in the conversion of dietary lignans. Anaerobe 12 (2006) 140-147
    • (2006) Anaerobe , vol.12 , pp. 140-147
    • Clavel, T.1    Borrmann, D.2    Braune, A.3    Blaut, J.D.M.4
  • 11
    • 0020478791 scopus 로고
    • Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes. Identification of the ligand trans to cysteinate in the native enzyme
    • Dawson J., Andersson L., and Sono M. Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes. Identification of the ligand trans to cysteinate in the native enzyme. J. Biol. Chem. 257 (1982) 3606-3617
    • (1982) J. Biol. Chem. , vol.257 , pp. 3606-3617
    • Dawson, J.1    Andersson, L.2    Sono, M.3
  • 13
    • 29544449397 scopus 로고    scopus 로고
    • The effects of dietary phytoestrogens on aromatase activity in human endometrial stromal cells
    • Edmunds K.M., Holloway A.C., Crankshaw D.J., Agarwal S.K., and Foster W.G. The effects of dietary phytoestrogens on aromatase activity in human endometrial stromal cells. Reprod. Nutr. Dev. 45 (2005) 709-720
    • (2005) Reprod. Nutr. Dev. , vol.45 , pp. 709-720
    • Edmunds, K.M.1    Holloway, A.C.2    Crankshaw, D.J.3    Agarwal, S.K.4    Foster, W.G.5
  • 14
    • 33746712854 scopus 로고    scopus 로고
    • Lead optimization providing a series of flavone derivatives as potent nonsteroidal inhibitors of the cytochrome P450 aromatase enzyme
    • Gobbi S., Cavalli A., Rampa A., Belluti F., Piazzi L., Paluszcak A., Hartmann R.W., Recanatini M., and Bisi A. Lead optimization providing a series of flavone derivatives as potent nonsteroidal inhibitors of the cytochrome P450 aromatase enzyme. J. Med. Chem. 49 (2006) 4777-4780
    • (2006) J. Med. Chem. , vol.49 , pp. 4777-4780
    • Gobbi, S.1    Cavalli, A.2    Rampa, A.3    Belluti, F.4    Piazzi, L.5    Paluszcak, A.6    Hartmann, R.W.7    Recanatini, M.8    Bisi, A.9
  • 15
    • 19444374982 scopus 로고    scopus 로고
    • Synthesis and characterization of azole isoflavone inhibitors of aromatase
    • Hackett J.C., Kim Y., Su B., and Brueggemeier R.W. Synthesis and characterization of azole isoflavone inhibitors of aromatase. Bioorg. Med. Chem. 13 (2005) 4063-4070
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 4063-4070
    • Hackett, J.C.1    Kim, Y.2    Su, B.3    Brueggemeier, R.W.4
  • 16
    • 0032214649 scopus 로고    scopus 로고
    • Databases for protein-ligand complexes
    • Hendlich M. Databases for protein-ligand complexes. Acta Crystallogr. D 54 (1998) 1178-1182
    • (1998) Acta Crystallogr. D , vol.54 , pp. 1178-1182
    • Hendlich, M.1
  • 17
    • 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., and Chen S. Molecular basis for the interaction of four different classes of substrates and inhibitors with human aromatase. Biochem. Pharmacol. 75 (2008) 1161-1169
    • (2008) Biochem. Pharmacol. , vol.75 , pp. 1161-1169
    • Hong, Y.1    Cho, M.2    Yuan, Y.3    Chen, S.4
  • 20
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G., Willet P., Glen R.C., Leach A.R., and Taylor R. Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol. 267 (1997) 727-748
    • (1997) J. Mol. Biol. , vol.267 , pp. 727-748
    • Jones, G.1    Willet, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 21
    • 0030013560 scopus 로고    scopus 로고
    • Binding characteristics of seven inhibitors of human aromatase: a site-directed mutagenesis study
    • Kao Y., Cam L.L., Laughton C.A., Zhou D., and Chen S. Binding characteristics of seven inhibitors of human aromatase: a site-directed mutagenesis study. Cancer Res. 56 (1996) 3451-3460
    • (1996) Cancer Res. , vol.56 , pp. 3451-3460
    • Kao, Y.1    Cam, L.L.2    Laughton, C.A.3    Zhou, D.4    Chen, S.5
  • 22
    • 0034819384 scopus 로고    scopus 로고
    • Evaluation of the mechanism of aromatase cytochrome P450. A site-directed mutagenesis study
    • Kao Y., Korzekwa K.R., Laughton C.A., and Chen S. Evaluation of the mechanism of aromatase cytochrome P450. A site-directed mutagenesis study. Eur. J. Biochem. 268 (2001) 243-251
    • (2001) Eur. J. Biochem. , vol.268 , pp. 243-251
    • Kao, Y.1    Korzekwa, K.R.2    Laughton, C.A.3    Chen, S.4
  • 23
    • 0031915796 scopus 로고    scopus 로고
    • Molecular basis of the inhibition of human aromatase (estrogen synthetase) by flavone and isoflavone phytoestrogens: a site-directed mutagenesis study
    • Kao Y., Zhou C., Sherman M., Laughton C.A., and Chen S. Molecular basis of the inhibition of human aromatase (estrogen synthetase) by flavone and isoflavone phytoestrogens: a site-directed mutagenesis study. Environ. Health Perspect. 106 (1998) 85-92
    • (1998) Environ. Health Perspect. , vol.106 , pp. 85-92
    • Kao, Y.1    Zhou, C.2    Sherman, M.3    Laughton, C.A.4    Chen, S.5
  • 24
    • 34547692960 scopus 로고    scopus 로고
    • A three-dimensional model of CYP19 aromatase for structure-based drug design
    • Karkola S., Höltje H., and Wähälä K. A three-dimensional model of CYP19 aromatase for structure-based drug design. J. Steroid Biochem. Mol. Biol. 105 (2007) 63-70
    • (2007) J. Steroid Biochem. Mol. Biol. , vol.105 , pp. 63-70
    • Karkola, S.1    Höltje, H.2    Wähälä, K.3
  • 25
    • 0022909044 scopus 로고
    • Inhibition of aromatase cytochrome P-450 (estrogen synthetase) by derivatives of α-naphthoflavone
    • Kellis Jr. J.T., Nesnow S., and Vickery L.E. Inhibition of aromatase cytochrome P-450 (estrogen synthetase) by derivatives of α-naphthoflavone. Biochem. Pharmacol. 35 (1986) 2887-2891
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 2887-2891
    • Kellis Jr., J.T.1    Nesnow, S.2    Vickery, L.E.3
  • 26
    • 0021271612 scopus 로고
    • Inhibition of human estrogen synthetase (aromatase) by flavones
    • Kellis Jr. J.T., and Vickery L.E. Inhibition of human estrogen synthetase (aromatase) by flavones. Science 225 (1984) 1032-1034
    • (1984) Science , vol.225 , pp. 1032-1034
    • Kellis Jr., J.T.1    Vickery, L.E.2
  • 27
    • 0023180688 scopus 로고
    • Purification and characterization of human placental aromatase cytochrome P-450
    • Kellis Jr. J.T., and Vickery L.E. Purification and characterization of human placental aromatase cytochrome P-450. J. Biol. Chem. 262 (1987) 4413-4420
    • (1987) J. Biol. Chem. , vol.262 , pp. 4413-4420
    • Kellis Jr., J.T.1    Vickery, L.E.2
  • 28
    • 0037598909 scopus 로고    scopus 로고
    • Phyto-oestrogen levels in foods: the design and construction of the VENUS database
    • Kiely M., Faughnan M., Wähälä K., and Brants H. Phyto-oestrogen levels in foods: the design and construction of the VENUS database. Br. J. Nutr. 89 (2003) S19-S23
    • (2003) Br. J. Nutr. , vol.89
    • Kiely, M.1    Faughnan, M.2    Wähälä, K.3    Brants, H.4
  • 29
    • 3242794236 scopus 로고    scopus 로고
    • Synthesis and aromatase inhibitory activity of novel pyridine-containing isoflavones
    • Kim Y.W., Hackett J.C., and Brueggemeier R.W. Synthesis and aromatase inhibitory activity of novel pyridine-containing isoflavones. J. Med. Chem. 47 (2004) 4032-4040
    • (2004) J. Med. Chem. , vol.47 , pp. 4032-4040
    • Kim, Y.W.1    Hackett, J.C.2    Brueggemeier, R.W.3
  • 30
    • 13944260141 scopus 로고    scopus 로고
    • Prediction of binding modes for ligands in the cytochromes P450 and other heme-containing proteins
    • Kirton S.B., Murray C.W., Verdonk M.L., and Taylor R.D. Prediction of binding modes for ligands in the cytochromes P450 and other heme-containing proteins. Proteins 58 (2005) 836-844
    • (2005) Proteins , vol.58 , pp. 836-844
    • Kirton, S.B.1    Murray, C.W.2    Verdonk, M.L.3    Taylor, R.D.4
  • 31
    • 33747732175 scopus 로고    scopus 로고
    • Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate
    • Kuhnel K., Blankenfeldt W., Terner J., and Schlichting I. Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate. J. Biol. Chem. 281 (2006) 23990-23998
    • (2006) J. Biol. Chem. , vol.281 , pp. 23990-23998
    • Kuhnel, K.1    Blankenfeldt, W.2    Terner, J.3    Schlichting, I.4
  • 33
    • 0032217117 scopus 로고    scopus 로고
    • Aromatase and 17β-hydroxysteroid dehydrogenase inhibition by flavonoids
    • Le Bail J.C., Laroche T., Marre-Fournier F., and Habrioux G. Aromatase and 17β-hydroxysteroid dehydrogenase inhibition by flavonoids. Cancer Lett. 133 (1998) 101-106
    • (1998) Cancer Lett. , vol.133 , pp. 101-106
    • Le Bail, J.C.1    Laroche, T.2    Marre-Fournier, F.3    Habrioux, G.4
  • 34
    • 0028813639 scopus 로고
    • Crystal structure of cytochrome P450cam complexed with its catalytic product, 5-exo-hydroxycamphor
    • Li H., Narasimhulu S., Havran L.M., Winkler J.D., and Poulos T.L. Crystal structure of cytochrome P450cam complexed with its catalytic product, 5-exo-hydroxycamphor. J. Am. Chem. Soc 117 (1995) 6297-6299
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 6297-6299
    • Li, H.1    Narasimhulu, S.2    Havran, L.M.3    Winkler, J.D.4    Poulos, T.L.5
  • 35
    • 33845400991 scopus 로고    scopus 로고
    • Epidemiologic evidence suggests that dietary phytoestrogen intake is associated with reduced risk of breast cancer
    • Lof M., and Weiderpass E. Epidemiologic evidence suggests that dietary phytoestrogen intake is associated with reduced risk of breast cancer. Nutr. Res. 26 (2006) 609-619
    • (2006) Nutr. Res. , vol.26 , pp. 609-619
    • Lof, M.1    Weiderpass, E.2
  • 36
    • 0034124357 scopus 로고    scopus 로고
    • Phyto-oestrogen content of berries, and plasma concentrations and urinary excretion of enterolactone after a single strawberry-meal in human subjects
    • Mazura W.M., Uehara M., Wähälä K., and Adlercreutz H. Phyto-oestrogen content of berries, and plasma concentrations and urinary excretion of enterolactone after a single strawberry-meal in human subjects. Br. J. Nutr. 83 (2000) 381-387
    • (2000) Br. J. Nutr. , vol.83 , pp. 381-387
    • Mazura, W.M.1    Uehara, M.2    Wähälä, K.3    Adlercreutz, H.4
  • 37
    • 18344372815 scopus 로고    scopus 로고
    • Intake of the plant lignans secoisolariciresinol, matairesinol, lariciresinol, and pinoresinol in Dutch men and women
    • Milder I.E., Feskens E.J., Arts I.C., de Mesquita H.B., Hollman P.C., and Kromhout D. Intake of the plant lignans secoisolariciresinol, matairesinol, lariciresinol, and pinoresinol in Dutch men and women. J. Nutr. 135 (2005) 1202-1207
    • (2005) J. Nutr. , vol.135 , pp. 1202-1207
    • Milder, I.E.1    Feskens, E.J.2    Arts, I.C.3    de Mesquita, H.B.4    Hollman, P.C.5    Kromhout, D.6
  • 38
    • 3242802726 scopus 로고    scopus 로고
    • Optimization of a liquid chromatography-tandem mass spectrometry method for quantification of the plant lignans secoisolariciresinol, matairesinol, lariciresinol, and pinoresinol in foods
    • Milder I.E.J., Arts I.C.W., Venema D.P., Lasaroms J.J.P., Wahala K., and Hollman P.C.H. Optimization of a liquid chromatography-tandem mass spectrometry method for quantification of the plant lignans secoisolariciresinol, matairesinol, lariciresinol, and pinoresinol in foods. J. Agric. Food Chem. 52 (2004) 4643-4651
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 4643-4651
    • Milder, I.E.J.1    Arts, I.C.W.2    Venema, D.P.3    Lasaroms, J.J.P.4    Wahala, K.5    Hollman, P.C.H.6
  • 39
    • 0030593681 scopus 로고    scopus 로고
    • ERβ: identification and characterization of a novel human estrogen receptor
    • Mosselman S., Polman J., and Dijkema R. ERβ: identification and characterization of a novel human estrogen receptor. FEBS Lett. 392 (1996) 49-53
    • (1996) FEBS Lett. , vol.392 , pp. 49-53
    • Mosselman, S.1    Polman, J.2    Dijkema, R.3
  • 40
    • 3242798960 scopus 로고    scopus 로고
    • Phytoestrogens and their human metabolites show distinct agonistic and antagonistic properties on estrogen receptor α (ERα) and ERβ in human cells
    • Mueller S.O., Simon S., Chae K., Metzler M., and Korach K.S. Phytoestrogens and their human metabolites show distinct agonistic and antagonistic properties on estrogen receptor α (ERα) and ERβ in human cells. Toxicol. Sci. 80 (2004) 14-25
    • (2004) Toxicol. Sci. , vol.80 , pp. 14-25
    • Mueller, S.O.1    Simon, S.2    Chae, K.3    Metzler, M.4    Korach, K.S.5
  • 41
    • 33947278808 scopus 로고    scopus 로고
    • Androgens and estrogens in the etiology and prevention of breast cancer
    • Muti P., Rogan E., and Cavalieri E. Androgens and estrogens in the etiology and prevention of breast cancer. Nutr. Cancer 56 (2006) 247-252
    • (2006) Nutr. Cancer , vol.56 , pp. 247-252
    • Muti, P.1    Rogan, E.2    Cavalieri, E.3
  • 42
    • 43549098380 scopus 로고    scopus 로고
    • Combining computational and biochemical studies for a rationale on the anti-aromatase activity of natural polyphenols
    • Neves M.A.C., Dinis T.C.P., Colombo G., and Sa e Melo M.L. Combining computational and biochemical studies for a rationale on the anti-aromatase activity of natural polyphenols. ChemMedChem 2 (2007) 1750-1762
    • (2007) ChemMedChem , vol.2 , pp. 1750-1762
    • Neves, M.A.C.1    Dinis, T.C.P.2    Colombo, G.3    Sa e Melo, M.L.4
  • 43
  • 44
    • 84872647271 scopus 로고    scopus 로고
    • A new class of nonsteroidal aromatase inhibitors: design and synthesis of chromone and xanthone derivatives and inhibition of the P450 enzymes aromatase and 17α-hydroxylase/C17,20-lyase
    • Recanatini M., Bisi A., Cavalli A., Belluti F., Gobbi S., Rampa A., Valenti P., Palzer M., Palusczak A., and Hartmann R.W. A new class of nonsteroidal aromatase inhibitors: design and synthesis of chromone and xanthone derivatives and inhibition of the P450 enzymes aromatase and 17α-hydroxylase/C17,20-lyase. J. Med. Chem. 44 (2001) 672-680
    • (2001) J. Med. Chem. , vol.44 , pp. 672-680
    • Recanatini, M.1    Bisi, A.2    Cavalli, A.3    Belluti, F.4    Gobbi, S.5    Rampa, A.6    Valenti, P.7    Palzer, M.8    Palusczak, A.9    Hartmann, R.W.10
  • 45
    • 22144453224 scopus 로고    scopus 로고
    • Molecular design of two sterol 14α-demethylase homology models and their interactions with the azole antifungals ketoconazole and bifonazole
    • Rupp B., Raub S., Marian C., and Höltje H. Molecular design of two sterol 14α-demethylase homology models and their interactions with the azole antifungals ketoconazole and bifonazole. J. Comput. Aid. Mol. Des. 19 (2005) 149-163
    • (2005) J. Comput. Aid. Mol. Des. , vol.19 , pp. 149-163
    • Rupp, B.1    Raub, S.2    Marian, C.3    Höltje, H.4
  • 47
    • 8444243681 scopus 로고    scopus 로고
    • Induction and inhibition of aromatase (CYP19) activity by natural and synthetic flavonoid compounds in H295R human adrenocortical carcinoma cells
    • Sanderson J.T., Hordijk J., Denison M.S., Springsteel M.F., Nantz M.H., and van den Berg M. Induction and inhibition of aromatase (CYP19) activity by natural and synthetic flavonoid compounds in H295R human adrenocortical carcinoma cells. Toxicol. Sci. 82 (2004) 70-79
    • (2004) Toxicol. Sci. , vol.82 , pp. 70-79
    • Sanderson, J.T.1    Hordijk, J.2    Denison, M.S.3    Springsteel, M.F.4    Nantz, M.H.5    van den Berg, M.6
  • 48
    • 0036319584 scopus 로고    scopus 로고
    • To block estrogen's synthesis or action: that is the question
    • Santen R. To block estrogen's synthesis or action: that is the question. J. Clin. Endocrinol. Metab. 87 (2002) 3007-3012
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , pp. 3007-3012
    • Santen, R.1
  • 49
    • 0141459632 scopus 로고    scopus 로고
    • 7,8-Benzoflavone: a phytotoxin from root exudates of invasive Russian knapweed
    • Stermitz F.R., Bais H.P., Foderaro T.A., and Vivanco J.M. 7,8-Benzoflavone: a phytotoxin from root exudates of invasive Russian knapweed. Phytochemistry 64 (2003) 493-497
    • (2003) Phytochemistry , vol.64 , pp. 493-497
    • Stermitz, F.R.1    Bais, H.P.2    Foderaro, T.A.3    Vivanco, J.M.4
  • 51
    • 27544469200 scopus 로고    scopus 로고
    • Lead optimization of 7-benzyloxy 2-(4′-pyridylmethyl)thioisoflavone aromatase inhibitors
    • Su B., Hackett J.C., Diaz Cruz E.S., Kim Y.W., and Brueggemeier R.W. Lead optimization of 7-benzyloxy 2-(4′-pyridylmethyl)thioisoflavone aromatase inhibitors. Bioorg. Med. Chem. 13 (2005) 6571-6577
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 6571-6577
    • Su, B.1    Hackett, J.C.2    Diaz Cruz, E.S.3    Kim, Y.W.4    Brueggemeier, R.W.5
  • 52
    • 60249099247 scopus 로고    scopus 로고
    • Tripos Inc, 2006. Sybyl Version 7.3, Tripos Inc, St. Louis, MO, USA
    • Tripos Inc., 2006. Sybyl Version 7.3, Tripos Inc., St. Louis, MO, USA.
  • 55
    • 0033661736 scopus 로고    scopus 로고
    • Human intestinal bacteria capable of transforming secoisolariciresinol diglucoside to mammalian lignans, enterodiol and enterolactone
    • Wang L.Q., Meselhy M.R., Li Y., Qin G.W., and Hattori M. Human intestinal bacteria capable of transforming secoisolariciresinol diglucoside to mammalian lignans, enterodiol and enterolactone. Chem. Pharm. Bull. (Tokyo) 48 (2000) 1606-1610
    • (2000) Chem. Pharm. Bull. (Tokyo) , vol.48 , pp. 1606-1610
    • Wang, L.Q.1    Meselhy, M.R.2    Li, Y.3    Qin, G.W.4    Hattori, M.5
  • 56
    • 0030945127 scopus 로고    scopus 로고
    • A nuclear paramagnetic relaxation study of the interaction of the cyclopentanedione substrate with chloroperoxidase
    • Wang X., and Goff H.M. A nuclear paramagnetic relaxation study of the interaction of the cyclopentanedione substrate with chloroperoxidase. Biochim. Biophys. Acta 1339 (1997) 88-96
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 88-96
    • Wang, X.1    Goff, H.M.2
  • 57
    • 0020490511 scopus 로고
    • Heme ligand replacement reactions of cytochrome P-450. Characterization of the bonding atom of the axial ligand trans to thiolate as oxygen
    • White R., and Coon M. Heme ligand replacement reactions of cytochrome P-450. Characterization of the bonding atom of the axial ligand trans to thiolate as oxygen. J. Biol. Chem. 257 (1982) 3073-3083
    • (1982) J. Biol. Chem. , vol.257 , pp. 3073-3083
    • White, R.1    Coon, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.