메뉴 건너뛰기




Volumn 95, Issue 7, 1998, Pages 927-937

The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen

Author keywords

[No Author keywords available]

Indexed keywords

DIETHYLSTILBESTROL; ESTROGEN RECEPTOR; TAMOXIFEN; TRANSCRIPTION FACTOR;

EID: 0032446607     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81717-1     Document Type: Article
Times cited : (2368)

References (59)
  • 1
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement
    • Adams, P.D., Pannu, N.S., Read, R.J., and Brünger, A.T. (1997). Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement. Proc. Natl. Acad. Sci. USA 94, 5018-5023.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5018-5023
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brünger, A.T.4
  • 3
    • 0029618368 scopus 로고
    • Steroid hormone receptors: Many actors in search of a plot
    • Beato, M., Herrlich, P., and Schutz, G. (1995). Steroid hormone receptors: many actors in search of a plot. Cell 83, 851-857.
    • (1995) Cell , vol.83 , pp. 851-857
    • Beato, M.1    Herrlich, P.2    Schutz, G.3
  • 4
    • 0025062215 scopus 로고
    • Role of the two activating domains of the oestrogen receptor in the cell-type and promoter-context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen
    • Berry, M., Metzger, D., and Chambon, P. (1990). Role of the two activating domains of the oestrogen receptor in the cell-type and promoter-context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen. EMBO J. 9, 2811-2818.
    • (1990) EMBO J. , vol.9 , pp. 2811-2818
    • Berry, M.1    Metzger, D.2    Chambon, P.3
  • 5
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
    • Bourguet, W., Ruff, M., Chambon, P., Gronemeyer, H., and Moras, D. (1995). Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α. Nature 375, 377-382.
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4. (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 9
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen, H., Lin, R.J., Schiltz, R.L., Chakravarti, D., Nash, A., Nagy, L., Privalsky, M.L., Nakatani, Y., and Evans, R.M. (1997). Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90, 569-580.
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6    Privalsky, M.L.7    Nakatani, Y.8    Evans, R.M.9
  • 10
    • 0026600841 scopus 로고
    • Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors
    • Danielian, P., White, R., Lees, J., and Parker, M. (1992). Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J. 11, 1025-1033.
    • (1992) EMBO J. , vol.11 , pp. 1025-1033
    • Danielian, P.1    White, R.2    Lees, J.3    Parker, M.4
  • 11
    • 0032230231 scopus 로고    scopus 로고
    • Nuclear receptor-binding sites of coactivators glucocorticoid receptor interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1): Multiple motifs with different binding specificities
    • Ding, S., Anderson, C., Ma, H., Hong, H., Uht, R., Kushner, P., and Stallcup, M. (1998). Nuclear receptor-binding sites of coactivators glucocorticoid receptor interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1): multiple motifs with different binding specificities. Mol. Endocrinol. 12, 302-313.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 302-313
    • Ding, S.1    Anderson, C.2    Ma, H.3    Hong, H.4    Uht, R.5    Kushner, P.6    Stallcup, M.7
  • 12
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. (1997). An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15, 132-134.
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 16
    • 0031026744 scopus 로고    scopus 로고
    • Clinical potential of new antiestrogens
    • Gradishar, W.J., and Jordan, V.C. (1997). Clinical potential of new antiestrogens. J. Clin. Oncol. 15, 840-852.
    • (1997) J. Clin. Oncol. , vol.15 , pp. 840-852
    • Gradishar, W.J.1    Jordan, V.C.2
  • 17
    • 0029898731 scopus 로고    scopus 로고
    • Tamoxifen: Teaching an old drug new tricks?
    • Grainger, D.J., and Metcalfe, J.C. (1996). Tamoxifen: teaching an old drug new tricks? Nat. Med. 2, 381-385.
    • (1996) Nat. Med. , vol.2 , pp. 381-385
    • Grainger, D.J.1    Metcalfe, J.C.2
  • 19
    • 0023681411 scopus 로고
    • Purification of T47D human progesterone receptor and immunochemical characterization with monoclonal antibodies
    • Greene, G., Harris, K., Bova, R., Kinders, R., Moore, B., and Nolan, C. (1988). Purification of T47D human progesterone receptor and immunochemical characterization with monoclonal antibodies. Mol. Endocrinol. 2, 714-726.
    • (1988) Mol. Endocrinol. , vol.2 , pp. 714-726
    • Greene, G.1    Harris, K.2    Bova, R.3    Kinders, R.4    Moore, B.5    Nolan, C.6
  • 22
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery, D., Kalkhoven, E., Hoare, S., and Parker, M. (1997). A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387, 733-736.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.4
  • 23
    • 0029979932 scopus 로고    scopus 로고
    • Carboxymethylation of the human estrogen receptor ligand-binding domain-estradiol complex: HPLC/ESMS peptide mapping shows that cysteine 447 does not react with iodoacetic acid
    • Hegy, G., Shackleton, C., Carlquist, M., Bonn, T., Engstrom, O., Sjoholm, P., and Witkowska, H. (1996). Carboxymethylation of the human estrogen receptor ligand-binding domain-estradiol complex: HPLC/ESMS peptide mapping shows that cysteine 447 does not react with iodoacetic acid. Steroids 61, 367-373.
    • (1996) Steroids , vol.61 , pp. 367-373
    • Hegy, G.1    Shackleton, C.2    Carlquist, M.3    Bonn, T.4    Engstrom, O.5    Sjoholm, P.6    Witkowska, H.7
  • 24
    • 0030950531 scopus 로고    scopus 로고
    • AF-2 activity and recruitment of steroid receptor coactivator 1 to the estrogen receptor depend on a lysine residue conserved in nuclear receptors
    • Henttu, P.M., Kalkhoven, E., and Parker, M.G. (1997). AF-2 activity and recruitment of steroid receptor coactivator 1 to the estrogen receptor depend on a lysine residue conserved in nuclear receptors. Mol. Cell. Biol. 17, 1832-1839.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1832-1839
    • Henttu, P.M.1    Kalkhoven, E.2    Parker, M.G.3
  • 25
    • 0029978605 scopus 로고    scopus 로고
    • GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors
    • Hong, H., Kohli, K., Trivedi, A., Johnson, D.L., and Stallcup, M.R. (1996). GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors. Proc. Natl. Acad. Sci. USA 93, 4948-4952.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4948-4952
    • Hong, H.1    Kohli, K.2    Trivedi, A.3    Johnson, D.L.4    Stallcup, M.R.5
  • 28
    • 0032126882 scopus 로고    scopus 로고
    • Antiestrogenic action of raloxifene and tamoxifen: Today and tomorrow
    • Jordan, V.C. (1998). Antiestrogenic action of raloxifene and tamoxifen: today and tomorrow. J. Natl. Cancer Inst. 90, 967-971.
    • (1998) J. Natl. Cancer Inst. , vol.90 , pp. 967-971
    • Jordan, V.C.1
  • 29
    • 0019941226 scopus 로고
    • Importance of the alkylaminoethoxy side-chain for the estrogenic and antiestrogenic actions of tamoxifen and trioxifene in the immature rat uterus
    • Jordan, V.C., and Gosden, B. (1982). Importance of the alkylaminoethoxy side-chain for the estrogenic and antiestrogenic actions of tamoxifen and trioxifene in the immature rat uterus. Mol. Cell. Endocrinol. 27, 291-306.
    • (1982) Mol. Cell. Endocrinol. , vol.27 , pp. 291-306
    • Jordan, V.C.1    Gosden, B.2
  • 32
    • 0002700643 scopus 로고
    • Halloween...masks and bones
    • S. Bailey, R. Hubbard, and D. Waller, eds. (Warrington, England: SERC Daresbury Laboratory)
    • Kleywegt, G.J., and Jones, T.A. (1994). Halloween...masks and bones. In From First Map to Final Model, S. Bailey, R. Hubbard, and D. Waller, eds. (Warrington, England: SERC Daresbury Laboratory).
    • (1994) From First Map to Final Model
    • Kleywegt, G.J.1    Jones, T.A.2
  • 33
    • 0028625491 scopus 로고
    • Insights from the study of animals lacking functional estrogen receptor
    • Korach, K. (1994). Insights from the study of animals lacking functional estrogen receptor. Science 266, 1524-1527.
    • (1994) Science , vol.266 , pp. 1524-1527
    • Korach, K.1
  • 34
    • 0031039888 scopus 로고    scopus 로고
    • Comparison of the ligand binding specificity and transcript tissue distribution of estrogen receptors alpha and beta
    • Kuiper, G.G., Carlsson, B., Grandien, K., Enmark, E., Haggblad, J., Nilsson, S., and Gustafsson, J.A. (1997). Comparison of the ligand binding specificity and transcript tissue distribution of estrogen receptors alpha and beta. Endocrinology 138, 863-870.
    • (1997) Endocrinology , vol.138 , pp. 863-870
    • Kuiper, G.G.1    Carlsson, B.2    Grandien, K.3    Enmark, E.4    Haggblad, J.5    Nilsson, S.6    Gustafsson, J.A.7
  • 35
    • 0023663885 scopus 로고
    • Functional domains of the human estrogen receptor
    • Kumar, V., Green, S., Stack, G., Berry, M., Jin, J.-R., and Chambon, P. (1987). Functional domains of the human estrogen receptor. Cell 51, 941-951.
    • (1987) Cell , vol.51 , pp. 941-951
    • Kumar, V.1    Green, S.2    Stack, G.3    Berry, M.4    Jin, J.-R.5    Chambon, P.6
  • 36
    • 0029841744 scopus 로고    scopus 로고
    • A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors
    • Le Douarin, B., Nielsen, A.L., Gamier, J.M., Ichinose, H., Jeanmougin, F., Losson, R., and Chambon, P. (1996). A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors. EMBO J. 15, 6701-6715.
    • (1996) EMBO J. , vol.15 , pp. 6701-6715
    • Le Douarin, B.1    Nielsen, A.L.2    Garnier, J.M.3    Ichinose, H.4    Jeanmougin, F.5    Losson, R.6    Chambon, P.7
  • 37
    • 0030872716 scopus 로고    scopus 로고
    • RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2
    • Li, H., Gomes, P.J., and Chen, J.D. (1997). RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc. Natl. Acad. Sci. USA 94, 8479-8484.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8479-8484
    • Li, H.1    Gomes, P.J.2    Chen, J.D.3
  • 38
    • 0001594912 scopus 로고
    • Raster3D version 2.0: A program for photorealistic molecular structures
    • Merritt, E.A., and Anderson, W.F. (1994). Raster3D Version 2.0: a program for photorealistic molecular structures. Acta Crystallogr. D 50, 219-220.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 219-220
    • Merritt, E.A.1    Anderson, W.F.2
  • 39
    • 0031833450 scopus 로고    scopus 로고
    • The nuclear receptor ligand-binding domain: Structure and function
    • Moras, D., and Gronemeyer, H. (1998). The nuclear receptor ligand-binding domain: structure and function. Curr. Opin. Cell Biol. 10, 384-391.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 384-391
    • Moras, D.1    Gronemeyer, H.2
  • 41
    • 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. D 53, 240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 42
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 43
    • 0032549531 scopus 로고    scopus 로고
    • Enhancement of estrogen receptor transcriptional activity by the coactivator GRIP-1 highlights the role of activation function 2 in determining estrogen receptor pharmacology
    • Norris, J.D., Fan, D., Stallcup, M.R., and McDonnell, D.P. (1998). Enhancement of estrogen receptor transcriptional activity by the coactivator GRIP-1 highlights the role of activation function 2 in determining estrogen receptor pharmacology. J. Biol. Chem. 273, 6679-6688.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6679-6688
    • Norris, J.D.1    Fan, D.2    Stallcup, M.R.3    McDonnell, D.P.4
  • 44
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor family
    • Onate, S.A., Tsai, S.Y., Tsai, M.-J., and O'Malley, B.W. (1995). Sequence and characterization of a coactivator for the steroid hormone receptor family. Science 270, 1354-1357.
    • (1995) Science , vol.270 , pp. 1354-1357
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.-J.3    O'Malley, B.W.4
  • 45
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997). Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 46
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid
    • Renaud, J., Rochel, N., Ruff, M., Vivat, V., Chambon, P., Gronemeyer, H., and Moras, D. (1995). Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature 378, 681-689.
    • (1995) Nature , vol.378 , pp. 681-689
    • Renaud, J.1    Rochel, N.2    Ruff, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6    Moras, D.7
  • 47
    • 0020067155 scopus 로고
    • Antiestrogen basicity - Activity relationships: A comparison of the estrogen receptor binding and antiuterotrophic potencies of several analogues of (Z)-1,2-diphenyl-1-[4-[2-(dimethylamino)ethoxy]phenyl]-1-butene (tamoxifen, Nolvadex) having altered basicity
    • Robertson, D.W., Katzenellenbogen, J.A., Hayes, J.R., and Katzenellenbogen, B.S. (1982). Antiestrogen basicity - activity relationships: a comparison of the estrogen receptor binding and antiuterotrophic potencies of several analogues of (Z)-1,2-diphenyl-1-[4-[2-(dimethylamino)ethoxy]phenyl]-1-butene (tamoxifen, Nolvadex) having altered basicity. J. Med. Chem. 25, 167-171.
    • (1982) J. Med. Chem. , vol.25 , pp. 167-171
    • Robertson, D.W.1    Katzenellenbogen, J.A.2    Hayes, J.R.3    Katzenellenbogen, B.S.4
  • 48
    • 0029058098 scopus 로고
    • Molecular characterization by mass spectrometry of the human estrogen receptor ligand-binding domain expressed in Escherichia coli
    • Seielstad, D., Carlson, K., Katzenellenbogen, J., Kushner, P., and Greene, G. (1995). Molecular characterization by mass spectrometry of the human estrogen receptor ligand-binding domain expressed in Escherichia coli. Mol. Endocrinol. 9, 647-658.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 647-658
    • Seielstad, D.1    Carlson, K.2    Katzenellenbogen, J.3    Kushner, P.4    Greene, G.5
  • 49
    • 0032490068 scopus 로고    scopus 로고
    • Breast cancer prevention trial shows major benefit, some risk
    • Smigel, K. (1998). Breast cancer prevention trial shows major benefit, some risk. J. Natl. Cancer Inst. 90, 647-648.
    • (1998) J. Natl. Cancer Inst. , vol.90 , pp. 647-648
    • Smigel, K.1
  • 51
    • 0032568527 scopus 로고    scopus 로고
    • Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains
    • Tanenbaum, D.M., Wang, Y., Williams, S.P., and Sigler, P.B. (1998). Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc. Natl. Acad. Sci. USA 95, 5998-6003.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5998-6003
    • Tanenbaum, D.M.1    Wang, Y.2    Williams, S.P.3    Sigler, P.B.4
  • 52
    • 0024440781 scopus 로고
    • The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties
    • Tora, L., Mullick, A., Metzger, D., Ponglikitmongkol, M., Park, I., and Chambon, P. (1989). The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties. EMBO J. 8, 1981-1986.
    • (1989) EMBO J. , vol.8 , pp. 1981-1986
    • Tora, L.1    Mullick, A.2    Metzger, D.3    Ponglikitmongkol, M.4    Park, I.5    Chambon, P.6
  • 53
    • 0030912539 scopus 로고    scopus 로고
    • The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function
    • Torchia, J., Rose, D., Inostroza, J., Kamel, Y., Westin, S., Glass, C., and Rosenfeld, M. (1997). The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387, 677-684.
    • (1997) Nature , vol.387 , pp. 677-684
    • Torchia, J.1    Rose, D.2    Inostroza, J.3    Kamel, Y.4    Westin, S.5    Glass, C.6    Rosenfeld, M.7
  • 54
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid receptor superfamily members
    • Tsai, M.J., and O'Malley, B.W. (1994). Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu. Rev. Biochem. 63, 451-486.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 451-486
    • Tsai, M.J.1    O'Malley, B.W.2
  • 55
    • 0029954339 scopus 로고    scopus 로고
    • TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors
    • Voegel, J.J., Heine, M.J.S., Zechel, C., Chambon, P., and Gronemeyer, H. (1996). TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15, 3667-3675.
    • (1996) EMBO J. , vol.15 , pp. 3667-3675
    • Voegel, J.J.1    Heine, M.J.S.2    Zechel, C.3    Chambon, P.4    Gronemeyer, H.5
  • 56
    • 0032518944 scopus 로고    scopus 로고
    • The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways
    • Voegel, J.J., Heine, M.J., Tini, M., Vivat, V., Chambon, P., and Gronemeyer, H. (1998). The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways. EMBO J. 17, 507-519.
    • (1998) EMBO J. , vol.17 , pp. 507-519
    • Voegel, J.J.1    Heine, M.J.2    Tini, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6
  • 57
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A.C., Laskowski, R.A., and Thornton, J.M. (1995). LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 58
    • 0027424372 scopus 로고
    • Structure-function analysis of the hormone binding domain of the human estrogen receptor by region-specific mutagenesis and phenotypic screening in yeast
    • Wrenn, C., and Katzenellenbogen, B. (1993). Structure-function analysis of the hormone binding domain of the human estrogen receptor by region-specific mutagenesis and phenotypic screening in yeast. J. Biol. Chem. 268, 24089-24098.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24089-24098
    • Wrenn, C.1    Katzenellenbogen, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.