메뉴 건너뛰기




Volumn 48, Issue 3, 2000, Pages 181-187

Plant seeds: An exciting model system for dissecting molecular and cellular regulation of metabolic processes

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0006080449     PISSN: 07929978     EISSN: 22238980     Source Type: Journal    
DOI: 10.1560/EEEP-KB7G-GGQH-5V0R     Document Type: Article
Times cited : (2)

References (45)
  • 1
    • 0020132174 scopus 로고
    • Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons
    • Chrispeels, M., Higgins, T., and Spencer, D. 1982a. Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons. J. Cell. Biol. 93:306–313.
    • (1982) J. Cell. Biol , vol.93 , pp. 306-313
    • Chrispeels, M.1    Higgins, T.2    Spencer, D.3
  • 2
    • 0345504761 scopus 로고    scopus 로고
    • The role of Opaque2 in the control of lysine-degrading activities in developing maize endosperm
    • Kemper, E.L., Neto, G.C., Papes, F., Moraes, K.C., Leite, A., and Arruda, P. 1999. The role of Opaque2 in the control of lysine-degrading activities in developing maize endosperm. Plant Cell 11:1981–1994.
    • (1999) Plant Cell , vol.11 , pp. 1981-1994
    • Kemper, E.L.1    Neto, G.C.2    Papes, F.3    Moraes, K.C.4    Leite, A.5    Arruda, P.6
  • 3
    • 0348199154 scopus 로고    scopus 로고
    • Aquaporins and water permeability of plant membranes
    • Maurel, C. 1997. Aquaporins and water permeability of plant membranes. Annu. Rev. Plant Physiol. Plant Mol. Biol. 48:399–429.
    • (1997) Annu. Rev. Plant Physiol. Plant Mol. Biol , vol.48 , pp. 399-429
    • Maurel, C.1
  • 4
    • 0030758692 scopus 로고    scopus 로고
    • The enzymology of lysine catabolism in rice seeds. Isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase/ saccharopine dehydrogenase bifunctional polypeptide
    • Gaziola, A., Teixeira, C.M.G., Lugli, J., Sodek, L., and Azevedo, R.A. 1997. The enzymology of lysine catabolism in rice seeds. Isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase/ saccharopine dehydrogenase bifunctional polypeptide. Eur. J. Biochem. 247:364–371.
    • (1997) Eur. J. Biochem , vol.247 , pp. 364-371
    • Gaziola, A.1    Teixeira, C.M.G.2    Lugli, J.3    Sodek, L.4    Azevedo, R.A.5
  • 5
    • 0030042427 scopus 로고    scopus 로고
    • Purification of characterization of the bifunctional enzyme lysine-ketoglutarate reductasesaccharopine dehydrogenase from maize
    • Goncalves-Butruille, M., Szajner, P., Torigoi, E., Leite, A., and Arruda, P. 1996. Purification of characterization of the bifunctional enzyme lysine-ketoglutarate reductasesaccharopine dehydrogenase from maize. Plant Physiol. 110:765–771.
    • (1996) Plant Physiol , vol.110 , pp. 765-771
    • Goncalves-Butruille, M.1    Szajner, P.2    Torigoi, E.3    Leite, A.4    Arruda, P.5
  • 6
    • 0033574441 scopus 로고    scopus 로고
    • Posttranslational removal of the carboxyterminal KDEL of the cysteine protease SH-EP occurs prior to maturation of the enzyme
    • Okomoto, T., Minamikawa, T., Edward, G., Vakharia, V., and Herman, E.M. 1999. Posttranslational removal of the carboxyterminal KDEL of the cysteine protease SH-EP occurs prior to maturation of the enzyme. J. Biol. Chem. 274:11390–11398.
    • (1999) J. Biol. Chem , vol.274 , pp. 11390-11398
    • Okomoto, T.1    Minamikawa, T.2    Edward, G.3    Vakharia, V.4    Herman, E.M.5
  • 7
    • 0021199211 scopus 로고
    • Familial hyperlysinemias: Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities
    • Markovitz, P.J., Chuang, D.T., and Cox, R.P. 1984. Familial hyperlysinemias:purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. J. Biol. Chem. 259:11643–11646.
    • (1984) J. Biol. Chem , vol.259 , pp. 11643-11646
    • Markovitz, P.J.1    Chuang, D.T.2    Cox, R.P.3
  • 8
    • 0030014157 scopus 로고    scopus 로고
    • Plant cells contain two functionally distinct vacuolar compartments
    • Paris, N., Stanley, C.M., Jones, R.L., and Rogers, J.C. 1996. Plant cells contain two functionally distinct vacuolar compartments. Cell 85:563–572.
    • (1996) Cell , vol.85 , pp. 563-572
    • Paris, N.1    Stanley, C.M.2    Jones, R.L.3    Rogers, J.C.4
  • 9
    • 0031224915 scopus 로고    scopus 로고
    • Molecular cloning and further characterization of a probable plant vacuolar sorting receptor
    • Paris, N., Rogers, S., Jiang, L., Kirsch, T., Beevers, T., Phillips, T., and Rogers, J. 1997. Molecular cloning and further characterization of a probable plant vacuolar sorting receptor. Plant Physiol. 115:29–39.
    • (1997) Plant Physiol , vol.115 , pp. 29-39
    • Paris, N.1    Rogers, S.2    Jiang, L.3    Kirsch, T.4    Beevers, T.5    Phillips, T.6    Rogers, J.7
  • 10
    • 0032189507 scopus 로고    scopus 로고
    • A cysteine endoprotease with a C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinsome, a putative lytic compartment
    • Schmid, M., Simpson, D., Kalousek, F., and Gietl, S. 1998. A cysteine endoprotease with a C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinsome, a putative lytic compartment. Planta 206:466–475.
    • (1998) Planta , vol.206 , pp. 466-475
    • Schmid, M.1    Simpson, D.2    Kalousek, F.3    Gietl, S.4
  • 11
    • 0344988979 scopus 로고
    • The rough endoplasmic reticulum is the site of reserve-protein synthesis in developing Phaseolus vulgaris cotyledons
    • Bollini, R. and Chrispeels, M. 1979. The rough endoplasmic reticulum is the site of reserve-protein synthesis in developing Phaseolus vulgaris cotyledons. Planta 146:487– 501.
    • (1979) Planta , vol.146 , pp. 487-501
    • Bollini, R.1    Chrispeels, M.2
  • 12
    • 0020061795 scopus 로고
    • Role of the endoplasmic reticulum in the synthesis of reserve proteins and the kinetics of their transport to protein bodies in developing pea cotyledons
    • Chrispeels, M.J., Higgins, T.J.V., Craig, S., and Spencer, D. 1982b. Role of the endoplasmic reticulum in the synthesis of reserve proteins and the kinetics of their transport to protein bodies in developing pea cotyledons. J. Cell. Biol. 93:5–14.
    • (1982) J. Cell. Biol , vol.93 , pp. 5-14
    • Chrispeels, M.J.1    Higgins, T.J.V.2    Craig, S.3    Spencer, D.4
  • 13
    • 0005150736 scopus 로고    scopus 로고
    • A novel composite locus of Arabidopsis encoding simulatenously two polypeptides with metabolically related but distinct functions in lysine catabolism
    • Tang, G., Zhu, X., Tang, X., and Galili, G. 2000. A novel composite locus of Arabidopsis encoding simulatenously two polypeptides with metabolically related but distinct functions in lysine catabolism. Plant J. 21:1–10.
    • (2000) Plant J , vol.21 , pp. 1-10
    • Tang, G.1    Zhu, X.2    Tang, X.3    Galili, G.4
  • 14
    • 0018091598 scopus 로고
    • Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedlings by immunofluorescence microscopy
    • Baumgartner, B., Tokuyasu, K.T., and Chrispeels, M.J. 1978. Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedlings by immunofluorescence microscopy. J. Cell. Biol. 79:10–19.
    • (1978) J. Cell. Biol , vol.79 , pp. 10-19
    • Baumgartner, B.1    Tokuyasu, K.T.2    Chrispeels, M.J.3
  • 15
    • 0027380560 scopus 로고
    • Assembly and transport of seed storage proteins. Trends Cell
    • Galili, G., Altschuler, Y., and Levanony, H. 1993. Assembly and transport of seed storage proteins. Trends Cell. Biol. 3:437–443.
    • (1993) Biol , vol.3 , pp. 437-443
    • Galili, G.1    Altschuler, Y.2    Levanony, H.3
  • 16
    • 0026478698 scopus 로고
    • Evidence for a novel route of wheat storage proteins to vacuoles
    • Levanony, H., Rubin, R., Altschuler, Y., and Galili, G. 1992. Evidence for a novel route of wheat storage proteins to vacuoles. J. Cell Biol. 119:1117–1128.
    • (1992) J. Cell Biol , vol.119 , pp. 1117-1128
    • Levanony, H.1    Rubin, R.2    Altschuler, Y.3    Galili, G.4
  • 17
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro, S. and Pelham, H.R.B. 1987. A C-terminal signal prevents secretion of luminal ER proteins. Cell 48:899–907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.B.2
  • 18
    • 0008283371 scopus 로고    scopus 로고
    • Protein bodies: Storage vacuoles in seeds
    • Galili, G. and Herman, E.M. 1997. Protein bodies:storage vacuoles in seeds. Adv. Bot. Res. 25:113–140.
    • (1997) Adv. Bot. Res , vol.25 , pp. 113-140
    • Galili, G.1    Herman, E.M.2
  • 19
    • 0034614933 scopus 로고    scopus 로고
    • Mass transport of proform of a KDEL-tailed proteinase (SH-EP) to protein storage vacuoles by ER-derived vesicle is involved in protein mobilization in germinating seeds
    • Toyooka, K., Okamoto, T., and Minamikawa, T. 2000. Mass transport of proform of a KDEL-tailed proteinase (SH-EP) to protein storage vacuoles by ER-derived vesicle is involved in protein mobilization in germinating seeds. J. Cell. Biol. 148:453–464.
    • (2000) J. Cell. Biol , vol.148 , pp. 453-464
    • Toyooka, K.1    Okamoto, T.2    Minamikawa, T.3
  • 20
    • 0002245187 scopus 로고
    • Structural aspects of protein accumulation in developing pea cotyledons I. Qualitative and quantitative changes in parenchyma cell vacuoles
    • Craig, S., Goodchild, D.J., and Hardham, A.R. 1979. Structural aspects of protein accumulation in developing pea cotyledons I. Qualitative and quantitative changes in parenchyma cell vacuoles. Aust. J. Plant Physiol. 6:81–98.
    • (1979) Aust. J. Plant Physiol , vol.6 , pp. 81-98
    • Craig, S.1    Goodchild, D.J.2    Hardham, A.R.3
  • 21
    • 0020527277 scopus 로고
    • In vivo and in vitro processing of seed reserve protein in the endoplasmic reticulum: Evidence for two glycosylation steps
    • Bollini, R., Vitale, A., Chrispeels, M.J. 1983. In vivo and in vitro processing of seed reserve protein in the endoplasmic reticulum:Evidence for two glycosylation steps. J. Cell. Biol. 96:999–1007.
    • (1983) J. Cell. Biol , vol.96 , pp. 999-1007
    • Bollini, R.1    Vitale, A.2    Chrispeels, M.J.3
  • 22
    • 0025443895 scopus 로고
    • An intrinsic tonoplast protein of protein storage vacuoles in seeds is structurally related to a bacterial solute transporter (GlpF)
    • Johnson, K., Hofte, H., and Chrispeels, M. 1990. An intrinsic tonoplast protein of protein storage vacuoles in seeds is structurally related to a bacterial solute transporter (GlpF). Plant Cell 2:525–532.
    • (1990) Plant Cell , vol.2 , pp. 525-532
    • Johnson, K.1    Hofte, H.2    Chrispeels, M.3
  • 23
    • 0030339563 scopus 로고    scopus 로고
    • The maize gamma-zein sequesters alpha-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm
    • Coleman, C.E., Herman, E.M., Takasaki, K., and Larkins, B.A. 1996. The maize gamma-zein sequesters alpha-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm. Plant Cell 8:2335–2345.
    • (1996) Plant Cell , vol.8 , pp. 2335-2345
    • Coleman, C.E.1    Herman, E.M.2    Takasaki, K.3    Larkins, B.A.4
  • 24
    • 0029411732 scopus 로고
    • The lysine-dependent stimulation of lysine catabolism in tobacco seeds requires calcium and protein phosphorylation
    • Karchi, H., Miron, D., Ben-Yaacov, S., and Galili, G. 1995. The lysine-dependent stimulation of lysine catabolism in tobacco seeds requires calcium and protein phosphorylation. Plant Cell 7:1963–1970.
    • (1995) Plant Cell , vol.7 , pp. 1963-1970
    • Karchi, H.1    Miron, D.2    Ben-Yaacov, S.3    Galili, G.4
  • 25
    • 0031131626 scopus 로고    scopus 로고
    • Cloning and subcellular location of an Arabidopsis receptor-like protein that shares common features with protein-sorting receptors of eukaryotic cells
    • Ahmed, S.U., Bar-Peled, M., and Raikhel, N.V. 1997. Cloning and subcellular location of an Arabidopsis receptor-like protein that shares common features with protein-sorting receptors of eukaryotic cells. Plant Physiol. 114:325–336.
    • (1997) Plant Physiol , vol.114 , pp. 325-336
    • Ahmed, S.U.1    Bar-Peled, M.2    Raikhel, N.V.3
  • 26
    • 0001438180 scopus 로고
    • An abundant, highly-conserved tonoplast protein in seeds
    • Johnson, K.D., Herman, E.M., and Chrispeels, M.J. 1989. An abundant, highly-conserved tonoplast protein in seeds. Plant Physiol. 91:1006–1013.
    • (1989) Plant Physiol , vol.91 , pp. 1006-1013
    • Johnson, K.D.1    Herman, E.M.2    Chrispeels, M.J.3
  • 27
    • 0031775092 scopus 로고    scopus 로고
    • Barley aleurone cells contain two types of vacuoles: Characterization of lytic organelles by use of fluorescent probes
    • Swanson, S., Bethke, P., and Jones, R. 1998. Barley aleurone cells contain two types of vacuoles:characterization of lytic organelles by use of fluorescent probes. Plant Cell 10:685–698.
    • (1998) Plant Cell , vol.10 , pp. 685-698
    • Swanson, S.1    Bethke, P.2    Jones, R.3
  • 28
    • 0031200912 scopus 로고    scopus 로고
    • Regulation of lysine catabolism through lysineketoglutarate reductase and saccharopine dehydrogenase in Arabidopsis
    • Tang, G., Miron, D., Zhu-Shimoni, J.X., and Galili, G. 1997. Regulation of lysine catabolism through lysineketoglutarate reductase and saccharopine dehydrogenase in Arabidopsis. Plant Cell 9:1–13.
    • (1997) Plant Cell , vol.9 , pp. 1-13
    • Tang, G.1    Miron, D.2    Zhu-Shimoni, J.X.3    Galili, G.4
  • 29
    • 0031795695 scopus 로고    scopus 로고
    • Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles
    • Hara-Nishimura, I., Shimada, T., Hatano, K., Takeuchi, Y., and Nishimura, M. 1998. Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles. Plant Cell 10:825–836.
    • (1998) Plant Cell , vol.10 , pp. 825-836
    • Hara-Nishimura, I.1    Shimada, T.2    Hatano, K.3    Takeuchi, Y.4    Nishimura, M.5
  • 30
    • 0032718660 scopus 로고    scopus 로고
    • Protein storage bodies and vacuoles
    • Herman, E.M. and Larkins, B.A. 1999. Protein storage bodies and vacuoles. Plant Cell 11:601–614.
    • (1999) Plant Cell , vol.11 , pp. 601-614
    • Herman, E.M.1    Larkins, B.A.2
  • 31
    • 0024978457 scopus 로고
    • Nucleotide sequence of cDNA for sulfhydrylendopeptidase (SH-EP) from cotyledons of germinating Vigna mungo seeds
    • Akasofu, H., Yamauchi, D., Mitsuhashi, W., and Minamikawa, T. 1989. Nucleotide sequence of cDNA for sulfhydrylendopeptidase (SH-EP) from cotyledons of germinating Vigna mungo seeds. Nucleic Acids Res 17:6733.
    • (1989) Nucleic Acids Res , vol.17 , pp. 6733
    • Akasofu, H.1    Yamauchi, D.2    Mitsuhashi, W.3    Minamikawa, T.4
  • 32
    • 0000430975 scopus 로고
    • Synthesis and deposition of zein in protein bodies of maize endosperm
    • Larkins, B.A. and Hurkman, W.J. 1978. Synthesis and deposition of zein in protein bodies of maize endosperm. Plant Physiol. 62:256–263.
    • (1978) Plant Physiol , vol.62 , pp. 256-263
    • Larkins, B.A.1    Hurkman, W.J.2
  • 33
    • 0034047474 scopus 로고    scopus 로고
    • Purification and characterization of bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase from developing soybean seeds
    • Miron, D., Ben-Yaacov, S., Reches, C., Schupper, A., and Galili, G. 2000. Purification and characterization of bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase from developing soybean seeds. Plant Physiol. 123:655–663.
    • (2000) Plant Physiol , vol.123 , pp. 655-663
    • Miron, D.1    Ben-Yaacov, S.2    Reches, C.3    Schupper, A.4    Galili, G.5
  • 34
    • 0031467950 scopus 로고    scopus 로고
    • In vitro dephosphorylation inhibits the activity of soybean lysine-ketoglutarate reductase in a lysine-regulated manner
    • Miron, D., Ben-Yaacov, S., Karchi, H., and Galili, G. 1997. In vitro dephosphorylation inhibits the activity of soybean lysine-ketoglutarate reductase in a lysine-regulated manner. Plant J. 12:1453–1458.
    • (1997) Plant J , vol.12 , pp. 1453-1458
    • Miron, D.1    Ben-Yaacov, S.2    Karchi, H.3    Galili, G.4
  • 35
    • 0028331761 scopus 로고
    • Lysine synthesis and catabolism are coordinately regulated during tobacco seed development
    • Karchi, H., Shaul, O., and Galili, G. 1994. Lysine synthesis and catabolism are coordinately regulated during tobacco seed development. Proc. Natl. Acad. Sci. USA 91:2577– 2581.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2577-2581
    • Karchi, H.1    Shaul, O.2    Galili, G.3
  • 36
    • 0028084173 scopus 로고
    • Storage proteins of vegetative plant tissues
    • Staswick, P.E. 1994. Storage proteins of vegetative plant tissues. Annu. Rev. Plant Physiol. Mol. Biol. 45:303–322.
    • (1994) Annu. Rev. Plant Physiol. Mol. Biol , vol.45 , pp. 303-322
    • Staswick, P.E.1
  • 37
    • 0030062575 scopus 로고    scopus 로고
    • Wheat storage proteins: Assembly, transport and deposition in protein bodies. Plant Physiol
    • Galili, G., Shimoni, Y., Giorini-Silfen, S., Levanony, H., Altschuler, Y., and Shani, N. 1996. Wheat storage proteins:Assembly, transport and deposition in protein bodies. Plant Physiol. Biochem. 34:245–252.
    • (1996) Biochem , vol.34 , pp. 245-252
    • Galili, G.1    Shimoni, Y.2    Giorini-Silfen, S.3    Levanony, H.4    Altschuler, Y.5    Shani, N.6
  • 38
    • 0032583163 scopus 로고    scopus 로고
    • Integral membrane protein sorting to vacuoles in plant cells: Evidence for two pathways
    • Jiang, L. and Rogers, J.C. 1998. Integral membrane protein sorting to vacuoles in plant cells:evidence for two pathways. J. Cell. Biol. 143:1183–1199.
    • (1998) J. Cell. Biol , vol.143 , pp. 1183-1199
    • Jiang, L.1    Rogers, J.C.2
  • 39
    • 0028833955 scopus 로고
    • Regulation of lysine and threonine synthesis
    • Galili, G. 1995. Regulation of lysine and threonine synthesis. Plant Cell 7:899–906.
    • (1995) Plant Cell , vol.7 , pp. 899-906
    • Galili, G.1
  • 40
    • 0001248948 scopus 로고
    • Seed specific expression of a bacterial desensitized aspartate kinase increases the production of seed threonine and methionine in transgenic tobacco
    • Karchi, H., Shaul, O., and Galili, G. 1993. Seed specific expression of a bacterial desensitized aspartate kinase increases the production of seed threonine and methionine in transgenic tobacco. Plant J. 3:721–727.
    • (1993) Plant J , vol.3 , pp. 721-727
    • Karchi, H.1    Shaul, O.2    Galili, G.3
  • 41
    • 0027691223 scopus 로고
    • Concerted regulation of lysine and threonine synthesis in tobacco plants expressing bacterial feedback-insensitive aspartate kinase and dihydrodipicolinate synthase. Plant Mol
    • Shaul, O. and Galili, G. 1993. Concerted regulation of lysine and threonine synthesis in tobacco plants expressing bacterial feedback-insensitive aspartate kinase and dihydrodipicolinate synthase. Plant Mol. Biol. 23:759–768.
    • (1993) Biol , vol.23 , pp. 759-768
    • Shaul, O.1    Galili, G.2
  • 42
    • 0031170901 scopus 로고    scopus 로고
    • The plant ER: A dynamic organelle composed of large number of discrete functional domains
    • Staehelin, L.A. 1997. The plant ER:A dynamic organelle composed of large number of discrete functional domains. Plant J. 11:1151–1165.
    • (1997) Plant J , vol.11 , pp. 1151-1165
    • Staehelin, L.A.1
  • 43
    • 0000018342 scopus 로고
    • The Golgi apparatus mediates the transport of phytohemagglutinin to the protein body in bean cotyledons
    • Chrispeels, M.J. 1983. The Golgi apparatus mediates the transport of phytohemagglutinin to the protein body in bean cotyledons. Planta 158:140–151.
    • (1983) Planta , vol.158 , pp. 140-151
    • Chrispeels, M.J.1
  • 44
    • 0033598774 scopus 로고    scopus 로고
    • Programmed cell death in castor bean endosperm is associated with the accumulation and release of a cysteine endopeptidase from ricinosomes
    • Schmid, M., Simpson, D., and Gietl, C. 1999. Programmed cell death in castor bean endosperm is associated with the accumulation and release of a cysteine endopeptidase from ricinosomes. Proc. Natl. Acad. Sci. USA 96:14159– 14164.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14159-14164
    • Schmid, M.1    Simpson, D.2    Gietl, C.3
  • 45
    • 0001188552 scopus 로고
    • Increased lysine synthesis in transgenic tobacco plants expressing a bacterial dihydrodipicolinate synthase in their chloroplasts
    • Shaul, O. and Galili, G. 1992. Increased lysine synthesis in transgenic tobacco plants expressing a bacterial dihydrodipicolinate synthase in their chloroplasts. Plant J. 2:203– 209.
    • (1992) Plant J , vol.2 , pp. 203-209
    • Shaul, O.1    Galili, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.