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Volumn 212, Issue 3, 1998, Pages 394-402

Laminin α1 chain G domain peptide, RKRLQVQLSIRT, inhibits epithelial branching morphogenesis of cultured embryonic mouse submandibular gland

Author keywords

Basement membrane; Laminin 2; Laminin 1; Morphogenesis; Organ culture; Submandibular gland; Synthetic peptide

Indexed keywords

INTEGRIN; LAMININ; UVOMORULIN; LAMININ A; LAMININ ALPHA2; PEPTIDE;

EID: 0031596408     PISSN: 10588388     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0177(199807)212:3<394::AID-AJA7>3.0.CO;2-C     Document Type: Article
Times cited : (41)

References (47)
  • 1
    • 0022239959 scopus 로고
    • Synthetic peptides competitively inhibit both direct binding to fibroblasts and functional biological assays for the purified cell-binding domain of fibronectin
    • Akiyama SK, Yamada KM. Synthetic peptides competitively inhibit both direct binding to fibroblasts and functional biological assays for the purified cell-binding domain of fibronectin. J. Biol. Chem. 1985;260:10402-10405.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10402-10405
    • Akiyama, S.K.1    Yamada, K.M.2
  • 2
    • 0001911828 scopus 로고    scopus 로고
    • Integrin-mediated cellular interactions with laminins
    • Ekblom P, Timpl R, eds. Amsterdam, The Netherlands: Harwood Academic Publishers
    • Aumailley M, Gimond C, Rousselle P. Integrin-mediated cellular interactions with laminins. In: Ekblom P, Timpl R, eds. The Laminins. Amsterdam, The Netherlands: Harwood Academic Publishers, 1996:127-158.
    • (1996) The Laminins , pp. 127-158
    • Aumailley, M.1    Gimond, C.2    Rousselle, P.3
  • 3
    • 0026703151 scopus 로고
    • Basement membrane heparan sulfate proteoglycan binds to laminin by its heparan sulfate chains and to nidogen by sites in the protein core
    • Battaglia C, Mayer U, Aumailley M, Timpl R. Basement membrane heparan sulfate proteoglycan binds to laminin by its heparan sulfate chains and to nidogen by sites in the protein core. Eur. J. Biochem 1992;208:359-366.
    • (1992) Eur. J. Biochem , vol.208 , pp. 359-366
    • Battaglia, C.1    Mayer, U.2    Aumailley, M.3    Timpl, R.4
  • 4
    • 0002830044 scopus 로고
    • Remodeling of the basement membrane as a mechanism of morphogenetic tissue interaction
    • Trelstad R, ed. New York: Alan R. Liss
    • Bernfield M, Banerjee SD, Koda J, Rapraeger A. Remodeling of the basement membrane as a mechanism of morphogenetic tissue interaction. In: Trelstad R, ed. The Role of Extracellular Matrix in Development. New York: Alan R. Liss, 1984:545-572.
    • (1984) The Role of Extracellular Matrix in Development , pp. 545-572
    • Bernfield, M.1    Banerjee, S.D.2    Koda, J.3    Rapraeger, A.4
  • 5
    • 0000729316 scopus 로고
    • The development in vitro of the submandibular and sublingual glands of Mus musculus
    • Borghese E. The development in vitro of the submandibular and sublingual glands of Mus musculus. J. Anat. 1950;84:287-302.
    • (1950) J. Anat. , vol.84 , pp. 287-302
    • Borghese, E.1
  • 7
    • 0030960916 scopus 로고    scopus 로고
    • Laminin E8 alveolarization site: Heparin sensitivity, cell surface receptors, and role in cell spreading
    • Chen L, Shick V, Matter ML, Laurie SM, Ogle RC, Laurie GW. Laminin E8 alveolarization site: Heparin sensitivity, cell surface receptors, and role in cell spreading. Am. J. Physiol. 1997;272:L494-L503.
    • (1997) Am. J. Physiol. , vol.272
    • Chen, L.1    Shick, V.2    Matter, M.L.3    Laurie, S.M.4    Ogle, R.C.5    Laurie, G.W.6
  • 8
    • 0029925628 scopus 로고    scopus 로고
    • Inhibition of laminin α1-chain expression leads to alteration of basement membrane assembly and cell differentiation
    • De Arcangelis A, Neuville P, Boukamel R, Lefebvre O, Kedinger M, Simon-Assmann P. Inhibition of laminin α1-chain expression leads to alteration of basement membrane assembly and cell differentiation. J Cell Biol 1996;133:417-430.
    • (1996) J Cell Biol , vol.133 , pp. 417-430
    • De Arcangelis, A.1    Neuville, P.2    Boukamel, R.3    Lefebvre, O.4    Kedinger, M.5    Simon-Assmann, P.6
  • 11
    • 0002633584 scopus 로고    scopus 로고
    • Laminin isoforms in development
    • Ekblom P, Timpl R, eds. Amsterdam, The Netherlands: Harwood Academic Publishers
    • Ekblom P, Durbeej M, Ekblom M. Laminin isoforms in development. In: Ekblom P, Timpl R, eds. The Laminins. Amsterdam, The Netherlands: Harwood Academic Publishers, 1996:185-216.
    • (1996) The Laminins , pp. 185-216
    • Ekblom, P.1    Durbeej, M.2    Ekblom, M.3
  • 12
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti JM, Campbell KP. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol. 1993;122:809-823.
    • (1993) J. Cell Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 13
    • 0026538680 scopus 로고
    • A synthetic peptide derived from the carboxy terminus of the laminin A chain represents a binding site for the α3β1 integrin
    • Gehlsen KR, Sriramarao P, Furcht LT, Skubitz APN. A synthetic peptide derived from the carboxy terminus of the laminin A chain represents a binding site for the α3β1 integrin. J. Cell Biol. 1992;117:449-459.
    • (1992) J. Cell Biol. , vol.117 , pp. 449-459
    • Gehlsen, K.R.1    Sriramarao, P.2    Furcht, L.T.3    Skubitz, A.P.N.4
  • 14
    • 84908559184 scopus 로고
    • Epithelio-mesenchymal specificity in the morphogenesis of mouse sub-mandibular rudiments in vitro
    • Grobstein C. Epithelio-mesenchymal specificity in the morphogenesis of mouse sub-mandibular rudiments in vitro. J. Exp. Zool. 1953;124: 383-413.
    • (1953) J. Exp. Zool. , vol.124 , pp. 383-413
    • Grobstein, C.1
  • 15
    • 0027013814 scopus 로고
    • Salivary gland morphogenesis: Possible involvement of collagenase
    • Hayakawa T, Kishi J, Nakanishi Y. Salivary gland morphogenesis: Possible involvement of collagenase. Matrix Supplement 1992;1:344-351.
    • (1992) Matrix Supplement , vol.1 , pp. 344-351
    • Hayakawa, T.1    Kishi, J.2    Nakanishi, Y.3
  • 16
    • 4243984509 scopus 로고
    • Laminin peptides promote acinar-like development of a human submandibular gland cell line (HSG) in vitro
    • Hoffman MP, Kibbey MC, Nomizu M, Kleinman HK. Laminin peptides promote acinar-like development of a human submandibular gland cell line (HSG) in vitro. Mol. Biol. Cell 1995;6:169a.
    • (1995) Mol. Biol. Cell , vol.6
    • Hoffman, M.P.1    Kibbey, M.C.2    Nomizu, M.3    Kleinman, H.K.4
  • 17
    • 0028960136 scopus 로고
    • Antibodies against domain E3 of laminin-1 and integrin α6 subunit perturb branching epithelial morphogenesis of submandibular gland, but by different modes
    • Kadoya Y, Kadoya K, Durbeej M, Holmvall K, Sorokin L, Ekblom P. Antibodies against domain E3 of laminin-1 and integrin α6 subunit perturb branching epithelial morphogenesis of submandibular gland, but by different modes. J. Cell Biol. 1995;129:521-534.
    • (1995) J. Cell Biol. , vol.129 , pp. 521-534
    • Kadoya, Y.1    Kadoya, K.2    Durbeej, M.3    Holmvall, K.4    Sorokin, L.5    Ekblom, P.6
  • 18
    • 0031059074 scopus 로고    scopus 로고
    • Importance of nidogen binding to laminin γ1 for branching epithelial morphogenesis of the submandibular gland
    • Kadoya Y, Salmivirta K, Talts JF, Kadoya K, Mayer U, Timpl R, Ekblom P. Importance of nidogen binding to laminin γ1 for branching epithelial morphogenesis of the submandibular gland. Development 1997;124:683-691.
    • (1997) Development , vol.124 , pp. 683-691
    • Kadoya, Y.1    Salmivirta, K.2    Talts, J.F.3    Kadoya, K.4    Mayer, U.5    Timpl, R.6    Ekblom, P.7
  • 19
    • 0025903916 scopus 로고
    • Reconstruction of the basement membrane in a cultured submandibular gland
    • Kadoya Y, Yamashina S. Reconstruction of the basement membrane in a cultured submandibular gland. Anat. Embryol. 1991;183:491-499.
    • (1991) Anat. Embryol. , vol.183 , pp. 491-499
    • Kadoya, Y.1    Yamashina, S.2
  • 20
    • 0027491315 scopus 로고
    • Distribution of α6 integrin subunit in developing mouse submandibular gland
    • Kadoya Y, Yamashina S. Distribution of α6 integrin subunit in developing mouse submandibular gland. J. Histochem. Cytochem. 1993;41:1707-1714.
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 1707-1714
    • Kadoya, Y.1    Yamashina, S.2
  • 21
    • 0031014760 scopus 로고    scopus 로고
    • Epidermal growth factor system is a physiological regulator of development of the mouse fetal submandibular gland and regulates expression of the α6-integrin subunit
    • Kashimata M, Gresik EG. Epidermal growth factor system is a physiological regulator of development of the mouse fetal submandibular gland and regulates expression of the α6-integrin subunit. Dev. Dyn. 1997;208:149-161.
    • (1997) Dev. Dyn. , vol.208 , pp. 149-161
    • Kashimata, M.1    Gresik, E.G.2
  • 22
    • 0023709019 scopus 로고
    • Role of laminin A chain in the development of epithelial cell polarity
    • Klein G, Langegger M, Timpl R, Ekblom P. Role of laminin A chain in the development of epithelial cell polarity. Cell 1988;55:331-341.
    • (1988) Cell , vol.55 , pp. 331-341
    • Klein, G.1    Langegger, M.2    Timpl, R.3    Ekblom, P.4
  • 23
    • 0008842849 scopus 로고    scopus 로고
    • Interaction of tumor cells with basement membranes and laminin-1
    • Ekblom P, Timpl R, eds. Amsterdam, The Netherlands: Harwood Academic Publishers
    • Martin GR, Liotta LA, Kleinman HK. Interaction of tumor cells with basement membranes and laminin-1. In: Ekblom P, Timpl R, eds. The Laminins. Amsterdam, The Netherlands: Harwood Academic Publishers, 1996:277-290.
    • (1996) The Laminins , pp. 277-290
    • Martin, G.R.1    Liotta, L.A.2    Kleinman, H.K.3
  • 24
    • 0028302929 scopus 로고
    • A novel laminin E8 cell adhesion site required for lung alveolar formation in vitro
    • Matter ML, Laurie GW. A novel laminin E8 cell adhesion site required for lung alveolar formation in vitro. J. Cell Biol. 1994;124:1083-1090.
    • (1994) J. Cell Biol. , vol.124 , pp. 1083-1090
    • Matter, M.L.1    Laurie, G.W.2
  • 25
    • 0030919488 scopus 로고    scopus 로고
    • The laminin α chains: Expression, developmental transitions, and chromosomal locations of α1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel α3 isoform
    • Miner JH, Patton BL, Lentz S, Gilbert DJ, Snider WD, Jenkins NA, Copeland NG, Sanes JR. The laminin α chains: Expression, developmental transitions, and chromosomal locations of α1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel α3 isoform. J. Cell Biol. 1997;137:685-701.
    • (1997) J. Cell Biol. , vol.137 , pp. 685-701
    • Miner, J.H.1    Patton, B.L.2    Lentz, S.3    Gilbert, D.J.4    Snider, W.D.5    Jenkins, N.A.6    Copeland, N.G.7    Sanes, J.R.8
  • 26
    • 0029965589 scopus 로고    scopus 로고
    • A mechanism for regulation of melanoma invasion: Ligation of α6β1 integrin by laminin G peptides
    • Nakahara H, Nomizu M, Akiyama SK, Yamada Y, Yeh Y, Chen W-T. A mechanism for regulation of melanoma invasion: Ligation of α6β1 integrin by laminin G peptides. J. Biol Chem. 1996;271:27221-27224.
    • (1996) J. Biol Chem. , vol.271 , pp. 27221-27224
    • Nakahara, H.1    Nomizu, M.2    Akiyama, S.K.3    Yamada, Y.4    Yeh, Y.5    Chen, W.-T.6
  • 27
    • 0029100640 scopus 로고
    • Identification of cell binding sites in the laminin α1 chain carboxyl-terminal globular domain by systematic screening of synthetic peptides
    • Nomizu M, Kim WH, Yamamura K, Utani A, Song S-Y, Otaka A, Roller PP, Kleinman HK, Yamada Y. Identification of cell binding sites in the laminin α1 chain carboxyl-terminal globular domain by systematic screening of synthetic peptides. J. Biol Chem. 1995;270:20583-20590.
    • (1995) J. Biol Chem. , vol.270 , pp. 20583-20590
    • Nomizu, M.1    Kim, W.H.2    Yamamura, K.3    Utani, A.4    Song, S.-Y.5    Otaka, A.6    Roller, P.P.7    Kleinman, H.K.8    Yamada, Y.9
  • 28
    • 0030605024 scopus 로고    scopus 로고
    • Active peptides from the carboxyl-terminal globular domain of laminin α2 and Drosophila α chains
    • Nomizu M, Song SY, Kuratomi Y, Tanaka M, Kim WH, Kleinman HK, Yamada Y. Active peptides from the carboxyl-terminal globular domain of laminin α2 and Drosophila α chains. FEBS Lett. 1996;396: 37-42.
    • (1996) FEBS Lett. , vol.396 , pp. 37-42
    • Nomizu, M.1    Song, S.Y.2    Kuratomi, Y.3    Tanaka, M.4    Kim, W.H.5    Kleinman, H.K.6    Yamada, Y.7
  • 29
    • 0026632905 scopus 로고
    • The all-D-configuration segment containing IKVAV sequence of laminin a chain has similar activities to the all-L-peptide in vitro and in vivo
    • Nomizu M, Utani A, Shiraishi N, Kibbey MC, Yamada Y, Roller PP. The all-D-configuration segment containing IKVAV sequence of laminin A chain has similar activities to the all-L-peptide in vitro and in vivo. J. Biol Chem. 1992;267:14118-14121.
    • (1992) J. Biol Chem. , vol.267 , pp. 14118-14121
    • Nomizu, M.1    Utani, A.2    Shiraishi, N.3    Kibbey, M.C.4    Yamada, Y.5    Roller, P.P.6
  • 31
    • 0027227388 scopus 로고
    • Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement membrane ligands
    • Pan T-C, Kluge M, Zhang R-Z, Fassler R, Timpl R, Chu M -L. Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement membrane ligands. Eur. J. Biochem. 1993;215:733-740.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 733-740
    • Pan, T.-C.1    Kluge, M.2    Zhang, R.-Z.3    Fassler, R.4    Timpl, R.5    Chu, M.L.6
  • 32
    • 0030068623 scopus 로고    scopus 로고
    • A novel recognition site on laminin for the α3β1 integrin
    • Pattaramalai S, Skubitz KM, Skubitz APN. A novel recognition site on laminin for the α3β1 integrin. Exp. Cell Res. 1996;222:281-290.
    • (1996) Exp. Cell Res. , vol.222 , pp. 281-290
    • Pattaramalai, S.1    Skubitz, K.M.2    Skubitz, A.P.N.3
  • 33
    • 0030579058 scopus 로고    scopus 로고
    • Identification of laminin α1 and α2 chain synthetic peptides that are active for attachment and neurite outgrowth with neuronal cell lines
    • Richard BL, Nomizu M, Yamada Y, Kleinman HK. Identification of laminin α1 and α2 chain synthetic peptides that are active for attachment and neurite outgrowth with neuronal cell lines. Exp. Cell Res. 1996;228:98-105.
    • (1996) Exp. Cell Res. , vol.228 , pp. 98-105
    • Richard, B.L.1    Nomizu, M.2    Yamada, Y.3    Kleinman, H.K.4
  • 34
    • 0023039303 scopus 로고
    • The AMeX method. A simplified technique of tissue processing and paraffin embedding with improved preservation of antigens for immunostaining
    • Sato Y, Mukai K, Watanabe S, Goto M, Shimosato Y. The AMeX method. A simplified technique of tissue processing and paraffin embedding with improved preservation of antigens for immunostaining. Am. J. Pathol. 1986;125:431-435.
    • (1986) Am. J. Pathol. , vol.125 , pp. 431-435
    • Sato, Y.1    Mukai, K.2    Watanabe, S.3    Goto, M.4    Shimosato, Y.5
  • 35
    • 0029060386 scopus 로고
    • Two separate domains of laminin promote lung organogenesis by different mechanisms of action
    • Schuger L, Skubitz APN, Murenas A, Gilbridge K. Two separate domains of laminin promote lung organogenesis by different mechanisms of action. Dev. Biol. 1995;169:520-532.
    • (1995) Dev. Biol. , vol.169 , pp. 520-532
    • Schuger, L.1    Skubitz, A.P.N.2    Murenas, A.3    Gilbridge, K.4
  • 36
    • 0025870487 scopus 로고
    • Identification of laminin domains involved in branching morphogenesis: Effects of anti-laminin monoclonal antibodies on mouse embryonic lung development
    • Schuger L, Skubitz APN, O'Shea S, Chang JF, Varani J. Identification of laminin domains involved in branching morphogenesis: Effects of anti-laminin monoclonal antibodies on mouse embryonic lung development. Dev. Biol. 1991;146:531-541.
    • (1991) Dev. Biol. , vol.146 , pp. 531-541
    • Schuger, L.1    Skubitz, A.P.N.2    O'Shea, S.3    Chang, J.F.4    Varani, J.5
  • 37
    • 0029582766 scopus 로고
    • Expression of laminin isoforms in mouse myogenic cells in vitro and in vivo
    • Schuler F, Sorokin L. Expression of laminin isoforms in mouse myogenic cells in vitro and in vivo. J. Cell Sci. 1995;108:3795-3805.
    • (1995) J. Cell Sci. , vol.108 , pp. 3795-3805
    • Schuler, F.1    Sorokin, L.2
  • 38
    • 0026347812 scopus 로고
    • Synthetic peptides from the carboxy-terminal globular domain of the A chain of laminin: Their ability to promote cell adhesion and neurite outgrowth, and interact with heparin and the β1 integrin subunit
    • Skubitz AP, Letourneau PC, Wayner E, Furcht LT. Synthetic peptides from the carboxy-terminal globular domain of the A chain of laminin: Their ability to promote cell adhesion and neurite outgrowth, and interact with heparin and the β1 integrin subunit. J Cell Biol 1991; 115: 1137-1148.
    • (1991) J Cell Biol , vol.115 , pp. 1137-1148
    • Skubitz, A.P.1    Letourneau, P.C.2    Wayner, E.3    Furcht, L.T.4
  • 39
    • 0025376296 scopus 로고
    • Integrin recognition of different cell-binding fragments of laminin (P1, E3, E8) and evidence that α6β1 but not α6β4 functions as a major receptor for fragment E8
    • Sonnenberg A, Linders CJT, Modderman PW, Damsky C, Aumailley M, Timpl R. Integrin recognition of different cell-binding fragments of laminin (P1, E3, E8) and evidence that α6β1 but not α6β4 functions as a major receptor for fragment E8. J. Cell Biol. 1990;110: 2145-2155.
    • (1990) J. Cell Biol. , vol.110 , pp. 2145-2155
    • Sonnenberg, A.1    Linders, C.J.T.2    Modderman, P.W.3    Damsky, C.4    Aumailley, M.5    Timpl, R.6
  • 40
    • 0026631140 scopus 로고
    • Monoclonal antibodies against laminin A chain fragment E3 and their effects on binding to cell and proteoglycan and on kidney development
    • Sorokin LM, Conzelmann S, Ekblom P, Battaglia C, Aumailley M, Timpl R. Monoclonal antibodies against laminin A chain fragment E3 and their effects on binding to cell and proteoglycan and on kidney development. Exp. Cell Res. 1992;201:137-144.
    • (1992) Exp. Cell Res. , vol.201 , pp. 137-144
    • Sorokin, L.M.1    Conzelmann, S.2    Ekblom, P.3    Battaglia, C.4    Aumailley, M.5    Timpl, R.6
  • 41
    • 0025148993 scopus 로고
    • Recognition of the laminin E8 cell-binding site by an integrin possessing the α6 subunit is essential for epithelial polarization in developing kidney tubules
    • Sorokin L, Sonnenberg A, Aumailley M, Timpl R, Ekblom P. Recognition of the laminin E8 cell-binding site by an integrin possessing the α6 subunit is essential for epithelial polarization in developing kidney tubules. J. Cell Biol. 1990;111:1265-1273.
    • (1990) J. Cell Biol. , vol.111 , pp. 1265-1273
    • Sorokin, L.1    Sonnenberg, A.2    Aumailley, M.3    Timpl, R.4    Ekblom, P.5
  • 42
    • 0002225901 scopus 로고    scopus 로고
    • Binding of laminins to extracellular matrix components
    • Ekblom P, Timpl R, eds. Amsterdam, The Netherlands: Harwood Academic Publishers
    • Timpl R. Binding of laminins to extracellular matrix components. In: Ekblom P, Timpl R, eds. The Laminins. Amsterdam, The Netherlands: Harwood Academic Publishers, 1996:97-125.
    • (1996) The Laminins , pp. 97-125
    • Timpl, R.1
  • 44
    • 0021267179 scopus 로고
    • Dualistic nature of adhesive protein function: Fibronectin and its biologically active peptide fragments can autoinhibit fibronectin function
    • Yamada KM, Kennedy DW. Dualistic nature of adhesive protein function: Fibronectin and its biologically active peptide fragments can autoinhibit fibronectin function. J. Cell Biol. 1984;99:29-36.
    • (1984) J. Cell Biol. , vol.99 , pp. 29-36
    • Yamada, K.M.1    Kennedy, D.W.2
  • 45
    • 0002517253 scopus 로고
    • Supramolecular organization of basement membranes
    • Rohrbach DH, Timpl R, eds. San Diego: Academic Press
    • Yurchenco PD, O'Rear J. Supramolecular organization of basement membranes. In: Rohrbach DH, Timpl R, eds. Molecular and Cellular Aspects of Basement Membranes. San Diego: Academic Press, 1993:20-47.
    • (1993) Molecular and Cellular Aspects of Basement Membranes , pp. 20-47
    • Yurchenco, P.D.1    O'Rear, J.2
  • 46
    • 0027416755 scopus 로고
    • Recombinant laminin G domain mediates myoblast adhesion and heparin binding
    • Yurchenco PD, Sung U, Ward MD, Yamada Y, O'Rear JJ. Recombinant laminin G domain mediates myoblast adhesion and heparin binding. J. Biol. Chem. 1993;268:8356-8365.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8356-8365
    • Yurchenco, P.D.1    Sung, U.2    Ward, M.D.3    Yamada, Y.4    O'Rear, J.J.5
  • 47
    • 0029935171 scopus 로고    scopus 로고
    • Fibulin-1 and fibulin-2 expression during organogenesis in the developing mouse embryo
    • Zhang H-Y, Timpl R, Sasaki T, Chu M-L, Ekblom P. Fibulin-1 and fibulin-2 expression during organogenesis in the developing mouse embryo. Dev. Dyn. 1996;205:348-364.
    • (1996) Dev. Dyn. , vol.205 , pp. 348-364
    • Zhang, H.-Y.1    Timpl, R.2    Sasaki, T.3    Chu, M.-L.4    Ekblom, P.5


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