메뉴 건너뛰기




Volumn 287, Issue 4, 2012, Pages 2739-2748

Molecular cloning of a xylosyltransferase that transfers the second xylose to O-glucosylated epidermal growth factor repeats of notch

Author keywords

[No Author keywords available]

Indexed keywords

CO-EXPRESSION; EMBRYONIC LETHALITY; ENDOPLASMIC RETICULUM; EPIDERMAL GROWTH FACTORS; EXTRACELLULAR DOMAINS; GENES ENCODING ENZYMES; GLYCANS; GLYCOSYL TRANSFERASE; HUMAN GENES; IN-VITRO; IN-VIVO; KNOCK OUTS; MEMBRANE-BOUND; MOLECULAR CLONING; N-ACETYLGLUCOSAMINE; NOTCH SIGNALING; O-FUCOSYLATION; O-LINKED; SF9 INSECT CELLS; TEMPERATURE DEPENDENT; TYPE II; XYLOSYLATION;

EID: 84856070820     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.302406     Document Type: Article
Times cited : (71)

References (46)
  • 1
    • 64249172203 scopus 로고    scopus 로고
    • The canonical Notch signaling pathway: Unfolding the activation mechanism
    • Kopan, R., and Ilagan, M. X. (2009) The canonical Notch signaling pathway: unfolding the activation mechanism. Cell 137, 216-233
    • (2009) Cell , vol.137 , pp. 216-233
    • Kopan, R.1    Ilagan, M.X.2
  • 2
    • 0034737738 scopus 로고    scopus 로고
    • Mammalian Notch1 is modified with two unusual forms of O-linked glycosylation found on epidermal growth factor-like modules
    • DOI 10.1074/jbc.275.13.9604
    • Moloney, D. J., Shair, L. H., Lu, F. M., Xia, J., Locke, R., Matta, K. L., and Haltiwanger, R. S. (2000) Mammalian Notch1 is modified with two unusual forms of O-linked glycosylation found on epidermal growth factor-like modules. J. Biol. Chem. 275, 9604-9611 (Pubitemid 30185192)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.13 , pp. 9604-9611
    • Moloney, D.J.1    Shair, L.H.2    Lu, F.M.3    Xia, J.4    Locke, R.5    Matta, K.L.6    Haltiwanger, R.S.7
  • 5
    • 0025192470 scopus 로고
    • The structure of (xylose)2glucose-O-serine 53 found in the first epidermal growth factor-like domain of bovine blood clotting factor IX
    • Hase, S., Nishimura, H., Kawabata, S., Iwanaga, S., and Ikenaka, T. (1990) The structure of (xylose)2glucose-O-serine 53 found in the first epidermal growth factor-like domain of bovine blood clotting factor IX. J. Biol. Chem. 265, 1858-1861
    • (1990) J. Biol. Chem. , vol.265 , pp. 1858-1861
    • Hase, S.1    Nishimura, H.2    Kawabata, S.3    Iwanaga, S.4    Ikenaka, T.5
  • 6
    • 77949896358 scopus 로고    scopus 로고
    • Mammalian Notch is modified by D-Xyl-α1,3-D-Xyl-α1-3-D-Glc- β1-O-Ser: Implementation of a method to study O-glucosylation
    • Whitworth, G. E., Zandberg, W. F., Clark, T., and Vocadlo, D. J. (2010) Mammalian Notch is modified by D-Xyl-α1,3-D-Xyl-α1-3-D-Glc-β1- O-Ser: implementation of a method to study O-glucosylation. Glycobiology 20, 287-299
    • (2010) Glycobiology , vol.20 , pp. 287-299
    • Whitworth, G.E.1    Zandberg, W.F.2    Clark, T.3    Vocadlo, D.J.4
  • 7
    • 0024377258 scopus 로고
    • 2-Glc)O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z
    • 2-Glc)O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z. J. Biol. Chem. 264, 20320-20325
    • (1989) J. Biol. Chem. , vol.264 , pp. 20320-20325
    • Nishimura, H.1    Kawabata, S.2    Kisiel, W.3    Hase, S.4    Ikenaka, T.5    Takao, T.6    Shimonishi, Y.7    Iwanaga, S.8
  • 8
    • 0026701391 scopus 로고
    • Human factor IX has a tetrasaccharideO-glycosidically linked to serine 61 through the fucose residue
    • Nishimura, H., Takao, T., Hase, S., Shimonishi, Y., and Iwanaga, S. (1992) Human factor IX has a tetrasaccharideO-glycosidically linked to serine 61 through the fucose residue. J. Biol. Chem. 267, 17520-17525
    • (1992) J. Biol. Chem. , vol.267 , pp. 17520-17525
    • Nishimura, H.1    Takao, T.2    Hase, S.3    Shimonishi, Y.4    Iwanaga, S.5
  • 9
    • 77954506026 scopus 로고    scopus 로고
    • Role of glycans and glycosyltransferases in the regulation of Notch signaling
    • Jafar-Nejad, H., Leonardi, J., and Fernandez-Valdivia, R. (2010) Role of glycans and glycosyltransferases in the regulation of Notch signaling. Glycobiology 20, 931-949
    • (2010) Glycobiology , vol.20 , pp. 931-949
    • Jafar-Nejad, H.1    Leonardi, J.2    Fernandez-Valdivia, R.3
  • 10
    • 35549010538 scopus 로고    scopus 로고
    • Regulation of Notch signaling by glycosylation
    • Stanley, P. (2007) Regulation of Notch signaling by glycosylation. Curr. Opin. Struct. Biol. 17, 530-535
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 530-535
    • Stanley, P.1
  • 11
    • 77955269485 scopus 로고    scopus 로고
    • Role of glycosylation of Notch in development
    • Takeuchi, H., and Haltiwanger, R. S. (2010) Role of glycosylation of Notch in development. Semin. Cell Dev. Biol. 21, 638-645
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 638-645
    • Takeuchi, H.1    Haltiwanger, R.S.2
  • 12
    • 0037074006 scopus 로고    scopus 로고
    • Regulation of Notch signaling by O-linked fucose
    • DOI 10.1016/S0092-8674(02)01114-5
    • Okajima, T., and Irvine, K. D. (2002) Regulation of Notch signaling by O-linked fucose. Cell 111, 893-904 (Pubitemid 36109160)
    • (2002) Cell , vol.111 , Issue.6 , pp. 893-904
    • Okajima, T.1    Irvine, K.D.2
  • 14
    • 0034253589 scopus 로고    scopus 로고
    • Fringe differentially modulates Jagged1 and Delta1 signaling through Notch1 and Notch2
    • Hicks, C., Johnston, S. H., diSibio, G., Collazo, A., Vogt, T. F., and Weinmaster, G. (2000) Fringe differentially modulates Jagged1 and Delta1 signaling through Notch1 and Notch2. Nat. Cell Biol. 2, 515-520
    • (2000) Nat. Cell Biol. , vol.2 , pp. 515-520
    • Hicks, C.1    Johnston, S.H.2    DiSibio, G.3    Collazo, A.4    Vogt, T.F.5    Weinmaster, G.6
  • 16
    • 0030845799 scopus 로고    scopus 로고
    • Serrate-mediated activation of Notch is specifically blocked by the product of the gene fringe in the dorsal compartment of the Drosophila wing imaginal disc
    • Fleming, R. J., Gu, Y., and Hukriede, N. A. (1997) Serrate-mediated activation of Notch is specifically blocked by the product of the gene fringe in the dorsal compartment of the Drosophila wing imaginal disc. Development 124, 2973-2981 (Pubitemid 27370912)
    • (1997) Development , vol.124 , Issue.15 , pp. 2973-2981
    • Fleming, R.J.1    Gu, Y.2    Hukriede, N.A.3
  • 17
    • 0030756962 scopus 로고    scopus 로고
    • Fringe modulates Notch-ligand interactions
    • DOI 10.1038/43191
    • Panin, V. M., Papayannopoulos, V., Wilson, R., and Irvine, K. D. (1997) Fringe modulates Notch-ligand interactions. Nature 387, 908-912 (Pubitemid 27289592)
    • (1997) Nature , vol.387 , Issue.6636 , pp. 908-912
    • Panin, V.M.1    Papayannopoulos, V.2    Wilson, R.3    Irvine, K.D.4
  • 18
    • 0242593940 scopus 로고    scopus 로고
    • Glycosyltransferase activity of Fringe modulates Notch-Delta interactions
    • DOI 10.1038/35019075
    • Brückner, K., Perez, L., Clausen, H., and Cohen, S. (2000) Glycosyltransferase activity of Fringe modulates Notch-Delta interactions. Nature 406, 411-415 (Pubitemid 30625560)
    • (2000) Nature , vol.406 , Issue.6794 , pp. 411-415
    • Bruckner, K.1    Perez, L.2    Clausen, H.3    Cohen, S.4
  • 19
    • 38649125625 scopus 로고    scopus 로고
    • Rumi Is a CAP10 Domain Glycosyltransferase that Modifies Notch and Is Required for Notch Signaling
    • DOI 10.1016/j.cell.2007.12.016, PII S0092867407016170
    • Acar, M., Jafar-Nejad, H., Takeuchi, H., Rajan, A., Ibrani, D., Rana, N. A., Pan, H., Haltiwanger, R. S., and Bellen, H. J. (2008) Rumi is a CAP10 domain glycosyltransferase that modifies Notch and is required for Notch signaling. Cell 132, 247-258 (Pubitemid 351172433)
    • (2008) Cell , vol.132 , Issue.2 , pp. 247-258
    • Acar, M.1    Jafar-Nejad, H.2    Takeuchi, H.3    Rajan, A.4    Ibrani, D.5    Rana, N.A.6    Pan, H.7    Haltiwanger, R.S.8    Bellen, H.J.9
  • 20
    • 79960763491 scopus 로고    scopus 로고
    • Multiple O-glucosylation sites on Notch function as a buffer against temperature-dependent loss of signaling
    • Leonardi, J., Fernandez-Valdivia, R., Li, Y. D., Simcox, A. A., and Jafar-Nejad, H. (2011) Multiple O-glucosylation sites on Notch function as a buffer against temperature-dependent loss of signaling. Development 138, 3569-3578
    • (2011) Development , vol.138 , pp. 3569-3578
    • Leonardi, J.1    Fernandez-Valdivia, R.2    Li, Y.D.3    Simcox, A.A.4    Jafar-Nejad, H.5
  • 25
    • 38449112888 scopus 로고    scopus 로고
    • Purification and substrate specificity of UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xylα1-3Xylα1-3Glcβ1-O-Ser on epidermal growth factor-like domains
    • DOI 10.1093/jb/mvm064
    • Ishimizu, T., Sano, K., Uchida, T., Teshima, H., Omichi, K., Hojo, H., Nakahara, Y., and Hase, S. (2007) Purification and substrate specificity of UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α1-3Xyl α1,3Glc β1-O-Ser on epidermal growth factor-like domains. J. Biochem. 141, 593-600 (Pubitemid 351455311)
    • (2007) Journal of Biochemistry , vol.141 , Issue.4 , pp. 593-600
    • Ishimizu, T.1    Sano, K.2    Uchida, T.3    Teshima, H.4    Omichi, K.5    Hojo, H.6    Nakahara, Y.7    Hase, S.8
  • 26
    • 0029799513 scopus 로고    scopus 로고
    • Detection of UDP-D-xylose:α-D-xyloside α1 → 3xylosyltransferase activity in human hepatoma cell line HepG2
    • Minamida, S., Aoki, K., Natsuka, S., Omichi, K., Fukase, K., Kusumoto, S., and Hase, S. (1996) Detection of UDP-D-xylose: α-D-xyloside α-3-xylosyltransferase activity in human hepatoma cell line HepG2. J. Biochem. 120, 1002-1006 (Pubitemid 26400024)
    • (1996) Journal of Biochemistry , vol.120 , Issue.5 , pp. 1002-1006
    • Minamida, S.1    Aoki, K.2    Natsuka, S.3    Omichi, K.4    Fukase, K.5    Kusumoto, S.6    Hase, S.7
  • 27
    • 0030901372 scopus 로고    scopus 로고
    • Presence of UDP-D-xylose: β-D-glucoside α-1,3-D- xylosyltransferase involved in the biosynthesis of the Xylα1-3Glcβ- Ser structure of glycoproteins in the human hepatoma cell line HepG2
    • Omichi, K., Aoki, K., Minamida, S., and Hase, S. (1997) Presence of UDPD- xylose: β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xylα1,3Glc β-Ser structure of glycoproteins in the human hepatoma cell line HepG2. Eur. J. Biochem. 245, 143-146 (Pubitemid 27142274)
    • (1997) European Journal of Biochemistry , vol.245 , Issue.1 , pp. 143-146
    • Omichi, K.1    Aoki, K.2    Minamida, S.3    Hase, S.4
  • 28
    • 76249087224 scopus 로고    scopus 로고
    • Identification of glycosyltransferase 8 family members as xylosyltransferases acting on O-glucosylated Notch epidermal growth factor repeats
    • Sethi, M. K., Buettner, F. F., Krylov, V. B., Takeuchi, H., Nifantiev, N. E., Haltiwanger, R. S., Gerardy-Schahn, R., and Bakker, H. (2010) Identification of glycosyltransferase 8 family members as xylosyltransferases acting on O-glucosylated Notch epidermal growth factor repeats. J. Biol. Chem. 285, 1582-1586
    • (2010) J. Biol. Chem. , vol.285 , pp. 1582-1586
    • Sethi, M.K.1    Buettner, F.F.2    Krylov, V.B.3    Takeuchi, H.4    Nifantiev, N.E.5    Haltiwanger, R.S.6    Gerardy-Schahn, R.7    Bakker, H.8
  • 30
    • 0037424256 scopus 로고    scopus 로고
    • Fringe modifies O-fucose on mouse Notch1 at epidermal growth factor-like repeats within the ligand-binding site and the Abruptex region
    • DOI 10.1074/jbc.M212221200
    • Shao, L., Moloney, D. J., and Haltiwanger, R. (2003) Fringe modifies O-fucose on mouse Notch1 at epidermal growth factor-like repeats within the ligand-binding site and the Abruptex region. J. Biol. Chem. 278, 7775-7782 (Pubitemid 36800510)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 7775-7782
    • Shao, L.1    Moloney, D.J.2    Haltiwanger, R.3
  • 31
    • 35548969455 scopus 로고    scopus 로고
    • Stereoselective synthesis of the 3-aminopropyl glycosides of α-D-xyl-(1→3)-β-D-glc and α-D-xyl-(1→3)-α-D- xyl-(1→3)-β-D-glc and of their corresponding N-octanoyl derivatives
    • DOI 10.1055/s-2007-990784
    • Krylov, V., Ustyuzhanina, N., Grachev, A., Bakker, H., and Nifantiev, N. (2007) Stereoselective synthesis of the 3-aminopropyl glycosides of α-D-Xyl-(1→3)β-D-Glc and α-D-Xyl-(1→3)-β-D-Xyl- (1→3)-β-D-Glc and of their corresponding N-octanoyl derivatives. Synthesis 2007, 3147-3154 (Pubitemid 350017488)
    • (2007) Synthesis , Issue.20 , pp. 3147-3154
    • Krylov, V.1    Ustyuzhanina, N.2    Grachev, A.3    Bakker, H.4    Nifantiev, N.5
  • 32
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 33
    • 0026793378 scopus 로고
    • 2-terminal fragment that includes the cytoplasmic and transmembrane domain is sufficient for Golgi retention
    • 2-terminal fragment that includes the cytoplasmic and transmembrane domain is sufficient for Golgi retention. J. Biol. Chem. 267, 9241-9247
    • (1992) J. Biol. Chem. , vol.267 , pp. 9241-9247
    • Russo, R.N.1    Shaper, N.L.2    Taatjes, D.J.3    Shaper, J.H.4
  • 34
    • 15744372996 scopus 로고    scopus 로고
    • O-fucosylation of notch occurs in the endoplasmic reticulum
    • DOI 10.1074/jbc.M414574200
    • Luo, Y., and Haltiwanger, R. S. (2005) O-Fucosylation of Notch occurs in the endoplasmic reticulum. J. Biol. Chem. 280, 11289-11294 (Pubitemid 40418435)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11289-11294
    • Luo, Y.1    Haltiwanger, R.S.2
  • 35
    • 0034644110 scopus 로고    scopus 로고
    • The Notch signalling regulator Fringe acts in the Golgi apparatus and requires the glycosyltransferase signature motif DxD
    • DOI 10.1016/S0960-9822(00)00578-9
    • Munro, S., and Freeman, M. (2000) The Notch signaling regulator fringe acts in the Golgi apparatus and requires the glycosyltransferase signature motif DXD. Curr. Biol. 10, 813-820 (Pubitemid 30597200)
    • (2000) Current Biology , vol.10 , Issue.14 , pp. 813-820
    • Munro, S.1    Freeman, M.2
  • 36
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • DOI 10.1016/j.jmb.2004.05.028, PII S0022283604005972
    • Bendtsen, J. D., Nielsen, H., von Heijne, G., and Brunak, S. (2004) Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol. 340, 783-795 (Pubitemid 38829638)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 37
    • 0023765635 scopus 로고
    • Glycogenin is the priming glucosyltransferase required for the initiation of glycogen biogenesis in rabbit skeletal muscle
    • Pitcher, J., Smythe, C., and Cohen, P. (1988) Glycogenin is the priming glucosyltransferase required for the initiation of glycogen biogenesis in rabbit skeletal muscle. Eur. J. Biochem. 176, 391-395
    • (1988) Eur. J. Biochem. , vol.176 , pp. 391-395
    • Pitcher, J.1    Smythe, C.2    Cohen, P.3
  • 38
    • 0028987945 scopus 로고
    • Drosophila UDP-glucose:Glycoprotein glucosyltransferase: Sequence and characterization of an enzyme that distinguishes between denatured and native proteins
    • Parker, C. G., Fessler, L. I., Nelson, R. E., and Fessler, J. H. (1995) Drosophila UDP-glucose:glycoprotein glucosyltransferase: sequence and characterization of an enzyme that distinguishes between denatured and native proteins. EMBO J. 14, 1294-1303
    • (1995) EMBO J. , vol.14 , pp. 1294-1303
    • Parker, C.G.1    Fessler, L.I.2    Nelson, R.E.3    Fessler, J.H.4
  • 39
    • 27244440999 scopus 로고    scopus 로고
    • Characterization of the LARGE family of putative glycosyltransferases associated with dystroglycanopathies
    • DOI 10.1093/glycob/cwi094
    • Grewal, P. K., McLaughlan, J. M., Moore, C. J., Browning, C. A., and Hewitt, J. E. (2005) Characterization of the LARGE family of putative glycosyltransferases associated with dystroglycanopathies. Glycobiology 15, 912-923 (Pubitemid 41511487)
    • (2005) Glycobiology , vol.15 , Issue.10 , pp. 912-923
    • Grewal, P.K.1    McLaughlan, J.M.2    Moore, C.J.3    Browning, C.A.4    Hewitt, J.E.5
  • 40
    • 0034975777 scopus 로고    scopus 로고
    • Mutant glycosyltransferase and altered glycosylation of α-dystroglycan in the myodystrophy mouse
    • DOI 10.1038/88865
    • Grewal, P. K., Holzfeind, P. J., Bittner, R. E., and Hewitt, J. E. (2001) Mutant glycosyltransferase and altered glycosylation of α-dystroglycan in the myodystrophy mouse. Nat. Genet. 28, 151-154 (Pubitemid 32538060)
    • (2001) Nature Genetics , vol.28 , Issue.2 , pp. 151-154
    • Grewal, P.K.1    Holzfeind, P.J.2    Bittner, R.E.3    Hewitt, J.E.4
  • 41
    • 57149096197 scopus 로고    scopus 로고
    • The diversity of O-linked glycans expressed during Drosophila melanogaster development reflects stage- and tissue-specific requirements for cell signaling
    • Aoki, K., Porterfield, M., Lee, S. S., Dong, B., Nguyen, K., McGlamry, K. H., and Tiemeyer, M. (2008) The diversity of O-linked glycans expressed during Drosophila melanogaster development reflects stage- and tissue-specific requirements for cell signaling. J. Biol. Chem. 283, 30385-30400
    • (2008) J. Biol. Chem. , vol.283 , pp. 30385-30400
    • Aoki, K.1    Porterfield, M.2    Lee, S.S.3    Dong, B.4    Nguyen, K.5    McGlamry, K.H.6    Tiemeyer, M.7
  • 42
    • 84856071317 scopus 로고    scopus 로고
    • Fringe benefits: Analysis of O-glycosylation and fringe elongation on the extracellular domain of Drosophila Notch
    • Rana, N. A., Xu, M. L., Moss, H., Rab, A., Leonardi, J., Jafar-Nejad, H., and Haltiwanger, R. S. (2010) Fringe benefits: Analysis of O-glycosylation and fringe elongation on the extracellular domain of Drosophila Notch. Glycobiology 20, 1486
    • (2010) Glycobiology , vol.20 , pp. 1486
    • Rana, N.A.1    Xu, M.L.2    Moss, H.3    Rab, A.4    Leonardi, J.5    Jafar-Nejad, H.6    Haltiwanger, R.S.7
  • 43
    • 80052422050 scopus 로고    scopus 로고
    • O-Glucose trisaccharide is present at high but variable stoichiometry at multiple sites on mouse Notch1
    • Rana, N. A., Nita-Lazar, A., Takeuchi, H., Kakuda, S., Luther, K. B., and Haltiwanger, R. S. (2011) O-Glucose trisaccharide is present at high but variable stoichiometry at multiple sites on mouse Notch1. J. Biol. Chem. 286, 31623-31637
    • (2011) J. Biol. Chem. , vol.286 , pp. 31623-31637
    • Rana, N.A.1    Nita-Lazar, A.2    Takeuchi, H.3    Kakuda, S.4    Luther, K.B.5    Haltiwanger, R.S.6
  • 44
    • 79953192555 scopus 로고    scopus 로고
    • The transmembrane domain of the molecular chaperone Cosmc directs its localization to the endoplasmic reticulum
    • Sun, Q., Ju, T., and Cummings, R. D. (2011) The transmembrane domain of the molecular chaperone Cosmc directs its localization to the endoplasmic reticulum. J. Biol. Chem. 286, 11529-11542
    • (2011) J. Biol. Chem. , vol.286 , pp. 11529-11542
    • Sun, Q.1    Ju, T.2    Cummings, R.D.3
  • 46
    • 5144227144 scopus 로고    scopus 로고
    • Motifs of two small residues can assist but are not sufficient to mediate transmembrane helix interactions
    • DOI 10.1016/j.jmb.2004.08.083, PII S0022283604010836
    • Schneider, D., and Engelman, D. M. (2004) Motifs of two small residues can assist but are not sufficient to mediate transmembrane helix interactions. J. Mol. Biol. 343, 799-804 (Pubitemid 39345944)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.4 , pp. 799-804
    • Schneider, D.1    Engelman, D.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.