메뉴 건너뛰기




Volumn 71, Issue 3-4, 1999, Pages 393-403

Adaptor proteins and T-cell antigen receptor signaling

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; LYMPHOCYTE ANTIGEN RECEPTOR; PROTEIN TYROSINE KINASE; T LYMPHOCYTE ANTIGEN;

EID: 0032917990     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0079-6107(98)00050-9     Document Type: Review
Times cited : (32)

References (53)
  • 1
    • 0030812812 scopus 로고    scopus 로고
    • Maintenance of human T-cell anergy: Blocking of IL-2 gene transcription by activated Rap1
    • Boussiotis V.A., Freeman G.J., Berezovskaya A., Barber D.L., Nadler L.M. Maintenance of human T-cell anergy: blocking of IL-2 gene transcription by activated Rap1. Science. 278:1997;124-128.
    • (1997) Science , vol.278 , pp. 124-128
    • Boussiotis, V.A.1    Freeman, G.J.2    Berezovskaya, A.3    Barber, D.L.4    Nadler, L.M.5
  • 2
    • 0028245832 scopus 로고
    • A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T-cells
    • Buday L., Egan S.E., Rodriguez Viciana P., Cantrell D.A., Downward J. A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T-cells. J. Biol. Chem. 269:1994;9019-9023.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9019-9023
    • Buday, L.1    Egan, S.E.2    Rodriguez Viciana, P.3    Cantrell, D.A.4    Downward, J.5
  • 3
    • 0029874657 scopus 로고    scopus 로고
    • T-cell antigen receptor signal transduction pathways
    • Cantrell D. T-cell antigen receptor signal transduction pathways. Annu. Rev. Immunol. 14:1996;259-274.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 259-274
    • Cantrell, D.1
  • 4
    • 0032537743 scopus 로고    scopus 로고
    • A coordinating role for Vav?
    • Cantrell D. A coordinating role for Vav? Curr. Biol. 8:1998;R535-R538.
    • (1998) Curr. Biol. , vol.8
    • Cantrell, D.1
  • 5
    • 0030175744 scopus 로고    scopus 로고
    • Regulation of antigen receptor signal transduction by protein tyrosine kinases
    • Chan A.C., Shaw A.S. Regulation of antigen receptor signal transduction by protein tyrosine kinases. Curr. Opin. Immunol. 8:1996;394-401.
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 394-401
    • Chan, A.C.1    Shaw, A.S.2
  • 7
    • 0031033292 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product
    • Crespo P., Schuebel K.E., Ostrom A.A., Gutkind J.S., Bustelo X.R. Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product. Nature. 385:1997;169-172.
    • (1997) Nature , vol.385 , pp. 169-172
    • Crespo, P.1    Schuebel, K.E.2    Ostrom, A.A.3    Gutkind, J.S.4    Bustelo, X.R.5
  • 9
    • 0027910431 scopus 로고
    • Association of Sos Ras exchange factor with Grb2 is implicated in tyrosine kinase signal transduction and transformation
    • Egan S.E., Giddings B.W., Brooks M.W., Buday L., Sizeland A.M., Weinberg R.A. Association of Sos Ras exchange factor with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature. 363:1993;45-51.
    • (1993) Nature , vol.363 , pp. 45-51
    • Egan, S.E.1    Giddings, B.W.2    Brooks, M.W.3    Buday, L.4    Sizeland, A.M.5    Weinberg, R.A.6
  • 10
    • 0029051695 scopus 로고
    • The SH3 domain-binding T-cell tyrosyl phosphoprotein p120: Demonstration of its identity with the c-cbl protooncogene product and in vivo complexes with Fyn, Grb2 and phosphatidylinositol 3-kinase
    • Fukazawa T., Reedquist K.A., Trub T., Soltoff S., Panchamoorthy G., Druker B., Cantley L., Shoelson S.E., Band H. The SH3 domain-binding T-cell tyrosyl phosphoprotein p120: demonstration of its identity with the c-cbl protooncogene product and in vivo complexes with Fyn, Grb2 and phosphatidylinositol 3-kinase. J. Biol. Chem. 270:1995;19141-19150.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19141-19150
    • Fukazawa, T.1    Reedquist, K.A.2    Trub, T.3    Soltoff, S.4    Panchamoorthy, G.5    Druker, B.6    Cantley, L.7    Shoelson, S.E.8    Band, H.9
  • 11
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi D.N., Ghosh P., Utz U., Fan Q.R., Biddison W.E., Wiley D.C. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature. 384:1996;134-141.
    • (1996) Nature , vol.384 , pp. 134-141
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddison, W.E.5    Wiley, D.C.6
  • 13
    • 0030576521 scopus 로고    scopus 로고
    • Peptide-surface association: The case of PDZ and PTB domains
    • Harrison S.C. Peptide-surface association: the case of PDZ and PTB domains. Cell. 86:1996;341-343.
    • (1996) Cell , vol.86 , pp. 341-343
    • Harrison, S.C.1
  • 14
    • 0029117423 scopus 로고
    • Specific association of the beta isoform of the p85 subunit of phosphatidylinositol-3 kinase with the proto-oncogene c-cbl
    • Hartley D., Meisner H., Corvera S. Specific association of the beta isoform of the p85 subunit of phosphatidylinositol-3 kinase with the proto-oncogene c-cbl. J. Biol. Chem. 270:1995;18260-18263.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18260-18263
    • Hartley, D.1    Meisner, H.2    Corvera, S.3
  • 15
    • 0030010956 scopus 로고    scopus 로고
    • Signaling through CD28/CTLA-4 family receptors: Puzzling participation of phosphatidylinositol-3 kinase
    • Hutchcroft J.E., Bierer B.E. Signaling through CD28/CTLA-4 family receptors: puzzling participation of phosphatidylinositol-3 kinase. J. Immunol. 156:1996;4071-4074.
    • (1996) J. Immunol. , vol.156 , pp. 4071-4074
    • Hutchcroft, J.E.1    Bierer, B.E.2
  • 17
    • 0029006745 scopus 로고
    • Cloning and characterization of cbl-b: A SH3 binding protein with homology to the c-cbl proto-oncogene
    • Keane M.M., Rivero-Lezcano O.M., Mitchell J.A., Robbins K.C., Lipkowitz S. Cloning and characterization of cbl-b: a SH3 binding protein with homology to the c-cbl proto-oncogene. Oncogene. 10:1995;2367-2377.
    • (1995) Oncogene , vol.10 , pp. 2367-2377
    • Keane, M.M.1    Rivero-Lezcano, O.M.2    Mitchell, J.A.3    Robbins, K.C.4    Lipkowitz, S.5
  • 18
    • 0030849128 scopus 로고    scopus 로고
    • The role of Grb2-associated proteins in T-cell activation
    • Koretzky G.A. The role of Grb2-associated proteins in T-cell activation. Immunol. Today. 18:1997;401-406.
    • (1997) Immunol. Today , vol.18 , pp. 401-406
    • Koretzky, G.A.1
  • 19
    • 0030950608 scopus 로고    scopus 로고
    • Modular peptide recognition domains in eukaryotic signaling
    • Kuriyan J., Cowburn D. Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. 26:1997;259-288.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 259-288
    • Kuriyan, J.1    Cowburn, D.2
  • 20
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • Lemmon M.A., Ferguson K.M., Schlessinger J. PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell. 85:1996;621-624.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 21
    • 0030614453 scopus 로고    scopus 로고
    • 2+-stimulated activation of nuclear factor of activated T-cells by a constitutively active Cbl mutant in T-cells
    • 2+-stimulated activation of nuclear factor of activated T-cells by a constitutively active Cbl mutant in T-cells. J. Biol. Chem. 272:1997;168-173.
    • (1997) J. Biol. Chem. , vol.272 , pp. 168-173
    • Liu, Y.C.1    Elly, C.2    Langdon, W.Y.3    Altman, A.4
  • 22
    • 0030948462 scopus 로고    scopus 로고
    • Serine phosphorylation of Cbl induced by phorbol ester enhances its association with 14-3-3 proteins in T-cells via a novel serine-rich 14-3-3-binding motif
    • Liu Y.C., Liu Y., Elly C., Yoshida H., Lipkowitz S., Altman A. Serine phosphorylation of Cbl induced by phorbol ester enhances its association with 14-3-3 proteins in T-cells via a novel serine-rich 14-3-3-binding motif. J. Biol. Chem. 272:1997;9979-9985.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9979-9985
    • Liu, Y.C.1    Liu, Y.2    Elly, C.3    Yoshida, H.4    Lipkowitz, S.5    Altman, A.6
  • 24
    • 10144243337 scopus 로고    scopus 로고
    • A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T-cells
    • Lupher M. Jr., Reedquist K.A., Miyake S., Langdon W.Y., Band H. A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T-cells. J. Biol. Chem. 271:1996;24063-24068.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24063-24068
    • Lupher M., Jr.1    Reedquist, K.A.2    Miyake, S.3    Langdon, W.Y.4    Band, H.5
  • 25
    • 0029281993 scopus 로고
    • SH3 domains: Minding your p's and q's
    • Mayer B.J., Eck M.J. SH3 domains: minding your p's and q's. Curr. Biol. 5:1995;364-367.
    • (1995) Curr. Biol. , vol.5 , pp. 364-367
    • Mayer, B.J.1    Eck, M.J.2
  • 26
    • 0029034440 scopus 로고
    • Interactions of Cbl with Grb2 and phosphatidylinositol 3′-kinase in activated Jurkat cells
    • Meisner H., Conway B.R., Hartley D., Czech M.P. Interactions of Cbl with Grb2 and phosphatidylinositol 3′-kinase in activated Jurkat cells. Mol. Cell. Biol. 15:1995;3571-3578.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3571-3578
    • Meisner, H.1    Conway, B.R.2    Hartley, D.3    Czech, M.P.4
  • 27
    • 0028101039 scopus 로고
    • In vivo association of Grb2 with pp116, a substrate of the T-cell antigen receptor-activated protein tyrosine kinase
    • Motto D.G., Ross S.E., Jackman J.K., Sun Q., Olson A.L., Findell P.R., Koretzky G.A. In vivo association of Grb2 with pp116, a substrate of the T-cell antigen receptor-activated protein tyrosine kinase. J. Biol. Chem. 269:1994;21608-21613.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21608-21613
    • Motto, D.G.1    Ross, S.E.2    Jackman, J.K.3    Sun, Q.4    Olson, A.L.5    Findell, P.R.6    Koretzky, G.A.7
  • 29
    • 0030959305 scopus 로고    scopus 로고
    • Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T-cell antigen receptor-stimulated protein tyrosine kinases
    • Musci M.A., Hendricks-Taylor L.R., Motto D.G., Paskind M., Kamens J., Turck C.W., Koretzky G.A. Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T-cell antigen receptor-stimulated protein tyrosine kinases. J. Biol. Chem. 272:1997;11674-11677.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11674-11677
    • Musci, M.A.1    Hendricks-Taylor, L.R.2    Motto, D.G.3    Paskind, M.4    Kamens, J.5    Turck, C.W.6    Koretzky, G.A.7
  • 30
    • 0029031806 scopus 로고
    • Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins
    • Neumeister E.N., Zhu Y., Richard S., Terhorst C., Chan A.C., Shaw A.S. Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins. Mol. Cell. Biol. 15:1995;3171-3178.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3171-3178
    • Neumeister, E.N.1    Zhu, Y.2    Richard, S.3    Terhorst, C.4    Chan, A.C.5    Shaw, A.S.6
  • 31
    • 0030889218 scopus 로고    scopus 로고
    • The product of the proto-oncogene c-cbl: A negative regulator of the Syk tyrosine kinase
    • Ota Y., Samelson L.E. The product of the proto-oncogene c-cbl: a negative regulator of the Syk tyrosine kinase. Science. 276:1997;418-420.
    • (1997) Science , vol.276 , pp. 418-420
    • Ota, Y.1    Samelson, L.E.2
  • 32
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T. Protein modules and signalling networks. Nature. 373:1995;573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 35
    • 0032563256 scopus 로고    scopus 로고
    • Impaired viability and profound block in thymocyte development in mice lacking the adaptor protein SLP-76
    • Pivniouk V., Tsitsikov E., Swinton P., Rathbun G., Alt F.W., Geha R.S. Impaired viability and profound block in thymocyte development in mice lacking the adaptor protein SLP-76. Cell. 94:1998;229-238.
    • (1998) Cell , vol.94 , pp. 229-238
    • Pivniouk, V.1    Tsitsikov, E.2    Swinton, P.3    Rathbun, G.4    Alt, F.W.5    Geha, R.S.6
  • 36
    • 0028198388 scopus 로고
    • Activation of phosphatidylinositol-3′ kinase by Src-family kinase SH3 binding to the p85 subunit
    • Pleiman C.M., Hertz W.M., Cambier J.C. Activation of phosphatidylinositol-3′ kinase by Src-family kinase SH3 binding to the p85 subunit. Science. 263:1994;1609-1612.
    • (1994) Science , vol.263 , pp. 1609-1612
    • Pleiman, C.M.1    Hertz, W.M.2    Cambier, J.C.3
  • 37
    • 0028227284 scopus 로고
    • SH3 domains of the adapter molecule Grb2 complex with two proteins in T-cells: The guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T-cell antigen receptor-activated tyrosine kinases
    • Reif K., Buday L., Downward J., Cantrell D.A. SH3 domains of the adapter molecule Grb2 complex with two proteins in T-cells: the guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T-cell antigen receptor-activated tyrosine kinases. J. Biol. Chem. 269:1994;14081-14087.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14081-14087
    • Reif, K.1    Buday, L.2    Downward, J.3    Cantrell, D.A.4
  • 38
    • 0032503687 scopus 로고    scopus 로고
    • PtdIns-3,4,5-P3: A regulatory nexus between tyrosine kinases and sustained calcium signals
    • Scharenberg A.M., Kinet J.P. PtdIns-3,4,5-P3: a regulatory nexus between tyrosine kinases and sustained calcium signals. Cell. 94:1998;5-8.
    • (1998) Cell , vol.94 , pp. 5-8
    • Scharenberg, A.M.1    Kinet, J.P.2
  • 39
    • 0029832241 scopus 로고    scopus 로고
    • Isolation and characterization of murine vav2, a member of the vav family of proto-oncogenes
    • Schuebel K.E., Bustelo X.R., Nielsen D.A., Song B.J.B.M., Goldman D., Lee I.J. Isolation and characterization of murine vav2, a member of the vav family of proto-oncogenes. Oncogene. 13:1996;363-371.
    • (1996) Oncogene , vol.13 , pp. 363-371
    • Schuebel, K.E.1    Bustelo, X.R.2    Nielsen, D.A.3    Song, B.J.B.M.4    Goldman, D.5    Lee, I.J.6
  • 40
    • 0030737886 scopus 로고    scopus 로고
    • Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production
    • da Silva A.J., Li Z., de Vera C., Canto E., Findell P., Rudd C.E. Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production. Proc. Natl. Acad. Sci. USA. 94:1997;7493-7498.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7493-7498
    • Da Silva, A.J.1    Li, Z.2    De Vera, C.3    Canto, E.4    Findell, P.5    Rudd, C.E.6
  • 42
    • 0031030988 scopus 로고    scopus 로고
    • The role of a lymphoid-restricted, Grb2-like SH3-SH2-SH3 protein in T-cell receptor signaling
    • Trub T., Frantz J.D., Miyazaki M., Band H., Shoelson S.E. The role of a lymphoid-restricted, Grb2-like SH3-SH2-SH3 protein in T-cell receptor signaling. J. Biol. Chem. 272:1997;894-902.
    • (1997) J. Biol. Chem. , vol.272 , pp. 894-902
    • Trub, T.1    Frantz, J.D.2    Miyazaki, M.3    Band, H.4    Shoelson, S.E.5
  • 43
    • 0029658306 scopus 로고    scopus 로고
    • P95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T-cells
    • Tuosto L., Michel F., Acuto O. p95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T-cells. J. Exp. Med. 184:1996;1161-1166.
    • (1996) J. Exp. Med. , vol.184 , pp. 1161-1166
    • Tuosto, L.1    Michel, F.2    Acuto, O.3
  • 44
    • 0030250114 scopus 로고    scopus 로고
    • Complex complexes: Signaling at the TCR
    • Wange R.L., Samelson L.E. Complex complexes: signaling at the TCR. Immunity. 5:1996;197-205.
    • (1996) Immunity , vol.5 , pp. 197-205
    • Wange, R.L.1    Samelson, L.E.2
  • 45
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss A., Littman D.R. Signal transduction by lymphocyte antigen receptors. Cell. 76:1994;263-274.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 46
    • 0028027340 scopus 로고
    • The T-cell antigen receptor: A multisubunit signaling complex
    • Weissman A.M. The T-cell antigen receptor: a multisubunit signaling complex. Chem. Immunol. 59:1994;1-18.
    • (1994) Chem. Immunol. , vol.59 , pp. 1-18
    • Weissman, A.M.1
  • 47
    • 0001584956 scopus 로고    scopus 로고
    • Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation
    • Wu J., Motto D.G., Koretzky G.A., Weiss A. Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation. Immunity. 4:1996;593-602.
    • (1996) Immunity , vol.4 , pp. 593-602
    • Wu, J.1    Motto, D.G.2    Koretzky, G.A.3    Weiss, A.4
  • 48
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T-cell activation
    • Xavier R., Brennan T., Li Q., McCormack C., Seed B. Membrane compartmentation is required for efficient T-cell activation. Immunity. 8:1998;723-732.
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 49
    • 0032541062 scopus 로고    scopus 로고
    • Uncoupling of nonreceptor tyrosine kinases from PLC-gamma1 in an SLP-76-deficient T-cell
    • Yablonski D., Kuhne M.R., Kadlecek T., Weiss A. Uncoupling of nonreceptor tyrosine kinases from PLC-gamma1 in an SLP-76-deficient T-cell. Science. 281:1998;413-416.
    • (1998) Science , vol.281 , pp. 413-416
    • Yablonski, D.1    Kuhne, M.R.2    Kadlecek, T.3    Weiss, A.4
  • 50
    • 0028915948 scopus 로고
    • Defective signalling through the T- and B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene
    • Zhang R., Alt F.W., Davidson L., Orkin S.H., Swat W. Defective signalling through the T- and B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene. Nature. 374:1995;470-473.
    • (1995) Nature , vol.374 , pp. 470-473
    • Zhang, R.1    Alt, F.W.2    Davidson, L.3    Orkin, S.H.4    Swat, W.5
  • 51
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The ZAP-70 tyrosine kinase substrate that links T-cell receptor to cellular activation
    • Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E. LAT: the ZAP-70 tyrosine kinase substrate that links T-cell receptor to cellular activation. Cell. 92:1998;83-92.
    • (1998) Cell , vol.92 , pp. 83-92
    • Zhang, W.1    Sloan-Lancaster, J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 52
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T-cell activation
    • Zhang, W., Trible, R.P., Samelson, L.E., 1998b. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T-cell activation. Immunity, 9, 239-246.
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3
  • 53
    • 0030764963 scopus 로고    scopus 로고
    • T-cell receptor-induced phosphorylation of Sos requires activity of CD45, Lck and protein kinase C, but not ERK
    • Zhao H., Li Y.Y., Fucini R.V., Ross S.E., Pessin J.E., Koretzky G.A. T-cell receptor-induced phosphorylation of Sos requires activity of CD45, Lck and protein kinase C, but not ERK. J. Biol. Chem. 272:1997;21625-21634.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21625-21634
    • Zhao, H.1    Li, Y.Y.2    Fucini, R.V.3    Ross, S.E.4    Pessin, J.E.5    Koretzky, G.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.