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Volumn 179, Issue 11, 2007, Pages 7653-7662

Kinetics of MHC-CD8 interaction at the T cell membrane

Author keywords

[No Author keywords available]

Indexed keywords

CD8 ANTIGEN; CHOLESTEROL OXIDASE; HETERODIMER; HOMODIMER; MAJOR HISTOCOMPATIBILITY ANTIGEN; PHOSPHOTRANSFERASE; SILVER; HISTOCOMPATIBILITY ANTIGEN; LYMPHOCYTE ANTIGEN RECEPTOR; PEPTIDE;

EID: 38349108802     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.179.11.7653     Document Type: Article
Times cited : (77)

References (60)
  • 1
    • 33644825525 scopus 로고    scopus 로고
    • CD8: Adhesion molecule, co-receptor and immuno-modulator
    • Cole, D. K., and G. F. Gao. 2004. CD8: adhesion molecule, co-receptor and immuno-modulator. Cell. Mol. Immunol. 1: 81-88.
    • (2004) Cell. Mol. Immunol , vol.1 , pp. 81-88
    • Cole, D.K.1    Gao, G.F.2
  • 7
    • 0034677055 scopus 로고    scopus 로고
    • Critical role for CD8 in T cell receptor binding and activation by peptide/major histocompatibility complex multimers
    • Daniels, M. A., and S. C. Jameson. 2000. Critical role for CD8 in T cell receptor binding and activation by peptide/major histocompatibility complex multimers. J. Exp. Med. 191: 335-346.
    • (2000) J. Exp. Med , vol.191 , pp. 335-346
    • Daniels, M.A.1    Jameson, S.C.2
  • 9
    • 33845745287 scopus 로고    scopus 로고
    • Influence of human CD8 on antigen recognition by T-cell receptor-transduced cells
    • Lyons, G. E., T. Moore, N. Brasic, M. Li, J. J. Roszkowski, and M. I. Nishimura. 2006. Influence of human CD8 on antigen recognition by T-cell receptor-transduced cells. Cancer Res. 66: 11455-11461.
    • (2006) Cancer Res , vol.66 , pp. 11455-11461
    • Lyons, G.E.1    Moore, T.2    Brasic, N.3    Li, M.4    Roszkowski, J.J.5    Nishimura, M.I.6
  • 11
    • 0032438551 scopus 로고    scopus 로고
    • High- and low-potency ligands with similar affinities for the TCR: The importance of kinetics in TCR signaling
    • Kersh, G. J., E. N. Kersh, D. H. Fremont, and P. M. Allen. 1998. High- and low-potency ligands with similar affinities for the TCR: the importance of kinetics in TCR signaling. Immunity 9: 817-826.
    • (1998) Immunity , vol.9 , pp. 817-826
    • Kersh, G.J.1    Kersh, E.N.2    Fremont, D.H.3    Allen, P.M.4
  • 13
    • 0036667342 scopus 로고    scopus 로고
    • Molecular coordination of alphaβ T-cell receptors and coreceptors CD8 and CD4 in their recognition of peptide-MHC ligands
    • Gao, G. F., Z. Rao, and J. I. Bell. 2002. Molecular coordination of alphaβ T-cell receptors and coreceptors CD8 and CD4 in their recognition of peptide-MHC ligands. Trends Immunol. 23: 408-413.
    • (2002) Trends Immunol , vol.23 , pp. 408-413
    • Gao, G.F.1    Rao, Z.2    Bell, J.I.3
  • 14
    • 20444381329 scopus 로고    scopus 로고
    • Spatial coordination of CD8 and TCR molecules controls antigen recognition by CD8+ T-cells
    • Pecht, I., and D. M. Gakamsky. 2005. Spatial coordination of CD8 and TCR molecules controls antigen recognition by CD8+ T-cells. FEBS Lett. 579: 3336-3341.
    • (2005) FEBS Lett , vol.579 , pp. 3336-3341
    • Pecht, I.1    Gakamsky, D.M.2
  • 15
    • 23944497170 scopus 로고    scopus 로고
    • Nonstimulatory peptides contribute to antigen-induced CD8-T cell receptor interaction at the immunological synapse
    • Yachi, P. P., J. Ampudia, N. R. Gascoigne, and T. Zal. 2005. Nonstimulatory peptides contribute to antigen-induced CD8-T cell receptor interaction at the immunological synapse. Nat. Immunol. 6: 785-792.
    • (2005) Nat. Immunol , vol.6 , pp. 785-792
    • Yachi, P.P.1    Ampudia, J.2    Gascoigne, N.R.3    Zal, T.4
  • 16
    • 0033625405 scopus 로고    scopus 로고
    • Role of CD8β domains in CD8 coreceptor function: Importance for MHC I binding, signaling, and positive selection of CD8+ T cells in the thymus
    • Bosselut, R., S. Kubo, T. Guinter, J. L. Kopacz, J. D. Altman, L. Feigenbaum, and A. Singer. 2000. Role of CD8β domains in CD8 coreceptor function: importance for MHC I binding, signaling, and positive selection of CD8+ T cells in the thymus. Immunity 12: 409-418.
    • (2000) Immunity , vol.12 , pp. 409-418
    • Bosselut, R.1    Kubo, S.2    Guinter, T.3    Kopacz, J.L.4    Altman, J.D.5    Feigenbaum, L.6    Singer, A.7
  • 17
    • 33748801200 scopus 로고    scopus 로고
    • CD8alphaβ has two distinct binding modes of interaction with peptide-major histocompatibility complex class I
    • Chang, H. C., K. Tan, and Y. M. Hsu. 2006. CD8alphaβ has two distinct binding modes of interaction with peptide-major histocompatibility complex class I. J. Biol. Chem. 281: 28090-28096.
    • (2006) J. Biol. Chem , vol.281 , pp. 28090-28096
    • Chang, H.C.1    Tan, K.2    Hsu, Y.M.3
  • 18
    • 0032191836 scopus 로고    scopus 로고
    • Structural basis of CD8 coreceptor function revealed by crystallographic analysis of a murine CD8alphaα ectodomain fragment in complex with H-2Kb
    • Kern, P. S., M. K. Teng, A. Smolyar, J. H. Liu, J. Liu, R. E. Hussey, R. Spoerl, H. C. Chang, E. L. Reinherz, and J. H. Wang. 1998. Structural basis of CD8 coreceptor function revealed by crystallographic analysis of a murine CD8alphaα ectodomain fragment in complex with H-2Kb. Immunity 9: 519-530.
    • (1998) Immunity , vol.9 , pp. 519-530
    • Kern, P.S.1    Teng, M.K.2    Smolyar, A.3    Liu, J.H.4    Liu, J.5    Hussey, R.E.6    Spoerl, R.7    Chang, H.C.8    Reinherz, E.L.9    Wang, J.H.10
  • 19
    • 2342663130 scopus 로고    scopus 로고
    • The CD8 isoform CD8alphaα is not a functional homologue of the TCR co-receptor CD8alphaα
    • Gangadharan, D., and H. Cheroutre. 2004. The CD8 isoform CD8alphaα is not a functional homologue of the TCR co-receptor CD8alphaα. Curr. Opin. Immunol. 16: 264-270.
    • (2004) Curr. Opin. Immunol , vol.16 , pp. 264-270
    • Gangadharan, D.1    Cheroutre, H.2
  • 20
    • 33748507804 scopus 로고    scopus 로고
    • Mapping the binding site on CD8 β for MHC class I reveals mutants with enhanced binding
    • Devine, L., D. Thakral, S. Nag, J. Dobbins, M. E. Hodsdon, and P. B. Kavathas. 2006. Mapping the binding site on CD8 β for MHC class I reveals mutants with enhanced binding. J. Immunol. 177: 3930-3938.
    • (2006) J. Immunol , vol.177 , pp. 3930-3938
    • Devine, L.1    Thakral, D.2    Nag, S.3    Dobbins, J.4    Hodsdon, M.E.5    Kavathas, P.B.6
  • 21
    • 0031573679 scopus 로고    scopus 로고
    • Comparison of the roles of CD8 α α and CD8 α β in interaction with MHC class I
    • Sun, J., and P. B. Kavathas. 1997. Comparison of the roles of CD8 α α and CD8 α β in interaction with MHC class I. J. Immunol. 159: 6077-6082.
    • (1997) J. Immunol , vol.159 , pp. 6077-6082
    • Sun, J.1    Kavathas, P.B.2
  • 23
    • 0033578825 scopus 로고    scopus 로고
    • Expression, purification, and functional analysis of murine ectodomain fragments of CD8alphaα and CD8alphaβ dimers
    • Kern, P., R. E. Hussey, R. Spoerl, E. L. Reinherz, and H. C. Chang. 1999. Expression, purification, and functional analysis of murine ectodomain fragments of CD8alphaα and CD8alphaβ dimers. J. Biol. Chem. 274: 27237-27243.
    • (1999) J. Biol. Chem , vol.274 , pp. 27237-27243
    • Kern, P.1    Hussey, R.E.2    Spoerl, R.3    Reinherz, E.L.4    Chang, H.C.5
  • 25
    • 0034741073 scopus 로고    scopus 로고
    • The CD8alphaβ co-receptor on double-positive thymocytes binds with differing affinities to the products of distinct class I MHC loci
    • Moody, A. M., Y. Xiong, H. C. Chang, and E. L. Reinherz. 2001. The CD8alphaβ co-receptor on double-positive thymocytes binds with differing affinities to the products of distinct class I MHC loci. Eur. J. Immunol. 31: 2791-2799.
    • (2001) Eur. J. Immunol , vol.31 , pp. 2791-2799
    • Moody, A.M.1    Xiong, Y.2    Chang, H.C.3    Reinherz, E.L.4
  • 27
    • 0026607073 scopus 로고
    • CD8 surface levels alter the fate of α/β T cell receptor-expressing thymocytes in transgenic mice
    • Lee, N. A., D. Y. Loh, and E. Lacy. 1992. CD8 surface levels alter the fate of α/β T cell receptor-expressing thymocytes in transgenic mice. J. Exp. Med. 175: 1013-1025.
    • (1992) J. Exp. Med , vol.175 , pp. 1013-1025
    • Lee, N.A.1    Loh, D.Y.2    Lacy, E.3
  • 28
    • 0026633043 scopus 로고
    • The level of CD8 expression can determine the outcome of thymic selection
    • Robey, E. A., F. Ramsdell, D. Kioussis, W. Sha, D. Loh, R. Axel, and B. J. Fowlkes. 1992. The level of CD8 expression can determine the outcome of thymic selection. Cell 69: 1089-1096.
    • (1992) Cell , vol.69 , pp. 1089-1096
    • Robey, E.A.1    Ramsdell, F.2    Kioussis, D.3    Sha, W.4    Loh, D.5    Axel, R.6    Fowlkes, B.J.7
  • 29
    • 17644395663 scopus 로고    scopus 로고
    • The T cell receptor: Critical role of the membrane environment in receptor assembly and function
    • Call, M. E., and K. W. Wucherpfennig. 2005. The T cell receptor: critical role of the membrane environment in receptor assembly and function. Annu. Rev. Immunol. 23: 101-125.
    • (2005) Annu. Rev. Immunol , vol.23 , pp. 101-125
    • Call, M.E.1    Wucherpfennig, K.W.2
  • 30
    • 0037184955 scopus 로고    scopus 로고
    • The organizing principle in the formation of the T cell receptor-CD3 complex
    • Call, M. E., J. Pyrdol, M. Wiedmann, and K. W. Wucherpfennig. 2002. The organizing principle in the formation of the T cell receptor-CD3 complex. Cell 111: 967-979.
    • (2002) Cell , vol.111 , pp. 967-979
    • Call, M.E.1    Pyrdol, J.2    Wiedmann, M.3    Wucherpfennig, K.W.4
  • 31
    • 0035182368 scopus 로고    scopus 로고
    • Identification of self through two-dimensional chemistry and synapses
    • Dustin, M. L., S. K. Bromley, M. M. Davis, and C. Zhu. 2001. Identification of self through two-dimensional chemistry and synapses. Annu. Rev. Cell Dev. Biol. 17: 133-157.
    • (2001) Annu. Rev. Cell Dev. Biol , vol.17 , pp. 133-157
    • Dustin, M.L.1    Bromley, S.K.2    Davis, M.M.3    Zhu, C.4
  • 32
    • 7244239240 scopus 로고    scopus 로고
    • Quantifying the effects of molecular orientation and length on two-dimensional receptor-ligand binding kinetics
    • Huang, J., J. Chen, S. E. Chesla, T. Yago, P. Mehta, R. P. McEver, C. Zhu, and M. Long. 2004. Quantifying the effects of molecular orientation and length on two-dimensional receptor-ligand binding kinetics. J. Biol. Chem. 279: 44915-44923.
    • (2004) J. Biol. Chem , vol.279 , pp. 44915-44923
    • Huang, J.1    Chen, J.2    Chesla, S.E.3    Yago, T.4    Mehta, P.5    McEver, R.P.6    Zhu, C.7    Long, M.8
  • 33
    • 34248222289 scopus 로고    scopus 로고
    • Impact of carrier stiffness and microtopology on two-dimensional kinetics of P-selectin and P-selectin glycoprotein ligand-1 (PSGL-1) interactions
    • Wu, L., B. Xiao, X. Jia, Y. Zhang, S. Lu, J. Chen, and M. Long. 2007. Impact of carrier stiffness and microtopology on two-dimensional kinetics of P-selectin and P-selectin glycoprotein ligand-1 (PSGL-1) interactions. J. Biol. Chem. 282: 9846-9854.
    • (2007) J. Biol. Chem , vol.282 , pp. 9846-9854
    • Wu, L.1    Xiao, B.2    Jia, X.3    Zhang, Y.4    Lu, S.5    Chen, J.6    Long, M.7
  • 34
    • 0035918315 scopus 로고    scopus 로고
    • Quantifying the impact of membrane microtopology on effective two-dimensional affinity
    • Williams, T. E., S. Nagarajan, P. Selvaraj, and C. Zhu. 2001. Quantifying the impact of membrane microtopology on effective two-dimensional affinity. J. Biol. Chem. 276: 13283-13288.
    • (2001) J. Biol. Chem , vol.276 , pp. 13283-13288
    • Williams, T.E.1    Nagarajan, S.2    Selvaraj, P.3    Zhu, C.4
  • 35
    • 0031682733 scopus 로고    scopus 로고
    • Measuring two-dimensional receptor-ligand binding kinetics by micropipette
    • Chesla, S. E., P. Selvaraj, and C. Zhu. 1998. Measuring two-dimensional receptor-ligand binding kinetics by micropipette. Biophys. J. 75: 1553-1572.
    • (1998) Biophys. J , vol.75 , pp. 1553-1572
    • Chesla, S.E.1    Selvaraj, P.2    Zhu, C.3
  • 37
    • 33747092261 scopus 로고    scopus 로고
    • Altered peptide ligands induce delayed CD8-T cell receptor interaction-a role for CD8 in distinguishing antigen quality
    • Yachi, P. P., J. Ampudia, T. Zal, and N. R. Gascoigne. 2006. Altered peptide ligands induce delayed CD8-T cell receptor interaction-a role for CD8 in distinguishing antigen quality. Immunity 25: 203-211.
    • (2006) Immunity , vol.25 , pp. 203-211
    • Yachi, P.P.1    Ampudia, J.2    Zal, T.3    Gascoigne, N.R.4
  • 38
  • 39
    • 0026468228 scopus 로고
    • Thymic depletion and peripheral activation of class I major histocompatibility complex-restricted T cells by soluble peptide in T-cell receptor transgenic mice
    • Mamalaki, C., T. Norton, Y. Tanaka, A. R. Townsend, P. Chandler, E. Simpson, and D. Kioussis. 1992. Thymic depletion and peripheral activation of class I major histocompatibility complex-restricted T cells by soluble peptide in T-cell receptor transgenic mice. Proc. Natl. Acad. Sci. USA. 89: 11342-11346.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11342-11346
    • Mamalaki, C.1    Norton, T.2    Tanaka, Y.3    Townsend, A.R.4    Chandler, P.5    Simpson, E.6    Kioussis, D.7
  • 41
    • 0027222072 scopus 로고
    • High occupancy binding of antigenic peptides to purified, immunoadsorbed H-2Db β 2m molecules
    • Burshtyn, D. N., and B. H. Barber. 1993. High occupancy binding of antigenic peptides to purified, immunoadsorbed H-2Db β 2m molecules. J. Immunol. 151: 3070-3081.
    • (1993) J. Immunol , vol.151 , pp. 3070-3081
    • Burshtyn, D.N.1    Barber, B.H.2
  • 44
    • 0035937132 scopus 로고    scopus 로고
    • T Cell Receptor Binding to a pMHCII Ligand Is Kinetically Distinct from and Independent of CD4
    • Xiong, Y., P. Kern, H. Chang, and E. Reinherz. 2001. T Cell Receptor Binding to a pMHCII Ligand Is Kinetically Distinct from and Independent of CD4. J. Biol. Chem. 276: 5659-5667.
    • (2001) J. Biol. Chem , vol.276 , pp. 5659-5667
    • Xiong, Y.1    Kern, P.2    Chang, H.3    Reinherz, E.4
  • 47
    • 0035399799 scopus 로고    scopus 로고
    • Critical role for CD8 in binding of MHC tetramers to TCR: CD8 antibodies block specific binding of human tumor-specific MHC-peptide tetramers to TCR
    • Denkberg, G., C. J. Cohen, and Y. Reiter. 2001. Critical role for CD8 in binding of MHC tetramers to TCR: CD8 antibodies block specific binding of human tumor-specific MHC-peptide tetramers to TCR. J. Immunol. 167: 270-276.
    • (2001) J. Immunol , vol.167 , pp. 270-276
    • Denkberg, G.1    Cohen, C.J.2    Reiter, Y.3
  • 48
    • 0036919051 scopus 로고    scopus 로고
    • Mouse MHC class I tetramers that are unable to bind to CD8 reveal the need for CD8 engagement in order to activate naive CD8 T cells
    • Schott, E., and H. L. Ploegh. 2002. Mouse MHC class I tetramers that are unable to bind to CD8 reveal the need for CD8 engagement in order to activate naive CD8 T cells. Eur. J. Immunol. 32: 3425-3434.
    • (2002) Eur. J. Immunol , vol.32 , pp. 3425-3434
    • Schott, E.1    Ploegh, H.L.2
  • 49
    • 10744222630 scopus 로고    scopus 로고
    • Anti-CD8 antibodies can inhibit or enhance peptide-MHC class I (pMHCI) multimer binding: This is paralleled by their effects on CTL activation and occurs in the absence of an interaction between pMHCI and CD8 on the cell surface
    • Wooldridge, L., S. L. Hutchinson, E. M. Choi, A. Lissina, E. Jones, F. Mirza, P. R. Dunbar, D. A. Price, V. Cerundolo, and A. K. Sewell. 2003. Anti-CD8 antibodies can inhibit or enhance peptide-MHC class I (pMHCI) multimer binding: this is paralleled by their effects on CTL activation and occurs in the absence of an interaction between pMHCI and CD8 on the cell surface. J. Immunol. 171: 6650-6660.
    • (2003) J. Immunol , vol.171 , pp. 6650-6660
    • Wooldridge, L.1    Hutchinson, S.L.2    Choi, E.M.3    Lissina, A.4    Jones, E.5    Mirza, F.6    Dunbar, P.R.7    Price, D.A.8    Cerundolo, V.9    Sewell, A.K.10
  • 50
    • 0036801024 scopus 로고    scopus 로고
    • Probing T cell membrane organization using dimeric MHC-Ig complexes
    • Fahmy, T. M., J. G. Bieler, and J. P. Schneck. 2002. Probing T cell membrane organization using dimeric MHC-Ig complexes. J. Immunol. Methods. 268: 93-106.
    • (2002) J. Immunol. Methods , vol.268 , pp. 93-106
    • Fahmy, T.M.1    Bieler, J.G.2    Schneck, J.P.3
  • 52
    • 0030916178 scopus 로고    scopus 로고
    • Adhesive bond dynamics in contacts between T lymphocytes and glass-supported planar bilayers reconstituted with the immunoglobulin-related adhesion molecule CD58
    • Dustin, M. L. 1997. Adhesive bond dynamics in contacts between T lymphocytes and glass-supported planar bilayers reconstituted with the immunoglobulin-related adhesion molecule CD58. J. Biol. Chem. 272: 15782-15788.
    • (1997) J. Biol. Chem , vol.272 , pp. 15782-15788
    • Dustin, M.L.1
  • 53
    • 0030679644 scopus 로고    scopus 로고
    • Low affinity interaction of human or rat T cell adhesion molecule CD2 with its ligand aligns adhering membranes to achieve high physiological affinity
    • Dustin, M. L., D. E. Golan, D. M. Zhu, J. M. Miller, W. Meier, E. A. Davies, and P. A. van der Merwe. 1997. Low affinity interaction of human or rat T cell adhesion molecule CD2 with its ligand aligns adhering membranes to achieve high physiological affinity. J. Biol. Chem. 272: 30889-30898.
    • (1997) J. Biol. Chem , vol.272 , pp. 30889-30898
    • Dustin, M.L.1    Golan, D.E.2    Zhu, D.M.3    Miller, J.M.4    Meier, W.5    Davies, E.A.6    van der Merwe, P.A.7
  • 55
    • 0035544006 scopus 로고    scopus 로고
    • Kinetic measurements of cell surface E-selectin/carbohydrate ligand interactions
    • Long, M., H. Zhao, K. S. Huang, and C. Zhu. 2001. Kinetic measurements of cell surface E-selectin/carbohydrate ligand interactions. Ann. Biomed. Eng. 29: 935-946.
    • (2001) Ann. Biomed. Eng , vol.29 , pp. 935-946
    • Long, M.1    Zhao, H.2    Huang, K.S.3    Zhu, C.4
  • 56
    • 29644439801 scopus 로고    scopus 로고
    • Two-dimensional kinetics regulation of alphaLβ2-ICAM-1 interaction by conformational changes of the alphaL-inserted domain
    • Zhang, F., W. D. Marcus, N. H. Goyal, P. Selvaraj, T. A. Springer, and C. Zhu. 2005. Two-dimensional kinetics regulation of alphaLβ2-ICAM-1 interaction by conformational changes of the alphaL-inserted domain. J. Biol. Chem. 280: 42207-42218.
    • (2005) J. Biol. Chem , vol.280 , pp. 42207-42218
    • Zhang, F.1    Marcus, W.D.2    Goyal, N.H.3    Selvaraj, P.4    Springer, T.A.5    Zhu, C.6
  • 57
    • 0033808440 scopus 로고    scopus 로고
    • Concurrent binding to multiple ligands: Kinetic rates of CD16b for membrane-bound IgG1 and IgG2
    • Williams, T. E., P. Selvaraj, and C. Zhu. 2000. Concurrent binding to multiple ligands: kinetic rates of CD16b for membrane-bound IgG1 and IgG2. Biophys. J. 79: 1858-1866.
    • (2000) Biophys. J , vol.79 , pp. 1858-1866
    • Williams, T.E.1    Selvaraj, P.2    Zhu, C.3
  • 58
    • 0033798612 scopus 로고    scopus 로고
    • Concurrent and independent binding of Fcγ receptors IIa and IIIb to surface-bound IgG
    • Williams, T. E., S. Nagarajan, P. Selvaraj, and C. Zhu. 2000. Concurrent and independent binding of Fcγ receptors IIa and IIIb to surface-bound IgG. Biophys. J. 79: 1867-1875.
    • (2000) Biophys. J , vol.79 , pp. 1867-1875
    • Williams, T.E.1    Nagarajan, S.2    Selvaraj, P.3    Zhu, C.4
  • 59
    • 0033165928 scopus 로고    scopus 로고
    • Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical
    • Ding, Y. H., B. M. Baker, D. N. Garboczi, W. E. Biddison, and D. C. Wiley. 1999. Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical. Immunity 11: 45-56.
    • (1999) Immunity , vol.11 , pp. 45-56
    • Ding, Y.H.1    Baker, B.M.2    Garboczi, D.N.3    Biddison, W.E.4    Wiley, D.C.5
  • 60
    • 0033555818 scopus 로고    scopus 로고
    • Orientation of the Ig domains of CD8 α β relative to MHC class I
    • Devine, L., J. Sun, M. R. Barr, and P. B. Kavathas. 1999. Orientation of the Ig domains of CD8 α β relative to MHC class I. J. Immunol. 162: 846-851.
    • (1999) J. Immunol , vol.162 , pp. 846-851
    • Devine, L.1    Sun, J.2    Barr, M.R.3    Kavathas, P.B.4


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