메뉴 건너뛰기




Volumn 199, Issue 10, 2004, Pages 1409-1420

CD8 T cell recognition of endogenously expressed Epstein-Barr virus nuclear antigen 1

Author keywords

Antigen presentation; Cytotoxic T lymphocytes; EBNA1; Epstein Barr virus

Indexed keywords

ALANINE; ALPHA INTERFERON; CD8 ANTIGEN; EPITOPE; EPSTEIN BARR VIRUS NUCLEAR ANTIGEN 1; GLYCINE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PROTEOME; UNCLASSIFIED DRUG; VIRUS ANTIGEN;

EID: 2542446376     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.20040121     Document Type: Article
Times cited : (138)

References (45)
  • 1
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class 1-restricted antigen processing
    • Pamer, E., and P. Cresswell. 1998. Mechanisms of MHC class 1-restricted antigen processing. Annu. Rev. Immunol. 16: 323-358.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 323-358
    • Pamer, E.1    Cresswell, P.2
  • 3
    • 0000942113 scopus 로고    scopus 로고
    • Epstein-Barr virus
    • D.M. Knipe, and P.M. Howley, editors. Lippincott Williams and Wilkins, Philadelphia
    • Rickinson, A.B., and E. Kieff. 2001. Epstein-Barr virus. In Fields Virology. D.M. Knipe, and P.M. Howley, editors. Lippincott Williams and Wilkins, Philadelphia. 2575-2627.
    • (2001) Fields Virology , pp. 2575-2627
    • Rickinson, A.B.1    Kieff, E.2
  • 4
    • 0033008462 scopus 로고    scopus 로고
    • Genetic evidence that EBNA-1 is needed for efficient, stable latent infection by Epstein-Barr virus
    • Lee, M.A., M.E. Diamond, and J.L. Yates. 1999. Genetic evidence that EBNA-1 is needed for efficient, stable latent infection by Epstein-Barr virus. J. Virol. 73:2974-2982.
    • (1999) J. Virol. , vol.73 , pp. 2974-2982
    • Lee, M.A.1    Diamond, M.E.2    Yates, J.L.3
  • 6
    • 0030775380 scopus 로고    scopus 로고
    • Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1
    • Levitskaya, J., A. Shapiro, A. Leonchiks, A. Ciechanover, and M.G. Masucci. 1997. Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1. Proc. Natl. Acad. Sci. USA. 94:12616-12621.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12616-12621
    • Levitskaya, J.1    Shapiro, A.2    Leonchiks, A.3    Ciechanover, A.4    Masucci, M.G.5
  • 7
    • 0031904016 scopus 로고    scopus 로고
    • A minimal glycine-alanine repeat prevents the interaction of ubiquitinated I kappaB alpha with the proteasome: A new mechanism for selective inhibition of proteolysis
    • Sharipo, A., M. Imreh, A. Leonchiks, S. Imreh, and M.G. Masucci. 1998. A minimal glycine-alanine repeat prevents the interaction of ubiquitinated I kappaB alpha with the proteasome: a new mechanism for selective inhibition of proteolysis. Nat. Med. 4:939-944.
    • (1998) Nat. Med. , vol.4 , pp. 939-944
    • Sharipo, A.1    Imreh, M.2    Leonchiks, A.3    Imreh, S.4    Masucci, M.G.5
  • 8
    • 0037022303 scopus 로고    scopus 로고
    • Functional p53 chimeras containing the Epstein-Barr virus Gly-Ala repeat are protected from Mdm2- and HPV-E6-induced proteolysis
    • Heessen, S., A. Leonchiks, N. Issaeva, A. Sharipo, G. Selivanova, M.G. Masucci, and N.P. Dantuma. 2002. Functional p53 chimeras containing the Epstein-Barr virus Gly-Ala repeat are protected from Mdm2- and HPV-E6-induced proteolysis. Proc. Natl. Acad. Sci. USA. 99:1532-1537.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1532-1537
    • Heessen, S.1    Leonchiks, A.2    Issaeva, N.3    Sharipo, A.4    Selivanova, G.5    Masucci, M.G.6    Dantuma, N.P.7
  • 10
    • 0025776826 scopus 로고
    • The Epstein-Barr-virus-encoded membrane protein LMP but not the nuclear antigen EBNA-1 induces rejection of transfected murine mammary carcinoma cells
    • Trivedi, P., M.G. Masucci, G. Winberg, and G. Klein. 1991. The Epstein-Barr-virus-encoded membrane protein LMP but not the nuclear antigen EBNA-1 induces rejection of transfected murine mammary carcinoma cells. Int. J. Cancer. 48:794-800.
    • (1991) Int. J. Cancer , vol.48 , pp. 794-800
    • Trivedi, P.1    Masucci, M.G.2    Winberg, G.3    Klein, G.4
  • 11
    • 0026734842 scopus 로고
    • Identification of target antigens for the human cytotoxic T cell response to Epstein-Barr virus (EBV): Implications for the immune control of EBV-positive malignancies
    • Murray, R.J., M.G. Kurilla, J.M. Brooks, W.A. Thomas, M. Rowe, E. Kieff, and A.B. Rickinson. 1992. Identification of target antigens for the human cytotoxic T cell response to Epstein-Barr virus (EBV): implications for the immune control of EBV-positive malignancies. J. Exp. Med. 176:157-168.
    • (1992) J. Exp. Med. , vol.176 , pp. 157-168
    • Murray, R.J.1    Kurilla, M.G.2    Brooks, J.M.3    Thomas, W.A.4    Rowe, M.5    Kieff, E.6    Rickinson, A.B.7
  • 12
    • 0026681729 scopus 로고
    • Localization of Epstein-Barr virus cytotoxic T cell epitopes using recombinant vaccinia - implications for vaccine development
    • Khanna, R., S.R. Burrows, M.G. Kurilla, C.A. Jacob, I.S. Misko, T.B. Sculley, E. Kieff, and D.J. Moss. 1992. Localization of Epstein-Barr virus cytotoxic T cell epitopes using recombinant vaccinia - implications for vaccine development. J. Exp. Med. 176:169-176.
    • (1992) J. Exp. Med. , vol.176 , pp. 169-176
    • Khanna, R.1    Burrows, S.R.2    Kurilla, M.G.3    Jacob, C.A.4    Misko, I.S.5    Sculley, T.B.6    Kieff, E.7    Moss, D.J.8
  • 14
    • 0034671572 scopus 로고    scopus 로고
    • The importance of exogenous antigen in priming the human CD8+ T cell response: Lessons from the EBV nuclear antigen EBNA1
    • Blake, N., T. Haigh, G. Shaka'a, D. Croom-Carter, and A. Rickinson. 2000. The importance of exogenous antigen in priming the human CD8+ T cell response: lessons from the EBV nuclear antigen EBNA1. J. Immunol. 165:7078-7087.
    • (2000) J. Immunol. , vol.165 , pp. 7078-7087
    • Blake, N.1    Haigh, T.2    Shaka'a, G.3    Croom-Carter, D.4    Rickinson, A.5
  • 15
    • 0036799565 scopus 로고    scopus 로고
    • Epstein-Barr virus-associated Burkitt lymphomagenesis selects for downregulation of the nuclear antigen EBNA2
    • Kelly, G., A. Bell, and A. Rickinson. 2002. Epstein-Barr virus-associated Burkitt lymphomagenesis selects for downregulation of the nuclear antigen EBNA2. Nat. Med. 8:1098-1104.
    • (2002) Nat. Med. , vol.8 , pp. 1098-1104
    • Kelly, G.1    Bell, A.2    Rickinson, A.3
  • 18
    • 0033559896 scopus 로고    scopus 로고
    • Differential responses to CD40 ligation among Burkitt lymphoma lines that are uniformly responsive to Epstein-Barr virus latent membrane protein 1
    • Henriquez, N.V., E. Floettmann, M. Salmon, M. Rowe, and A.B. Rickinson. 1999. Differential responses to CD40 ligation among Burkitt lymphoma lines that are uniformly responsive to Epstein-Barr virus latent membrane protein 1. J. Immunol. 162:3298-3307.
    • (1999) J. Immunol. , vol.162 , pp. 3298-3307
    • Henriquez, N.V.1    Floettmann, E.2    Salmon, M.3    Rowe, M.4    Rickinson, A.B.5
  • 19
    • 0031469361 scopus 로고    scopus 로고
    • CD40-activated human B cells: An alternative source of highly efficient antigen presenting cells to generate autologous antigen-specific T cells for adoptive immunotherapy
    • Schultze, J.L., S. Michalak, M.J. Seamon, G. Dranoff, K. Jung, J. Daley, J.C. Delgado, J.G. Gribben, and L.M. Nadler. 1997. CD40-activated human B cells: an alternative source of highly efficient antigen presenting cells to generate autologous antigen-specific T cells for adoptive immunotherapy. J. Clin. Invest. 100:2757-2765.
    • (1997) J. Clin. Invest. , vol.100 , pp. 2757-2765
    • Schultze, J.L.1    Michalak, S.2    Seamon, M.J.3    Dranoff, G.4    Jung, K.5    Daley, J.6    Delgado, J.C.7    Gribben, J.G.8    Nadler, L.M.9
  • 20
    • 0029034074 scopus 로고
    • Class I major histocompatibility complex@restricted cytotoxic T lymphocytes specific for Epstein-Barr virus (EBV) nuclear antigens fail to lyse the EBV-transformed B lymphoblastoid lines against which they were raised
    • Hill, A.B., S.P. Lee, J.S. Haurum, N. Murray, Q.Y. Yao, M. Rowe, N. Signoret, A.B. Rickinson, and A.J. McMichael. 1995. Class I major histocompatibility complex@restricted cytotoxic T lymphocytes specific for Epstein-Barr virus (EBV) nuclear antigens fail to lyse the EBV-transformed B lymphoblastoid lines against which they were raised. J. Exp. Med. 181:2221-2228.
    • (1995) J. Exp. Med. , vol.181 , pp. 2221-2228
    • Hill, A.B.1    Lee, S.P.2    Haurum, J.S.3    Murray, N.4    Yao, Q.Y.5    Rowe, M.6    Signoret, N.7    Rickinson, A.B.8    McMichael, A.J.9
  • 22
    • 0028265113 scopus 로고
    • Endoplasmic reticulum signal sequence facilitated transport of peptide epitopes restores immunogenicity of an antigen processing defective tumor cell line
    • Khanna, R., S.R. Burrows, V. Argaet, and D.J. Moss. 1994. Endoplasmic reticulum signal sequence facilitated transport of peptide epitopes restores immunogenicity of an antigen processing defective tumor cell line. Int. Immunol. 6:639-645.
    • (1994) Int. Immunol. , vol.6 , pp. 639-645
    • Khanna, R.1    Burrows, S.R.2    Argaet, V.3    Moss, D.J.4
  • 23
    • 0031573606 scopus 로고    scopus 로고
    • Engagement of CD40 antigen with soluble CD40 ligand up-regulates peptide transporter expression and restores endogenous processing function in Burkitt's lymphoma cells
    • Khanna, R., L. Cooper, N. Kienzle, D.J. Moss, S.R. Burrows, and K.K. Khanna. 1997. Engagement of CD40 antigen with soluble CD40 ligand up-regulates peptide transporter expression and restores endogenous processing function in Burkitt's lymphoma cells. J. Immunol. 159:5782-5785.
    • (1997) J. Immunol. , vol.159 , pp. 5782-5785
    • Khanna, R.1    Cooper, L.2    Kienzle, N.3    Moss, D.J.4    Burrows, S.R.5    Khanna, K.K.6
  • 24
    • 0037145321 scopus 로고    scopus 로고
    • Proteasome inhibitors reconstitute the presentation of cytotoxic T-cell epitopes in Epstein-Barr virus-associated tumors
    • Gavioli, R., S. Vertuani, and M.G. Masucci. 2002. Proteasome inhibitors reconstitute the presentation of cytotoxic T-cell epitopes in Epstein-Barr virus-associated tumors. Int. J. Cancer. 101:532-538.
    • (2002) Int. J. Cancer , vol.101 , pp. 532-538
    • Gavioli, R.1    Vertuani, S.2    Masucci, M.G.3
  • 25
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., R.F. Standaert, W.S. Lane, S. Choi, E.J. Corey, and S.L. Schreiber. 1995. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science. 268:726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 26
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
    • Meng, L., R. Mohan, B.H. Kwok, M. Elofsson, N. Sin, and C.M. Crews. 1999. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl. Acad. Sci. USA. 96:10403-10408.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10403-10408
    • Meng, L.1    Mohan, R.2    Kwok, B.H.3    Elofsson, M.4    Sin, N.5    Crews, C.M.6
  • 27
    • 0000870917 scopus 로고    scopus 로고
    • Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae
    • Lee, D.H., and A.L. Goldberg. 1996. Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae. J. Biol. Chem. 271: 27280-27284.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27280-27284
    • Lee, D.H.1    Goldberg, A.L.2
  • 28
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert, U., L.C. Anton, J. Gibbs, C.C. Norbury, J.W. Yewdell, and J.R. Bennink. 2000. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature. 404:770-774.
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 29
    • 0034643348 scopus 로고    scopus 로고
    • The major substrates for TAP in vivo are derived from newly synthesized proteins
    • Reits, E.A., J.C. Vos, M. Gromme, and J. Neefjes. 2000. The major substrates for TAP in vivo are derived from newly synthesized proteins. Nature. 404:774-778.
    • (2000) Nature , vol.404 , pp. 774-778
    • Reits, E.A.1    Vos, J.C.2    Gromme, M.3    Neefjes, J.4
  • 30
    • 0035823481 scopus 로고    scopus 로고
    • Targeting of EBNA1 for rapid intracellular degradation overrides the inhibitory effects of the Gly-Ala repeat domain and restores CD8+ T cell recognition
    • Tellam, J., M. Sherritt, S. Thomson, R. Tellam, D.J. Moss, S.R. Burrows, E. Wiertz, and R. Khanna. 2001. Targeting of EBNA1 for rapid intracellular degradation overrides the inhibitory effects of the Gly-Ala repeat domain and restores CD8+ T cell recognition. J. Biol. Chem. 276:33353-33360.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33353-33360
    • Tellam, J.1    Sherritt, M.2    Thomson, S.3    Tellam, R.4    Moss, D.J.5    Burrows, S.R.6    Wiertz, E.7    Khanna, R.8
  • 31
    • 0032472871 scopus 로고    scopus 로고
    • Murine cytotoxic T lymphocytes recognize an epitope in an EBNA-1 fragment, but fail to lyse EBNA-1-expressing mouse cells
    • Mukherjee, S., P. Trivedi, D.M. Dorfman, G. Klein, and A. Townsend. 1998. Murine cytotoxic T lymphocytes recognize an epitope in an EBNA-1 fragment, but fail to lyse EBNA-1-expressing mouse cells. J. Exp. Med. 187:445-450.
    • (1998) J. Exp. Med. , vol.187 , pp. 445-450
    • Mukherjee, S.1    Trivedi, P.2    Dorfman, D.M.3    Klein, G.4    Townsend, A.5
  • 32
    • 0034682502 scopus 로고    scopus 로고
    • Inhibition of proteasomal degradation by the gly-Ala repeat of Epstein-Barr virus is influenced by the length of the repeat and the strength of the degradation signal
    • Dantuma, N.P., S. Heessen, K. Lindsten, M. Jellne, and M.G. Masucci. 2000. Inhibition of proteasomal degradation by the gly-Ala repeat of Epstein-Barr virus is influenced by the length of the repeat and the strength of the degradation signal. Proc. Natl. Acad. Sci. USA. 97:8381-8385.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8381-8385
    • Dantuma, N.P.1    Heessen, S.2    Lindsten, K.3    Jellne, M.4    Masucci, M.G.5
  • 33
    • 0030002902 scopus 로고    scopus 로고
    • Different responses are elicited in cytotoxic T lymphocytes by different levels of T cell receptor occupancy
    • Valitutti, S., S. Muller, M. Dessing, and A. Lanzavecchia. 1996. Different responses are elicited in cytotoxic T lymphocytes by different levels of T cell receptor occupancy. J. Exp. Med. 183:1917-1921.
    • (1996) J. Exp. Med. , vol.183 , pp. 1917-1921
    • Valitutti, S.1    Muller, S.2    Dessing, M.3    Lanzavecchia, A.4
  • 34
    • 0030926777 scopus 로고    scopus 로고
    • Lactacystin and clasto-lactacystin beta-lactone modify multiple proteasome beta-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation
    • Craiu, A., M. Gaczynska, T. Akopian, C.F. Gramm, G. Fenteany, A.L. Goldberg, and K.L. Rock. 1997. Lactacystin and clasto-lactacystin beta-lactone modify multiple proteasome beta-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation. J. Biol. Chem. 272:13437-13445.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13437-13445
    • Craiu, A.1    Gaczynska, M.2    Akopian, T.3    Gramm, C.F.4    Fenteany, G.5    Goldberg, A.L.6    Rock, K.L.7
  • 35
    • 0141707939 scopus 로고    scopus 로고
    • ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells
    • Guermonprez, P., L. Saveanu, M. Kleijmeer, J. Davoust, P. Van Endert, and S. Amigorena. 2003. ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells. Nature. 425:397-402.
    • (2003) Nature , vol.425 , pp. 397-402
    • Guermonprez, P.1    Saveanu, L.2    Kleijmeer, M.3    Davoust, J.4    Van Endert, P.5    Amigorena, S.6
  • 37
    • 0041971307 scopus 로고    scopus 로고
    • Self-inhibition of synthesis and antigen presentation by Epstein-Barr virus-encoded EBNA1
    • Yin, Y., B. Manoury, and R. Fahraeus. 2003. Self-inhibition of synthesis and antigen presentation by Epstein-Barr virus-encoded EBNA1. Science. 301:1371-1374.
    • (2003) Science , vol.301 , pp. 1371-1374
    • Yin, Y.1    Manoury, B.2    Fahraeus, R.3
  • 40
    • 0032866173 scopus 로고    scopus 로고
    • Inhibition of antigen presentation by the glycine/alanine repeat domain is not conserved in simian homologues of Epstein-Barr virus nuclear antigen 1
    • Blake, N.W., A. Moghaddam, P. Rao, A. Kaur, R. Glickman, Y.G. Cho, A. Marchini, T. Haigh, R.P. Johnson, A.B. Rickinson, et al. 1999. Inhibition of antigen presentation by the glycine/alanine repeat domain is not conserved in simian homologues of Epstein-Barr virus nuclear antigen 1. J. Virol. 73:7381-7389.
    • (1999) J. Virol. , vol.73 , pp. 7381-7389
    • Blake, N.W.1    Moghaddam, A.2    Rao, P.3    Kaur, A.4    Glickman, R.5    Cho, Y.G.6    Marchini, A.7    Haigh, T.8    Johnson, R.P.9    Rickinson, A.B.10
  • 41
    • 0242331731 scopus 로고    scopus 로고
    • Cytolytic CD4(+)-T-cell clones reactive to EBNA1 inhibit Epstein-Barr virus-induced B-cell proliferation
    • Nikiforow, S., K. Bottomly, G. Miller, and C. Munz. 2003. Cytolytic CD4(+)-T-cell clones reactive to EBNA1 inhibit Epstein-Barr virus-induced B-cell proliferation. J. Virol. 77: 12088-12104.
    • (2003) J. Virol. , vol.77 , pp. 12088-12104
    • Nikiforow, S.1    Bottomly, K.2    Miller, G.3    Munz, C.4
  • 42
    • 0032147126 scopus 로고    scopus 로고
    • Antigen presenting phenotype of Hodgkin Reed-Sternberg cells: Analysis of the HLA class I processing pathway and the effects of interleukin 10 on Epstein-Barr virus-specific cytotoxic T cell recognition
    • Lee, S.P., C.M. Constandinou, W.A. Thomas, D. Croom-Carter, N.W. Blake, P.G. Murray, J. Crocker, and A.B. Rickinson. 1998. Antigen presenting phenotype of Hodgkin Reed-Sternberg cells: analysis of the HLA class I processing pathway and the effects of interleukin 10 on Epstein-Barr virus-specific cytotoxic T cell recognition. Blood. 92:1020-1030.
    • (1998) Blood , vol.92 , pp. 1020-1030
    • Lee, S.P.1    Constandinou, C.M.2    Thomas, W.A.3    Croom-Carter, D.4    Blake, N.W.5    Murray, P.G.6    Crocker, J.7    Rickinson, A.B.8
  • 43
    • 0034235814 scopus 로고    scopus 로고
    • CTL control of EBV in nasopharyngeal carcinoma (NPC): EBV-specific CTL responses in the blood and tumors of NPC patients and the antigen-processing function of the tumor cells
    • Lee, S.P., A.T. Chan, S.T. Cheung, W.A. Thomas, D. Croomcarter, C.W. Dawson, C.H. Tsai, S.F. Leung, P.J. Johnson, and D.P. Huang. 2000. CTL control of EBV in nasopharyngeal carcinoma (NPC): EBV-specific CTL responses in the blood and tumors of NPC patients and the antigen-processing function of the tumor cells. J. Immunol. 165:573-582.
    • (2000) J. Immunol. , vol.165 , pp. 573-582
    • Lee, S.P.1    Chan, A.T.2    Cheung, S.T.3    Thomas, W.A.4    Croomcarter, D.5    Dawson, C.W.6    Tsai, C.H.7    Leung, S.F.8    Johnson, P.J.9    Huang, D.P.10
  • 44
    • 0031964512 scopus 로고    scopus 로고
    • Molecular characterization of antigen-processing function in Nasopharyngeal Carcinoma (NPC): Evidence for efficient presentation of Epstein-Barr virus cytotoxic T-cell epitopes by NPC cells
    • Khanna, R., P. Busson, S.R. Burrows, C. Raffoux, D.J. Moss, J.M. Nicholls, and L. Cooper. 1998. Molecular characterization of antigen-processing function in Nasopharyngeal Carcinoma (NPC): evidence for efficient presentation of Epstein-Barr virus cytotoxic T-cell epitopes by NPC cells. Cancer Res. 58:310-314.
    • (1998) Cancer Res. , vol.58 , pp. 310-314
    • Khanna, R.1    Busson, P.2    Burrows, S.R.3    Raffoux, C.4    Moss, D.J.5    Nicholls, J.M.6    Cooper, L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.