메뉴 건너뛰기




Volumn 156, Issue 9, 1996, Pages 3275-3284

Unusual uniformity of the N-linked oligosaccharides of HLA-A, -B, and -C glycoproteins

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE LINKED OLIGOSACCHARIDE; GLYCAN; GLYCOPROTEIN; HLA A ANTIGEN; HLA ANTIGEN CLASS 1; HLA B ANTIGEN; HLA C ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1;

EID: 9244233286     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (44)

References (64)
  • 1
    • 0027333426 scopus 로고
    • Peptide binding by major histocompatibility complex molecules
    • Barber, L. D., and P. Parham. 1993. Peptide binding by major histocompatibility complex molecules. Annu. Rev. Cell Biol. 9:163.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 163
    • Barber, L.D.1    Parham, P.2
  • 2
    • 0029284306 scopus 로고
    • NK cell recognition of major histocompatibility class I molecules
    • Lanier, L. L., and J. Phillips. 1995. NK cell recognition of major histocompatibility class I molecules. Semin. Immunol. 7:75.
    • (1995) Semin. Immunol. , vol.7 , pp. 75
    • Lanier, L.L.1    Phillips, J.2
  • 3
    • 0023187442 scopus 로고
    • The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens
    • Bjorkman, P. J., M. A. Saper, B. Samraoui, W. S. Bennett, J. L. Striminger, and D. C. Wiley. 1987. The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens. Nature 329:512.
    • (1987) Nature , vol.329 , pp. 512
    • Bjorkman, P.J.1    Saper, M.A.2    Samraoui, B.3    Bennett, W.S.4    Striminger, J.L.5    Wiley, D.C.6
  • 5
    • 0026718034 scopus 로고
    • Reptilian class I major histocompatibility complex genes reveal conserved elements in class I structure
    • Grossberger, D., and P. Parham. 1992. Reptilian class I major histocompatibility complex genes reveal conserved elements in class I structure. Immunogenetics 36:166.
    • (1992) Immunogenetics , vol.36 , pp. 166
    • Grossberger, D.1    Parham, P.2
  • 6
    • 0020678474 scopus 로고
    • Structure of class I major histocompatibility antigens
    • Kimball, E. S., and J. E. Coligan. 1983. Structure of class I major histocompatibility antigens. Contemp. Top. Mol. Immunol. 9:1.
    • (1983) Contemp. Top. Mol. Immunol. , vol.9 , pp. 1
    • Kimball, E.S.1    Coligan, J.E.2
  • 7
    • 0017622587 scopus 로고
    • Carbohydrate moiety of HLA antigens: Antigenic properties and amino acid sequences around the site of glycosylation
    • Parham, P., B. N. Alpert, H. T. Orr, and J. L. Strominger. 1977. Carbohydrate moiety of HLA antigens: antigenic properties and amino acid sequences around the site of glycosylation. J. Biol. Chem. 252:7555.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7555
    • Parham, P.1    Alpert, B.N.2    Orr, H.T.3    Strominger, J.L.4
  • 9
    • 0025831493 scopus 로고
    • Refined structure of the human histocompatibility antigen HLA-A2 at 2.6Å resolution
    • Saper, M. A., P. J. Bjorkman, and D. C. Wiley. 1991. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6Å resolution. J. Mol. Biol. 219: 277.
    • (1991) J. Mol. Biol. , vol.219 , pp. 277
    • Saper, M.A.1    Bjorkman, P.J.2    Wiley, D.C.3
  • 10
    • 0022508249 scopus 로고
    • Expression and function of a nonglycosylated major histocompatibility class I antigen
    • Miyazaki, J., E. Appella, H. Zhao, J. Forman, and K. Ozato. 1986. Expression and function of a nonglycosylated major histocompatibility class I antigen. J. Exp. Med. 163:856.
    • (1986) J. Exp. Med. , vol.163 , pp. 856
    • Miyazaki, J.1    Appella, E.2    Zhao, H.3    Forman, J.4    Ozato, K.5
  • 12
    • 0023624345 scopus 로고
    • Site-directed mutagenesis of class I HLA genes: Role of glycosylation in surface expression and functional recognition
    • Barbosa, J. A., J. Santos-Aguado, S. J. Mentzer, J. L. Strominger, S. J. Burakoff, and P. A. Biro. 1987. Site-directed mutagenesis of class I HLA genes: role of glycosylation in surface expression and functional recognition. J. Exp. Med. 166: 1329.
    • (1987) J. Exp. Med. , vol.166 , pp. 1329
    • Barbosa, J.A.1    Santos-Aguado, J.2    Mentzer, S.J.3    Strominger, J.L.4    Burakoff, S.J.5    Biro, P.A.6
  • 13
    • 0028897989 scopus 로고
    • The Bw4 public epitopc of HLA-B molecules confers reactivity with natural killer cell clones that express NKB1, a putative HLA receptor
    • Gumperz, J. E., V. Litwin, J. H. Phillips, L. L. Lanier, and P. Parham. 1995. The Bw4 public epitopc of HLA-B molecules confers reactivity with natural killer cell clones that express NKB1, a putative HLA receptor. J. Exp. Med. 181:1133.
    • (1995) J. Exp. Med. , vol.181 , pp. 1133
    • Gumperz, J.E.1    Litwin, V.2    Phillips, J.H.3    Lanier, L.L.4    Parham, P.5
  • 14
    • 0028906481 scopus 로고
    • Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules
    • Zhang, Q., M. Tector, and R. D. Salter. 1995. Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules. J. Biol. Chem. 270:3944.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3944
    • Zhang, Q.1    Tector, M.2    Salter, R.D.3
  • 15
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou, W-J., P. H. Cameron, D. Y. Thomas, and J. J. M. Bergeron. 1993. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364:771.
    • (1993) Nature , vol.364 , pp. 771
    • Ou, W.-J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 16
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond, C., I. Braakman, and A. Helenius. 1994. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA 91:913.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 913
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 17
    • 0026022577 scopus 로고
    • Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules
    • Degen, E., and D. B. Williams. 1991. Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules. J. Cell. Biol. 112: 1099.
    • (1991) J. Cell. Biol. , vol.112 , pp. 1099
    • Degen, E.1    Williams, D.B.2
  • 18
    • 0023883452 scopus 로고
    • 2-microglobulin: Differential effects of inhibition of glycosylation on class I subunit association
    • 2-microglobulin: differential effects of inhibition of glycosylation on class I subunit association. Eur. J. Immunol. 18:801.
    • (1988) Eur. J. Immunol. , vol.18 , pp. 801
    • Neefjes, J.J.1    Ploegh, H.L.2
  • 19
    • 0028947585 scopus 로고
    • b subsets to serve as TCR ligands for allo-specific CTL clones: Potential role for N-linked glycosylation
    • b subsets to serve as TCR ligands for allo-specific CTL clones: potential role for N-linked glycosylation. J. Exp. Med. 181:1773.
    • (1995) J. Exp. Med. , vol.181 , pp. 1773
    • Shen, L.1    Kane, K.P.2
  • 20
    • 0024582870 scopus 로고
    • Specific immune responses restored by alteration in carbohydrate chains of surface molecules on antigen presenting cells
    • Boog, C. J. P., J. J. Neefjes, J. Boes, H. L. Ploegh, and C. J. M. Melief. 1989. Specific immune responses restored by alteration in carbohydrate chains of surface molecules on antigen presenting cells. Eur. J. Immunol. 19:537.
    • (1989) Eur. J. Immunol. , vol.19 , pp. 537
    • Boog, C.J.P.1    Neefjes, J.J.2    Boes, J.3    Ploegh, H.L.4    Melief, C.J.M.5
  • 21
  • 22
    • 0027410441 scopus 로고
    • The Ly-49 and NKR-P1 gene families encoding lectin-like receptors on natural killer cells: The NK gene complex
    • Yokoyama, W. M., and W. E. Seaman. 1993. The Ly-49 and NKR-P1 gene families encoding lectin-like receptors on natural killer cells: the NK gene complex. Annu. Rev. Immunol. 11:613.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 613
    • Yokoyama, W.M.1    Seaman, W.E.2
  • 23
    • 0028040122 scopus 로고
    • Ly-49 mediates EL4 lymphoma adhesion to isolated class I major histocompatibility complex molecules
    • Kane, K. P. 1994. Ly-49 mediates EL4 lymphoma adhesion to isolated class I major histocompatibility complex molecules. J. Exp. Med. 179:1011.
    • (1994) J. Exp. Med. , vol.179 , pp. 1011
    • Kane, K.P.1
  • 24
    • 0028277286 scopus 로고
    • A natural killer cell receptor specific for a major histocompatibility complex class I molecule
    • Daniels, B. F., F. M. Karlhofer, W. E. Seaman, and W. M. Yokoyama. 1994. A natural killer cell receptor specific for a major histocompatibility complex class I molecule. J. Exp. Med. 180:687.
    • (1994) J. Exp. Med. , vol.180 , pp. 687
    • Daniels, B.F.1    Karlhofer, F.M.2    Seaman, W.E.3    Yokoyama, W.M.4
  • 26
    • 0029015726 scopus 로고
    • Molecular clones of the p58 natural killer cell receptor reveal immunogobulin-related molecules with diversity in both the extra- and intracellular domains
    • Wagtmann, N., R. Biassoni, C. Cantoni, S. Verdiani, M. Mainati, M. Vitale, C. Bottino, L. Moretta, A. Moretta, and E. O. Long. 1995. Molecular clones of the p58 natural killer cell receptor reveal immunogobulin-related molecules with diversity in both the extra- and intracellular domains. Immunity 2:439.
    • (1995) Immunity , vol.2 , pp. 439
    • Wagtmann, N.1    Biassoni, R.2    Cantoni, C.3    Verdiani, S.4    Mainati, M.5    Vitale, M.6    Bottino, C.7    Moretta, L.8    Moretta, A.9    Long, E.O.10
  • 27
    • 0029003984 scopus 로고
    • Cloning of immunoglobulin-superfamily members associated with HLA-C and HLA-B recognition by human natural killer cells
    • Colonna, M., and J. Samaridis. 1995. Cloning of immunoglobulin-superfamily members associated with HLA-C and HLA-B recognition by human natural killer cells. Science 268:405.
    • (1995) Science , vol.268 , pp. 405
    • Colonna, M.1    Samaridis, J.2
  • 29
    • 0027132097 scopus 로고
    • HLA-C is the inhibitory ligand that determines dominant resistance to lysis by NK1- and NK2-specific natural killer cells
    • Colonna, M., G. Borsellino, M. Falco, G. B. Ferrara, and J. L. Strominger. 1993. HLA-C is the inhibitory ligand that determines dominant resistance to lysis by NK1- and NK2-specific natural killer cells. Proc. Natl. Acad. Sci. USA 90:12000.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 12000
    • Colonna, M.1    Borsellino, G.2    Falco, M.3    Ferrara, G.B.4    Strominger, J.L.5
  • 30
    • 0027959069 scopus 로고
    • NK3-specific natural killer cells are selectively inhibited by Bw4-positive HLA alleles with isoleucine 80
    • Cells, M., A. Longo, G. B. Ferrara, J. L. Strominger, and M. Colonn. 1994. NK3-specific natural killer cells are selectively inhibited by Bw4-positive HLA alleles with isoleucine 80. J. Exp. Med. 180:1235.
    • (1994) J. Exp. Med. , vol.180 , pp. 1235
    • Cells, M.1    Longo, A.2    Ferrara, G.B.3    Strominger, J.L.4    Colonn, M.5
  • 32
    • 0028987607 scopus 로고
    • The origins of HLA-A,B,C polymorphism
    • Parham, P., E. J. Adams, and K. L. Arnett. 1995. The origins of HLA-A,B,C polymorphism. Immunol. Rev. 143:141.
    • (1995) Immunol. Rev. , vol.143 , pp. 141
    • Parham, P.1    Adams, E.J.2    Arnett, K.L.3
  • 33
    • 0024542612 scopus 로고
    • Production of human cells expressing individual transferred HLA-A, -B -C genes using an HLA-A, -B and -C null human cell line
    • Shimizu, Y., and R. DeMars. 1989. Production of human cells expressing individual transferred HLA-A, -B -C genes using an HLA-A, -B and -C null human cell line. J. Immunol. 142:3320.
    • (1989) J. Immunol. , vol.142 , pp. 3320
    • Shimizu, Y.1    DeMars, R.2
  • 34
    • 0028332836 scopus 로고
    • NKB1: A natural killer receptor involved in the recognition of polymorphic HLA-B molecules
    • Litwin, V., J. Gumperz, P. Parham, J. H. Phillips, and L. L. Lanier. 1994. NKB1: a natural killer receptor involved in the recognition of polymorphic HLA-B molecules. J. Exp. Med. 180:537.
    • (1994) J. Exp. Med. , vol.180 , pp. 537
    • Litwin, V.1    Gumperz, J.2    Parham, P.3    Phillips, J.H.4    Lanier, L.L.5
  • 35
    • 0029240323 scopus 로고
    • Overlap in the repertoires of peptides bound in vivo by a group of related class I HLA-B allotypes
    • Barber, L. D., B. Gillece-Castro, L. Percival, X. Li, C. Clayberger, and P. Parham. 1995. Overlap in the repertoires of peptides bound in vivo by a group of related class I HLA-B allotypes. Curr. Biol. 5:179.
    • (1995) Curr. Biol. , vol.5 , pp. 179
    • Barber, L.D.1    Gillece-Castro, B.2    Percival, L.3    Li, X.4    Clayberger, C.5    Parham, P.6
  • 36
    • 0019511748 scopus 로고
    • Monoclonal antibodies against two separate alloantigenic sites of HLA-B40
    • Parham, P. 1981. Monoclonal antibodies against two separate alloantigenic sites of HLA-B40. Immunogenetics 13:509.
    • (1981) Immunogenetics , vol.13 , pp. 509
    • Parham, P.1
  • 37
    • 0020300724 scopus 로고
    • Recognition of HLA-B27 and related antigen by a monoclonal antibody
    • Ellis, S. A., C. Taylor, and A. McMichael. 1982. Recognition of HLA-B27 and related antigen by a monoclonal antibody. Hum. Immunol. 5:49.
    • (1982) Hum. Immunol. , vol.5 , pp. 49
    • Ellis, S.A.1    Taylor, C.2    McMichael, A.3
  • 39
    • 0019285686 scopus 로고
    • A monoclonal antibody that recognizes an antigenic determinant shared by HLA-A2 and B17
    • McMichael, A. J., P. Parham, N. Rust, and F. Brodsky. 1980. A monoclonal antibody that recognizes an antigenic determinant shared by HLA-A2 and B17. Hum. Immunol. 1:121.
    • (1980) Hum. Immunol. , vol.1 , pp. 121
    • McMichael, A.J.1    Parham, P.2    Rust, N.3    Brodsky, F.4
  • 40
    • 0018154865 scopus 로고
    • Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens: New tools for genetic analysis
    • Barnstable, C. J., W. F. Bodmer, G. Brown, G. Galfre, C. Milstein, A. F. Williams, and A. Ziegler. 1978. Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens: new tools for genetic analysis. Cell 14:9.
    • (1978) Cell , vol.14 , pp. 9
    • Barnstable, C.J.1    Bodmer, W.F.2    Brown, G.3    Galfre, G.4    Milstein, C.5    Williams, A.F.6    Ziegler, A.7
  • 41
    • 0018698764 scopus 로고
    • Purification of immunologically active HLA-A and -B antigens by a series of monoclonal antibody columns
    • Parham, P. 1979. Purification of immunologically active HLA-A and -B antigens by a series of monoclonal antibody columns. J. Biol. Chem. 254:8709.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8709
    • Parham, P.1
  • 42
    • 0023338172 scopus 로고
    • Tissue-specific N-glycosylation, site-specific oligosaccaride patterns and lentil lectin recognition of rat Thy-1
    • Parekh, R. B., A. G. D. Tse, R. A. Dwek, A. F. Williams, and T. W. Rademacher. 1987. Tissue-specific N-glycosylation, site-specific oligosaccaride patterns and lentil lectin recognition of rat Thy-1. EMBO J. 6:1233.
    • (1987) EMBO J. , vol.6 , pp. 1233
    • Parekh, R.B.1    Tse, A.G.D.2    Dwek, R.A.3    Williams, A.F.4    Rademacher, T.W.5
  • 43
    • 0029164230 scopus 로고
    • Non-selective and efficient fluorescent labelling of glycans using 2-amino benzamide and anthranilic acid
    • Bigge, J. C., T. P. Patel, J. A. Bruce, P. N. Goulding, S. M. Charles, and R. B. Parekh. 1995. Non-selective and efficient fluorescent labelling of glycans using 2-amino benzamide and anthranilic acid. Anal. Biochem. 230:229.
    • (1995) Anal. Biochem. , vol.230 , pp. 229
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 44
    • 0027525106 scopus 로고
    • The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2
    • Madden, D. R., D. N. Garboczi, and D. C. Wiley. 1993. The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2. Cell 75:693.
    • (1993) Cell , vol.75 , pp. 693
    • Madden, D.R.1    Garboczi, D.N.2    Wiley, D.C.3
  • 46
    • 0024350397 scopus 로고
    • HLA-C locus antigens seen by one-dimensional isoelectric focusing: Definition of the so far known HLA-C specificities and the two subtypes
    • Hajek-Rosenmayr, A., L. Jungl, M. Stammler, and M. Kimbauer. 1989. HLA-C locus antigens seen by one-dimensional isoelectric focusing: definition of the so far known HLA-C specificities and the two subtypes. Hum. Immunol. 26:227.
    • (1989) Hum. Immunol. , vol.26 , pp. 227
    • Hajek-Rosenmayr, A.1    Jungl, L.2    Stammler, M.3    Kimbauer, M.4
  • 47
    • 0017237293 scopus 로고
    • Structure of HLA antigens: Amino acid and carbohydrate compositions and NH2-terminal sequences of four antigen preparations
    • Terhorst, C., P. Parham, D. L. Mann, and J. L. Strominger. 1976. Structure of HLA antigens: amino acid and carbohydrate compositions and NH2-terminal sequences of four antigen preparations. Proc. Natl. Acad. Sci. USA 73:910.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 910
    • Terhorst, C.1    Parham, P.2    Mann, D.L.3    Strominger, J.L.4
  • 48
    • 0029121541 scopus 로고
    • Single amino acid substitutions can influence the NK-mediated recognition of HLA-C molecules: Role of serine-77 and lysine-80 in the target cell protection from lysis mediated by "group 2" or "group 1" NK clones
    • Biassoni, R., M. Falco, A. Cambiaggi, P. Costa, S. Verdiani, D. Pende, R. Conte, C. D. Donato, P. Parham, and L. Moretta. 1995. Single amino acid substitutions can influence the NK-mediated recognition of HLA-C molecules: role of serine-77 and lysine-80 in the target cell protection from lysis mediated by "group 2" or "group 1" NK clones. J. Exp. Med. 182:605.
    • (1995) J. Exp. Med. , vol.182 , pp. 605
    • Biassoni, R.1    Falco, M.2    Cambiaggi, A.3    Costa, P.4    Verdiani, S.5    Pende, D.6    Conte, R.7    Donato, C.D.8    Parham, P.9    Moretta, L.10
  • 49
    • 0021956734 scopus 로고
    • Oligosaccaride microheterogenetity of the murine major histocompatibility antigens: Reproducible site specific patterns of sialylation and branching in aspargine-linked oligosaccharides
    • Swiedler, S. J., J. H. Freed, A. L. Tarentino, T. H. Plummer, and G. W. Hart. 1985. Oligosaccaride microheterogenetity of the murine major histocompatibility antigens: reproducible site specific patterns of sialylation and branching in aspargine-linked oligosaccharides. J. Biol. Chem. 260:4046.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4046
    • Swiedler, S.J.1    Freed, J.H.2    Tarentino, A.L.3    Plummer, T.H.4    Hart, G.W.5
  • 51
    • 0019888536 scopus 로고
    • Similarities and differences between the fibronectins of normal and transformed hamster cells
    • Wagner, D. D., R. Ivatt, A. T. Destree, and R. O. Hynes. 1981. Similarities and differences between the fibronectins of normal and transformed hamster cells. J. Biol. Chem. 256:11708.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11708
    • Wagner, D.D.1    Ivatt, R.2    Destree, A.T.3    Hynes, R.O.4
  • 52
    • 0018854072 scopus 로고
    • Increase of asparagine-linked oligosaccharides with branched outer chains caused by cell transformation
    • Takasaki, S., H. Ikehira, and A. Kobata. 1980. Increase of asparagine-linked oligosaccharides with branched outer chains caused by cell transformation. Biochem. Biophys. Res. Commun. 92:735.
    • (1980) Biochem. Biophys. Res. Commun. , vol.92 , pp. 735
    • Takasaki, S.1    Ikehira, H.2    Kobata, A.3
  • 53
    • 11944272604 scopus 로고
    • Environmental effects on protein glycosylation
    • Goochee, C. F., and T. Monica. 1990. Environmental effects on protein glycosylation. Biotechnology 8:421.
    • (1990) Biotechnology , vol.8 , pp. 421
    • Goochee, C.F.1    Monica, T.2
  • 54
    • 0017748275 scopus 로고
    • Molecular structure of human histocompatibility antigens: The HLA-C series
    • Snary, D., C. J. Bamstable, W. F. Bodmer, and M. J. Crumpton. 1977. Molecular structure of human histocompatibility antigens: the HLA-C series. Eur. J. Immunol. 7:580.
    • (1977) Eur. J. Immunol. , vol.7 , pp. 580
    • Snary, D.1    Bamstable, C.J.2    Bodmer, W.F.3    Crumpton, M.J.4
  • 55
    • 0029001798 scopus 로고
    • Low HLA-C expression at cell surfaces correlates with increased turnover of heavy chain mRNA
    • McCutcheon, J. A., J. Gumperz, K. D. Smith, C. T. Lutz, and P. Parham. 1995. Low HLA-C expression at cell surfaces correlates with increased turnover of heavy chain mRNA. J. Exp. Med. 181:2085.
    • (1995) J. Exp. Med. , vol.181 , pp. 2085
    • McCutcheon, J.A.1    Gumperz, J.2    Smith, K.D.3    Lutz, C.T.4    Parham, P.5
  • 56
    • 0026671264 scopus 로고
    • Distinctive polymorphism at the HLA-C locus: Implications for the expression of HLA-C
    • Zemmour, J., and P. Parham. 1992. Distinctive polymorphism at the HLA-C locus: implications for the expression of HLA-C. J. Exp. Med. 176:937.
    • (1992) J. Exp. Med. , vol.176 , pp. 937
    • Zemmour, J.1    Parham, P.2
  • 57
    • 0024430777 scopus 로고
    • Restriction of Epstein-Barr virus-specific cytotoxic T cells by HLA-A, -B and -C molecules
    • Chen, B. P., V. Lam, E. E. Kraus, R. DeMars, and P. M. Sondel. 1989. Restriction of Epstein-Barr virus-specific cytotoxic T cells by HLA-A, -B and -C molecules. Hum. Immunol. 26:137.
    • (1989) Hum. Immunol. , vol.26 , pp. 137
    • Chen, B.P.1    Lam, V.2    Kraus, E.E.3    Demars, R.4    Sondel, P.M.5
  • 60
    • 0019934863 scopus 로고
    • Structural and numerical variations of the carbohydrate moiety of immunoglobulin G
    • Mizuochi, T., T. Taniguchi, A. Shimizu, and A. Kobata. 1982. Structural and numerical variations of the carbohydrate moiety of immunoglobulin G. J. Immunol. 129:2016.
    • (1982) J. Immunol. , vol.129 , pp. 2016
    • Mizuochi, T.1    Taniguchi, T.2    Shimizu, A.3    Kobata, A.4
  • 62
    • 0023646675 scopus 로고
    • Tertiary structure in N-linked oligosaccharides
    • Homans, S. W., R. A. Dwek, and T. W. Rademacher. 1987. Tertiary structure in N-linked oligosaccharides. Biochemistry 26:6553.
    • (1987) Biochemistry , vol.26 , pp. 6553
    • Homans, S.W.1    Dwek, R.A.2    Rademacher, T.W.3
  • 63
    • 0017655393 scopus 로고
    • Analysis of H-2 and Ia molecules by two-dimensional gel electrophoresis
    • Jones, P. P. 1977. Analysis of H-2 and Ia molecules by two-dimensional gel electrophoresis. J. Exp. Med. 146:1261.
    • (1977) J. Exp. Med. , vol.146 , pp. 1261
    • Jones, P.P.1
  • 64
    • 0020446650 scopus 로고
    • Differential regulation of mouse H-2 alloantigens
    • Le, A. V., and D. Doyle. 1982. Differential regulation of mouse H-2 alloantigens. Biochemistry 21:5730.
    • (1982) Biochemistry , vol.21 , pp. 5730
    • Le, A.V.1    Doyle, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.