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Volumn 160, Issue 6, 1998, Pages 2809-2814

Direct binding of the MHC class I molecule H-2L(d) to CD8: Interaction with the amino terminus of a mature cell surface protein

Author keywords

[No Author keywords available]

Indexed keywords

CD8 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; T LYMPHOCYTE RECEPTOR;

EID: 0032520789     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (13)

References (67)
  • 1
    • 0023747640 scopus 로고
    • The Lyt-2 molecule recognizes residues in the class I α3 domain in allogeneic cytotoxic T cell responses
    • Connolly, J. M., T. A. Potter, E. M. Wormstall, and T. H. Hansen. 1988. The Lyt-2 molecule recognizes residues in the class I α3 domain in allogeneic cytotoxic T cell responses. J. Exp. Med. 168:325.
    • (1988) J. Exp. Med. , vol.168 , pp. 325
    • Connolly, J.M.1    Potter, T.A.2    Wormstall, E.M.3    Hansen, T.H.4
  • 3
    • 0025864122 scopus 로고
    • Mutations in CD8 that affect interactions with HLA class 1 and monoclonal anti-CD8 antibodies
    • Sanders, S. K., R. O. Fox, and P. Kavathas. 1991. Mutations in CD8 that affect interactions with HLA class 1 and monoclonal anti-CD8 antibodies. J. Exp. Med. 174:371.
    • (1991) J. Exp. Med. , vol.174 , pp. 371
    • Sanders, S.K.1    Fox, R.O.2    Kavathas, P.3
  • 4
    • 0026600162 scopus 로고
    • Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 Å resolution
    • Leahy, D. J., R. Axel, and W. A. Hendrickson. 1992. Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 Å resolution. Cell 68: 1145.
    • (1992) Cell , vol.68 , pp. 1145
    • Leahy, D.J.1    Axel, R.2    Hendrickson, W.A.3
  • 5
    • 0028322932 scopus 로고
    • The role of charge and multiple faces of the CD8 alpha/alpha homodimer in binding to major histocompatibility complex class I molecules: Support for a bivalent model
    • Giblin, P. A., D. J. Leahy, J. Mennone, and P. B. Kavathas. 1994. The role of charge and multiple faces of the CD8 alpha/alpha homodimer in binding to major histocompatibility complex class I molecules: support for a bivalent model. Proc. Natl. Acad. Sci. USA 91:1716.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1716
    • Giblin, P.A.1    Leahy, D.J.2    Mennone, J.3    Kavathas, P.B.4
  • 6
    • 0028838283 scopus 로고
    • Interaction between CD8 and major histocompatibility complex (MHC) class I mediated by multiple contact surfaces that include the α2 and α3 domains of MHC class I
    • Sun, J., D. J. Leahy, and P. B. Kavathas. 1995. Interaction between CD8 and major histocompatibility complex (MHC) class I mediated by multiple contact surfaces that include the α2 and α3 domains of MHC class I. J. Exp. Med. 182:1275.
    • (1995) J. Exp. Med. , vol.182 , pp. 1275
    • Sun, J.1    Leahy, D.J.2    Kavathas, P.B.3
  • 9
    • 0029150969 scopus 로고
    • Involvement of both major histocompatibility complex class II alpha and beta chains in CD4 function indicates a role for ordered oligomerization in T cell activation
    • Konig, R., X. Shen, and R. N. Germain. 1995. Involvement of both major histocompatibility complex class II alpha and beta chains in CD4 function indicates a role for ordered oligomerization in T cell activation. J. Exp. Med. 182:779.
    • (1995) J. Exp. Med. , vol.182 , pp. 779
    • Konig, R.1    Shen, X.2    Germain, R.N.3
  • 13
    • 0027231906 scopus 로고
    • A soluble form of the human CD8 alpha chain expressed in the baculovirus system: Biochemical characterization and binding to MHC class I
    • Alcover, A., F. Herve, J. P. Boursier, G. Spagnoli, D. Olive, R. A. Mariuzza, and O. Acuto. 1993. A soluble form of the human CD8 alpha chain expressed in the baculovirus system: biochemical characterization and binding to MHC class I. Mol. Immunol. 30:55.
    • (1993) Mol. Immunol. , vol.30 , pp. 55
    • Alcover, A.1    Herve, F.2    Boursier, J.P.3    Spagnoli, G.4    Olive, D.5    Mariuzza, R.A.6    Acuto, O.7
  • 14
    • 0027169408 scopus 로고
    • Mouse CD4 binds MHC class II with extremely low affinity
    • Weber, S., and K. Karjalainen. 1993. Mouse CD4 binds MHC class II with extremely low affinity. Int. Immunol. 5:695.
    • (1993) Int. Immunol. , vol.5 , pp. 695
    • Weber, S.1    Karjalainen, K.2
  • 18
    • 0003104975 scopus 로고    scopus 로고
    • A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists
    • Lyons, D. S., S. A. Lieberman, J. Hampl, J. J. Boniface, Y.-H. Chien, L. J. Berg, and M. M. Davis. 1996. A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists. Immunity 5:53.
    • (1996) Immunity , vol.5 , pp. 53
    • Lyons, D.S.1    Lieberman, S.A.2    Hampl, J.3    Boniface, J.J.4    Chien, Y.-H.5    Berg, L.J.6    Davis, M.M.7
  • 19
    • 0029013301 scopus 로고
    • Lack of strict correlation of functional sensitization with the apparent affinity of MHC/peptide complexes for the T cell receptor
    • Al-Ramadi, B. K., M. T. Jelonek, L. F. Boyd, D. H. Margulies, and A. L. M. Bothwell. 1995. Lack of strict correlation of functional sensitization with the apparent affinity of MHC/peptide complexes for the T cell receptor. J. Immunol. 155:662.
    • (1995) J. Immunol. , vol.155 , pp. 662
    • Al-Ramadi, B.K.1    Jelonek, M.T.2    Boyd, L.F.3    Margulies, D.H.4    Bothwell, A.L.M.5
  • 20
    • 0028797801 scopus 로고
    • CD8 modulation of T-cell antigen receptor-ligand interactions on living cytotoxic T lymphocytes
    • Luescher, I. F., E. Vivier, A. Layer, J. Mahiou, F. Godeau, B. Malissen, and P. Romero. 1995. CD8 modulation of T-cell antigen receptor-ligand interactions on living cytotoxic T lymphocytes. Nature 373:353.
    • (1995) Nature , vol.373 , pp. 353
    • Luescher, I.F.1    Vivier, E.2    Layer, A.3    Mahiou, J.4    Godeau, F.5    Malissen, B.6    Romero, P.7
  • 24
    • 0027205314 scopus 로고
    • Direct detection of major histocompatibility complex class I binding to antigenic peptides using surface plasmon resonance: Peptide immobilization and characterization of binding specificity
    • Khilko, S. N., M. Corr, L. F. Boyd, A. Lees, J. K. Inman, and D. H. Margulies. 1993. Direct detection of major histocompatibility complex class I binding to antigenic peptides using surface plasmon resonance: peptide immobilization and characterization of binding specificity. J. Biol. Chem. 268:15425.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15425
    • Khilko, S.N.1    Corr, M.2    Boyd, L.F.3    Lees, A.4    Inman, J.K.5    Margulies, D.H.6
  • 25
    • 0004274687 scopus 로고
    • Multivalent requirement for the stimulation of alloreactive T cells: Studies with engineered soluble MHC class 1 proteins in vitro and in vivo
    • I. K. Egorov, and C. S. David, eds. Springer-Verlag, Berlin, Heidelberg
    • Margulies, D. H., L. F. Boyd, S. Kozlowski, L. Kjer-Nielsen, R. Lopez, J. Schneck, and R. Hunziker. 1990. Multivalent requirement for the stimulation of alloreactive T cells: studies with engineered soluble MHC class 1 proteins in vitro and in vivo. In Transgenic Mice and Mutants in MHC Research. I. K. Egorov, and C. S. David, eds. Springer-Verlag, Berlin, Heidelberg, p. 39.
    • (1990) Transgenic Mice and Mutants in MHC Research , pp. 39
    • Margulies, D.H.1    Boyd, L.F.2    Kozlowski, S.3    Kjer-Nielsen, L.4    Lopez, R.5    Schneck, J.6    Hunziker, R.7
  • 26
    • 0024520409 scopus 로고
    • Inhibition of an allospecific T cell hybridoma by soluble class I proteins and peptides: Estimation of the affinity of a T cell receptor for MHC
    • Schneck, J., W. L. Maloy, J. E. Coligan, and D. H. Margulies. 1989. Inhibition of an allospecific T cell hybridoma by soluble class I proteins and peptides: estimation of the affinity of a T cell receptor for MHC. Cell 56:47.
    • (1989) Cell , vol.56 , pp. 47
    • Schneck, J.1    Maloy, W.L.2    Coligan, J.E.3    Margulies, D.H.4
  • 27
    • 0030947854 scopus 로고    scopus 로고
    • Naive alloreactive CD8 T cells are activated by purified major histocompatibility complex class I and antigenic peptide
    • Goldstein, J., H. Mostowsky, J. Tung, H. Hon, M. Brunswick, and S. Kozlowski. 1997. Naive alloreactive CD8 T cells are activated by purified major histocompatibility complex class I and antigenic peptide. Eur. J. Immunol. 27.
    • (1997) Eur. J. Immunol. , vol.27
    • Goldstein, J.1    Mostowsky, H.2    Tung, J.3    Hon, H.4    Brunswick, M.5    Kozlowski, S.6
  • 29
    • 0026500119 scopus 로고
    • The hinge region of the CD8 alpha chain: Structure, antigenicity, and utility in expression of immunoglobulin superfamily domains
    • Classon, B. J., M. H. Brown, D. Garnett, C. Somoza, A. N. Barclay, A. C. Willis, and A. F. Williams. 1992. The hinge region of the CD8 alpha chain: structure, antigenicity, and utility in expression of immunoglobulin superfamily domains. Int. Immunol. 4:215.
    • (1992) Int. Immunol. , vol.4 , pp. 215
    • Classon, B.J.1    Brown, M.H.2    Garnett, D.3    Somoza, C.4    Barclay, A.N.5    Willis, A.C.6    Williams, A.F.7
  • 30
    • 0345311675 scopus 로고
    • Molecular cloning of Lyt-3, a membrane glycoprotein marking a subset of mouse T lymphocytes: Molecular homology to immunoglobulin and T cell receptor variable and joining regions
    • Nakauchi, H., Y. Shinkai, and K. Okumura. 1987. Molecular cloning of Lyt-3, a membrane glycoprotein marking a subset of mouse T lymphocytes: molecular homology to immunoglobulin and T cell receptor variable and joining regions. Proc. Natl. Acad. Sci. USA 84:4210.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4210
    • Nakauchi, H.1    Shinkai, Y.2    Okumura, K.3
  • 31
    • 0018652555 scopus 로고
    • Xonogeneic monoclonal antibodies to mouse lymphoid differentiation antigens
    • Ledbetter, J. A., and L. A. Herzenberg. 1979. Xonogeneic monoclonal antibodies to mouse lymphoid differentiation antigens. Immunol. Rev. 47:63.
    • (1979) Immunol. Rev. , vol.47 , pp. 63
    • Ledbetter, J.A.1    Herzenberg, L.A.2
  • 33
    • 0027983589 scopus 로고
    • Determinant selection of major histocompatibility complex class I-restricted antigenic peptides is explained by class I-peptide affinity and is strongly influenced by nondominant anchor residues
    • Chen, W., S. Khilko, J. Fecondo, D. H. Margulies, and J. McCluskey. 1994. Determinant selection of major histocompatibility complex class I-restricted antigenic peptides is explained by class I-peptide affinity and is strongly influenced by nondominant anchor residues. J. Exp. Med. 180:1471.
    • (1994) J. Exp. Med. , vol.180 , pp. 1471
    • Chen, W.1    Khilko, S.2    Fecondo, J.3    Margulies, D.H.4    McCluskey, J.5
  • 36
    • 0028104782 scopus 로고
    • High-affinity reactions between antigen-specific T-cell receptors and peptides associated with allogeneic and syngeneic major histocompatibility complex class I proteins
    • Sykulev, Y., A. Brunmark, T. J. Tsomides, S. Kageyama, M. Jackson, P. A. Peterson, and H. N. Eisen. 1994. High-affinity reactions between antigen-specific T-cell receptors and peptides associated with allogeneic and syngeneic major histocompatibility complex class I proteins. Proc. Natl. Acad. Sci. USA 91:11487.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11487
    • Sykulev, Y.1    Brunmark, A.2    Tsomides, T.J.3    Kageyama, S.4    Jackson, M.5    Peterson, P.A.6    Eisen, H.N.7
  • 38
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi, D. N., P. Ghosh, U. Utz, Q. R Fan, W. E. Biddison, and D. C. Wiley. 1996. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384:134.
    • (1996) Nature , vol.384 , pp. 134
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddison, W.E.5    Wiley, D.C.6
  • 39
    • 0031020557 scopus 로고    scopus 로고
    • Immunology: Feeling out the receptor
    • Padlan, E. A., and D. H. Margulies. 1997. Immunology: feeling out the receptor. Curr. Biol. 7:R17.
    • (1997) Curr. Biol. , vol.7
    • Padlan, E.A.1    Margulies, D.H.2
  • 40
    • 0025831493 scopus 로고
    • Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution
    • Saper, M. A., P. J. Bjorkman, and D. C. Wiley. 1991. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å 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
  • 41
    • 0028150789 scopus 로고
    • Three-dimensional structure of a peptide extending from one end of a class I MHC binding sue
    • Collins, E. J., D. N. Garboczi, and D. C. Wiley. 1994. Three-dimensional structure of a peptide extending from one end of a class I MHC binding sue. Nature 371:626.
    • (1994) Nature , vol.371 , pp. 626
    • Collins, E.J.1    Garboczi, D.N.2    Wiley, D.C.3
  • 43
    • 0021054687 scopus 로고
    • Immunoprecipitation of insulin receptors by antibodies against class I antigens of the murine H-2 major histocompatibility complex
    • Chvatchko, Y., E. Van Obberghen, N. Kiger, and M. Fehlmann. 1983. Immunoprecipitation of insulin receptors by antibodies against class I antigens of the murine H-2 major histocompatibility complex. FEBS Lett. 163:207.
    • (1983) FEBS Lett. , vol.163 , pp. 207
    • Chvatchko, Y.1    Van Obberghen, E.2    Kiger, N.3    Fehlmann, M.4
  • 44
    • 0022369048 scopus 로고
    • Molecular association between major histocompatibility complex class I antigens and insulin receptors in mouse liver membranes
    • Fehlmann, M., J. F. Peyron, M. Samson, E. Van Obberghen, D. Brandenburg, and N. Brossette. 1985. Molecular association between major histocompatibility complex class I antigens and insulin receptors in mouse liver membranes. Proc. Natl. Acad. Sci. USA 82:8634.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8634
    • Fehlmann, M.1    Peyron, J.F.2    Samson, M.3    Van Obberghen, E.4    Brandenburg, D.5    Brossette, N.6
  • 45
    • 0344017448 scopus 로고
    • The major histocompatibility complex class I heavy chain as a structural subunit of the human cell membrane insulin receptor: Implications for the range of biological functions of histocompatibility antigens
    • Due, C., M. Simonsen, and L. Olsson. 1986. The major histocompatibility complex class I heavy chain as a structural subunit of the human cell membrane insulin receptor: implications for the range of biological functions of histocompatibility antigens. Proc. Natl. Acad. Sci. USA 83:6007.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6007
    • Due, C.1    Simonsen, M.2    Olsson, L.3
  • 46
    • 0022448575 scopus 로고
    • Class I histocompatibility antigens and insulin receptors: Evidence for interactions
    • Phillips, M. L., M. L. Moule, T. L. Delovitch, and C. C. Yip. 1986. Class I histocompatibility antigens and insulin receptors: evidence for interactions. Proc. Natl. Acad. Sci. USA 83:3474.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3474
    • Phillips, M.L.1    Moule, M.L.2    Delovitch, T.L.3    Yip, C.C.4
  • 47
    • 0024378113 scopus 로고
    • Specific molecular interaction between the insulin receptor and a D product of MHC class I
    • Verland, S., M. Simonsen, S. Gammeltoft, H. Allen, R. A. Flavell, and L. Olsson. 1989. Specific molecular interaction between the insulin receptor and a D product of MHC class I. J. Immunol. 143:945.
    • (1989) J. Immunol. , vol.143 , pp. 945
    • Verland, S.1    Simonsen, M.2    Gammeltoft, S.3    Allen, H.4    Flavell, R.A.5    Olsson, L.6
  • 48
    • 0025695564 scopus 로고
    • Dynamic measurements of the associations between class I MHC antigens and insulin receptors
    • Edidin, M., and J. Reiland. 1990. Dynamic measurements of the associations between class I MHC antigens and insulin receptors. Mol. Immunol. 27:1313.
    • (1990) Mol. Immunol. , vol.27 , pp. 1313
    • Edidin, M.1    Reiland, J.2
  • 49
    • 0027516036 scopus 로고
    • Chemical cross-linking detects association of insulin receptors with four different class I human leukocyte antigen molecules on cell surfaces
    • Reiland, J., and M. Edidin. 1993. Chemical cross-linking detects association of insulin receptors with four different class I human leukocyte antigen molecules on cell surfaces. Diabetes 42:619.
    • (1993) Diabetes , vol.42 , pp. 619
    • Reiland, J.1    Edidin, M.2
  • 50
    • 0023680256 scopus 로고
    • Evidence for specific association between class I major histocompatibility genes and the CD8 molecules of human suppressor/cytotoxic cells
    • Blue, M. L., K. A. Craig, P. Anderson, K. R. Branton, Jr., and S. F. Schlossman. 1988. Evidence for specific association between class I major histocompatibility genes and the CD8 molecules of human suppressor/cytotoxic cells. Cell 29:413.
    • (1988) Cell , vol.29 , pp. 413
    • Blue, M.L.1    Craig, K.A.2    Anderson, P.3    Branton Jr., K.R.4    Schlossman, S.F.5
  • 51
    • 0023010578 scopus 로고
    • Novel interleukin-2 receptor subunit detected by cross-linking under high-affinity conditions
    • Sharon, M., R. D. Klausner, B. R. Cullen, R. Chizzonite, and W. J. Leonard. 1986. Novel interleukin-2 receptor subunit detected by cross-linking under high-affinity conditions. Science 234:859.
    • (1986) Science , vol.234 , pp. 859
    • Sharon, M.1    Klausner, R.D.2    Cullen, B.R.3    Chizzonite, R.4    Leonard, W.J.5
  • 52
    • 0023896057 scopus 로고
    • Luteinizing hormone triggers a molecular association between its receptor and the major histocompatibility complex class I antigen to produce cell activation
    • Solano, A. R., M. L. Sanchez, M. L. Sardanons, L. Dada, and E. J. Podesta. 1988. Luteinizing hormone triggers a molecular association between its receptor and the major histocompatibility complex class I antigen to produce cell activation. Endocrinology 122:2080.
    • (1988) Endocrinology , vol.122 , pp. 2080
    • Solano, A.R.1    Sanchez, M.L.2    Sardanons, M.L.3    Dada, L.4    Podesta, E.J.5
  • 53
    • 0024043855 scopus 로고
    • Molecular and biological interaction between major histocompatibility complex class I antigens and luteinizing hormone receptors or beta-adrenergic receptors triggers cellular response in mice
    • Solano, A. R., G. Cremaschi, M. L. Sanchez, E. Borda, L. Sterin-Borda, and E. J. Podesta. 1988. Molecular and biological interaction between major histocompatibility complex class I antigens and luteinizing hormone receptors or beta-adrenergic receptors triggers cellular response in mice. Proc. Natl. Acad. Sci. USA 85:5087.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5087
    • Solano, A.R.1    Cremaschi, G.2    Sanchez, M.L.3    Borda, E.4    Sterin-Borda, L.5    Podesta, E.J.6
  • 54
    • 0023869747 scopus 로고
    • Norepinephrine inhibits gamma-interferon-induced major histocompatibility class II (Ia) antigen expression on cultured astrocytes via β-2-adrenergic signal transduction mechanisms
    • Frohman, E. M., B. Vayuvegula, S. Gupta, and S. van den Noort. 1988. Norepinephrine inhibits gamma-interferon-induced major histocompatibility class II (Ia) antigen expression on cultured astrocytes via β-2-adrenergic signal transduction mechanisms. Proc. Natl. Acad. Sci. USA 85:1292.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1292
    • Frohman, E.M.1    Vayuvegula, B.2    Gupta, S.3    Van Den Noort, S.4
  • 55
    • 0027940742 scopus 로고
    • Increased proliferative activity, loss of beta-adrenergic receptor function and class I major histocompatibility complex antigen surface expression in a modified lymphoma cell line
    • Cremaschi, G. A., S. Miguel, C. Cazaux, and L. Sterin-Borda. 1994. Increased proliferative activity, loss of beta-adrenergic receptor function and class I major histocompatibility complex antigen surface expression in a modified lymphoma cell line. Cell. Signal. 6:781.
    • (1994) Cell. Signal. , vol.6 , pp. 781
    • Cremaschi, G.A.1    Miguel, S.2    Cazaux, C.3    Sterin-Borda, L.4
  • 56
    • 0021327659 scopus 로고
    • Interaction between major histocompatibility complex antigens and epidermal growth factor receptors on human cells
    • Schreiber, A. B., J. Schlessinger, and M. Edidin. 1984. Interaction between major histocompatibility complex antigens and epidermal growth factor receptors on human cells. J. Cell Biol. 98:725.
    • (1984) J. Cell Biol. , vol.98 , pp. 725
    • Schreiber, A.B.1    Schlessinger, J.2    Edidin, M.3
  • 58
    • 0028052724 scopus 로고
    • Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual peptide side-chains
    • Parker, K. C., M. A. Bednarek, and J. E. Coligan. 1994. Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual peptide side-chains. J. Immunol. 152:163.
    • (1994) J. Immunol. , vol.152 , pp. 163
    • Parker, K.C.1    Bednarek, M.A.2    Coligan, J.E.3
  • 59
    • 0028685741 scopus 로고
    • Assembly and transport of class I MHC-peptide complexes
    • Cresswell, P., M. J. Androlewicz, and B. Ortmann. 1994. Assembly and transport of class I MHC-peptide complexes. Ciba Found. Symp. 187:150.
    • (1994) Ciba Found. Symp. , vol.187 , pp. 150
    • Cresswell, P.1    Androlewicz, M.J.2    Ortmann, B.3
  • 60
    • 0028181429 scopus 로고
    • Regulation of MHC class I transport by the molecular chaperone. calnexin (p88, IP90)
    • Jackson, M. R., M. F. Cohen-Doyle, P. A. Peterson, and D. B. Williams. 1994. Regulation of MHC class I transport by the molecular chaperone. calnexin (p88, IP90). Science 263:384.
    • (1994) Science , vol.263 , pp. 384
    • Jackson, M.R.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Williams, D.B.4
  • 61
    • 0028858641 scopus 로고
    • TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man
    • Carreno, B. M., J. C. Solheim, M. Harris, I. Stroynowski, J. M. Connolly, and T. H. Hansen. 1995. TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man. J. Immunol. 155:4726.
    • (1995) J. Immunol. , vol.155 , pp. 4726
    • Carreno, B.M.1    Solheim, J.C.2    Harris, M.3    Stroynowski, I.4    Connolly, J.M.5    Hansen, T.H.6
  • 62
    • 0028932360 scopus 로고
    • The molecular chaperone calnexin binds Glc1 Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins
    • Ware, F. E., A. Vassilakos, P. A. Peterson, M. R. Jackson, M. A. Lehrman, and D. B. Williams. 1995. The molecular chaperone calnexin binds Glc1 Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J. Biol. Chem. 270:4697.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4697
    • Ware, F.E.1    Vassilakos, A.2    Peterson, P.A.3    Jackson, M.R.4    Lehrman, M.A.5    Williams, D.B.6
  • 63
    • 0028883409 scopus 로고
    • Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines
    • Ora, A., and A. Helenius. 1995. Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines. J. Biol. Chem. 270:26060.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26060
    • Ora, A.1    Helenius, A.2
  • 64
    • 0029925940 scopus 로고    scopus 로고
    • The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules
    • Vassilakos, A., M. F. Cohen-Doyle, P. A. Peterson, M. R. Jackson, and D. B. Williams. 1996. The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J. 15:1495.
    • (1996) EMBO J. , vol.15 , pp. 1495
    • Vassilakos, A.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Jackson, M.R.4    Williams, D.B.5
  • 65
    • 0029813510 scopus 로고    scopus 로고
    • MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains
    • Suh, W. K., E. K. Mitchell, Y. Yang, P. A. Peterson, G. L. Waneck, and D. B. Williams 1996. MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains. J. Exp. Med. 184:337.
    • (1996) J. Exp. Med. , vol.184 , pp. 337
    • Suh, W.K.1    Mitchell, E.K.2    Yang, Y.3    Peterson, P.A.4    Waneck, G.L.5    Williams, D.B.6
  • 66
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • Sadasivan, B., P. J. Lehner, B. Ortmann, T. Spies, and P. Cresswell. 1996. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5:103.
    • (1996) Immunity , vol.5 , pp. 103
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 67
    • 0031567996 scopus 로고    scopus 로고
    • Are transporter associated with antigen processing (TAP) and tapasin class I MHC chaperones?
    • Solheim, J. C., B. M. Carreno, and T. H. Hansen. 1997. Are transporter associated with antigen processing (TAP) and tapasin class I MHC chaperones? J. Immunol. 158:541.
    • (1997) J. Immunol. , vol.158 , pp. 541
    • Solheim, J.C.1    Carreno, B.M.2    Hansen, T.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.