메뉴 건너뛰기




Volumn 28, Issue 3, 2007, Pages 115-123

Open conformers: the hidden face of MHC-I molecules

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; NATURAL KILLER CELL RECEPTOR;

EID: 33847155383     PISSN: 14714906     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.it.2007.01.002     Document Type: Review
Times cited : (88)

References (98)
  • 1
    • 0037290828 scopus 로고    scopus 로고
    • Assembly and export of MHC class I peptide ligands
    • Antoniou A.N., et al. Assembly and export of MHC class I peptide ligands. Curr. Opin. Immunol. 15 (2003) 75-81
    • (2003) Curr. Opin. Immunol. , vol.15 , pp. 75-81
    • Antoniou, A.N.1
  • 2
    • 0031051852 scopus 로고    scopus 로고
    • Misfolded major histocompatibility complex class heavy chains are translocated into the cytoplasm and degraded by the proteasome
    • Hughes E.A., et al. Misfolded major histocompatibility complex class heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 1896-1901
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 1896-1901
    • Hughes, E.A.1
  • 3
    • 13944250933 scopus 로고    scopus 로고
    • Human cytomegalovirus protein US11 provokes an unfolded protein response that may facilitate the degradation of class I major histocompatibility complex products
    • Tirosh B., et al. Human cytomegalovirus protein US11 provokes an unfolded protein response that may facilitate the degradation of class I major histocompatibility complex products. J. Virol. 79 (2005) 2768-2779
    • (2005) J. Virol. , vol.79 , pp. 2768-2779
    • Tirosh, B.1
  • 4
    • 26244455510 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing and cross-presentation
    • Cresswell P., et al. Mechanisms of MHC class I-restricted antigen processing and cross-presentation. Immunol. Rev. 207 (2005) 145-157
    • (2005) Immunol. Rev. , vol.207 , pp. 145-157
    • Cresswell, P.1
  • 5
    • 1542615649 scopus 로고    scopus 로고
    • Inhibitory NK-cell receptors on T cells: witness of the past, actors of the future
    • Vivier E., and Anfossi N. Inhibitory NK-cell receptors on T cells: witness of the past, actors of the future. Nat. Rev. Immunol. 4 (2004) 190-198
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 190-198
    • Vivier, E.1    Anfossi, N.2
  • 6
    • 0025358734 scopus 로고
    • 2-microglobulin
    • 2-microglobulin. J. Exp. Med. 171 (1990) 1431-1442
    • (1990) J. Exp. Med. , vol.171 , pp. 1431-1442
    • Schnabl, E.1
  • 7
    • 0026077235 scopus 로고
    • Molecular definition of a polymorphic antigen (LA45) of free HLA-A and -B heavy chains found on the surfaces of activated B and T cells
    • Madrigal J.A., et al. Molecular definition of a polymorphic antigen (LA45) of free HLA-A and -B heavy chains found on the surfaces of activated B and T cells. J. Exp. Med. 174 (1991) 1085-1095
    • (1991) J. Exp. Med. , vol.174 , pp. 1085-1095
    • Madrigal, J.A.1
  • 8
    • 0025869911 scopus 로고
    • Human immunodeficiency virus type 1 gp120 mimics a hidden monomorphic epitope borne by class I major histocompatibility complex heavy chains
    • Grassi F., et al. Human immunodeficiency virus type 1 gp120 mimics a hidden monomorphic epitope borne by class I major histocompatibility complex heavy chains. J. Exp. Med. 174 (1991) 53-62
    • (1991) J. Exp. Med. , vol.174 , pp. 53-62
    • Grassi, F.1
  • 9
    • 0026643624 scopus 로고
    • 2m-free MHC class I molecules induced on activated T cells
    • 2m-free MHC class I molecules induced on activated T cells. Cell. Immunol. 142 (1992) 103-113
    • (1992) Cell. Immunol. , vol.142 , pp. 103-113
    • DeMaria, S.1
  • 10
    • 0345676519 scopus 로고    scopus 로고
    • Why certain antibodies cross-react with HLA-A and HLA-G: epitope mapping of two common MHC class I reagents
    • Sernee M.F., et al. Why certain antibodies cross-react with HLA-A and HLA-G: epitope mapping of two common MHC class I reagents. Mol. Immunol. 35 (1998) 177-188
    • (1998) Mol. Immunol. , vol.35 , pp. 177-188
    • Sernee, M.F.1
  • 11
    • 0033546416 scopus 로고    scopus 로고
    • Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules
    • Arosa F.A., et al. Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules. J. Biol. Chem. 274 (1999) 16917-16922
    • (1999) J. Biol. Chem. , vol.274 , pp. 16917-16922
    • Arosa, F.A.1
  • 12
    • 0042635849 scopus 로고    scopus 로고
    • 2-Microglobulin-free HLA class I heavy chain epitope mimicry by monoclonal antibody HC-10-specific peptide
    • 2-Microglobulin-free HLA class I heavy chain epitope mimicry by monoclonal antibody HC-10-specific peptide. J. Immunol. 171 (2003) 1918-1926
    • (2003) J. Immunol. , vol.171 , pp. 1918-1926
    • Perosa, F.1
  • 13
    • 11144230937 scopus 로고    scopus 로고
    • Misfolding of major histocompatibility complex class I molecules in activated T cells allows cis-interactions with receptors and signaling molecules and is associated with tyrosine phosphorylation
    • Santos S.G., et al. Misfolding of major histocompatibility complex class I molecules in activated T cells allows cis-interactions with receptors and signaling molecules and is associated with tyrosine phosphorylation. J. Biol. Chem. 279 (2004) 53062-53070
    • (2004) J. Biol. Chem. , vol.279 , pp. 53062-53070
    • Santos, S.G.1
  • 14
    • 26244456282 scopus 로고    scopus 로고
    • Recognition of open conformers of classical MHC by chaperones and monoclonal antibodies
    • Hansen T.H., et al. Recognition of open conformers of classical MHC by chaperones and monoclonal antibodies. Immunol. Rev. 207 (2005) 100-111
    • (2005) Immunol. Rev. , vol.207 , pp. 100-111
    • Hansen, T.H.1
  • 15
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world
    • Stefani M. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim. Biophys. Acta 1739 (2004) 5-25
    • (2004) Biochim. Biophys. Acta , vol.1739 , pp. 5-25
    • Stefani, M.1
  • 16
    • 0022369048 scopus 로고
    • Molecular association between major histocompatibility complex class I antigens and insulin receptors in mouse liver membranes
    • Fehlmann M., et al. Molecular association between major histocompatibility complex class I antigens and insulin receptors in mouse liver membranes. Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 8634-8637
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 8634-8637
    • Fehlmann, M.1
  • 17
    • 0022448575 scopus 로고
    • Class I histocompatibility antigens and insulin receptors: evidence for interactions
    • Phillips M.L., et al. Class I histocompatibility antigens and insulin receptors: evidence for interactions. Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 3474-3478
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 3474-3478
    • Phillips, M.L.1
  • 18
    • 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., et al. 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. U. S. A. 83 (1986) 6007-6011
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 6007-6011
    • Due, C.1
  • 19
    • 0022521981 scopus 로고
    • Cross-linking of insulin receptors to MHC antigens in human B lymphocytes: evidence for selective molecular interactions
    • Samson M., et al. Cross-linking of insulin receptors to MHC antigens in human B lymphocytes: evidence for selective molecular interactions. J. Immunol. 137 (1986) 2293-2298
    • (1986) J. Immunol. , vol.137 , pp. 2293-2298
    • Samson, M.1
  • 20
    • 0021327659 scopus 로고
    • Interaction between major histocompatibility complex antigens and epidermal growth factor receptors on human cells
    • Schreiber A.B., et al. Interaction between major histocompatibility complex antigens and epidermal growth factor receptors on human cells. J. Cell Biol. 98 (1984) 725-731
    • (1984) J. Cell Biol. , vol.98 , pp. 725-731
    • Schreiber, A.B.1
  • 21
    • 0023736047 scopus 로고
    • Possible association between IL-2 receptors and class I HLA molecules on T cells
    • Sharon M., et al. Possible association between IL-2 receptors and class I HLA molecules on T cells. J. Immunol. 141 (1988) 3512-3515
    • (1988) J. Immunol. , vol.141 , pp. 3512-3515
    • Sharon, M.1
  • 22
    • 0025277170 scopus 로고
    • Flow cytometry resonance energy transfer suggests an association between low-affinity interleukin 2 binding sites and HLA class I molecules
    • Harel-Bellan A., et al. Flow cytometry resonance energy transfer suggests an association between low-affinity interleukin 2 binding sites and HLA class I molecules. Biochem. J. 268 (1990) 35-40
    • (1990) Biochem. J. , vol.268 , pp. 35-40
    • Harel-Bellan, A.1
  • 23
    • 0021947668 scopus 로고
    • Compound receptors in the cell membrane: ruminations from the borderland of immunology and physiology
    • Simonsen M., et al. Compound receptors in the cell membrane: ruminations from the borderland of immunology and physiology. Prog. Allergy 36 (1985) 151-176
    • (1985) Prog. Allergy , vol.36 , pp. 151-176
    • Simonsen, M.1
  • 24
    • 0023948787 scopus 로고
    • Function by association? MHC antigens and membrane receptor complexes
    • Edidin M. Function by association? MHC antigens and membrane receptor complexes. Immunol. Today 9 (1988) 218-219
    • (1988) Immunol. Today , vol.9 , pp. 218-219
    • Edidin, M.1
  • 25
    • 0030700848 scopus 로고    scopus 로고
    • Interaction of class I human leukocyte antigen (HLA-I) molecules with insulin receptors and its effect on the insulin-signaling cascade
    • Ramalingam T.S., et al. Interaction of class I human leukocyte antigen (HLA-I) molecules with insulin receptors and its effect on the insulin-signaling cascade. Mol. Biol. Cell 8 (1997) 2463-2474
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2463-2474
    • Ramalingam, T.S.1
  • 26
    • 33847165409 scopus 로고    scopus 로고
    • The impact of environmental signals in the growth and survival of human T cells
    • Damjanovich S. (Ed), Springer Verlag
    • Arosa F.A., et al. The impact of environmental signals in the growth and survival of human T cells. In: Damjanovich S. (Ed). Biophysical Aspects of Transmembrane Signaling Vol. 8 (2005), Springer Verlag 1-32
    • (2005) Biophysical Aspects of Transmembrane Signaling , vol.8 , pp. 1-32
    • Arosa, F.A.1
  • 27
    • 0023680256 scopus 로고
    • Evidence for specific association between class I major histocompatibility antigens and the CD8 molecules of human suppressor/cytotoxic cells
    • Blue M.L., et al. Evidence for specific association between class I major histocompatibility antigens and the CD8 molecules of human suppressor/cytotoxic cells. Cell 54 (1988) 413-421
    • (1988) Cell , vol.54 , pp. 413-421
    • Blue, M.L.1
  • 28
    • 0344833815 scopus 로고
    • Physical association between the CD8 and HLA class I molecules on the surface of activated human T lymphocytes
    • Bushkin Y., et al. Physical association between the CD8 and HLA class I molecules on the surface of activated human T lymphocytes. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 3985-3989
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 3985-3989
    • Bushkin, Y.1
  • 29
    • 0025899488 scopus 로고
    • Biochemical and functional association between CD8 and H-2 at the surface of a T cell clone
    • Auphan N., et al. Biochemical and functional association between CD8 and H-2 at the surface of a T cell clone. Mol. Immunol. 28 (1991) 827-837
    • (1991) Mol. Immunol. , vol.28 , pp. 827-837
    • Auphan, N.1
  • 30
    • 0032520789 scopus 로고    scopus 로고
    • d to CD8: interaction with the amino terminus of a mature cell surface protein
    • d to CD8: interaction with the amino terminus of a mature cell surface protein. J. Immunol. 160 (1998) 2809-2814
    • (1998) J. Immunol. , vol.160 , pp. 2809-2814
    • Jelonek, M.T.1
  • 32
    • 5044232231 scopus 로고    scopus 로고
    • Conformational flexibility of the MHC class I α1-α2 domain in peptide bound and free states: a molecular dynamics simulation study
    • Zacharias M., and Springer S. Conformational flexibility of the MHC class I α1-α2 domain in peptide bound and free states: a molecular dynamics simulation study. Biophys. J. 87 (2004) 2203-2214
    • (2004) Biophys. J. , vol.87 , pp. 2203-2214
    • Zacharias, M.1    Springer, S.2
  • 33
    • 0034610781 scopus 로고    scopus 로고
    • Crystal structure of the hereditary hemochromatosis protein HFE complexed with transferrin receptor
    • Bennett M.J., et al. Crystal structure of the hereditary hemochromatosis protein HFE complexed with transferrin receptor. Nature 403 (2000) 46-53
    • (2000) Nature , vol.403 , pp. 46-53
    • Bennett, M.J.1
  • 34
    • 24044466482 scopus 로고    scopus 로고
    • Structure of a pheromone receptor-associated MHC molecule with an open and empty groove
    • 10.1371/journal.pbio.0030257
    • Olson R., et al. Structure of a pheromone receptor-associated MHC molecule with an open and empty groove. PLoS Biol. 3 (2005) e257. http://biology.plosjournals.org 10.1371/journal.pbio.0030257
    • (2005) PLoS Biol. , vol.3
    • Olson, R.1
  • 35
    • 0033020518 scopus 로고    scopus 로고
    • The transferrin receptor binding site on HFE, the class I MHC-related protein mutated in hereditary hemochromatosis
    • Lebrón J.A., and Bjorkman P.J. The transferrin receptor binding site on HFE, the class I MHC-related protein mutated in hereditary hemochromatosis. J. Mol. Biol. 289 (1999) 1109-1118
    • (1999) J. Mol. Biol. , vol.289 , pp. 1109-1118
    • Lebrón, J.A.1    Bjorkman, P.J.2
  • 36
    • 33745190019 scopus 로고    scopus 로고
    • MHC homologs in the nervous system - they haven't lost their groove
    • Olson R., et al. MHC homologs in the nervous system - they haven't lost their groove. Curr. Opin. Neurobiol. 16 (2005) 351-357
    • (2005) Curr. Opin. Neurobiol. , vol.16 , pp. 351-357
    • Olson, R.1
  • 37
    • 1942540796 scopus 로고    scopus 로고
    • Supine orientation of a murine MHC class I molecule on the membrane bilayer
    • Mitra A.K., et al. Supine orientation of a murine MHC class I molecule on the membrane bilayer. Curr. Biol. 14 (2004) 718-724
    • (2004) Curr. Biol. , vol.14 , pp. 718-724
    • Mitra, A.K.1
  • 38
    • 24744437984 scopus 로고    scopus 로고
    • 2-microglobulin on functional recognition of H-2Kb by the NK cell inhibitory receptor Ly49C
    • 2-microglobulin on functional recognition of H-2Kb by the NK cell inhibitory receptor Ly49C. J. Immunol. 175 (2005) 3542-3553
    • (2005) J. Immunol. , vol.175 , pp. 3542-3553
    • Benoit, L.A.1
  • 39
    • 26844481034 scopus 로고    scopus 로고
    • 2-microglobulin-free HLA-G molecules
    • 2-microglobulin-free HLA-G molecules. J. Immunol. 175 (2005) 4866-4874
    • (2005) J. Immunol. , vol.175 , pp. 4866-4874
    • Gonen-Gross, T.1
  • 40
    • 0027219916 scopus 로고
    • In vivo dimeric association of class I MHC heavy chains. Possible relationship to class I MHC heavy chain-beta 2-microglobulin dissociation
    • Capps G.G., et al. In vivo dimeric association of class I MHC heavy chains. Possible relationship to class I MHC heavy chain-beta 2-microglobulin dissociation. J. Immunol. 151 (1993) 159-169
    • (1993) J. Immunol. , vol.151 , pp. 159-169
    • Capps, G.G.1
  • 41
    • 0026670158 scopus 로고
    • Self-association of class I major histocompatibility complex molecules in liposome and cell surface membranes
    • Chakrabarti A., et al. Self-association of class I major histocompatibility complex molecules in liposome and cell surface membranes. Biochemistry 31 (1991) 7182-7189
    • (1991) Biochemistry , vol.31 , pp. 7182-7189
    • Chakrabarti, A.1
  • 42
    • 0028181870 scopus 로고
    • Clustering of class I HLA molecules on the surfaces of activated and transformed human cells
    • Matko J., et al. Clustering of class I HLA molecules on the surfaces of activated and transformed human cells. J. Immunol. 152 (1994) 3353-3360
    • (1994) J. Immunol. , vol.152 , pp. 3353-3360
    • Matko, J.1
  • 43
    • 12644304905 scopus 로고    scopus 로고
    • HLA class I and II antigens are partially co-clustered in the plasma membrane of human lymphoblastoid cells
    • Jenei A., et al. HLA class I and II antigens are partially co-clustered in the plasma membrane of human lymphoblastoid cells. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 7269-7274
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 7269-7274
    • Jenei, A.1
  • 44
    • 0034040718 scopus 로고    scopus 로고
    • Human major histocompatibility molecules have the intrinsic ability to form homotypic associations
    • Triantafilou K., et al. Human major histocompatibility molecules have the intrinsic ability to form homotypic associations. Hum. Immunol. 61 (2000) 585-598
    • (2000) Hum. Immunol. , vol.61 , pp. 585-598
    • Triantafilou, K.1
  • 45
    • 0037189545 scopus 로고    scopus 로고
    • HLA-B27 misfolding is associated with aberrant intermolecular disulfide bond formation (dimerization) in the endoplasmic reticulum
    • Dangoria N.S., et al. HLA-B27 misfolding is associated with aberrant intermolecular disulfide bond formation (dimerization) in the endoplasmic reticulum. J. Biol. Chem. 277 (2002) 23459-23468
    • (2002) J. Biol. Chem. , vol.277 , pp. 23459-23468
    • Dangoria, N.S.1
  • 46
    • 0037058924 scopus 로고    scopus 로고
    • Disulfide bond-mediated dimerization of HLA-G on the cell surface
    • Boyson J.E., et al. Disulfide bond-mediated dimerization of HLA-G on the cell surface. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 16180-16185
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16180-16185
    • Boyson, J.E.1
  • 47
    • 0037352755 scopus 로고    scopus 로고
    • Lymphoblastoid cells express HLA-B27 homodimers both intracellularly and at the cell surface following endosomal recycling
    • Bird L.A., et al. Lymphoblastoid cells express HLA-B27 homodimers both intracellularly and at the cell surface following endosomal recycling. Eur. J. Immunol. 33 (2003) 748-759
    • (2003) Eur. J. Immunol. , vol.33 , pp. 748-759
    • Bird, L.A.1
  • 48
    • 1542305542 scopus 로고    scopus 로고
    • Formation of HLA-B27 homodimers and their relationship to assembly kinetics
    • Antoniou A.N., et al. Formation of HLA-B27 homodimers and their relationship to assembly kinetics. J. Biol. Chem. 279 (2004) 8895-8902
    • (2004) J. Biol. Chem. , vol.279 , pp. 8895-8902
    • Antoniou, A.N.1
  • 49
    • 0037339447 scopus 로고    scopus 로고
    • 2-microglobulin: implications in activation of cytotoxic T lymphocytes
    • 2-microglobulin: implications in activation of cytotoxic T lymphocytes. Int. Immunol. 15 (2003) 331-339
    • (2003) Int. Immunol. , vol.15 , pp. 331-339
    • Bodnár, A.1
  • 50
    • 0028343150 scopus 로고
    • Exogenous peptide ligand influences the expression and half-life of free HLA class I heavy chains ubiquitously detected at the cell surface
    • Carreno B.M., and Hansen T.H. Exogenous peptide ligand influences the expression and half-life of free HLA class I heavy chains ubiquitously detected at the cell surface. Eur. J. Immunol. 24 (1994) 1285-1292
    • (1994) Eur. J. Immunol. , vol.24 , pp. 1285-1292
    • Carreno, B.M.1    Hansen, T.H.2
  • 51
    • 0030997739 scopus 로고    scopus 로고
    • Probing the stability of class I major histocompatibility complex (MHC) molecules on the surface of human cells
    • Edidin M., et al. Probing the stability of class I major histocompatibility complex (MHC) molecules on the surface of human cells. Immunogenetics 46 (1997) 41-45
    • (1997) Immunogenetics , vol.46 , pp. 41-45
    • Edidin, M.1
  • 52
    • 0029933768 scopus 로고    scopus 로고
    • 2-microglobulin-free HLA class I α-chains on activated T cells requires internalization of HLA class I heterodimers
    • 2-microglobulin-free HLA class I α-chains on activated T cells requires internalization of HLA class I heterodimers. Immunology 88 (1996) 104-109
    • (1996) Immunology , vol.88 , pp. 104-109
    • Pickl, W.F.1
  • 53
    • 33644504500 scopus 로고    scopus 로고
    • Lack of tyrosine 320 impairs spontaneous endocytosis and enhances release of HLA-B27 molecules
    • Santos S.G., et al. Lack of tyrosine 320 impairs spontaneous endocytosis and enhances release of HLA-B27 molecules. J. Immunol. 176 (2006) 2942-2949
    • (2006) J. Immunol. , vol.176 , pp. 2942-2949
    • Santos, S.G.1
  • 54
    • 0027302856 scopus 로고
    • 2-microglobulin free HLA class I α-chains. Qualitative and quantitative characterization
    • 2-microglobulin free HLA class I α-chains. Qualitative and quantitative characterization. J. Immunol. 151 (1993) 2613-2622
    • (1993) J. Immunol. , vol.151 , pp. 2613-2622
    • Pickl, W.F.1
  • 55
    • 0042209905 scopus 로고    scopus 로고
    • Soluble nonclassical HLA generated by the metalloproteinase pathway
    • Dong Y., et al. Soluble nonclassical HLA generated by the metalloproteinase pathway. Hum. Immunol. 64 (2003) 802-810
    • (2003) Hum. Immunol. , vol.64 , pp. 802-810
    • Dong, Y.1
  • 56
    • 26244453677 scopus 로고    scopus 로고
    • Cyclosporin A regulates human NK cell apoptosis induced by soluble HLA-I or by target cells
    • Poggi A., and Zocchi M.R. Cyclosporin A regulates human NK cell apoptosis induced by soluble HLA-I or by target cells. Autoimmun. Rev. 4 (2005) 532-536
    • (2005) Autoimmun. Rev. , vol.4 , pp. 532-536
    • Poggi, A.1    Zocchi, M.R.2
  • 57
    • 0023187205 scopus 로고
    • Major histocompatibility complex class I molecules internalized via coated pits in T lymphocytes
    • Machy P., et al. Major histocompatibility complex class I molecules internalized via coated pits in T lymphocytes. Nature 328 (1987) 724-726
    • (1987) Nature , vol.328 , pp. 724-726
    • Machy, P.1
  • 58
    • 0023761567 scopus 로고
    • Receptor-like nature of class I HLA: endocytosis via coated pits
    • Dasgupta, et al. Receptor-like nature of class I HLA: endocytosis via coated pits. J. Immunol. 141 (1988) 2577-2580
    • (1988) J. Immunol. , vol.141 , pp. 2577-2580
    • Dasgupta1
  • 59
    • 0025828481 scopus 로고
    • 2-microglobulin
    • 2-microglobulin. J. Immunol. 146 (1991) 1862-1867
    • (1991) J. Immunol. , vol.146 , pp. 1862-1867
    • Hochman, J.H.1
  • 60
    • 1842284757 scopus 로고    scopus 로고
    • Constitutive endocytosis of HLA class I antigens requires a specific portion of the intracytoplasmic tail that shares structural features with other endocytosed molecules
    • Vega M.A., and Strominger J.L. Constitutive endocytosis of HLA class I antigens requires a specific portion of the intracytoplasmic tail that shares structural features with other endocytosed molecules. Proc. Natl. Acad. Sci. U. S. A. 86 (1998) 2688-2692
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 2688-2692
    • Vega, M.A.1    Strominger, J.L.2
  • 61
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino J.S., and Traub L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72 (2003) 395-447
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 62
    • 14644390830 scopus 로고    scopus 로고
    • Tails of wonder: endocytic-sorting motifs key for exogenous antigen presentation
    • Lizee G., et al. Tails of wonder: endocytic-sorting motifs key for exogenous antigen presentation. Trends Immunol. 26 (2005) 141-149
    • (2005) Trends Immunol. , vol.26 , pp. 141-149
    • Lizee, G.1
  • 63
    • 0037236457 scopus 로고    scopus 로고
    • The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: 'parasites' of the endocytosis pathway
    • Benichou S., and Benmerah A. The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: 'parasites' of the endocytosis pathway. Med. Sci. (Paris) 19 (2003) 100-106
    • (2003) Med. Sci. (Paris) , vol.19 , pp. 100-106
    • Benichou, S.1    Benmerah, A.2
  • 64
    • 0027197418 scopus 로고
    • 2-microglobulin-associated, and a free, nonphosphorylated, chain of MHC class I
    • 2-microglobulin-associated, and a free, nonphosphorylated, chain of MHC class I. J. Immunol. 151 (1993) 211-224
    • (1993) J. Immunol. , vol.151 , pp. 211-224
    • Thor, G.1
  • 65
    • 0028989586 scopus 로고
    • 2-microglobulin from HLA class I heavy chains correlates with acquisition of epitopes in the cytoplasmic tail
    • 2-microglobulin from HLA class I heavy chains correlates with acquisition of epitopes in the cytoplasmic tail. J. Immunol. 154 (1995) 5205-5215
    • (1995) J. Immunol. , vol.154 , pp. 5205-5215
    • Little, A.M.1
  • 66
    • 0028206917 scopus 로고
    • T cell activation results in physical modification of the mouse CD8 beta chain
    • Casabo L.G., et al. T cell activation results in physical modification of the mouse CD8 beta chain. J. Immunol. 152 (1994) 397-404
    • (1994) J. Immunol. , vol.152 , pp. 397-404
    • Casabo, L.G.1
  • 67
    • 0035890470 scopus 로고    scopus 로고
    • Hormone-triggered conformational changes within the insulin-receptor ectodomain: requirement for transmembrane anchors
    • Florke R.R., et al. Hormone-triggered conformational changes within the insulin-receptor ectodomain: requirement for transmembrane anchors. Biochem. J. 360 (2001) 189-198
    • (2001) Biochem. J. , vol.360 , pp. 189-198
    • Florke, R.R.1
  • 68
    • 0028937776 scopus 로고
    • Distinct association of transferrin receptor with HLA class I molecules on HUT-102B and JY cells
    • Matyus L., et al. Distinct association of transferrin receptor with HLA class I molecules on HUT-102B and JY cells. Immunol. Lett. 44 (1995) 203-208
    • (1995) Immunol. Lett. , vol.44 , pp. 203-208
    • Matyus, L.1
  • 69
    • 3342924000 scopus 로고    scopus 로고
    • IL-2 and IL-15 receptor α-subunits are co-expressed in a supramolecular receptor cluster in lipid rafts of T cells
    • Vamosi G., et al. IL-2 and IL-15 receptor α-subunits are co-expressed in a supramolecular receptor cluster in lipid rafts of T cells. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 11082-11087
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 11082-11087
    • Vamosi, G.1
  • 70
    • 0017113838 scopus 로고
    • Interaction of HLA molecules with non-immunological ligands as an explanation of HLA and disease associations
    • Svejgaard A., and Ryder L.P. Interaction of HLA molecules with non-immunological ligands as an explanation of HLA and disease associations. Lancet 2 (1976) 547-549
    • (1976) Lancet , vol.2 , pp. 547-549
    • Svejgaard, A.1    Ryder, L.P.2
  • 71
    • 0025339432 scopus 로고
    • Regulation of insulin receptor functions by a peptide derived from a major histocompatibility complex class I antigen
    • Stagsted J., et al. Regulation of insulin receptor functions by a peptide derived from a major histocompatibility complex class I antigen. Cell 62 (1990) 297-307
    • (1990) Cell , vol.62 , pp. 297-307
    • Stagsted, J.1
  • 72
    • 0031987167 scopus 로고    scopus 로고
    • Journey beyond immunology. Regulation of receptor internalization by major histocompatibility complex class I (MHC-I) and effect of peptides derived from MHC-I
    • Stagsted J. Journey beyond immunology. Regulation of receptor internalization by major histocompatibility complex class I (MHC-I) and effect of peptides derived from MHC-I. APMIS Suppl. 85 (1998) 1-40
    • (1998) APMIS Suppl. , vol.85 , pp. 1-40
    • Stagsted, J.1
  • 73
    • 0032750029 scopus 로고    scopus 로고
    • Signal transduction by the major histocompatibility complex class I molecule
    • Pedersen A.E., et al. Signal transduction by the major histocompatibility complex class I molecule. APMIS Suppl. 107 (1999) 887-895
    • (1999) APMIS Suppl. , vol.107 , pp. 887-895
    • Pedersen, A.E.1
  • 74
    • 1542287259 scopus 로고    scopus 로고
    • Cis association of Ly49A with MHC class I restricts natural killer cell inhibition
    • Doucey M.A., et al. Cis association of Ly49A with MHC class I restricts natural killer cell inhibition. Nat. Immunol. 5 (2004) 328-336
    • (2004) Nat. Immunol. , vol.5 , pp. 328-336
    • Doucey, M.A.1
  • 75
    • 33646551477 scopus 로고    scopus 로고
    • The SHP-1 protein tyrosine phosphatase negatively modulates glucose homeostasis
    • Dubois M.J., et al. The SHP-1 protein tyrosine phosphatase negatively modulates glucose homeostasis. Nat. Med. 12 (2006) 549-556
    • (2006) Nat. Med. , vol.12 , pp. 549-556
    • Dubois, M.J.1
  • 76
    • 0036675186 scopus 로고    scopus 로고
    • Regulation of insulin action by CEACAM1
    • Najjar S.M. Regulation of insulin action by CEACAM1. Trends Endocrinol. Metab. 13 (2002) 240-245
    • (2002) Trends Endocrinol. Metab. , vol.13 , pp. 240-245
    • Najjar, S.M.1
  • 77
    • 26444529548 scopus 로고    scopus 로고
    • The involvement of NK cells in ankylosing spondylitis
    • Azuz-Lieberman, et al. The involvement of NK cells in ankylosing spondylitis. Int. Immunol. 17 (2005) 837-845
    • (2005) Int. Immunol. , vol.17 , pp. 837-845
    • Azuz-Lieberman1
  • 78
    • 3042627644 scopus 로고    scopus 로고
    • Non-immune functions of MHC class I glycoproteins in normal and malignant cells
    • Fishman D., et al. Non-immune functions of MHC class I glycoproteins in normal and malignant cells. (Folia Biol.) Praha 50 (2004) 35-42
    • (2004) (Folia Biol.) Praha , vol.50 , pp. 35-42
    • Fishman, D.1
  • 79
    • 33644663445 scopus 로고    scopus 로고
    • The role of supramolecular protein complexes and membrane potential in transmembrane signaling processes of lymphocytes
    • Vamosi G., et al. The role of supramolecular protein complexes and membrane potential in transmembrane signaling processes of lymphocytes. Immunol. Lett. 104 (2006) 53-58
    • (2006) Immunol. Lett. , vol.104 , pp. 53-58
    • Vamosi, G.1
  • 80
    • 33646885101 scopus 로고    scopus 로고
    • Clustering class I MHC modulates sensitivity of T cell recognition
    • Fooksman D.R., et al. Clustering class I MHC modulates sensitivity of T cell recognition. J. Immunol. 176 (2006) 6673-6680
    • (2006) J. Immunol. , vol.176 , pp. 6673-6680
    • Fooksman, D.R.1
  • 81
    • 33744524670 scopus 로고    scopus 로고
    • Efficient leukocyte Ig-like receptor signaling and crystal structure of disulfide-linked HLA-G dimers
    • Shiroishi M., et al. Efficient leukocyte Ig-like receptor signaling and crystal structure of disulfide-linked HLA-G dimers. J. Biol. Chem. 281 (2006) 10439-10447
    • (2006) J. Biol. Chem. , vol.281 , pp. 10439-10447
    • Shiroishi, M.1
  • 82
    • 1442326724 scopus 로고    scopus 로고
    • Recognition of classical and heavy chain forms of HLA-B27 by leukocyte receptors
    • Allen R.L., and Trowsdale J. Recognition of classical and heavy chain forms of HLA-B27 by leukocyte receptors. Curr. Mol. Med. 4 (2004) 59-65
    • (2004) Curr. Mol. Med. , vol.4 , pp. 59-65
    • Allen, R.L.1    Trowsdale, J.2
  • 83
    • 18744401630 scopus 로고    scopus 로고
    • MHC-I recognition by receptors on myelomonocytic cells: new tricks for old dogs?
    • Raine T., and Allen R. MHC-I recognition by receptors on myelomonocytic cells: new tricks for old dogs?. Bioessays 27 (2005) 542-550
    • (2005) Bioessays , vol.27 , pp. 542-550
    • Raine, T.1    Allen, R.2
  • 85
    • 1442351145 scopus 로고    scopus 로고
    • The immunobiology of HLA-B27: variations on a theme
    • Colbert R.A. The immunobiology of HLA-B27: variations on a theme. Curr. Mol. Med. 4 (2004) 21-30
    • (2004) Curr. Mol. Med. , vol.4 , pp. 21-30
    • Colbert, R.A.1
  • 86
    • 0036903889 scopus 로고    scopus 로고
    • Increased level of HLA-B27 expression in ankylosing spondylitis patients compared with healthy HLA-B27-positive subjects: a possible further susceptibility factor for the development of disease
    • Cauli A., et al. Increased level of HLA-B27 expression in ankylosing spondylitis patients compared with healthy HLA-B27-positive subjects: a possible further susceptibility factor for the development of disease. Rheumatology 41 (2002) 1375-1379
    • (2002) Rheumatology , vol.41 , pp. 1375-1379
    • Cauli, A.1
  • 87
    • 33750201148 scopus 로고    scopus 로고
    • Consistent patterns of expression of HLA class I free heavy chains in healthy individuals and raised expression in spondyloarthropathy patients point to physiological and pathological roles
    • Raine T., et al. Consistent patterns of expression of HLA class I free heavy chains in healthy individuals and raised expression in spondyloarthropathy patients point to physiological and pathological roles. Rheumatology 45 (2006) 1338-1344
    • (2006) Rheumatology , vol.45 , pp. 1338-1344
    • Raine, T.1
  • 88
    • 0024043855 scopus 로고
    • Molecular and biological interaction between major histocompatibility complex class I antigens and luteinizing hormone receptors or β-adrenergic receptors triggers cellular response in mice
    • Solano A.R., et al. Molecular and biological interaction between major histocompatibility complex class I antigens and luteinizing hormone receptors or β-adrenergic receptors triggers cellular response in mice. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 5087-5091
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 5087-5091
    • Solano, A.R.1
  • 89
    • 0025994306 scopus 로고
    • The action of luteinizing hormone on the testis
    • Neuman, et al. The action of luteinizing hormone on the testis. J. Steroid Biochem. Mol. Biol. 40 (1991) 441-451
    • (1991) J. Steroid Biochem. Mol. Biol. , vol.40 , pp. 441-451
    • Neuman1
  • 90
    • 0021234846 scopus 로고
    • 2-microglobulin chain of HLA complex
    • 2-microglobulin chain of HLA complex. Science 224 (1984) 509-511
    • (1984) Science , vol.224 , pp. 509-511
    • Curry, R.A.1
  • 91
    • 1842363252 scopus 로고
    • HLA class I molecules are associated with CD1a heavy chains on normal human thymus cells
    • Amiot M., et al. HLA class I molecules are associated with CD1a heavy chains on normal human thymus cells. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 4451-4454
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 4451-4454
    • Amiot, M.1
  • 92
    • 0022543626 scopus 로고
    • A new HLA-linked T cell membrane molecule, related to the beta chain of the clonotypic receptor, is associated with T3
    • Bushkin Y., et al. A new HLA-linked T cell membrane molecule, related to the beta chain of the clonotypic receptor, is associated with T3. J. Exp. Med. 164 (1986) 458-473
    • (1986) J. Exp. Med. , vol.164 , pp. 458-473
    • Bushkin, Y.1
  • 93
    • 0028101424 scopus 로고
    • Lateral organization of the ICAM-1 molecule at the surface of human lymphoblasts: a possible model for its co-distribution with the IL-2 receptor, class I and class II HLA molecules
    • Bene L., et al. Lateral organization of the ICAM-1 molecule at the surface of human lymphoblasts: a possible model for its co-distribution with the IL-2 receptor, class I and class II HLA molecules. Eur. J. Immunol. 24 (1994) 2115-2123
    • (1994) Eur. J. Immunol. , vol.24 , pp. 2115-2123
    • Bene, L.1
  • 94
    • 6044239560 scopus 로고    scopus 로고
    • Membrane topography of HLA I, HLA II, and ICAM-1 is affected by IFN-γ in lipid rafts of uveal melanomas
    • Bene L., et al. Membrane topography of HLA I, HLA II, and ICAM-1 is affected by IFN-γ in lipid rafts of uveal melanomas. Biochem. Biophys. Res. Commun. 322 (2004) 678-683
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 678-683
    • Bene, L.1
  • 96
    • 0033554898 scopus 로고    scopus 로고
    • sα-MHC I complexes after desensitization of human platelets with iloprost
    • sα-MHC I complexes after desensitization of human platelets with iloprost. Eur. J. Biochem. 259 (1999) 167-174
    • (1999) Eur. J. Biochem. , vol.259 , pp. 167-174
    • Ferreira, P.1
  • 97
    • 0022635340 scopus 로고
    • The interaction between gamma-type endorphins and HLA class I antigens
    • Claas F.H., et al. The interaction between gamma-type endorphins and HLA class I antigens. Hum. Immunol. 15 (1986) 347-356
    • (1986) Hum. Immunol. , vol.15 , pp. 347-356
    • Claas, F.H.1
  • 98
    • 0025910784 scopus 로고
    • Internalization of MHC class I molecules is a prerequisite for endocytosis of endorphin by lymphocytes
    • Mommaas A.M., et al. Internalization of MHC class I molecules is a prerequisite for endocytosis of endorphin by lymphocytes. Clin. Exp. Immunol. 84 (1991) 170-174
    • (1991) Clin. Exp. Immunol. , vol.84 , pp. 170-174
    • Mommaas, A.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.