메뉴 건너뛰기




Volumn 20, Issue 2, 1999, Pages 195-205

HLA-DM and the MHC class II antigen presentation pathway

Author keywords

Antigen presentation; Antigen processing; HLA DM; Invariant chain; Major histocompatibility complex; T lymphocytes

Indexed keywords

CD4 ANTIGEN; HLA DM ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MEMBRANE PROTEIN; PEPTIDE; PROTEIN;

EID: 0033506678     PISSN: 0257277X     EISSN: None     Source Type: Journal    
DOI: 10.1007/bf02790403     Document Type: Review
Times cited : (44)

References (67)
  • 1
    • 0022894853 scopus 로고
    • Isolation and characterization of antigen-Ia complexes involved in T cell recognition
    • 1 Buus S, Sette A, Colon SM, Jenis DM, Grey HM: Isolation and characterization of antigen-Ia complexes involved in T cell recognition. Cell 1986;47:1071-1077.
    • (1986) Cell , vol.47 , pp. 1071-1077
    • Buus, S.1    Sette, A.2    Colon, S.M.3    Jenis, D.M.4    Grey, H.M.5
  • 2
    • 0021968677 scopus 로고
    • Binding of immunogenic peptides to Ia histocompatibility molecules
    • 2 Babbitt BP, Allen PM, Matsueda, G, Haber E, Unanue ER: Binding of immunogenic peptides to Ia histocompatibility molecules. Nature 1985;317:359-361.
    • (1985) Nature , vol.317 , pp. 359-361
    • Babbitt, B.P.1    Allen, P.M.2    Matsueda, G.3    Haber, E.4    Unanue, E.R.5
  • 4
    • 0025313181 scopus 로고
    • Regulation of antigen presentation by acidic pH
    • 4 Jensen PE: Regulation of antigen presentation by acidic pH. J Exp Med 1990;171:1779-1789.
    • (1990) J Exp Med , vol.171 , pp. 1779-1789
    • Jensen, P.E.1
  • 5
    • 0025998830 scopus 로고
    • Enhanced binding of peptide antigen to purified class II major histocompatibility glycoproteins at acidic pH
    • 5 Jensen PE: Enhanced binding of peptide antigen to purified class II major histocompatibility glycoproteins at acidic pH. J Exp Med 1991;174:1111-1120.
    • (1991) J Exp Med , vol.174 , pp. 1111-1120
    • Jensen, P.E.1
  • 6
    • 0026671228 scopus 로고
    • Long-lived complexes between peptide and class II MHC are formed at low pH with no requirement for pH neutralization
    • 6 Jensen PE: Long-lived complexes between peptide and class II MHC are formed at low pH with no requirement for pH neutralization. J Exp Med 1992;176:793-798.
    • (1992) J Exp Med , vol.176 , pp. 793-798
    • Jensen, P.E.1
  • 7
    • 0027155945 scopus 로고
    • Acidification and disulfide reduction can be sufficient to allow intact proteins to bind class II MHC
    • 7 Jensen PE: Acidification and disulfide reduction can be sufficient to allow intact proteins to bind class II MHC. J Immunol 1993; 150:3347-3356.
    • (1993) J Immunol , vol.150 , pp. 3347-3356
    • Jensen, P.E.1
  • 9
    • 0025870669 scopus 로고
    • A role for peptide in determining MHC class II structure
    • 9 Sadegh-Nasseri S, Germain RN: A role for peptide in determining MHC class II structure. Nature 1991;353:167-170.
    • (1991) Nature , vol.353 , pp. 167-170
    • Sadegh-Nasseri, S.1    Germain, R.N.2
  • 10
    • 0030030896 scopus 로고    scopus 로고
    • Evidence for a conformational change in a class II MHC molecule occurring in the same pH range that enhances antigen binding
    • 10 Boniface JJ, Lyons DS, Wettstein DA, Allbritton NL, Davis MM: Evidence for a conformational change in a class II MHC molecule occurring in the same pH range that enhances antigen binding. J Exp MEd 1996;183:119-126.
    • (1996) J Exp MEd , vol.183 , pp. 119-126
    • Boniface, J.J.1    Lyons, D.S.2    Wettstein, D.A.3    Allbritton, N.L.4    Davis, M.M.5
  • 11
    • 0030068236 scopus 로고    scopus 로고
    • A structural transition in class II MHC proteins at mildly acidic pH
    • 11 Runnels HA, Moore JC, Jensen PE: A structural transition in class II MHC proteins at mildly acidic pH. J Exp Med 1996;183:127-136.
    • (1996) J Exp Med , vol.183 , pp. 127-136
    • Runnels, H.A.1    Moore, J.C.2    Jensen, P.E.3
  • 12
    • 0025826118 scopus 로고
    • MHC class II structure, occupancy and surface expression determined by post-endoplasmic reticulum antigen binding
    • 12 Germain RN, Hendrix LR: MHC class II structure, occupancy and surface expression determined by post-endoplasmic reticulum antigen binding. Nature 1991;353: 134-139.
    • (1991) Nature , vol.353 , pp. 134-139
    • Germain, R.N.1    Hendrix, L.R.2
  • 13
    • 0024346257 scopus 로고
    • Stable assocuation of processed antigen with antigen-presenting cell membranes
    • 13 Jensen PE: Stable assocuation of processed antigen with antigen-presenting cell membranes. J Immunol 1989;143:420-425.
    • (1989) J Immunol , vol.143 , pp. 420-425
    • Jensen, P.E.1
  • 14
    • 0026505030 scopus 로고
    • Irreversible association of peptides with class II MHC molecules in living cells
    • 14 Lanzavecchia A, Reid PA, Watts C: Irreversible association of peptides with class II MHC molecules in living cells. Nature 1992;357: 249-252.
    • (1992) Nature , vol.357 , pp. 249-252
    • Lanzavecchia, A.1    Reid, P.A.2    Watts, C.3
  • 15
    • 0026571278 scopus 로고
    • The human class II MHC protein HLA-DR1 assembles as empty αβ heterodimers in the absence of antigenic peptide
    • 15 Stern LJ, Wiley DC: The Human Class II MHC Protein HLA-DR1 Assembles as Empty αβ Heterodimers in the Absence of Antigenic Peptide. Cell 1992;68: 465-477.
    • (1992) Cell , vol.68 , pp. 465-477
    • Stern, L.J.1    Wiley, D.C.2
  • 16
    • 0026643116 scopus 로고
    • pH dependence and exchange of high and low responder peptides binding to a class II MHC molecule
    • 16 Reay PA, Wettstein DA, Davis MM: pH dependence and exchange of high and low responder peptides binding to a class II MHC molecule. EMBO J 1992;11:2829-2839.
    • (1992) EMBO J , vol.11 , pp. 2829-2839
    • Reay, P.A.1    Wettstein, D.A.2    Davis, M.M.3
  • 17
    • 0029084023 scopus 로고
    • DM enhances peptide binding to class II MHC by release of invariant chain-derived peptide
    • 17 Sherman MA, Weber DA, Jensen PE: DM enhances peptide binding to class II MHC by release of invariant chain-derived peptide. Immunity 1995;3:197-205.
    • (1995) Immunity , vol.3 , pp. 197-205
    • Sherman, M.A.1    Weber, D.A.2    Jensen, P.E.3
  • 18
    • 0025056497 scopus 로고
    • Defective processing and presentation of exogenous antigens in mutants with normal HLA class II genes
    • 18 Mellins E, Smith L, Arp B, Cotner T, Celis E, Pious D: Defective processing and presentation of exogenous antigens in mutants with normal HLA class II genes. Nature 1990;343:71-74.
    • (1990) Nature , vol.343 , pp. 71-74
    • Mellins, E.1    Smith, L.2    Arp, B.3    Cotner, T.4    Celis, E.5    Pious, D.6
  • 19
    • 0025838717 scopus 로고
    • A gene required for class II-restricted antigen presentation maps to the major histocompatibility complex
    • 19 Mellins E, Kempin S, Smith L, Monji T, Pious D: A gene required for class II-restricted antigen presentation maps to the major histocompatibility complex. J Exp Med 1991;174:1607-1615.
    • (1991) J Exp Med , vol.174 , pp. 1607-1615
    • Mellins, E.1    Kempin, S.2    Smith, L.3    Monji, T.4    Pious, D.5
  • 20
    • 0026440236 scopus 로고
    • HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides
    • 20 Riberdy JM, Newcomb JR, Surman MJ, Barbosa JA, Cresswell P: HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides. Nature 1992;360:474-477.
    • (1992) Nature , vol.360 , pp. 474-477
    • Riberdy, J.M.1    Newcomb, J.R.2    Surman, M.J.3    Barbosa, J.A.4    Cresswell, P.5
  • 21
    • 0027095930 scopus 로고
    • Invariant chain peptides in most HLA-DR molecules of anantigen-processing mutant
    • 21 Sette A, Ceman S, Kubo RT, Sakaguchi K, Appella E, Hunt DF, et al.: Invariant chain peptides in most HLA-DR molecules of anantigen-processing mutant. Science 1992;258:1801-1804.
    • (1992) Science , vol.258 , pp. 1801-1804
    • Sette, A.1    Ceman, S.2    Kubo, R.T.3    Sakaguchi, K.4    Appella, E.5    Hunt, D.F.6
  • 22
    • 0028217255 scopus 로고
    • HLA-DMA and DMB genes are both required for MHC class II/peptide complex formation in antigen-presenting cells
    • 22 Fling Sp, Arp B, Pious: HLA-DMA and DMB genes are both required for MHC class II/peptide complex formation in antigen-presenting cells. Nature 1994; 368:554-558.
    • (1994) Nature , vol.368 , pp. 554-558
    • Fling, S.1    Arp, B.2    Pious3
  • 23
    • 0028350714 scopus 로고
    • An essential role for HLA-DM in antigen presentation by class II major histocompatibility molecules
    • 23 Morris P, Shaman J, Attaya M, Amaya M, Goodman S, Bergman C, et al.: An essential role for HLA-DM in antigen presentation by class II major histocompatibility molecules. Nature 1994;368:551-554.
    • (1994) Nature , vol.368 , pp. 551-554
    • Morris, P.1    Shaman, J.2    Attaya, M.3    Amaya, M.4    Goodman, S.5    Bergman, C.6
  • 24
    • 0025940456 scopus 로고
    • New class II-like genes in the murine MHC
    • 24 Cho SG, Attaya M, Monaco JJ: New class II-like genes in the murine MHC. Nature 1991;353: 573-576.
    • (1991) Nature , vol.353 , pp. 573-576
    • Cho, S.G.1    Attaya, M.2    Monaco, J.J.3
  • 26
    • 0032168861 scopus 로고    scopus 로고
    • The structure of HLA-DM, the peptide exchange catalyst that loads antigen onto class II MHC molecules during antigen presentation
    • 26 Mosyak L, Zaller DM, Wiley DC: The structure of HLA-DM, the peptide exchange catalyst that loads antigen onto class II MHC molecules during antigen presentation. Immunity 1998;9:377-383.
    • (1998) Immunity , vol.9 , pp. 377-383
    • Mosyak, L.1    Zaller, D.M.2    Wiley, D.C.3
  • 29
    • 0028981178 scopus 로고
    • HLA-DM induces CLIP dissociation from MHC class II ab dimers and facilitates peptide loading
    • 29 Denzin LK, Cresswell P: HLA-DM induces CLIP dissociation from MHC class II ab dimers and facilitates peptide loading. Cell 1995;82:155-165.
    • (1995) Cell , vol.82 , pp. 155-165
    • Denzin, L.K.1    Cresswell, P.2
  • 30
    • 0029824101 scopus 로고    scopus 로고
    • Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM
    • 30 Weber DA, Evavold BD, Jensen PE: Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM. Science 1996; 274:618-620.
    • (1996) Science , vol.274 , pp. 618-620
    • Weber, D.A.1    Evavold, B.D.2    Jensen, P.E.3
  • 31
    • 0028880008 scopus 로고
    • Self-release of CLIP in peptide loading of HLA-DR molecules
    • 31 Kropshofer H, Vogt AB, Stern LJ, Hammerling GJ: Self-release of CLIP in peptide loading of HLA-DR molecules. Science 1995;270: 1357-1359.
    • (1995) Science , vol.270 , pp. 1357-1359
    • Kropshofer, H.1    Vogt, A.B.2    Stern, L.J.3    Hammerling, G.J.4
  • 32
    • 0028823585 scopus 로고
    • The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3
    • 32 Ghosh P, Amaya M, Mellins E, Wiley DC: The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3. Nature 1995;378:457-462.
    • (1995) Nature , vol.378 , pp. 457-462
    • Ghosh, P.1    Amaya, M.2    Mellins, E.3    Wiley, D.C.4
  • 33
    • 0028921633 scopus 로고
    • Binding of major histocompatibilty complex class II to the invariant chain-derived peptide, CLIP, is regulated by allelic polymorphism in class II
    • 33 Sette A, Southwood S, Miller J, Appella E: Binding of major histocompatibilty complex class II to the invariant chain-derived peptide, CLIP, is regulated by allelic polymorphism in class II. J Exp Med 1995;181:677-683.
    • (1995) J Exp Med , vol.181 , pp. 677-683
    • Sette, A.1    Southwood, S.2    Miller, J.3    Appella, E.4
  • 34
    • 0028845966 scopus 로고
    • Evidence for invariant chain 85-101 (CLIP) binding in the antigen binding site of MHC class II molecules
    • 34 Bangia N, Watts TH: Evidence for invariant chain 85-101 (CLIP) binding in the antigen binding site of MHC class II molecules. Int Immunol 1995;7:1585-1591.
    • (1995) Int Immunol , vol.7 , pp. 1585-1591
    • Bangia, N.1    Watts, T.H.2
  • 35
    • 0029807634 scopus 로고    scopus 로고
    • Human histocompatibility leukocyte antigen (HLA)-DM edits peptides presented by HLA-DR according to their ligand binding motifs
    • 35 van Ham SM, Gruneberg U, Malcherek G, Broker I, Melms A, Trowsdale J: Human histocompatibility leukocyte antigen (HLA)-DM edits peptides presented by HLA-DR according to their ligand binding motifs. J Exp Med 1996; 184:2019-2024.
    • (1996) J Exp Med , vol.184 , pp. 2019-2024
    • Van Ham, S.M.1    Gruneberg, U.2    Malcherek, G.3    Broker, I.4    Melms, A.5    Trowsdale, J.6
  • 37
    • 0028348369 scopus 로고
    • Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
    • 37 Stern LJ, Brown JH, Jardetzky TS, Gorga JC, Urban RG, Strominger JL, et al.: Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 1994;368: 215-221.
    • (1994) Nature , vol.368 , pp. 215-221
    • Stern, L.J.1    Brown, J.H.2    Jardetzky, T.S.3    Gorga, J.C.4    Urban, R.G.5    Strominger, J.L.6
  • 39
    • 0027074320 scopus 로고
    • Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule
    • 39 Fahnestock ML, Tamir I, Narhi L, Bjorkman PJ: Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule. Science 1992; 258:1658-1662.
    • (1992) Science , vol.258 , pp. 1658-1662
    • Fahnestock, M.L.1    Tamir, I.2    Narhi, L.3    Bjorkman, P.J.4
  • 40
    • 0030060377 scopus 로고    scopus 로고
    • Mice lacking H@-M complexes, engimatic elements of the MHC class II peptide-loading pathway
    • 40 Miyazaki T, Wolf P, Tourne S, Waltzinger C, Dierich A, Barois N, et al.: Mice lacking H@-M complexes, engimatic elements of the MHC class II peptide-loading pathway. Cell 1996;84:531-541.
    • (1996) Cell , vol.84 , pp. 531-541
    • Miyazaki, T.1    Wolf, P.2    Tourne, S.3    Waltzinger, C.4    Dierich, A.5    Barois, N.6
  • 41
    • 0027489002 scopus 로고
    • The segment of invariant chain that is critical for association with major histocompatibility complex class II molecules contains the sequence of a peptide eluted from class II polypeptide
    • 41 Freisewinkel IM, Schenck K, Koch N: The segment of invariant chain that is critical for association with major histocompatibility complex class II molecules contains the sequence of a peptide eluted from class II polypeptide. Proc Natl Acad Sci USA 1993; 90:9703-9706.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9703-9706
    • Freisewinkel, I.M.1    Schenck, K.2    Koch, N.3
  • 42
    • 0028233882 scopus 로고
    • Mapping functional regions in the lumenal domain of the class II-associated invariant chain
    • 42 Bijlmakers MJ, Benaroch P, Ploegh HL: Mapping functional regions in the lumenal domain of the class II-associated invariant chain. J Exp Med 1994;180:623-629.
    • (1994) J Exp Med , vol.180 , pp. 623-629
    • Bijlmakers, M.J.1    Benaroch, P.2    Ploegh, H.L.3
  • 43
    • 0028136262 scopus 로고
    • The CLIP region of invariant chain plays a critical role in regulating major histocompatibility complex class II folding , transport, and peptide occupancy
    • 43 Romagnoli P, Germain RN: The CLIP region of invariant chain plays a critical role in regulating major histocompatibility complex class II folding , transport, and peptide occupancy. J Exp Med 1994;180:1107-1113.
    • (1994) J Exp Med , vol.180 , pp. 1107-1113
    • Romagnoli, P.1    Germain, R.N.2
  • 44
    • 0029131499 scopus 로고
    • Kinetics of the reaction between the invariant chain (85-99) peptide and proteins of the murine class II MHC
    • 44 Liang MN, Beeson C, Mason K, McConnell HM: kinetics of the reaction between the invariant chain (85-99) peptide and proteins of the murine class II MHC. Int Immunol 1995;7:1397-1404.
    • (1995) Int Immunol , vol.7 , pp. 1397-1404
    • Liang, M.N.1    Beeson, C.2    Mason, K.3    McConnell, H.M.4
  • 45
    • 0033082484 scopus 로고    scopus 로고
    • Class II-associated invariant chain peptide-independent binding of inavariant chain to class II MHC molecules
    • 45 Thayer WP, Ignatowicz L, Weber DA, Jensen PE: Class II-associated invariant chain peptide-independent binding of inavariant chain to class II MHC molecules. J Immunol 1999;162:1502-1509.
    • (1999) J Immunol , vol.162 , pp. 1502-1509
    • Thayer, W.P.1    Ignatowicz, L.2    Weber, D.A.3    Jensen, P.E.4
  • 46
    • 0029114962 scopus 로고
    • Structural features of the invariant chain fragment CLIP controlling rapid release from HLA-DR molecules and inhibition of peptide binding
    • 46 Kropshofer H, Vogt AB, Hammerling GJ: Structural features of the invariant chain fragment CLIP controlling rapid release from HLA-DR molecules and inhibition of peptide binding. Proc Natl Acad Sci USA 1995;92:8313-8317.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8313-8317
    • Kropshofer, H.1    Vogt, A.B.2    Hammerling, G.J.3
  • 47
    • 0030832073 scopus 로고    scopus 로고
    • Interaction of MHC class II molecules with the invariant chain: Role of the invariant chain (81-90) region
    • 47 Stumptner P, Benaroch P: Interaction of MHC class II molecules with the invariant chain: role of the invariant chain (81-90) region. EMBO J 1997;16:5807-5818.
    • (1997) EMBO J , vol.16 , pp. 5807-5818
    • Stumptner, P.1    Benaroch, P.2
  • 48
    • 0032055577 scopus 로고    scopus 로고
    • Identification of a sequence that mediates promiscuous binding of invariant chain to MHC class II allotypes
    • 48 Siebenkotten IM, Carstens C, Koch N: Identification of a sequence that mediates promiscuous binding of invariant chain to MHC class II allotypes. J Immunol 1998; 160:3355-3362.
    • (1998) J Immunol , vol.160 , pp. 3355-3362
    • Siebenkotten, I.M.1    Carstens, C.2    Koch, N.3
  • 49
    • 0029845011 scopus 로고    scopus 로고
    • Evidence that binding site occupancy is necessary and sufficient for effective major histocompatibility complex (MHC) class II transport through the secretory pathway redefines the primary function of class II-associated invariant chain peptides (CLIP)
    • 49 Zhong G, Castellino F, Romagnoli P, Germain RN: Evidence that binding site occupancy is necessary and sufficient for effective major histocompatibility complex (MHC) class II transport through the secretory pathway redefines the primary function of class II-associated invariant chain peptides (CLIP). J Exp Med 1996; 184:2061-2066.
    • (1996) J Exp Med , vol.184 , pp. 2061-2066
    • Zhong, G.1    Castellino, F.2    Romagnoli, P.3    Germain, R.N.4
  • 51
    • 0030048126 scopus 로고    scopus 로고
    • H2-M mutant mice are defective in the peptide loading of class II molecules, antigen presentation, and T cell repertoire selection
    • 51 Martin WD, Hicks GG, Mendiratta SK, Leva HI Ruley HE, Van Kaer L: H2-M mutant mice are defective in the peptide loading of class II molecules, antigen presentation, and T cell repertoire selection. Cell 1996;84:543-550.
    • (1996) Cell , vol.84 , pp. 543-550
    • Martin, W.D.1    Hicks, G.G.2    Mendiratta, S.K.3    Leva, H.I.4    Ruley, H.E.5    Van Kaer, L.6
  • 53
    • 0029853195 scopus 로고    scopus 로고
    • Invariant chain and DM edit self-peptide presentation by Major Histocompatibility Complex (MHC) class II moloecules
    • 53 Katz JF, Stebbins C, Appella E, Sant AJ: Invariant chain and DM edit self-peptide presentation by Major Histocompatibility Complex (MHC) class II moloecules. J Exp Med 196;184:1747-1753.
    • J Exp Med , vol.196 , Issue.184 , pp. 1747-1753
    • Katz, J.F.1    Stebbins, C.2    Appella, E.3    Sant, A.J.4
  • 54
    • 0030984711 scopus 로고    scopus 로고
    • Selective binding of bacterial toxins to major histocompatibility complex class II-expressing cells is controlled by invariant chain and HLA-DM
    • 54 Lavoie PM, Thibodeau J, Cloutier I, Busch R, Sekaly RP: Selective binding of bacterial toxins to major histocompatibility complex class II-expressing cells is controlled by invariant chain and HLA-DM. Proc Natl Acad Sci USA 1997;94:6892-6897.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6892-6897
    • Lavoie, P.M.1    Thibodeau, J.2    Cloutier, I.3    Busch, R.4    Sekaly, R.P.5
  • 55
    • 0030990387 scopus 로고    scopus 로고
    • In the absence of the invariant chain, HLA-DR molecules display a distinct array of peptides which influenced by the presence or absence of HLA-DM
    • 55 Lightstone L, Hargreaves R, Bobek G, Peterson M, Aichinger G, Lombardi G, et al.: In the absence of the invariant chain, HLA-DR molecules display a distinct array of peptides which influenced by the presence or absence of HLA-DM. Proc Natl Acad Sci USA 1997;94:5772-5777.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5772-5777
    • Lightstone, L.1    Hargreaves, R.2    Bobek, G.3    Peterson, M.4    Aichinger, G.5    Lombardi, G.6
  • 56
    • 0030790791 scopus 로고    scopus 로고
    • Functionality of major histocompatibility complex class II molecules in mice doubly deficient for invariant chain and H-2M complexes
    • 56 Tourne S, Miyazaki T, Wolf P, Ploegh H, Benoist C, Mathis D: Functionality of major histocompatibility complex class II molecules in mice doubly deficient for invariant chain and H-2M complexes. Proc Natl Acad Sci USA 1997;94:9255-9260.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9255-9260
    • Tourne, S.1    Miyazaki, T.2    Wolf, P.3    Ploegh, H.4    Benoist, C.5    Mathis, D.6
  • 58
    • 0031984942 scopus 로고    scopus 로고
    • Invariant chain-independent function of H-2M in the formation of endogenous peptide-major histocompatibility complex class II complexes in vivo
    • 58 Kovats S, Grubin CE, Eastman S, deRoos P, Dongre A, Van Kaer L, et al.: Invariant chain-independent function of H-2M in the formation of endogenous peptide-major histocompatibility complex class II complexes in vivo. J Exp Med 1998;187:245-251.
    • (1998) J Exp Med , vol.187 , pp. 245-251
    • Kovats, S.1    Grubin, C.E.2    Eastman, S.3    DeRoos, P.4    Dongre, A.5    Van Kaer, L.6
  • 59
    • 0030046476 scopus 로고    scopus 로고
    • Lowering the tone: Mechanisms of immunodominance among epitopes with low affinity for MHC
    • 59 Fairchild PJ, Wraith DC: Lowering the tone: mechanisms of immunodominance among epitopes with low affinity for MHC. Immunol Today 1996;17:80-85.
    • (1996) Immunol Today , vol.17 , pp. 80-85
    • Fairchild, P.J.1    Wraith, D.C.2
  • 60
    • 0027439013 scopus 로고
    • An auto antigenic T cell epitope from unstable complexes with class II MHC: A novel route for escape from tolerance induction
    • 60 Fairchild PJ, Wildgoose R, Artherton E, Webb S, Wraith DC: An auto antigenic T cell epitope from unstable complexes with class II MHC: a novel route for escape from tolerance induction. Int Immunol 1993;5:1151-1158.
    • (1993) Int Immunol , vol.5 , pp. 1151-1158
    • Fairchild, P.J.1    Wildgoose, R.2    Artherton, E.3    Webb, S.4    Wraith, D.C.5
  • 61
    • 0028338977 scopus 로고
    • Direct binding of autoimmune disease related T cell epitopes to purified Lewis rat MHC class II molecules
    • 61 Joosten I, Wauben MH, Holewijn MC, Reske K, Pedersen LO, Roosenboom CF, et al.: Direct binding of autoimmune disease related T cell epitopes to purified Lewis rat MHC class II molecules. Int Immunol 1994;6:751-759.
    • (1994) Int Immunol , vol.6 , pp. 751-759
    • Joosten, I.1    Wauben, M.H.2    Holewijn, M.C.3    Reske, K.4    Pedersen, L.O.5    Roosenboom, C.F.6
  • 62
    • 0030067815 scopus 로고    scopus 로고
    • The class II MHC I-Ag7 molecules from non-obese diabetic mice are poor peptide binders
    • 62 Carrasco-Marin E, Shimizu J, Kanagawa O, Unanue ER: The class II MHC I-Ag7 molecules from non-obese diabetic mice are poor peptide binders. J Immunol 1996; 156:450-458.
    • (1996) J Immunol , vol.156 , pp. 450-458
    • Carrasco-Marin, E.1    Shimizu, J.2    Kanagawa, O.3    Unanue, E.R.4
  • 63
    • 0032076555 scopus 로고    scopus 로고
    • Differential tolerance in induced T cells recognizing distinct epitopes of myelin basic protein
    • 63 Harrington CJ, Paez A, Hunkapiller T, Mannikko V, Brabb T, Ahearn M, et al.: Differential tolerance in induced T cells recognizing distinct epitopes of myelin basic protein. Immunity 1998; 8:571-580.
    • (1998) Immunity , vol.8 , pp. 571-580
    • Harrington, C.J.1    Paez, A.2    Hunkapiller, T.3    Mannikko, V.4    Brabb, T.5    Ahearn, M.6
  • 66
    • 0029055938 scopus 로고
    • Antigen presentation mediated by recycling of surface HLA-DR molecules
    • 66 Pinet V, Vergelli M, Martin R, Bakke O, Long EO: Antigen presentation mediated by recycling of surface HLA-DR molecules. Nature 1995;375:603-606.
    • (1995) Nature , vol.375 , pp. 603-606
    • Pinet, V.1    Vergelli, M.2    Martin, R.3    Bakke, O.4    Long, E.O.5
  • 67
    • 0027326680 scopus 로고
    • A europium fluoro-immunoassay for measuring binding of antigen to class II MHC glycoproteins
    • 67 Tompkins SM, Rota PA, Moore JC, Jensen PE: A europium fluoro-immunoassay for measuring binding of antigen to class II MHC glycoproteins. J Immunol Methods 1993;163:209-216.
    • (1993) J Immunol Methods , vol.163 , pp. 209-216
    • Tompkins, S.M.1    Rota, P.A.2    Moore, J.C.3    Jensen, P.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.