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Volumn 6, Issue JUL, 2015, Pages

MHC class II auto-antigen presentation is unconventional

Author keywords

Auto antigens; Cathepsin sensitivity; Cell free antigen processing system; Extracellular processing; HLA DR antigens; Immunodominance; Paralyzed DC

Indexed keywords

AUTOANTIGEN; CATHEPSIN; COLLAGEN TYPE 2; EPITOPE; GELATINASE B; GLIADIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2;

EID: 84938502645     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2015.00372     Document Type: Short Survey
Times cited : (27)

References (50)
  • 1
    • 84920683669 scopus 로고    scopus 로고
    • Determinants of immunodominance for CD4 T cells
    • Kim A, Sadegh-Nasseri S. Determinants of immunodominance for CD4 T cells. Curr Opin Immunol (2015) 34:9-15. doi: 10.1016/j.coi.2014.12.005
    • (2015) Curr Opin Immunol , vol.34 , pp. 9-15
    • Kim, A.1    Sadegh-Nasseri, S.2
  • 2
    • 0033966413 scopus 로고    scopus 로고
    • Cathepsins and compartmentalization in antigen presentation
    • Riese RJ, Chapman HA. Cathepsins and compartmentalization in antigen presentation. Curr Opin Immunol (2000) 12(1):107-13. doi:10.1016/S0952-7915(99)00058-8
    • (2000) Curr Opin Immunol , vol.12 , Issue.1 , pp. 107-113
    • Riese, R.J.1    Chapman, H.A.2
  • 3
    • 0028350714 scopus 로고
    • An essential role for HLA-DM in antigen presentation by class II major histocompatibility molecules
    • 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(6471):551-4. doi:10.1038/368551a0
    • (1994) Nature , vol.368 , Issue.6471 , pp. 551-554
    • Morris, P.1    Shaman, J.2    Attaya, M.3    Amaya, M.4    Goodman, S.5    Bergman, C.6
  • 4
    • 33846952190 scopus 로고    scopus 로고
    • HLA-DM targets the hydrogen bond between the histidine at position beta81 and peptide to dissociate HLA-DR-peptide complexes
    • Narayan K, Chou CL, Kim A, Hartman IZ, Dalai S, Khoruzhenko S, et al. HLA-DM targets the hydrogen bond between the histidine at position beta81 and peptide to dissociate HLA-DR-peptide complexes. Nat Immunol (2007) 8(1):92-100. doi:10.1038/ni1414
    • (2007) Nat Immunol , vol.8 , Issue.1 , pp. 92-100
    • Narayan, K.1    Chou, C.L.2    Kim, A.3    Hartman, I.Z.4    Dalai, S.5    Khoruzhenko, S.6
  • 6
    • 84875264080 scopus 로고    scopus 로고
    • Expanding roles for GILT in immunity
    • West LC, Cresswell P. Expanding roles for GILT in immunity. Curr Opin Immunol (2013) 25(1):103-8. doi:10.1016/j.coi.2012.11.006
    • (2013) Curr Opin Immunol , vol.25 , Issue.1 , pp. 103-108
    • West, L.C.1    Cresswell, P.2
  • 7
    • 84929515864 scopus 로고    scopus 로고
    • Conformational instability governed by disulfide bonds partitions the dominant from subdominant helper T-cell responses specific for HIV-1 envelope glycoprotein gp120
    • Nguyen HN, Steede NK, Robinson JE, Landry SJ. Conformational instability governed by disulfide bonds partitions the dominant from subdominant helper T-cell responses specific for HIV-1 envelope glycoprotein gp120. Vaccine (2015) 33(25):2887-96. doi:10.1016/j.vaccine.2015.04.082
    • (2015) Vaccine , vol.33 , Issue.25 , pp. 2887-2896
    • Nguyen, H.N.1    Steede, N.K.2    Robinson, J.E.3    Landry, S.J.4
  • 8
    • 84881319397 scopus 로고    scopus 로고
    • HLA-DO as the optimizer of epitope selection for MHC class II antigen presentation
    • Poluektov YO, Kim A, Hartman IZ, Sadegh-Nasseri S. HLA-DO as the optimizer of epitope selection for MHC class II antigen presentation. PLoS One (2013) 8(8):e71228. doi:10.1371/journal.pone.0071228
    • (2013) PLoS One , vol.8 , Issue.8
    • Poluektov, Y.O.1    Kim, A.2    Hartman, I.Z.3    Sadegh-Nasseri, S.4
  • 9
    • 84883669568 scopus 로고    scopus 로고
    • HLA-DO and its role in MHC class II antigen presentation
    • Poluektov YO, Kim A, Sadegh-Nasseri S. HLA-DO and its role in MHC class II antigen presentation. Front Immunol (2013) 4:260. doi:10.3389/fimmu.2013.00260
    • (2013) Front Immunol , vol.4 , pp. 260
    • Poluektov, Y.O.1    Kim, A.2    Sadegh-Nasseri, S.3
  • 10
    • 84872023632 scopus 로고    scopus 로고
    • Sibling rivalry: competition between MHC class II family members inhibits immunity
    • Denzin LK, Cresswell P. Sibling rivalry: competition between MHC class II family members inhibits immunity. Nat Struct Mol Biol (2013) 20(1):7-10. doi:10.1038/nsmb.2484
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.1 , pp. 7-10
    • Denzin, L.K.1    Cresswell, P.2
  • 11
    • 78149357976 scopus 로고    scopus 로고
    • A reductionist cell-free major histocompatibility complex class II antigen processing system identifies immunodominant epitopes
    • Hartman IZ, Kim A, Cotter RJ, Walter K, Dalai SK, Boronina T, et al. A reductionist cell-free major histocompatibility complex class II antigen processing system identifies immunodominant epitopes. Nat Med (2010) 16:1333-40. doi:10.1038/nm.2248
    • (2010) Nat Med , vol.16 , pp. 1333-1340
    • Hartman, I.Z.1    Kim, A.2    Cotter, R.J.3    Walter, K.4    Dalai, S.K.5    Boronina, T.6
  • 12
    • 79951679620 scopus 로고    scopus 로고
    • Routes to manipulate MHC class II antigen presentation
    • van den Hoorn T, Paul P, Jongsma ML, Neefjes J. Routes to manipulate MHC class II antigen presentation. Curr Opin Immunol (2011) 23(1):88-95. doi:10.1016/j.coi.2010.11.002
    • (2011) Curr Opin Immunol , vol.23 , Issue.1 , pp. 88-95
    • van den Hoorn, T.1    Paul, P.2    Jongsma, M.L.3    Neefjes, J.4
  • 13
    • 84867325424 scopus 로고    scopus 로고
    • HLA-DM constrains epitope selection in the human CD4 T cell response to vaccinia virus by favoring the presentation of peptides with longer HLA-DM-mediated half-lives
    • Yin L, Calvo-Calle JM, Dominguez-Amorocho O, Stern LJ. HLA-DM constrains epitope selection in the human CD4 T cell response to vaccinia virus by favoring the presentation of peptides with longer HLA-DM-mediated half-lives. J Immunol (2012) 189(8):3983-94. doi:10.4049/jimmunol.1200626
    • (2012) J Immunol , vol.189 , Issue.8 , pp. 3983-3994
    • Yin, L.1    Calvo-Calle, J.M.2    Dominguez-Amorocho, O.3    Stern, L.J.4
  • 14
    • 77957796763 scopus 로고    scopus 로고
    • Monocyte-derived dendritic cells exhibit increased levels of lysosomal proteolysis as compared to other human dendritic cell populations
    • McCurley N, Mellman I. Monocyte-derived dendritic cells exhibit increased levels of lysosomal proteolysis as compared to other human dendritic cell populations. PLoS One (2010) 5(8):e11949. doi:10.1371/journal.pone.0011949
    • (2010) PLoS One , vol.5 , Issue.8
    • McCurley, N.1    Mellman, I.2
  • 15
    • 14844340568 scopus 로고    scopus 로고
    • Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate
    • Delamarre L, Pack M, Chang H, Mellman I, Trombetta ES. Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate. Science (2005) 307(5715):1630-4. doi:10.1126/science.1108003
    • (2005) Science , vol.307 , Issue.5715 , pp. 1630-1634
    • Delamarre, L.1    Pack, M.2    Chang, H.3    Mellman, I.4    Trombetta, E.S.5
  • 16
    • 0037470438 scopus 로고    scopus 로고
    • Activation of lysosomal function during dendritic cell maturation
    • Trombetta ES, Ebersold M, Garrett W, Pypaert M, Mellman I. Activation of lysosomal function during dendritic cell maturation. Science (2003) 299(5611):1400-3. doi:10.1126/science.1080106
    • (2003) Science , vol.299 , Issue.5611 , pp. 1400-1403
    • Trombetta, E.S.1    Ebersold, M.2    Garrett, W.3    Pypaert, M.4    Mellman, I.5
  • 17
    • 84885978134 scopus 로고    scopus 로고
    • Proteases: essential actors in processing antigens and intracellular toll-like receptors
    • Manoury B. Proteases: essential actors in processing antigens and intracellular toll-like receptors. Front Immunol (2013) 4:299. doi:10.3389/fimmu.2013.00299
    • (2013) Front Immunol , vol.4 , pp. 299
    • Manoury, B.1
  • 18
    • 26244445000 scopus 로고    scopus 로고
    • The lysosomal cysteine proteases in MHC class II antigen presentation
    • Hsing LC, Rudensky AY. The lysosomal cysteine proteases in MHC class II antigen presentation. Immunol Rev (2005) 207:229-41. doi:10.1111/j.0105-2896.2005.00310.x
    • (2005) Immunol Rev , vol.207 , pp. 229-241
    • Hsing, L.C.1    Rudensky, A.Y.2
  • 19
    • 30044444910 scopus 로고    scopus 로고
    • Endosomal proteases in antigen presentation
    • Chapman HA. Endosomal proteases in antigen presentation. Curr Opin Immunol (2006) 18(1):78-84. doi:10.1016/j.coi.2005.11.011
    • (2006) Curr Opin Immunol , vol.18 , Issue.1 , pp. 78-84
    • Chapman, H.A.1
  • 20
    • 0033695299 scopus 로고    scopus 로고
    • Proteolysis in MHC class II antigen presentation: who's in charge?
    • Villadangos JA, Ploegh HL. Proteolysis in MHC class II antigen presentation: who's in charge?. Immunity (2000) 12(3):233-9. doi:10.1016/S1074-7613(00)80176-4
    • (2000) Immunity , vol.12 , Issue.3 , pp. 233-239
    • Villadangos, J.A.1    Ploegh, H.L.2
  • 21
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • Honey K, Rudensky AY. Lysosomal cysteine proteases regulate antigen presentation. Nat Rev Immunol (2003) 3(6):472-82. doi:10.1038/nri1110
    • (2003) Nat Rev Immunol , vol.3 , Issue.6 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 22
    • 0036177422 scopus 로고    scopus 로고
    • Specific role for cathepsin S in the generation of antigenic peptides in vivo
    • Pluger EB, Boes M, Alfonso C, Schroter CJ, Kalbacher H, Ploegh HL, et al. Specific role for cathepsin S in the generation of antigenic peptides in vivo. Eur J Immunol (2002) 32(2):467-76. doi:10.1002/1521-4141(200202)32:2<467::AID-IMMU467>3.0.CO;2-Y
    • (2002) Eur J Immunol , vol.32 , Issue.2 , pp. 467-476
    • Pluger, E.B.1    Boes, M.2    Alfonso, C.3    Schroter, C.J.4    Kalbacher, H.5    Ploegh, H.L.6
  • 23
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
    • Riese RJ, Wolf PR, Bromme D, Natkin LR, Villadangos JA, Ploegh HL, et al. Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity (1996) 4(4):357-66. doi:10.1016/S1074-7613(00)80249-6
    • (1996) Immunity , vol.4 , Issue.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.R.2    Bromme, D.3    Natkin, L.R.4    Villadangos, J.A.5    Ploegh, H.L.6
  • 24
    • 2442549710 scopus 로고    scopus 로고
    • Impaired invariant chain degradation and antigen presentation and diminished collagen-induced arthritis in cathepsin S null mice
    • Nakagawa TY, Brissette WH, Lira PD, Griffiths RJ, Petrushova N, Stock J, et al. Impaired invariant chain degradation and antigen presentation and diminished collagen-induced arthritis in cathepsin S null mice. Immunity (1999) 10(2):207-17. doi:10.1016/S1074-7613(00)80021-7
    • (1999) Immunity , vol.10 , Issue.2 , pp. 207-217
    • Nakagawa, T.Y.1    Brissette, W.H.2    Lira, P.D.3    Griffiths, R.J.4    Petrushova, N.5    Stock, J.6
  • 25
    • 0032540474 scopus 로고    scopus 로고
    • Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus
    • Nakagawa T, Roth W, Wong P, Nelson A, Farr A, Deussing J, et al. Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus. Science (1998) 280(5362):450-3. doi:10.1126/science.280.5362.450
    • (1998) Science , vol.280 , Issue.5362 , pp. 450-453
    • Nakagawa, T.1    Roth, W.2    Wong, P.3    Nelson, A.4    Farr, A.5    Deussing, J.6
  • 26
    • 0036167693 scopus 로고    scopus 로고
    • Destructive processing by asparagine endopeptidase limits presentation of a dominant T cell epitope in MBP
    • Manoury B, Mazzeo D, Fugger L, Viner N, Ponsford M, Streeter H, et al. Destructive processing by asparagine endopeptidase limits presentation of a dominant T cell epitope in MBP. Nat Immunol (2002) 3(2):169-74. doi:10.1038/ni754
    • (2002) Nat Immunol , vol.3 , Issue.2 , pp. 169-174
    • Manoury, B.1    Mazzeo, D.2    Fugger, L.3    Viner, N.4    Ponsford, M.5    Streeter, H.6
  • 27
    • 0038579799 scopus 로고    scopus 로고
    • Creation versus destruction of T cell epitopes in the class II MHC pathway
    • Watts C, Moss CX, Mazzeo D, West MA, Matthews SP, Li DN, et al. Creation versus destruction of T cell epitopes in the class II MHC pathway. Ann N Y Acad Sci (2003) 987:9-14. doi:10.1111/j.1749-6632.2003.tb06028.x
    • (2003) Ann N Y Acad Sci , vol.987 , pp. 9-14
    • Watts, C.1    Moss, C.X.2    Mazzeo, D.3    West, M.A.4    Matthews, S.P.5    Li, D.N.6
  • 28
    • 0032516003 scopus 로고    scopus 로고
    • Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation
    • Deussing J, Roth W, Saftig P, Peters C, Ploegh HL, Villadangos JA. Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation. Proc Natl Acad Sci U S A (1998) 95(8):4516-21. doi:10.1073/pnas.95.8.4516
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.8 , pp. 4516-4521
    • Deussing, J.1    Roth, W.2    Saftig, P.3    Peters, C.4    Ploegh, H.L.5    Villadangos, J.A.6
  • 29
    • 84920649458 scopus 로고    scopus 로고
    • Divergent paths for the selection of immunodominant epitopes from distinct antigenic sources
    • Kim A, Hartman IZ, Poore B, Boronina T, Cole RN, Song N, et al. Divergent paths for the selection of immunodominant epitopes from distinct antigenic sources. Nat Commun (2014) 5:5369. doi:10.1038/ncomms6369
    • (2014) Nat Commun , vol.5 , pp. 5369
    • Kim, A.1    Hartman, I.Z.2    Poore, B.3    Boronina, T.4    Cole, R.N.5    Song, N.6
  • 30
    • 56349147815 scopus 로고    scopus 로고
    • Cathepsin E regulates the presentation of tetanus toxin C-fragment in PMA activated primary human B cells
    • Burster T, Reich M, Zaidi N, Voelter W, Boehm BO, Kalbacher H. Cathepsin E regulates the presentation of tetanus toxin C-fragment in PMA activated primary human B cells. Biochem Biophys Res Commun (2008) 377(4):1299-303. doi:10.1016/j.bbrc.2008.10.162
    • (2008) Biochem Biophys Res Commun , vol.377 , Issue.4 , pp. 1299-1303
    • Burster, T.1    Reich, M.2    Zaidi, N.3    Voelter, W.4    Boehm, B.O.5    Kalbacher, H.6
  • 31
    • 72949106010 scopus 로고    scopus 로고
    • Cathepsin G: roles in antigen presentation and beyond
    • Burster T, Macmillan H, Hou T, Boehm BO, Mellins ED. Cathepsin G: roles in antigen presentation and beyond. Mol Immunol (2010) 47(4):658-65. doi:10.1016/j.molimm.2009.10.003
    • (2010) Mol Immunol , vol.47 , Issue.4 , pp. 658-665
    • Burster, T.1    Macmillan, H.2    Hou, T.3    Boehm, B.O.4    Mellins, E.D.5
  • 32
    • 84855476371 scopus 로고    scopus 로고
    • Register shifting of an insulin peptide-MHC complex allows diabetogenic T cells to escape thymic deletion
    • Mohan JF, Petzold SJ, Unanue ER. Register shifting of an insulin peptide-MHC complex allows diabetogenic T cells to escape thymic deletion. J Exp Med (2011) 208(12):2375-83. doi:10.1084/jem.20111502
    • (2011) J Exp Med , vol.208 , Issue.12 , pp. 2375-2383
    • Mohan, J.F.1    Petzold, S.J.2    Unanue, E.R.3
  • 33
    • 84903543514 scopus 로고    scopus 로고
    • Cysteine cathepsins and extracellular matrix degradation
    • Fonovic M, Turk B. Cysteine cathepsins and extracellular matrix degradation. Biochim Biophys Acta (2014) 1840(8):2560-70. doi:10.1016/j.bbagen.2014.03.017
    • (2014) Biochim Biophys Acta , vol.1840 , Issue.8 , pp. 2560-2570
    • Fonovic, M.1    Turk, B.2
  • 34
    • 84896549845 scopus 로고    scopus 로고
    • Cysteine cathepsins in neurological disorders
    • Pislar A, Kos J. Cysteine cathepsins in neurological disorders. Mol Neurobiol (2014) 49(2):1017-30. doi:10.1007/s12035-013-8576-6
    • (2014) Mol Neurobiol , vol.49 , Issue.2 , pp. 1017-1030
    • Pislar, A.1    Kos, J.2
  • 36
    • 4944223135 scopus 로고    scopus 로고
    • Pathogenic human thyroglobulin peptides in HLA-DR3 transgenic mouse model of autoimmune thyroiditis
    • Flynn JC, McCormick DJ, Brusic V, Wan Q, Panos JC, Giraldo AA, et al. Pathogenic human thyroglobulin peptides in HLA-DR3 transgenic mouse model of autoimmune thyroiditis. Cell Immunol (2004) 229(2):79-85. doi:10.1016/j.cellimm.2004.07.002
    • (2004) Cell Immunol , vol.229 , Issue.2 , pp. 79-85
    • Flynn, J.C.1    McCormick, D.J.2    Brusic, V.3    Wan, Q.4    Panos, J.C.5    Giraldo, A.A.6
  • 37
    • 71049188177 scopus 로고    scopus 로고
    • Monitoring compartment-specific substrate cleavage by cathepsins B, K, L, and S at physiological pH and redox conditions
    • Jordans S, Jenko-Kokalj S, Kuhl NM, Tedelind S, Sendt W, Bromme D, et al. Monitoring compartment-specific substrate cleavage by cathepsins B, K, L, and S at physiological pH and redox conditions. BMC Biochem (2009) 10:23. doi:10.1186/1471-2091-10-23
    • (2009) BMC Biochem , vol.10 , pp. 23
    • Jordans, S.1    Jenko-Kokalj, S.2    Kuhl, N.M.3    Tedelind, S.4    Sendt, W.5    Bromme, D.6
  • 38
    • 80051924280 scopus 로고    scopus 로고
    • Uveitis-associated epitopes of retinal antigens are pathogenic in the humanized mouse model of uveitis and identify autoaggressive T cells
    • Mattapallil MJ, Silver PB, Mattapallil JJ, Horai R, Karabekian Z, McDowell JH, et al. Uveitis-associated epitopes of retinal antigens are pathogenic in the humanized mouse model of uveitis and identify autoaggressive T cells. J Immunol (2011) 187(4):1977-85. doi:10.4049/jimmunol.1101247
    • (2011) J Immunol , vol.187 , Issue.4 , pp. 1977-1985
    • Mattapallil, M.J.1    Silver, P.B.2    Mattapallil, J.J.3    Horai, R.4    Karabekian, Z.5    McDowell, J.H.6
  • 39
    • 0035666656 scopus 로고    scopus 로고
    • Cathepsin S and an asparagine-specific endoprotease dominate the proteolytic processing of human myelin basic protein in vitro
    • Beck H, Schwarz G, Schroter CJ, Deeg M, Baier D, Stevanovic S, et al. Cathepsin S and an asparagine-specific endoprotease dominate the proteolytic processing of human myelin basic protein in vitro. Eur J Immunol (2001) 31(12):3726-36. doi:10.1002/1521-4141(200112)31:12<3726::AID-IMMU3726>3.0.CO;2-O
    • (2001) Eur J Immunol , vol.31 , Issue.12 , pp. 3726-3736
    • Beck, H.1    Schwarz, G.2    Schroter, C.J.3    Deeg, M.4    Baier, D.5    Stevanovic, S.6
  • 40
    • 0037183929 scopus 로고    scopus 로고
    • Structural basis for gluten intolerance in celiac sprue
    • Shan L, Molberg O, Parrot I, Hausch F, Filiz F, Gray GM, et al. Structural basis for gluten intolerance in celiac sprue. Science (2002) 297(5590):2275-9. doi:10.1126/science.1074129
    • (2002) Science , vol.297 , Issue.5590 , pp. 2275-2279
    • Shan, L.1    Molberg, O.2    Parrot, I.3    Hausch, F.4    Filiz, F.5    Gray, G.M.6
  • 41
    • 84921470210 scopus 로고    scopus 로고
    • Molecular mechanisms for contribution of MHC molecules to autoimmune diseases
    • Sollid LM, Pos W, Wucherpfennig KW. Molecular mechanisms for contribution of MHC molecules to autoimmune diseases. Curr Opin Immunol (2014) 31C:24-30. doi:10.1016/j.coi.2014.08.005
    • (2014) Curr Opin Immunol , vol.31C , pp. 24-30
    • Sollid, L.M.1    Pos, W.2    Wucherpfennig, K.W.3
  • 42
    • 84938513013 scopus 로고    scopus 로고
    • Mechanisms of induction of paralysed dendritic cells with poor antigen presentation function following systemic inflammatory response syndrome
    • Villadangos J. Mechanisms of induction of paralysed dendritic cells with poor antigen presentation function following systemic inflammatory response syndrome. J Immunol (2015) 194(1 Suppl):113.4.
    • (2015) J Immunol , vol.194 , Issue.1 , pp. 113.4
    • Villadangos, J.1
  • 43
    • 0032547858 scopus 로고    scopus 로고
    • Crystal structure of HLA-DR2 (DRA*0101, DRB1*1501) complexed with a peptide from human myelin basic protein
    • Smith KJ, Pyrdol J, Gauthier L, Wiley DC, Wucherpfennig KW. Crystal structure of HLA-DR2 (DRA*0101, DRB1*1501) complexed with a peptide from human myelin basic protein. J Exp Med (1998) 188(8):1511-20. doi:10.1084/jem.188.8.1511
    • (1998) J Exp Med , vol.188 , Issue.8 , pp. 1511-1520
    • Smith, K.J.1    Pyrdol, J.2    Gauthier, L.3    Wiley, D.C.4    Wucherpfennig, K.W.5
  • 44
    • 26644468528 scopus 로고    scopus 로고
    • Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule
    • Li Y, Huang Y, Lue J, Quandt JA, Martin R, Mariuzza RA. Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule. EMBO J (2005) 24(17):2968-79. doi:10.1038/sj.emboj.7600771
    • (2005) EMBO J , vol.24 , Issue.17 , pp. 2968-2979
    • Li, Y.1    Huang, Y.2    Lue, J.3    Quandt, J.A.4    Martin, R.5    Mariuzza, R.A.6
  • 45
    • 33646038285 scopus 로고    scopus 로고
    • Small molecules that enhance the catalytic efficiency of HLA-DM
    • Nicholson MJ, Moradi B, Seth NP, Xing X, Cuny GD, Stein RL, et al. Small molecules that enhance the catalytic efficiency of HLA-DM. J Immunol (2006) 176(7):4208-20. doi:10.4049/jimmunol.176.7.4208
    • (2006) J Immunol , vol.176 , Issue.7 , pp. 4208-4220
    • Nicholson, M.J.1    Moradi, B.2    Seth, N.P.3    Xing, X.4    Cuny, G.D.5    Stein, R.L.6
  • 46
    • 84875625575 scopus 로고    scopus 로고
    • A novel pathway of presentation by class II-MHC molecules involving peptides or denatured proteins important in autoimmunity
    • Mohan JF, Unanue ER. A novel pathway of presentation by class II-MHC molecules involving peptides or denatured proteins important in autoimmunity. Mol Immunol (2013) 55(2):166-8. doi:10.1016/j.molimm.2012.10.024
    • (2013) Mol Immunol , vol.55 , Issue.2 , pp. 166-168
    • Mohan, J.F.1    Unanue, E.R.2
  • 47
    • 84894354624 scopus 로고    scopus 로고
    • Monoclonal antibody blocking the recognition of an insulin peptide-MHC complex modulates type 1 diabetes
    • Zhang L, Crawford F, Yu L, Michels A, Nakayama M, Davidson HW, et al. Monoclonal antibody blocking the recognition of an insulin peptide-MHC complex modulates type 1 diabetes. Proc Natl Acad Sci U S A (2014) 111(7):2656-61. doi:10.1073/pnas.1323436111
    • (2014) Proc Natl Acad Sci U S A , vol.111 , Issue.7 , pp. 2656-2661
    • Zhang, L.1    Crawford, F.2    Yu, L.3    Michels, A.4    Nakayama, M.5    Davidson, H.W.6
  • 48
    • 77954643719 scopus 로고    scopus 로고
    • Diabetogenic T cells recognize insulin bound to IAg7 in an unexpected, weakly binding register
    • Stadinski BD, Zhang L, Crawford F, Marrack P, Eisenbarth GS, Kappler JW. Diabetogenic T cells recognize insulin bound to IAg7 in an unexpected, weakly binding register. Proc Natl Acad Sci U S A (2010) 107(24):10978-83. doi:10.1073/pnas.1006545107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.24 , pp. 10978-10983
    • Stadinski, B.D.1    Zhang, L.2    Crawford, F.3    Marrack, P.4    Eisenbarth, G.S.5    Kappler, J.W.6
  • 49
    • 84886837181 scopus 로고    scopus 로고
    • Pathogenic CD4(+) T cells recognizing an unstable peptide of insulin are directly recruited into islets bypassing local lymph nodes
    • Mohan JF, Calderon B, Anderson MS, Unanue ER. Pathogenic CD4(+) T cells recognizing an unstable peptide of insulin are directly recruited into islets bypassing local lymph nodes. J Exp Med (2013) 210(11):2403-14. doi:10.1084/jem.20130582
    • (2013) J Exp Med , vol.210 , Issue.11 , pp. 2403-2414
    • Mohan, J.F.1    Calderon, B.2    Anderson, M.S.3    Unanue, E.R.4
  • 50
    • 84908134654 scopus 로고    scopus 로고
    • A minor subset of Batf3-dependent antigen-presenting cells in islets of Langerhans is essential for the development of autoimmune diabetes
    • Ferris ST, Carrero JA, Mohan JF, Calderon B, Murphy KM, Unanue ER. A minor subset of Batf3-dependent antigen-presenting cells in islets of Langerhans is essential for the development of autoimmune diabetes. Immunity (2014) 41(4):657-69. doi:10.1016/j.immuni.2014.09.012
    • (2014) Immunity , vol.41 , Issue.4 , pp. 657-669
    • Ferris, S.T.1    Carrero, J.A.2    Mohan, J.F.3    Calderon, B.4    Murphy, K.M.5    Unanue, E.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.