메뉴 건너뛰기




Volumn 51, Issue 24, 2008, Pages 7834-7842

Citrullination of linear and cyclic altered peptide ligands from myelin basic protein (MBP87-99) epitope elicits a Th1 polarized response by T cells isolated from multiple sclerosis patients: Implications in triggering disease

Author keywords

[No Author keywords available]

Indexed keywords

CITRULLINE; EPITOPE; MYELIN BASIC PROTEIN; MYELIN BASIC PROTEIN CYCLO[87-99][91 CITRULLINE 96 ALANINE 97 CITRULLINE]; MYELIN BASIC PROTEIN[87-99][91 CITRULLINE 96 ALANINE 97 CITRULLINE]; UNCLASSIFIED DRUG;

EID: 58149088749     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm800891n     Document Type: Article
Times cited : (49)

References (56)
  • 2
    • 43049177977 scopus 로고    scopus 로고
    • Multiple sclerosis: Immunopathogenesis and controversies in defining the cause
    • Holmoy, T.; Hestvik, A. L. Multiple sclerosis: immunopathogenesis and controversies in defining the cause. Curr. Opin. Infect. Dis. 2008, 21, 271-278.
    • (2008) Curr. Opin. Infect. Dis , vol.21 , pp. 271-278
    • Holmoy, T.1    Hestvik, A.L.2
  • 3
    • 0043022062 scopus 로고    scopus 로고
    • New and emerging treatment options for multiple sclerosis
    • Polman, C. H.; Uitdehaag, B. M. New and emerging treatment options for multiple sclerosis. Lancet Neurol. 2003, 2, 563-566.
    • (2003) Lancet Neurol , vol.2 , pp. 563-566
    • Polman, C.H.1    Uitdehaag, B.M.2
  • 4
    • 0029939467 scopus 로고    scopus 로고
    • Multiple sclerosis: A coordinated immunological attack against myelin in the central nervous system
    • Steinman, L. Multiple sclerosis: a coordinated immunological attack against myelin in the central nervous system. Cell 1996, 85, 299-302.
    • (1996) Cell , vol.85 , pp. 299-302
    • Steinman, L.1
  • 5
    • 0027333348 scopus 로고
    • Tickling the TCR: Selective T-cell functions stimulated by altered peptide ligands
    • Evavold, B. D.; Sloan-Lancaster, J.; Allen, P. M. Tickling the TCR: selective T-cell functions stimulated by altered peptide ligands. Immunol. Today 1993, 14, 602-609.
    • (1993) Immunol. Today , vol.14 , pp. 602-609
    • Evavold, B.D.1    Sloan-Lancaster, J.2    Allen, P.M.3
  • 6
    • 0026434554 scopus 로고
    • Separation of IL-4 production from Th cell proliferation by an altered T cell receptor ligand
    • Evavold, B. D.; Allen, P. M. Separation of IL-4 production from Th cell proliferation by an altered T cell receptor ligand. Science 1991, 252, 1308-1310.
    • (1991) Science , vol.252 , pp. 1308-1310
    • Evavold, B.D.1    Allen, P.M.2
  • 7
    • 51249090471 scopus 로고    scopus 로고
    • T helper cell type 1 (Th1), Th2 and Th17 responses to myelin basic protein and disease activity in multiple sclerosis
    • Hedegaard, C. J.; Krakauer, M.; Bendtzen, K.; Lund, H.; Sellebjerg, F.; Nielsen, C. H. T helper cell type 1 (Th1), Th2 and Th17 responses to myelin basic protein and disease activity in multiple sclerosis. Immunology 2008, 125, 161-169.
    • (2008) Immunology , vol.125 , pp. 161-169
    • Hedegaard, C.J.1    Krakauer, M.2    Bendtzen, K.3    Lund, H.4    Sellebjerg, F.5    Nielsen, C.H.6
  • 8
    • 46849118301 scopus 로고    scopus 로고
    • Design of novel cyclic altered peptide ligands of myelin basic protein MBP83-99 that modulate immune responses in SJL/J mice
    • Katsara, M.; Deraos, G.; Tselios, T.; Matsoukas, J.; Apostolopoulos, V. Design of novel cyclic altered peptide ligands of myelin basic protein MBP83-99 that modulate immune responses in SJL/J mice. J. Med. Chem. 2008, 51, 3971-3978.
    • (2008) J. Med. Chem , vol.51 , pp. 3971-3978
    • Katsara, M.1    Deraos, G.2    Tselios, T.3    Matsoukas, J.4    Apostolopoulos, V.5
  • 12
    • 0033679767 scopus 로고    scopus 로고
    • Degano, M.; Garcia, K. C.; Apostolopoulos, V.; Rudolph, M. G.; Teyton, L.; Wilson, I. A. A functional hot spot for antigen recognition in a superagonist TCR/MHC complex. Immunity 2000, 12, 251-261.
    • Degano, M.; Garcia, K. C.; Apostolopoulos, V.; Rudolph, M. G.; Teyton, L.; Wilson, I. A. A functional hot spot for antigen recognition in a superagonist TCR/MHC complex. Immunity 2000, 12, 251-261.
  • 13
    • 0034235460 scopus 로고    scopus 로고
    • Altered peptide ligand-mediated TCR antagonism can be modulated by a change in a single amino acid residue within the CDR3 beta of an MHC class I-restricted TCR
    • Kalergis, A. M.; Nathenson, S. G. Altered peptide ligand-mediated TCR antagonism can be modulated by a change in a single amino acid residue within the CDR3 beta of an MHC class I-restricted TCR. J. Immunol. 2000, 165, 280-285.
    • (2000) J. Immunol , vol.165 , pp. 280-285
    • Kalergis, A.M.1    Nathenson, S.G.2
  • 14
    • 0035869451 scopus 로고    scopus 로고
    • A structural difference limited to one residue of the antigenic peptide can profoundly alter the biological outcome of the TCR-peptide/MHC class I interaction
    • Thomson, C. T.; Kalergis, A. M.; Sacchettini, J. C.; Nathenson, S. G. A structural difference limited to one residue of the antigenic peptide can profoundly alter the biological outcome of the TCR-peptide/MHC class I interaction. J. Immunol. 2001, 166, 3994-3997.
    • (2001) J. Immunol , vol.166 , pp. 3994-3997
    • Thomson, C.T.1    Kalergis, A.M.2    Sacchettini, J.C.3    Nathenson, S.G.4
  • 15
    • 0033786776 scopus 로고    scopus 로고
    • Encephalitogenic potential of the myelin basic protein peptide (amino acids 83-99) in multiple sclerosis: Results of a phase II clinical trial with an altered peptide ligand
    • Bielekova, B.; Goodwin, B.; Richert, N.; Cortese, I.; Kondo, T.; Afshar, G.; Gran, B.; Eaton, J.; Antel, J.; Frank, J. A.; McFarland, H. F.; Martin, R. Encephalitogenic potential of the myelin basic protein peptide (amino acids 83-99) in multiple sclerosis: results of a phase II clinical trial with an altered peptide ligand. Nat. Med. 2000, 6, 1167-1175.
    • (2000) Nat. Med , vol.6 , pp. 1167-1175
    • Bielekova, B.1    Goodwin, B.2    Richert, N.3    Cortese, I.4    Kondo, T.5    Afshar, G.6    Gran, B.7    Eaton, J.8    Antel, J.9    Frank, J.A.10    McFarland, H.F.11    Martin, R.12
  • 16
    • 0033762708 scopus 로고    scopus 로고
    • NBI-5788, an altered MBP83-99 peptide, induces a T-helper 2-like immune response in multiple sclerosis patients
    • Crowe, P. D.; Qin, Y.; Conlon, P. J.; Antel, J. P. NBI-5788, an altered MBP83-99 peptide, induces a T-helper 2-like immune response in multiple sclerosis patients. Ann. Neurol. 2000, 48, 758-765.
    • (2000) Ann. Neurol , vol.48 , pp. 758-765
    • Crowe, P.D.1    Qin, Y.2    Conlon, P.J.3    Antel, J.P.4
  • 17
    • 0033791462 scopus 로고    scopus 로고
    • Induction of a non-encephalitogenic type 2 T helper-cell autoimmune response in multiple sclerosis after administration of an altered peptide ligand in a placebo-controlled, randomized phase II trial. The Altered Peptide Ligand in Relapsing MS Study Group
    • Kappos, L.; Comi, G.; Panitch, H.; Oger, J.; Antel, J.; Conlon, P.; Steinman, L. Induction of a non-encephalitogenic type 2 T helper-cell autoimmune response in multiple sclerosis after administration of an altered peptide ligand in a placebo-controlled, randomized phase II trial. The Altered Peptide Ligand in Relapsing MS Study Group. Nat. Med. 2000, 6, 1176-1182.
    • (2000) Nat. Med , vol.6 , pp. 1176-1182
    • Kappos, L.1    Comi, G.2    Panitch, H.3    Oger, J.4    Antel, J.5    Conlon, P.6    Steinman, L.7
  • 18
    • 0036046080 scopus 로고    scopus 로고
    • Persistence of immune responses to altered and native myelin antigens in patients with multiple sclerosis treated with altered peptide ligand
    • Kim, H. J.; Antel, J. P.; Duquette, P.; Alleva, D. G.; Conlon, P. J.; Bar-Or, A. Persistence of immune responses to altered and native myelin antigens in patients with multiple sclerosis treated with altered peptide ligand. Clin. Immunol. 2002, 104, 105-114.
    • (2002) Clin. Immunol , vol.104 , pp. 105-114
    • Kim, H.J.1    Antel, J.P.2    Duquette, P.3    Alleva, D.G.4    Conlon, P.J.5    Bar-Or, A.6
  • 20
    • 0033535525 scopus 로고    scopus 로고
    • Design and synthesis of a potent cyclic analogue of the myelin basic protein epitope MBP72-85: Importance of the Ala81 carboxyl group and of a cyclic conformation for induction of experimental allergic encephalomyelitis
    • Tselios, T.; Probert, L.; Daliani, I.; Matsoukas, E.; Troganis, A.; Gerothanassis, I. P.; Mavromoustakos, T.; Moore, G. J.; Matsoukas, J. M. Design and synthesis of a potent cyclic analogue of the myelin basic protein epitope MBP72-85: importance of the Ala81 carboxyl group and of a cyclic conformation for induction of experimental allergic encephalomyelitis. J. Med. Chem. 1999, 42, 1170-1177.
    • (1999) J. Med. Chem , vol.42 , pp. 1170-1177
    • Tselios, T.1    Probert, L.2    Daliani, I.3    Matsoukas, E.4    Troganis, A.5    Gerothanassis, I.P.6    Mavromoustakos, T.7    Moore, G.J.8    Matsoukas, J.M.9
  • 22
    • 0033866356 scopus 로고    scopus 로고
    • Treatment of experimental allergic encephalomyelitis (EAE) induced by guinea pig myelin basic protein epitope 72-85 with a human MBP(87-99) analogue and effects of cyclic peptides
    • Tselios, T.; Daliani, I.; Probert, L.; Deraos, S.; Matsoukas, E.; Roy, S.; Pires, J.; Moore, G.; Matsoukas, J. Treatment of experimental allergic encephalomyelitis (EAE) induced by guinea pig myelin basic protein epitope 72-85 with a human MBP(87-99) analogue and effects of cyclic peptides. Bioorg. Med. Chem. 2000, 8, 1903-1909.
    • (2000) Bioorg. Med. Chem , vol.8 , pp. 1903-1909
    • Tselios, T.1    Daliani, I.2    Probert, L.3    Deraos, S.4    Matsoukas, E.5    Roy, S.6    Pires, J.7    Moore, G.8    Matsoukas, J.9
  • 25
    • 0034625091 scopus 로고    scopus 로고
    • Deimination of myelin basic protein. 1. Effect of deimination of arginyl residues of myelin basic protein on its structure and susceptibility to digestion by cathepsin D
    • Pritzker, L. B.; Joshi, S.; Gowan, J. J.; Harauz, G.; Moscarello, M. A. Deimination of myelin basic protein. 1. Effect of deimination of arginyl residues of myelin basic protein on its structure and susceptibility to digestion by cathepsin D. Biochemistry 2000, 39, 5374-5381.
    • (2000) Biochemistry , vol.39 , pp. 5374-5381
    • Pritzker, L.B.1    Joshi, S.2    Gowan, J.J.3    Harauz, G.4    Moscarello, M.A.5
  • 26
    • 0034625146 scopus 로고    scopus 로고
    • Deimination of myelin basic protein. 2. Effect of methylation of MBP on its deimination by peptidylarginine deiminase
    • Pritzker, L. B.; Joshi, S.; Harauz, G.; Moscarello, M. A. Deimination of myelin basic protein. 2. Effect of methylation of MBP on its deimination by peptidylarginine deiminase. Biochemistry 2000, 39, 5382-5388.
    • (2000) Biochemistry , vol.39 , pp. 5382-5388
    • Pritzker, L.B.1    Joshi, S.2    Harauz, G.3    Moscarello, M.A.4
  • 27
    • 0033845902 scopus 로고    scopus 로고
    • Enhanced T cell responsiveness to citrulline-containing myelin basic protein in multiple sclerosis patients
    • Tranquill, L. R.; Cao, L.; Ling, N. C.; Kalbacher, H.; Martin, R. M.; Whitaker, J. N. Enhanced T cell responsiveness to citrulline-containing myelin basic protein in multiple sclerosis patients. Mult. Scler. 2000, 6, 220-225.
    • (2000) Mult. Scler , vol.6 , pp. 220-225
    • Tranquill, L.R.1    Cao, L.2    Ling, N.C.3    Kalbacher, H.4    Martin, R.M.5    Whitaker, J.N.6
  • 28
    • 0028091406 scopus 로고
    • Citrulline-containing myelin basic protein is recognized by T-cell lines derived from multiple sclerosis patients and healthy individuals
    • Martin, R.; Whitaker, J. N.; Rhame, L.; Goodin, R. R.; McFarland, H. F. Citrulline-containing myelin basic protein is recognized by T-cell lines derived from multiple sclerosis patients and healthy individuals. Neurology 1994, 44, 123-129.
    • (1994) Neurology , vol.44 , pp. 123-129
    • Martin, R.1    Whitaker, J.N.2    Rhame, L.3    Goodin, R.R.4    McFarland, H.F.5
  • 29
    • 0032578555 scopus 로고    scopus 로고
    • Expression and crystallization of the complex of HLA-DR2 (DRA, DRB1*1501) and an immunodominant peptide of human myelin basic protein
    • Gauthier, L.; Smith, K. J.; Pyrdol, J.; Kalandadze, A.; Strominger, J. L.; Wiley, D. C.; Wucherpfennig, K. W. Expression and crystallization of the complex of HLA-DR2 (DRA, DRB1*1501) and an immunodominant peptide of human myelin basic protein. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 11828-11833.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 11828-11833
    • Gauthier, L.1    Smith, K.J.2    Pyrdol, J.3    Kalandadze, A.4    Strominger, J.L.5    Wiley, D.C.6    Wucherpfennig, K.W.7
  • 30
    • 0032547858 scopus 로고    scopus 로고
    • Crystal structure of HLA-DR2 (DRA*0101, DRB1*1501) complexed with a peptide from human myelin basic protein
    • Smith, K. J.; Pyrdol, J.; Gauthier, L.; Wiley, D. C.; Wucherpfennig, K. W. Crystal structure of HLA-DR2 (DRA*0101, DRB1*1501) complexed with a peptide from human myelin basic protein. J. Exp. Med. 1998, 188, 1511-1520.
    • (1998) J. Exp. Med , vol.188 , pp. 1511-1520
    • Smith, K.J.1    Pyrdol, J.2    Gauthier, L.3    Wiley, D.C.4    Wucherpfennig, K.W.5
  • 31
    • 0029074729 scopus 로고
    • Structure of human T-cell receptors specific for an immunodominant myelin basic protein peptide: Positioning of T-cell receptors on HLA-DR2/peptide complexes
    • Wucherpfennig, K. W.; Hafler, D. A.; Strominger, J. L. Structure of human T-cell receptors specific for an immunodominant myelin basic protein peptide: positioning of T-cell receptors on HLA-DR2/peptide complexes. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 8896-8900.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 8896-8900
    • Wucherpfennig, K.W.1    Hafler, D.A.2    Strominger, J.L.3
  • 32
    • 18244392426 scopus 로고    scopus 로고
    • Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor
    • Hahn, M.; Nicholson, M. J.; Pyrdol, J.; Wucherpfennig, K. W. Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor. Nat. Immunol. 2005, 6, 490-496.
    • (2005) Nat. Immunol , vol.6 , pp. 490-496
    • Hahn, M.1    Nicholson, M.J.2    Pyrdol, J.3    Wucherpfennig, K.W.4
  • 33
    • 0000190904 scopus 로고
    • The carbamido diacetyl reaction: A test for citrulline
    • Fearon, W. R. The carbamido diacetyl reaction: a test for citrulline. Biochem. J. 1939, 33, 902-907.
    • (1939) Biochem. J , vol.33 , pp. 902-907
    • Fearon, W.R.1
  • 34
    • 0033567008 scopus 로고    scopus 로고
    • Highly deiminated isoform of myelin basic protein from multiple sclerosis brain causes fragmentation of lipid vesicles
    • Boggs, J. M.; Rangaraj, G.; Koshy, K. M.; Ackerley, C.; Wood, D. D.; Moscarello, M. A. Highly deiminated isoform of myelin basic protein from multiple sclerosis brain causes fragmentation of lipid vesicles. J. Neurosci. Res. 1999, 57, 529-535.
    • (1999) J. Neurosci. Res , vol.57 , pp. 529-535
    • Boggs, J.M.1    Rangaraj, G.2    Koshy, K.M.3    Ackerley, C.4    Wood, D.D.5    Moscarello, M.A.6
  • 35
    • 33745331328 scopus 로고    scopus 로고
    • Gyorgy, B.; Toth, E.; Tarcsa, E.; Falus, A.; Buzas, E. I. Citrullination: a posttranslational modification in health and disease. Int. J. Biochem. Cell Biol. 2006, 38, 1662-1677.
    • Gyorgy, B.; Toth, E.; Tarcsa, E.; Falus, A.; Buzas, E. I. Citrullination: a posttranslational modification in health and disease. Int. J. Biochem. Cell Biol. 2006, 38, 1662-1677.
  • 37
    • 42149104690 scopus 로고    scopus 로고
    • Rheumatoid factor and anti-CCP autoantibodies in rheumatoid arthritis: A review
    • Lee, A. N.; Beck, C. E.; Hall, M. Rheumatoid factor and anti-CCP autoantibodies in rheumatoid arthritis: a review. Clin. Lab. Sci. 2008, 21, 15-18.
    • (2008) Clin. Lab. Sci , vol.21 , pp. 15-18
    • Lee, A.N.1    Beck, C.E.2    Hall, M.3
  • 38
    • 33746214870 scopus 로고    scopus 로고
    • Cutting edge: Unique T cells that recognize citrullinated peptides are a feature of protein immunization
    • Ireland, J.; Herzog, J.; Unanue, E. R. Cutting edge: unique T cells that recognize citrullinated peptides are a feature of protein immunization. J. Immunol. 2006, 177, 1421-1425.
    • (2006) J. Immunol , vol.177 , pp. 1421-1425
    • Ireland, J.1    Herzog, J.2    Unanue, E.R.3
  • 39
    • 0038107566 scopus 로고    scopus 로고
    • Cutting edge: The conversion of arginine to citrulline allows for a high-affinity peptide interaction with the rheumatoid arthritis-associated HLA-DRB1*0401 MHC class II molecule
    • Hill, J. A.; Southwood, S.; Sette, A.; Jevnikar, A. M.; Bell, D. A.; Cairns, E. Cutting edge: the conversion of arginine to citrulline allows for a high-affinity peptide interaction with the rheumatoid arthritis-associated HLA-DRB1*0401 MHC class II molecule. J. Immunol. 2003, 171, 538-541.
    • (2003) J. Immunol , vol.171 , pp. 538-541
    • Hill, J.A.1    Southwood, S.2    Sette, A.3    Jevnikar, A.M.4    Bell, D.A.5    Cairns, E.6
  • 40
    • 33846914679 scopus 로고    scopus 로고
    • The role of citrullinated proteins suggests a novel mechanism in the pathogenesis of multiple sclerosis
    • Moscarello, M. A.; Mastronardi, F. G.; Wood, D. D. The role of citrullinated proteins suggests a novel mechanism in the pathogenesis of multiple sclerosis. Neurochem. Res. 2007, 32, 251-256.
    • (2007) Neurochem. Res , vol.32 , pp. 251-256
    • Moscarello, M.A.1    Mastronardi, F.G.2    Wood, D.D.3
  • 41
    • 0032146341 scopus 로고    scopus 로고
    • Citrullinated myelin basic protein induces experimental autoimmune encephalomyelitis in Lewis rats through a diverse T cell repertoire
    • Cao, L.; Sun, D.; Whitaker, J. N. Citrullinated myelin basic protein induces experimental autoimmune encephalomyelitis in Lewis rats through a diverse T cell repertoire. J. Neuroimmunol. 1998, 88, 21-29.
    • (1998) J. Neuroimmunol , vol.88 , pp. 21-29
    • Cao, L.1    Sun, D.2    Whitaker, J.N.3
  • 42
    • 0142234077 scopus 로고    scopus 로고
    • Multiple sclerosis: An important role for post-translational modifications of myelin basic protein in pathogenesis
    • Kim, J. K.; Mastronardi, F. G.; Wood, D. D.; Lubman, D. M.; Zand, R.; Moscarello, M. A. Multiple sclerosis: an important role for post-translational modifications of myelin basic protein in pathogenesis. Mol. Cell. Proteomics 2003, 2, 453-462.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 453-462
    • Kim, J.K.1    Mastronardi, F.G.2    Wood, D.D.3    Lubman, D.M.4    Zand, R.5    Moscarello, M.A.6
  • 43
    • 33846927285 scopus 로고    scopus 로고
    • A tale of two citrullines - structural and functional aspects of myelin basic protein deimination in health and disease
    • Harauz, G.; Musse, A. A. A tale of two citrullines - structural and functional aspects of myelin basic protein deimination in health and disease. Neurochem. Res. 2007, 32, 137-158.
    • (2007) Neurochem. Res , vol.32 , pp. 137-158
    • Harauz, G.1    Musse, A.A.2
  • 44
    • 0024567052 scopus 로고
    • The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein
    • Wood, D. D.; Moscarello, M. A. The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein. J. Biol. Chem. 1989, 264, 5121-5127.
    • (1989) J. Biol. Chem , vol.264 , pp. 5121-5127
    • Wood, D.D.1    Moscarello, M.A.2
  • 45
    • 17844386546 scopus 로고    scopus 로고
    • Citrullination of central nervous system proteins during the development of experimental autoimmune encephalomyelitis
    • Raijmakers, R.; Vogelzangs, J.; Croxford, J. L.; Wesseling, P.; van Venrooij, W. J.; Pruijn, G. J. Citrullination of central nervous system proteins during the development of experimental autoimmune encephalomyelitis. J. Comp. Neurol. 2005, 486, 243-253.
    • (2005) J. Comp. Neurol , vol.486 , pp. 243-253
    • Raijmakers, R.1    Vogelzangs, J.2    Croxford, J.L.3    Wesseling, P.4    van Venrooij, W.J.5    Pruijn, G.J.6
  • 46
    • 0028906889 scopus 로고
    • Patterns of cytokine secretion by autoreactive proteolipid protein-specific T cell clones during the course of multiple sclerosis
    • Correale, J.; Gilmore, W.; McMillan, M.; Li, S.; McCarthy, K.; Le, T.; Weiner, L. P. Patterns of cytokine secretion by autoreactive proteolipid protein-specific T cell clones during the course of multiple sclerosis. J. Immunol. 1995, 154, 2959-2968.
    • (1995) J. Immunol , vol.154 , pp. 2959-2968
    • Correale, J.1    Gilmore, W.2    McMillan, M.3    Li, S.4    McCarthy, K.5    Le, T.6    Weiner, L.P.7
  • 47
    • 0038278670 scopus 로고    scopus 로고
    • Role of interleukin-10 in the induction and function of natural and antigen-induced regulatory T cells
    • Wraith, D. C. Role of interleukin-10 in the induction and function of natural and antigen-induced regulatory T cells. J. Autoimmun. 2003, 20, 273-275.
    • (2003) J. Autoimmun , vol.20 , pp. 273-275
    • Wraith, D.C.1
  • 48
    • 33748316568 scopus 로고    scopus 로고
    • Regulatory T-cells: Immunomodulators in health and disease
    • Scalzo, K.; Plebanski, M.; Apostolopoulos, V. Regulatory T-cells: immunomodulators in health and disease. Curr. Top. Med. Chem. 2006, 6, 1759-1768.
    • (2006) Curr. Top. Med. Chem , vol.6 , pp. 1759-1768
    • Scalzo, K.1    Plebanski, M.2    Apostolopoulos, V.3
  • 49
    • 37849037724 scopus 로고    scopus 로고
    • Putative bioactive conformations of amide linked cyclic myelin basic protein peptide analogues associated with experimental autoimmune encephalomyelitis
    • Spyranti, Z.; Dalkas, G. A.; Spyroulias, G. A.; Mantzourani, E. D.; Mavromoustakos, T.; Friligou, I.; Matsoukas, J. M.; Tselios, T. V. Putative bioactive conformations of amide linked cyclic myelin basic protein peptide analogues associated with experimental autoimmune encephalomyelitis. J. Med. Chem. 2007, 50, 6039-6047.
    • (2007) J. Med. Chem , vol.50 , pp. 6039-6047
    • Spyranti, Z.1    Dalkas, G.A.2    Spyroulias, G.A.3    Mantzourani, E.D.4    Mavromoustakos, T.5    Friligou, I.6    Matsoukas, J.M.7    Tselios, T.V.8
  • 50
    • 33748599264 scopus 로고    scopus 로고
    • A putative bioactive conformation for the altered peptide ligand of myelin basic protein and inhibitor of experimental autoimmune encephalomyelitis [Arg91, Ala96] MBP87-99
    • Mantzourani, E. D.; Tselios, T. V.; Grdadolnik, S. G.; Brancale, A.; Platts, J. A.; Matsoukas, J. M.; Mavromoustakos, T. M. A putative bioactive conformation for the altered peptide ligand of myelin basic protein and inhibitor of experimental autoimmune encephalomyelitis [Arg91, Ala96] MBP87-99. J. Mol. Graphics Modell. 2006, 25, 17-29.
    • (2006) J. Mol. Graphics Modell , vol.25 , pp. 17-29
    • Mantzourani, E.D.1    Tselios, T.V.2    Grdadolnik, S.G.3    Brancale, A.4    Platts, J.A.5    Matsoukas, J.M.6    Mavromoustakos, T.M.7
  • 51
    • 34548306797 scopus 로고    scopus 로고
    • Molecular dynamics at the receptor level of immunodominant myelin basic protein epitope 87-99 implicated in multiple sclerosis and its antagonists altered peptide ligands: Triggering of immune response
    • Mantzourani, E. D.; Platts, J. A.; Brancale, A.; Mavromoustakos, T. M.; Tselios, T. V. Molecular dynamics at the receptor level of immunodominant myelin basic protein epitope 87-99 implicated in multiple sclerosis and its antagonists altered peptide ligands: triggering of immune response. J. Mol. Graphics Modell. 2007, 26, 471-481.
    • (2007) J. Mol. Graphics Modell , vol.26 , pp. 471-481
    • Mantzourani, E.D.1    Platts, J.A.2    Brancale, A.3    Mavromoustakos, T.M.4    Tselios, T.V.5
  • 52
    • 33751015761 scopus 로고    scopus 로고
    • Comparison of proposed putative active conformations of myelin basic protein epitope 87-99 linear altered peptide ligands by spectroscopic and modelling studies: The role of positions 91 and 96 in T-cell receptor activation
    • Mantzourani, E. D.; Tselios, T. V.; Grdadolnik, S. G.; Platts, J. A.; Brancale, A.; Deraos, G. N.; Matsoukas, J. M.; Mavromoustakos, T. M. Comparison of proposed putative active conformations of myelin basic protein epitope 87-99 linear altered peptide ligands by spectroscopic and modelling studies: the role of positions 91 and 96 in T-cell receptor activation. J. Med. Chem. 2006, 49, 6683-6691.
    • (2006) J. Med. Chem , vol.49 , pp. 6683-6691
    • Mantzourani, E.D.1    Tselios, T.V.2    Grdadolnik, S.G.3    Platts, J.A.4    Brancale, A.5    Deraos, G.N.6    Matsoukas, J.M.7    Mavromoustakos, T.M.8
  • 53
    • 0021117698 scopus 로고
    • Citrulline in proteins from the enzymatic deimination of arginine residues
    • Rothnagel, J. A.; Rogers, G. E. Citrulline in proteins from the enzymatic deimination of arginine residues. Methods Enzymol. 1984, 107, 624-631.
    • (1984) Methods Enzymol , vol.107 , pp. 624-631
    • Rothnagel, J.A.1    Rogers, G.E.2
  • 55
    • 33645408056 scopus 로고    scopus 로고
    • Balancing solvation and intramolecular interactions: Toward a consistent generalized Born force field
    • Chen, J.; Im, W.; Brooks, C. L. Balancing solvation and intramolecular interactions: toward a consistent generalized Born force field. J. Am. Chem. Soc. 2006, 128, 3728-3736.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 3728-3736
    • Chen, J.1    Im, W.2    Brooks, C.L.3
  • 56
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J.-P.; Ciccotti, G.; Berendsen, H. J. C. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 1977, 23, 327-341.
    • (1977) J. Comput. Phys , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.