메뉴 건너뛰기




Volumn 272, Issue 1, 2016, Pages 151-168

Mechanistic understanding and significance of small peptides interaction with MHC class II molecules for therapeutic applications

Author keywords

antigen presentation; MHC class II molecules; MHC loading enhancers; small peptides

Indexed keywords

DIPEPTIDE; HLA DM ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PEPTIDE;

EID: 84975527586     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/imr.12435     Document Type: Review
Times cited : (17)

References (185)
  • 1
    • 40249118205 scopus 로고    scopus 로고
    • Crossreactive T cells spotlight the germline rules for αβ T cell-receptor interactions with MHC molecules
    • Dai S, et al. Crossreactive T cells spotlight the germline rules for αβ T cell-receptor interactions with MHC molecules. Immunity 2008;28:324–334.
    • (2008) Immunity , vol.28 , pp. 324-334
    • Dai, S.1
  • 2
    • 22744441535 scopus 로고    scopus 로고
    • How the T cell repertoire becomes peptide and MHC specific
    • Huseby ES, et al. How the T cell repertoire becomes peptide and MHC specific. Cell 2005;122:247–260.
    • (2005) Cell , vol.122 , pp. 247-260
    • Huseby, E.S.1
  • 3
    • 77954723327 scopus 로고    scopus 로고
    • + T cells elicit host immune responses to MHC class II – ovarian cancer through CCL5 secretion and CD40-mediated licensing of dendritic cells
    • + T cells elicit host immune responses to MHC class II – ovarian cancer through CCL5 secretion and CD40-mediated licensing of dendritic cells. J Immunol 2010;184:5654–5662.
    • (2010) J Immunol , vol.184 , pp. 5654-5662
    • Nesbeth, Y.C.1
  • 5
    • 0028215537 scopus 로고
    • T cell deletion in high antigen dose therapy of autoimmune encephalomyelitis
    • Critchfield JM, et al. T cell deletion in high antigen dose therapy of autoimmune encephalomyelitis. Science 1994;263:1139–1143.
    • (1994) Science , vol.263 , pp. 1139-1143
    • Critchfield, J.M.1
  • 6
    • 0030200438 scopus 로고    scopus 로고
    • Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins
    • Kim E, Cho K-O, Rothschild A, Sheng M. Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins. Neuron 1996;17:103–113.
    • (1996) Neuron , vol.17 , pp. 103-113
    • Kim, E.1    Cho, K.-O.2    Rothschild, A.3    Sheng, M.4
  • 7
    • 0026078307 scopus 로고
    • Development of the CD4 and CD8 lineage of T-cells – instruction versus selection
    • Borgulya P, Kishi H, Muller U, Kirberg J, Vonboehmer H. Development of the CD4 and CD8 lineage of T-cells – instruction versus selection. EMBO J 1991;10:913–918.
    • (1991) EMBO J , vol.10 , pp. 913-918
    • Borgulya, P.1    Kishi, H.2    Muller, U.3    Kirberg, J.4    Vonboehmer, H.5
  • 8
    • 0035425004 scopus 로고    scopus 로고
    • B7 interactions with CD28 and CTLA-4 control tolerance or induction of mucosal inflammation in chronic experimental colitis
    • Liu ZJ, et al. B7 interactions with CD28 and CTLA-4 control tolerance or induction of mucosal inflammation in chronic experimental colitis. J Immunol 2001;167:1830–1838.
    • (2001) J Immunol , vol.167 , pp. 1830-1838
    • Liu, Z.J.1
  • 9
    • 0030061494 scopus 로고    scopus 로고
    • Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area
    • Dustin ML, Ferguson LM, Chan PY, Springer TA, Golan DE. Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area. J Cell Biol 1996;132:465–474.
    • (1996) J Cell Biol , vol.132 , pp. 465-474
    • Dustin, M.L.1    Ferguson, L.M.2    Chan, P.Y.3    Springer, T.A.4    Golan, D.E.5
  • 10
    • 0029864882 scopus 로고    scopus 로고
    • Conformational changes induced in the protein tyrosine kinase p72(syk) by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides
    • Kimura T, Sakamoto H, Appella E, Siraganian RP. Conformational changes induced in the protein tyrosine kinase p72(syk) by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides. Mol Cell Biol 1996;16:1471–1478.
    • (1996) Mol Cell Biol , vol.16 , pp. 1471-1478
    • Kimura, T.1    Sakamoto, H.2    Appella, E.3    Siraganian, R.P.4
  • 11
    • 0034254791 scopus 로고    scopus 로고
    • Redundant and opposing functions of two tyrosine kinases, Btk and Lyn, in mast cell activation
    • Kawakami Y, et al. Redundant and opposing functions of two tyrosine kinases, Btk and Lyn, in mast cell activation. J Immunol 2000;165:1210–1219.
    • (2000) J Immunol , vol.165 , pp. 1210-1219
    • Kawakami, Y.1
  • 12
    • 46349107222 scopus 로고    scopus 로고
    • Anchor side chains of short peptide fragments trigger ligand-exchange of class II MHC molecules
    • Gupta S, et al. Anchor side chains of short peptide fragments trigger ligand-exchange of class II MHC molecules. PLoS ONE 2008;3:e1814.
    • (2008) PLoS ONE , vol.3
    • Gupta, S.1
  • 13
    • 33748475526 scopus 로고    scopus 로고
    • Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis
    • Delamarre L, Couture R, Mellman I, Trombetta ES. Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis. J Exp Med 2006;203:2049–2055.
    • (2006) J Exp Med , vol.203 , pp. 2049-2055
    • Delamarre, L.1    Couture, R.2    Mellman, I.3    Trombetta, E.S.4
  • 14
    • 84975463421 scopus 로고    scopus 로고
    • Differential lysosomal proteolysis in antigen presenting cells determines antigen fate and immunogenicity
    • Delamarre L, Mellman OI, Trombetta S. Differential lysosomal proteolysis in antigen presenting cells determines antigen fate and immunogenicity. Cell Struct Funct 2005;30:74.
    • (2005) Cell Struct Funct , vol.30 , pp. 74
    • Delamarre, L.1    Mellman, O.I.2    Trombetta, S.3
  • 15
    • 0025014816 scopus 로고
    • Co-localization of molecules involved in antigen processing and presentation in an early endocytic compartment
    • Guagliardi LE, Koppelman B, Blum JS, Marks MS, Cresswell P, Brodsky FM. Co-localization of molecules involved in antigen processing and presentation in an early endocytic compartment. Nature 1990;343:133–139.
    • (1990) Nature , vol.343 , pp. 133-139
    • Guagliardi, L.E.1    Koppelman, B.2    Blum, J.S.3    Marks, M.S.4    Cresswell, P.5    Brodsky, F.M.6
  • 16
    • 0025286210 scopus 로고
    • Quantitation of antigen-presenting cell MHC class II/peptide complexes necessary for T-cell stimulation
    • Harding CV, Unanue ER. Quantitation of antigen-presenting cell MHC class II/peptide complexes necessary for T-cell stimulation. Nature 1990;346:574–576.
    • (1990) Nature , vol.346 , pp. 574-576
    • Harding, C.V.1    Unanue, E.R.2
  • 17
    • 0025324091 scopus 로고
    • Structure, function, and diversity of class I major histocompatibility complex molecules
    • Bjorkman PJ, Parham P. Structure, function, and diversity of class I major histocompatibility complex molecules. Annu Rev Biochem 1990;59:253–288.
    • (1990) Annu Rev Biochem , vol.59 , pp. 253-288
    • Bjorkman, P.J.1    Parham, P.2
  • 18
    • 0033581935 scopus 로고    scopus 로고
    • Selecting and maintaining a diverse T-cell repertoire
    • Goldrath AW, Bevan MJ. Selecting and maintaining a diverse T-cell repertoire. Nature 1999;402:255–262.
    • (1999) Nature , vol.402 , pp. 255-262
    • Goldrath, A.W.1    Bevan, M.J.2
  • 19
    • 33846018428 scopus 로고    scopus 로고
    • Small organic compounds enhance antigen loading of class II major histocompatibility complex proteins by targeting the polymorphic P1 pocket
    • Hoepner S, et al. Small organic compounds enhance antigen loading of class II major histocompatibility complex proteins by targeting the polymorphic P1 pocket. J Biol Chem 2006;281:38535–38542.
    • (2006) J Biol Chem , vol.281 , pp. 38535-38542
    • Hoepner, S.1
  • 20
    • 0036170875 scopus 로고    scopus 로고
    • The scent of genetic compatibility: sexual selection and the major histocompatibility complex
    • Penn DJ. The scent of genetic compatibility: sexual selection and the major histocompatibility complex. Ethology 2002;108:1–21.
    • (2002) Ethology , vol.108 , pp. 1-21
    • Penn, D.J.1
  • 21
    • 84867491795 scopus 로고    scopus 로고
    • MHC-based vaccination approaches: progress and perspectives
    • Mehra NK, Kaur G. MHC-based vaccination approaches: progress and perspectives. Expert Rev Mol Med 2003;5:1–17.
    • (2003) Expert Rev Mol Med , vol.5 , pp. 1-17
    • Mehra, N.K.1    Kaur, G.2
  • 22
    • 84961606289 scopus 로고    scopus 로고
    • Histocompatibility antigens
    • Mehra NK. Histocompatibility antigens. Encyclopedia Life Sci 2001. doi:10.1038/npg.els.0001234.
    • (2001) Encyclopedia Life Sci
    • Mehra, N.K.1
  • 23
    • 0034214403 scopus 로고    scopus 로고
    • Peptide and peptide mimetic inhibitors of antigen presentation by HLA-DR class II MHC molecules. Design, structure-activity relationships, and X-ray crystal structures
    • Bolin DR, et al. Peptide and peptide mimetic inhibitors of antigen presentation by HLA-DR class II MHC molecules. Design, structure-activity relationships, and X-ray crystal structures. J Med Chem 2000;43:2135–2148.
    • (2000) J Med Chem , vol.43 , pp. 2135-2148
    • Bolin, D.R.1
  • 24
    • 0031051784 scopus 로고    scopus 로고
    • MHC class I and class II structures
    • Jones EY. MHC class I and class II structures. Curr Opin Immunol 1997;9:75–79.
    • (1997) Curr Opin Immunol , vol.9 , pp. 75-79
    • Jones, E.Y.1
  • 25
    • 67650424362 scopus 로고    scopus 로고
    • A short history of HLA
    • Thorsby E. A short history of HLA. Tissue Antigens 2009;74:101–116.
    • (2009) Tissue Antigens , vol.74 , pp. 101-116
    • Thorsby, E.1
  • 26
    • 5044232231 scopus 로고    scopus 로고
    • Conformational flexibility of the MHC class I alpha(1)-alpha(2) domain in peptide bound and free states: a molecular dynamics simulation study
    • Zacharias M, Springer S. Conformational flexibility of the MHC class I alpha(1)-alpha(2) domain in peptide bound and free states: a molecular dynamics simulation study. Biophys J 2004;87:2203–2214.
    • (2004) Biophys J , vol.87 , pp. 2203-2214
    • Zacharias, M.1    Springer, S.2
  • 28
    • 72949086403 scopus 로고    scopus 로고
    • Peptide binding to MHC class I and II proteins: new avenues from new methods
    • Yaneva R, Schneeweiss C, Zacharias M, Springer S. Peptide binding to MHC class I and II proteins: new avenues from new methods. Mol Immunol 2010;47:649–657.
    • (2010) Mol Immunol , vol.47 , pp. 649-657
    • Yaneva, R.1    Schneeweiss, C.2    Zacharias, M.3    Springer, S.4
  • 30
    • 0027217789 scopus 로고
    • Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1
    • Brown JH, et al. Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1. Nature 1993;364:33.
    • (1993) Nature , vol.364 , pp. 33
    • Brown, J.H.1
  • 33
    • 80051918929 scopus 로고    scopus 로고
    • Small molecule modulators of MHC class II antigen presentation: mechanistic insights and implications for therapeutic application
    • Call MJ. Small molecule modulators of MHC class II antigen presentation: mechanistic insights and implications for therapeutic application. Mol Immunol 2011;48:1735–1743.
    • (2011) Mol Immunol , vol.48 , pp. 1735-1743
    • Call, M.J.1
  • 34
    • 1842372075 scopus 로고    scopus 로고
    • Immunoselection in vivo: independent loss of MHC class I and melanocyte differentiation antigen expression in metastatic melanoma
    • Jäger E, et al. Immunoselection in vivo: independent loss of MHC class I and melanocyte differentiation antigen expression in metastatic melanoma. Int J Cancer 1997;71:142–147.
    • (1997) Int J Cancer , vol.71 , pp. 142-147
    • Jäger, E.1
  • 36
    • 82255164138 scopus 로고    scopus 로고
    • Towards a systems understanding of MHC class I and MHC class II antigen presentation
    • Neefjes J, Jongsma ML, Paul P, Bakke O. Towards a systems understanding of MHC class I and MHC class II antigen presentation. Nat Rev Immunol 2011;11:823–836.
    • (2011) Nat Rev Immunol , vol.11 , pp. 823-836
    • Neefjes, J.1    Jongsma, M.L.2    Paul, P.3    Bakke, O.4
  • 37
    • 0034173387 scopus 로고    scopus 로고
    • Intracellular surveillance: controlling the assembly of MHC class I-peptide complexes
    • Cresswell P. Intracellular surveillance: controlling the assembly of MHC class I-peptide complexes. Traffic 2000;1:301–305.
    • (2000) Traffic , vol.1 , pp. 301-305
    • Cresswell, P.1
  • 38
    • 0032900957 scopus 로고    scopus 로고
    • Opposing motor activities of dynein and kinesin determine retention and transport of MHC class II-containing compartments
    • Wubbolts R, et al. Opposing motor activities of dynein and kinesin determine retention and transport of MHC class II-containing compartments. J Cell Sci 1999;112:785–795.
    • (1999) J Cell Sci , vol.112 , pp. 785-795
    • Wubbolts, R.1
  • 39
    • 34247891741 scopus 로고    scopus 로고
    • More than one reason to rethink the use of peptides in vaccine design
    • Purcell AW, McCluskey J, Rossjohn J. More than one reason to rethink the use of peptides in vaccine design. Nat Rev Drug Discovery 2007;6:404–414.
    • (2007) Nat Rev Drug Discovery , vol.6 , pp. 404-414
    • Purcell, A.W.1    McCluskey, J.2    Rossjohn, J.3
  • 41
    • 0028313992 scopus 로고
    • Assembly, transport, and function of MHC class-II molecules
    • Cresswell P. Assembly, transport, and function of MHC class-II molecules. Annu Rev Immunol 1994;12:259–293.
    • (1994) Annu Rev Immunol , vol.12 , pp. 259-293
    • Cresswell, P.1
  • 42
    • 0025083334 scopus 로고
    • Invariant chain trimers are sequestered in the rough endoplasmic-reticulum in the absence of association with HLA class-II antigens
    • Marks MS, Blum JS, Cresswell P. Invariant chain trimers are sequestered in the rough endoplasmic-reticulum in the absence of association with HLA class-II antigens. J Cell Biol 1990;111:839–855.
    • (1990) J Cell Biol , vol.111 , pp. 839-855
    • Marks, M.S.1    Blum, J.S.2    Cresswell, P.3
  • 43
    • 0026088251 scopus 로고
    • Formation of a nine-subunit complex by HLA class-II glycoproteins and the invariant chain
    • Roche PA, Marks MS, Cresswell P. Formation of a nine-subunit complex by HLA class-II glycoproteins and the invariant chain. Nature 1991;354:392–394.
    • (1991) Nature , vol.354 , pp. 392-394
    • Roche, P.A.1    Marks, M.S.2    Cresswell, P.3
  • 44
    • 0019962031 scopus 로고
    • Membrane insertion and oligomeric assembly of HLA-DR histocompatibility antigens
    • Kvist S, Wiman K, Claesson L, Peterson PA, Dobberstein B. Membrane insertion and oligomeric assembly of HLA-DR histocompatibility antigens. Cell 1982;29:61–69.
    • (1982) Cell , vol.29 , pp. 61-69
    • Kvist, S.1    Wiman, K.2    Claesson, L.3    Peterson, P.A.4    Dobberstein, B.5
  • 45
    • 69149103002 scopus 로고    scopus 로고
    • MHC II and the endocytic pathway: regulation by invariant chain
    • Landsverk OJB, Bakke O, Gregers TF. MHC II and the endocytic pathway: regulation by invariant chain. Scand J Immunol 2009;70:184–193.
    • (2009) Scand J Immunol , vol.70 , pp. 184-193
    • Landsverk, O.J.B.1    Bakke, O.2    Gregers, T.F.3
  • 46
    • 0026015909 scopus 로고
    • Invariant chain promotes egress of poorly expressed, haplotype-mismatched class II major histocompatibility complex A alpha A beta dimers from the endoplasmic reticulum/cis-Golgi compartment
    • Layet C, Germain RN. Invariant chain promotes egress of poorly expressed, haplotype-mismatched class II major histocompatibility complex A alpha A beta dimers from the endoplasmic reticulum/cis-Golgi compartment. Proc Natl Acad Sci USA 1991;88:2346–2350.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2346-2350
    • Layet, C.1    Germain, R.N.2
  • 47
    • 0025602116 scopus 로고
    • Intracellular transport of class II MHC molecules directed by invariant chain
    • Lotteau V, et al. Intracellular transport of class II MHC molecules directed by invariant chain. Nature 1990;348:600–605.
    • (1990) Nature , vol.348 , pp. 600-605
    • Lotteau, V.1
  • 48
    • 0020422255 scopus 로고
    • Biosynthesis and glycosylation of the invariant chain associated with HLA-DR antigens
    • Machamer CE, Cresswell P. Biosynthesis and glycosylation of the invariant chain associated with HLA-DR antigens. J Immunol 1982;129:2564–2569.
    • (1982) J Immunol , vol.129 , pp. 2564-2569
    • Machamer, C.E.1    Cresswell, P.2
  • 49
    • 0020407888 scopus 로고
    • Detection of two distinct class II α: β: Ii complexes in the syrian hamster
    • Sung E, Duncan WR, Streilein JW, Jones PP. Detection of two distinct class II α: β: Ii complexes in the syrian hamster. Immunogenetics 1982;16:425–433.
    • (1982) Immunogenetics , vol.16 , pp. 425-433
    • Sung, E.1    Duncan, W.R.2    Streilein, J.W.3    Jones, P.P.4
  • 51
    • 0027536939 scopus 로고
    • Mice lacking the MHC class II-associated invariant chain
    • Viville S, et al. Mice lacking the MHC class II-associated invariant chain. Cell 1993;72:635–648.
    • (1993) Cell , vol.72 , pp. 635-648
    • Viville, S.1
  • 52
    • 1042278900 scopus 로고    scopus 로고
    • Class II MHC peptide loading by the professionals
    • Bryant P, Ploegh H. Class II MHC peptide loading by the professionals. Curr Opin Immunol 2004;16:96–102.
    • (2004) Curr Opin Immunol , vol.16 , pp. 96-102
    • Bryant, P.1    Ploegh, H.2
  • 53
    • 0026583941 scopus 로고
    • Inhibition of endosomal proteolytic activity by leupeptin blocks surface expression of MHC class-II molecules and their conversion to SDS resistant alpha-beta-heterodimers in endosomes
    • Neefjes JJ, Ploegh HL. Inhibition of endosomal proteolytic activity by leupeptin blocks surface expression of MHC class-II molecules and their conversion to SDS resistant alpha-beta-heterodimers in endosomes. EMBO J 1992;11:411–416.
    • (1992) EMBO J , vol.11 , pp. 411-416
    • Neefjes, J.J.1    Ploegh, H.L.2
  • 54
    • 0028362563 scopus 로고
    • Transport and intracellular distribution of MHC class II molecules and associated invariant chain in normal and antigen-processing mutant cell lines
    • Riberdy JM, Avva RR, Geuze HJ, Cresswell P. Transport and intracellular distribution of MHC class II molecules and associated invariant chain in normal and antigen-processing mutant cell lines. J Cell Biol 1994;125:1225–1237.
    • (1994) J Cell Biol , vol.125 , pp. 1225-1237
    • Riberdy, J.M.1    Avva, R.R.2    Geuze, H.J.3    Cresswell, P.4
  • 55
    • 0026440236 scopus 로고
    • HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides
    • 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
  • 56
    • 0025249197 scopus 로고
    • The biosynthetic-pathway of MHC class-II but not class-I molecules intersects the endocytic route
    • Neefjes JJ, Stollorz V, Peters PJ, Geuze HJ, Ploegh HL. The biosynthetic-pathway of MHC class-II but not class-I molecules intersects the endocytic route. Cell 1990;61:171–183.
    • (1990) Cell , vol.61 , pp. 171-183
    • Neefjes, J.J.1    Stollorz, V.2    Peters, P.J.3    Geuze, H.J.4    Ploegh, H.L.5
  • 57
    • 0030030896 scopus 로고    scopus 로고
    • Evidence for a conformational change in a class II major histocompatibility complex molecule occurring in the same pH range where antigen binding is enhanced
    • Boniface JJ, Lyons DS, Wettstein DA, Allbritton NL, Davis MM. Evidence for a conformational change in a class II major histocompatibility complex molecule occurring in the same pH range where antigen binding is enhanced. 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
  • 59
    • 37749018903 scopus 로고    scopus 로고
    • Biogenesis and function of multivesicular bodies
    • Piper RC, Katzmann DJ. Biogenesis and function of multivesicular bodies. Annu Rev Cell Dev Biol 2007;23:519–547.
    • (2007) Annu Rev Cell Dev Biol , vol.23 , pp. 519-547
    • Piper, R.C.1    Katzmann, D.J.2
  • 60
    • 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;299:1400–1403.
    • (2003) Science , vol.299 , pp. 1400-1403
    • Trombetta, E.S.1    Ebersold, M.2    Garrett, W.3    Pypaert, M.4    Mellman, I.5
  • 61
    • 84890050541 scopus 로고    scopus 로고
    • HLA-DM and HLA-DO, key regulators of MHC-II processing and presentation
    • Mellins ED, Stern LJ. HLA-DM and HLA-DO, key regulators of MHC-II processing and presentation. Curr Opin Immunol 2014;26:115–122.
    • (2014) Curr Opin Immunol , vol.26 , pp. 115-122
    • Mellins, E.D.1    Stern, L.J.2
  • 62
    • 62149092612 scopus 로고    scopus 로고
    • MHC class II transport at a glance
    • Berger AC, Roche PA. MHC class II transport at a glance. J Cell Sci 2009;122:1–4.
    • (2009) J Cell Sci , vol.122 , pp. 1-4
    • Berger, A.C.1    Roche, P.A.2
  • 63
    • 0029837980 scopus 로고    scopus 로고
    • Direct vesicular transport of MHC class II molecules from lysosomal structures to the cell surface
    • Wubbolts R, et al. Direct vesicular transport of MHC class II molecules from lysosomal structures to the cell surface. J Cell Biol 1996;135:611–622.
    • (1996) J Cell Biol , vol.135 , pp. 611-622
    • Wubbolts, R.1
  • 64
    • 0028354134 scopus 로고
    • 2 Processing pathways for the MHC class II-restricted presentation of exogenous influenza-virus antigen
    • Pinet V, Malnati MS, Long EO. 2 Processing pathways for the MHC class II-restricted presentation of exogenous influenza-virus antigen. J Immunol 1994;152:4852–4860.
    • (1994) J Immunol , vol.152 , pp. 4852-4860
    • Pinet, V.1    Malnati, M.S.2    Long, E.O.3
  • 65
    • 47249089545 scopus 로고    scopus 로고
    • Major histocompatibility complex class II-peptide complexes internalize using a clathrin-and dynamin-independent endocytosis pathway
    • Walseng E, Bakke O, Roche PA. Major histocompatibility complex class II-peptide complexes internalize using a clathrin-and dynamin-independent endocytosis pathway. J Biol Chem 2008;283:14717–14727.
    • (2008) J Biol Chem , vol.283 , pp. 14717-14727
    • Walseng, E.1    Bakke, O.2    Roche, P.A.3
  • 67
    • 0021360513 scopus 로고
    • Differential requirements for antigen processing by macrophages for lysozyme-specific T cell hybridomas
    • Allen P, Unanue E. Differential requirements for antigen processing by macrophages for lysozyme-specific T cell hybridomas. J Immunol 1984;132:1077–1079.
    • (1984) J Immunol , vol.132 , pp. 1077-1079
    • Allen, P.1    Unanue, E.2
  • 68
    • 0028038426 scopus 로고
    • MHC-dependent antigen-processing and peptide presentation – providing ligands for T-lymphocyte activation
    • Germain RN. MHC-dependent antigen-processing and peptide presentation – providing ligands for T-lymphocyte activation. Cell 1994;76:287–299.
    • (1994) Cell , vol.76 , pp. 287-299
    • Germain, R.N.1
  • 69
    • 0027155945 scopus 로고
    • Acidification and disulfide reduction can be sufficient to allow intact proteins to bind class-II MHC
    • 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
  • 70
    • 0037321893 scopus 로고    scopus 로고
    • Small-molecular compounds enhance the loading of APC with encephalitogenic MBP protein
    • Marin-Esteban V, Falk K, Rotzschke O. Small-molecular compounds enhance the loading of APC with encephalitogenic MBP protein. J Autoimmun 2003;20:63–69.
    • (2003) J Autoimmun , vol.20 , pp. 63-69
    • Marin-Esteban, V.1    Falk, K.2    Rotzschke, O.3
  • 71
    • 0029055938 scopus 로고
    • Antigen presentation mediated by recycling of surface HLA-DR molecules
    • 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
  • 72
    • 18544397838 scopus 로고    scopus 로고
    • T cell response to myelin basic protein in the context of the multiple sclerosis-associated HLA-DR15 haplotype: peptide binding, immunodominance and effector functions of T cells
    • Vergelli M, et al. T cell response to myelin basic protein in the context of the multiple sclerosis-associated HLA-DR15 haplotype: peptide binding, immunodominance and effector functions of T cells. J Neuroimmunol 1997;77:195–203.
    • (1997) J Neuroimmunol , vol.77 , pp. 195-203
    • Vergelli, M.1
  • 73
    • 0036227429 scopus 로고    scopus 로고
    • Diversity in MHC class II antigen presentation
    • Robinson JH, Delvig AA. Diversity in MHC class II antigen presentation. Immunology 2002;105:252–262.
    • (2002) Immunology , vol.105 , pp. 252-262
    • Robinson, J.H.1    Delvig, A.A.2
  • 74
    • 0037194733 scopus 로고    scopus 로고
    • Dendritic cell maturation triggers retrograde MHC class II transport from lysosomes to the plasma membrane
    • Chow A, Toomre D, Garrett W, Mellman I. Dendritic cell maturation triggers retrograde MHC class II transport from lysosomes to the plasma membrane. Nature 2002;418:988–994.
    • (2002) Nature , vol.418 , pp. 988-994
    • Chow, A.1    Toomre, D.2    Garrett, W.3    Mellman, I.4
  • 75
    • 0036144745 scopus 로고    scopus 로고
    • Tetraspan microdomains distinct from lipid rafts enrich select peptide-MHC class II complexes
    • Kropshofer H, et al. Tetraspan microdomains distinct from lipid rafts enrich select peptide-MHC class II complexes. Nat Immunol 2002;3:61–68.
    • (2002) Nat Immunol , vol.3 , pp. 61-68
    • Kropshofer, H.1
  • 76
    • 0034252971 scopus 로고    scopus 로고
    • Concentration of MHC class II molecules in lipid rafts facilitates antigen presentation
    • Anderson HA, Hiltbold EM, Roche PA. Concentration of MHC class II molecules in lipid rafts facilitates antigen presentation. Nat Immunol 2000;1:156–162.
    • (2000) Nat Immunol , vol.1 , pp. 156-162
    • Anderson, H.A.1    Hiltbold, E.M.2    Roche, P.A.3
  • 77
    • 0037310832 scopus 로고    scopus 로고
    • MHC class II-peptide complexes and APC lipid rafts accumulate at the immunological synapse
    • Hiltbold EM, Poloso NJ, Roche PA. MHC class II-peptide complexes and APC lipid rafts accumulate at the immunological synapse. J Immunol 2003;170:1329–1338.
    • (2003) J Immunol , vol.170 , pp. 1329-1338
    • Hiltbold, E.M.1    Poloso, N.J.2    Roche, P.A.3
  • 78
    • 0031059765 scopus 로고    scopus 로고
    • MHC class II restricted antigen presentation
    • Pieters J. MHC class II restricted antigen presentation. Curr Opin Immunol 1997;9:89–96.
    • (1997) Curr Opin Immunol , vol.9 , pp. 89-96
    • Pieters, J.1
  • 79
    • 0028821308 scopus 로고
    • How MHC class II molecules reach the endocytic pathway
    • Benaroch P, et al. How MHC class II molecules reach the endocytic pathway. EMBO J 1995;14:37–49.
    • (1995) EMBO J , vol.14 , pp. 37-49
    • Benaroch, P.1
  • 80
    • 21244444628 scopus 로고    scopus 로고
    • AP2 clathrin adaptor complex, but not AP1, controls the access of the major histocompatibility complex (MHC) class II to endosomes
    • Dugast M, Toussaint H, Dousset C, Benaroch P. AP2 clathrin adaptor complex, but not AP1, controls the access of the major histocompatibility complex (MHC) class II to endosomes. J Biol Chem 2005;280:19656–19664.
    • (2005) J Biol Chem , vol.280 , pp. 19656-19664
    • Dugast, M.1    Toussaint, H.2    Dousset, C.3    Benaroch, P.4
  • 82
    • 0141832121 scopus 로고    scopus 로고
    • Mhc-guided processing: binding of large antigen fragments
    • Sercarz EE, Maverakis E. Mhc-guided processing: binding of large antigen fragments. Nat Rev Immunol 2003;3:621–629.
    • (2003) Nat Rev Immunol , vol.3 , pp. 621-629
    • Sercarz, E.E.1    Maverakis, E.2
  • 83
    • 0026768974 scopus 로고
    • Truncation variants of peptides isolated from MHC class II molecules suggest sequence motifs
    • Rudensky AY, Preston-Hurlburt P, Al-Ramadi BK, Rothbard J, Janeway CA. Truncation variants of peptides isolated from MHC class II molecules suggest sequence motifs. Nature 1992;359:429–431.
    • (1992) Nature , vol.359 , pp. 429-431
    • Rudensky, A.Y.1    Preston-Hurlburt, P.2    Al-Ramadi, B.K.3    Rothbard, J.4    Janeway, C.A.5
  • 84
    • 0027941809 scopus 로고
    • MHC class II function preserved by low-affinity peptide interactions preceding stable binding
    • Sadegh-Nasseri S, Stern LJ, Wiley DC, Germain RN. MHC class II function preserved by low-affinity peptide interactions preceding stable binding. Nature 1994;370:647–650.
    • (1994) Nature , vol.370 , pp. 647-650
    • Sadegh-Nasseri, S.1    Stern, L.J.2    Wiley, D.C.3    Germain, R.N.4
  • 85
    • 58849104457 scopus 로고    scopus 로고
    • The HLA genomic loci map: expression, interaction, diversity and disease
    • Shiina T, Hosomichi K, Inoko H, Kulski JK. The HLA genomic loci map: expression, interaction, diversity and disease. J Hum Genet 2009;54:15–39.
    • (2009) J Hum Genet , vol.54 , pp. 15-39
    • Shiina, T.1    Hosomichi, K.2    Inoko, H.3    Kulski, J.K.4
  • 87
    • 0242581740 scopus 로고    scopus 로고
    • Exploration of the P6/P7 region of the peptide-binding site of the human class II major histocompatability complex protein HLA-DR1
    • Zavala-Ruiz Z, et al. Exploration of the P6/P7 region of the peptide-binding site of the human class II major histocompatability complex protein HLA-DR1. J Biol Chem 2003;278:44904–44912.
    • (2003) J Biol Chem , vol.278 , pp. 44904-44912
    • Zavala-Ruiz, Z.1
  • 88
    • 70349240535 scopus 로고    scopus 로고
    • The binding of antigenic peptides to HLA-DR is influenced by interactions between pocket 6 and pocket 9
    • James EA, Moustakas AK, Bui J, Nouv R, Papadopoulos GK, Kwok WW. The binding of antigenic peptides to HLA-DR is influenced by interactions between pocket 6 and pocket 9. J Immunol 2009;183:3249–3258.
    • (2009) J Immunol , vol.183 , pp. 3249-3258
    • James, E.A.1    Moustakas, A.K.2    Bui, J.3    Nouv, R.4    Papadopoulos, G.K.5    Kwok, W.W.6
  • 89
    • 0036174635 scopus 로고    scopus 로고
    • Binding interactions between peptides and proteins of the class II major histocompatibility complex
    • McFarland BJ, Beeson C. Binding interactions between peptides and proteins of the class II major histocompatibility complex. Med Res Rev 2002;22:168–203.
    • (2002) Med Res Rev , vol.22 , pp. 168-203
    • McFarland, B.J.1    Beeson, C.2
  • 90
    • 0034695675 scopus 로고    scopus 로고
    • Determinants of the peptide-induced conformational change in the human class II major histocompatibility complex protein HLA-DR1
    • Sato AK, et al. Determinants of the peptide-induced conformational change in the human class II major histocompatibility complex protein HLA-DR1. J Biol Chem 2000;275:2165–2173.
    • (2000) J Biol Chem , vol.275 , pp. 2165-2173
    • Sato, A.K.1
  • 91
    • 0025013141 scopus 로고
    • Characterization of the specificity of peptide binding to four DR haplotypes
    • O'Sullivan D, et al. Characterization of the specificity of peptide binding to four DR haplotypes. J Immunol 1990;145:1799–1808.
    • (1990) J Immunol , vol.145 , pp. 1799-1808
    • O'Sullivan, D.1
  • 92
    • 33846952190 scopus 로고    scopus 로고
    • HLA-DM targets the hydrogen bond between the histidine at position β81 and peptide to dissociate HLA-DR–peptide complexes
    • Narayan K, et al. HLA-DM targets the hydrogen bond between the histidine at position β81 and peptide to dissociate HLA-DR–peptide complexes. Nat Immunol 2007;8:92–100.
    • (2007) Nat Immunol , vol.8 , pp. 92-100
    • Narayan, K.1
  • 93
    • 0030770701 scopus 로고    scopus 로고
    • How HLA-DM affects the peptide repertoire bound to HLA-DR molecules
    • Vogt AB, Kropshofer H, Hammerling GJ. How HLA-DM affects the peptide repertoire bound to HLA-DR molecules. Hum Immunol 1997;54:170–179.
    • (1997) Hum Immunol , vol.54 , pp. 170-179
    • Vogt, A.B.1    Kropshofer, H.2    Hammerling, G.J.3
  • 94
    • 0029824101 scopus 로고    scopus 로고
    • Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM
    • Weber DA, Evavold BD, Jensen PE. Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM. Science 1996;274:618–621.
    • (1996) Science , vol.274 , pp. 618-621
    • Weber, D.A.1    Evavold, B.D.2    Jensen, P.E.3
  • 95
    • 0037169536 scopus 로고    scopus 로고
    • Ligand exchange of major histocompatibility complex class II proteins is triggered by H-bond donor groups of small molecules
    • Falk K, et al. Ligand exchange of major histocompatibility complex class II proteins is triggered by H-bond donor groups of small molecules. J Biol Chem 2002;277:2709–2715.
    • (2002) J Biol Chem , vol.277 , pp. 2709-2715
    • Falk, K.1
  • 96
    • 0028981178 scopus 로고
    • HLA-DM induces CLIP dissociation from MHC class II αβ dimers and facilitates peptide loading
    • Denzin LK, Cresswell P. HLA-DM induces CLIP dissociation from MHC class II αβ dimers and facilitates peptide loading. Cell 1995;82:155–165.
    • (1995) Cell , vol.82 , pp. 155-165
    • Denzin, L.K.1    Cresswell, P.2
  • 98
    • 0030068236 scopus 로고    scopus 로고
    • A structural transition in class II major histocompatibility complex proteins at mildly acidic pH
    • Runnels HA, Moore JC, Jensen PE. A structural transition in class II major histocompatibility complex 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
  • 99
    • 0036882073 scopus 로고    scopus 로고
    • The final cut: how ERAP1 trims MHC ligands to size
    • Falk K, Rötzschke O. The final cut: how ERAP1 trims MHC ligands to size. Nat Immunol 2002;3:1121–1122.
    • (2002) Nat Immunol , vol.3 , pp. 1121-1122
    • Falk, K.1    Rötzschke, O.2
  • 100
    • 0034603779 scopus 로고    scopus 로고
    • A three-step kinetic mechanism for peptide binding to MHC class II proteins
    • Joshi RV, Zarutskie JA, Stern LJ. A three-step kinetic mechanism for peptide binding to MHC class II proteins. Biochemistry (Mosc) 2000;39:3751–3762.
    • (2000) Biochemistry (Mosc) , vol.39 , pp. 3751-3762
    • Joshi, R.V.1    Zarutskie, J.A.2    Stern, L.J.3
  • 101
    • 0033120523 scopus 로고    scopus 로고
    • Stable peptide binding to MHC class II molecule is rapid and is determined by a receptive conformation shaped by prior association with low affinity peptides
    • Natarajan SK, Assadi M, Sadegh-Nasseri S. Stable peptide binding to MHC class II molecule is rapid and is determined by a receptive conformation shaped by prior association with low affinity peptides. J Immunol 1999;162:4030–4036.
    • (1999) J Immunol , vol.162 , pp. 4030-4036
    • Natarajan, S.K.1    Assadi, M.2    Sadegh-Nasseri, S.3
  • 102
    • 0033559513 scopus 로고    scopus 로고
    • Sodium dodecyl sulfate stability of HLA-DR1 complexes correlates with burial of hydrophobic residues in pocket 1
    • Natarajan SK, Stern LJ, Sadegh-Nasseri S. Sodium dodecyl sulfate stability of HLA-DR1 complexes correlates with burial of hydrophobic residues in pocket 1. J Immunol 1999;162:3463–3470.
    • (1999) J Immunol , vol.162 , pp. 3463-3470
    • Natarajan, S.K.1    Stern, L.J.2    Sadegh-Nasseri, S.3
  • 103
    • 0028285075 scopus 로고
    • Separation of subcellular compartments containing distinct functional forms of MHC class-II
    • Qiu Y, Xu XX, Wandingerness A, Dalke DP, Pierce SK. Separation of subcellular compartments containing distinct functional forms of MHC class-II. J Cell Biol 1994;125:595–605.
    • (1994) J Cell Biol , vol.125 , pp. 595-605
    • Qiu, Y.1    Xu, X.X.2    Wandingerness, A.3    Dalke, D.P.4    Pierce, S.K.5
  • 104
    • 0032212792 scopus 로고    scopus 로고
    • Formation of a highly peptide-receptive state of class II MHC
    • Rabinowitz JD, et al. Formation of a highly peptide-receptive state of class II MHC. Immunity 1998;9:699–709.
    • (1998) Immunity , vol.9 , pp. 699-709
    • Rabinowitz, J.D.1
  • 105
    • 0033594995 scopus 로고    scopus 로고
    • Conformational variants of class II MHC/peptide complexes induced by N-and C-terminal extensions of minimal peptide epitopes
    • Rötzschke O, Falk K, Mack J, Lau J, Jung G, Strominger J. Conformational variants of class II MHC/peptide complexes induced by N-and C-terminal extensions of minimal peptide epitopes. Proc Natl Acad Sci USA 1999;96:7445–7450.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7445-7450
    • Rötzschke, O.1    Falk, K.2    Mack, J.3    Lau, J.4    Jung, G.5    Strominger, J.6
  • 106
    • 0038302912 scopus 로고    scopus 로고
    • Altered positive selection due to corecognition of floppy peptide/MHC II conformers supports an integrative model of thymic selection
    • Viret C, He X, Janeway CA. Altered positive selection due to corecognition of floppy peptide/MHC II conformers supports an integrative model of thymic selection. Proc Natl Acad Sci USA 2003;100:5354–5359.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5354-5359
    • Viret, C.1    He, X.2    Janeway, C.A.3
  • 107
    • 0041929390 scopus 로고    scopus 로고
    • T cell recognition of distinct peptide: I-Au conformers in murine experimental autoimmune encephalomyelitis
    • Huang JC, Han M, Minguela A, Pastor S, Qadri A, Ward ES. T cell recognition of distinct peptide: I-Au conformers in murine experimental autoimmune encephalomyelitis. J Immunol 2003;171:2467–2477.
    • (2003) J Immunol , vol.171 , pp. 2467-2477
    • Huang, J.C.1    Han, M.2    Minguela, A.3    Pastor, S.4    Qadri, A.5    Ward, E.S.6
  • 108
    • 0037173034 scopus 로고    scopus 로고
    • Distinct recognition by two subsets of T cells of an MHC class II-peptide complex
    • Pu Z, Carrero JA, Unanue ER. Distinct recognition by two subsets of T cells of an MHC class II-peptide complex. Proc Natl Acad Sci USA 2002;99:8844–8849.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8844-8849
    • Pu, Z.1    Carrero, J.A.2    Unanue, E.R.3
  • 109
    • 1842633890 scopus 로고    scopus 로고
    • T cells distinguish MHC-peptide complexes formed in separate vesicles and edited by H2-DM
    • Pu Z, Lovitch SB, Bikoff EK, Unanue ER. T cells distinguish MHC-peptide complexes formed in separate vesicles and edited by H2-DM. Immunity 2004;20:467–476.
    • (2004) Immunity , vol.20 , pp. 467-476
    • Pu, Z.1    Lovitch, S.B.2    Bikoff, E.K.3    Unanue, E.R.4
  • 111
    • 0033522437 scopus 로고    scopus 로고
    • A conformational change in the human major histocompatibility complex protein HLA-DR1 induced by peptide binding
    • Zarutskie JA, et al. A conformational change in the human major histocompatibility complex protein HLA-DR1 induced by peptide binding. Biochemistry (Mosc) 1999;38:5878–5887.
    • (1999) Biochemistry (Mosc) , vol.38 , pp. 5878-5887
    • Zarutskie, J.A.1
  • 112
    • 10944263783 scopus 로고    scopus 로고
    • Chemical analogues” of HLA-DM can induce a peptide-receptive state in HLA-DR molecules
    • Marin-Esteban V, Falk K, Rotzschke O. “Chemical analogues” of HLA-DM can induce a peptide-receptive state in HLA-DR molecules. J Biol Chem 2004;279:50684–50690.
    • (2004) J Biol Chem , vol.279 , pp. 50684-50690
    • Marin-Esteban, V.1    Falk, K.2    Rotzschke, O.3
  • 114
  • 115
    • 59949104315 scopus 로고    scopus 로고
    • Flexibility of the MHC class II peptide binding cleft in the bound, partially filled, and empty states: a molecular dynamics simulation study
    • Yaneva R, Springer S, Zacharias M. Flexibility of the MHC class II peptide binding cleft in the bound, partially filled, and empty states: a molecular dynamics simulation study. Biopolymers 2009;91:14–27.
    • (2009) Biopolymers , vol.91 , pp. 14-27
    • Yaneva, R.1    Springer, S.2    Zacharias, M.3
  • 116
    • 33847206969 scopus 로고    scopus 로고
    • IL-17 family cytokines and the expanding diversity of effector T cell lineages
    • Weaver CT, Hatton RD, Mangan PR, Harrington LE. IL-17 family cytokines and the expanding diversity of effector T cell lineages. Annu Rev Immunol 2007;25:821–852.
    • (2007) Annu Rev Immunol , vol.25 , pp. 821-852
    • Weaver, C.T.1    Hatton, R.D.2    Mangan, P.R.3    Harrington, L.E.4
  • 117
    • 52649167708 scopus 로고    scopus 로고
    • CD4 T cells: fates, functions, and faults
    • Zhu J, Paul WE. CD4 T cells: fates, functions, and faults. Blood 2008;112:1557–1569.
    • (2008) Blood , vol.112 , pp. 1557-1569
    • Zhu, J.1    Paul, W.E.2
  • 118
    • 1642384289 scopus 로고    scopus 로고
    • Helper T cells, dendritic cells and CTL Immunity
    • Behrens G, et al. Helper T cells, dendritic cells and CTL Immunity. Immunol Cell Biol 2004;82:84–90.
    • (2004) Immunol Cell Biol , vol.82 , pp. 84-90
    • Behrens, G.1
  • 119
    • 21144438325 scopus 로고    scopus 로고
    • A RING-type ubiquitin ligase family member required to repress follicular helper T cells and autoimmunity
    • Vinuesa CG, et al. A RING-type ubiquitin ligase family member required to repress follicular helper T cells and autoimmunity. Nature 2005;435:452–458.
    • (2005) Nature , vol.435 , pp. 452-458
    • Vinuesa, C.G.1
  • 120
    • 34848837625 scopus 로고    scopus 로고
    • Peptides as tools and drugs for immunotherapies
    • Beck A, et al. Peptides as tools and drugs for immunotherapies. J Pept Sci 2007;13:588–602.
    • (2007) J Pept Sci , vol.13 , pp. 588-602
    • Beck, A.1
  • 122
    • 0037024461 scopus 로고    scopus 로고
    • Cancer immunotherapy with peptide-based vaccines: what have we achieved? Where are we going?
    • Parmiani G, et al. Cancer immunotherapy with peptide-based vaccines: what have we achieved? Where are we going? J Natl Cancer Inst 2002;94:805–818.
    • (2002) J Natl Cancer Inst , vol.94 , pp. 805-818
    • Parmiani, G.1
  • 123
    • 84885390747 scopus 로고    scopus 로고
    • Cancer treatment using peptides: current therapies and future prospects
    • Thundimadathil J. Cancer treatment using peptides: current therapies and future prospects. J Amino Acids 2012;2012:1–13.
    • (2012) J Amino Acids , vol.2012 , pp. 1-13
    • Thundimadathil, J.1
  • 124
    • 34547128664 scopus 로고    scopus 로고
    • Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association
    • Grotenbreg GM, et al. Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association. J Biol Chem 2007;282:21425–21436.
    • (2007) J Biol Chem , vol.282 , pp. 21425-21436
    • Grotenbreg, G.M.1
  • 125
    • 84872554985 scopus 로고    scopus 로고
    • HLA-DM: arbiter conformationis
    • Ferrante A. HLA-DM: arbiter conformationis. Immunology 2013;138:85–92.
    • (2013) Immunology , vol.138 , pp. 85-92
    • Ferrante, A.1
  • 126
    • 1642495746 scopus 로고    scopus 로고
    • Enhanced catalytic action of HLA-DM on the exchange of peptides lacking backbone hydrogen bonds between their N-terminal region and the MHC class II alpha-chain
    • Stratikos E, Wiley DC, Stern LJ. Enhanced catalytic action of HLA-DM on the exchange of peptides lacking backbone hydrogen bonds between their N-terminal region and the MHC class II alpha-chain. J Immunol 2004;172:1109–1117.
    • (2004) J Immunol , vol.172 , pp. 1109-1117
    • Stratikos, E.1    Wiley, D.C.2    Stern, L.J.3
  • 127
    • 68749117718 scopus 로고    scopus 로고
    • HLA-DM mediates peptide exchange by interacting transiently and repeatedly with HLA-DR1
    • Narayan K, Su KW, Chou CL, Khoruzhenko S, Sadegh-Nasseri S. HLA-DM mediates peptide exchange by interacting transiently and repeatedly with HLA-DR1. Mol Immunol 2009;46:3157–3162.
    • (2009) Mol Immunol , vol.46 , pp. 3157-3162
    • Narayan, K.1    Su, K.W.2    Chou, C.L.3    Khoruzhenko, S.4    Sadegh-Nasseri, S.5
  • 129
    • 0026093582 scopus 로고
    • A new human HLA class II-related locus, DM
    • Kelly AP, Monaco JJ, Cho S, Trowsdale J. A new human HLA class II-related locus, DM. Nature 1991;353:571–573.
    • (1991) Nature , vol.353 , pp. 571-573
    • Kelly, A.P.1    Monaco, J.J.2    Cho, S.3    Trowsdale, J.4
  • 130
    • 0041429632 scopus 로고    scopus 로고
    • Interaction of HLA-DR with an acidic face of HLA-DM disrupts sequence-dependent interactions with peptides
    • Pashine A, et al. Interaction of HLA-DR with an acidic face of HLA-DM disrupts sequence-dependent interactions with peptides. Immunity 2003;19:183–192.
    • (2003) Immunity , vol.19 , pp. 183-192
    • Pashine, A.1
  • 131
    • 17444451528 scopus 로고    scopus 로고
    • Functional HLA-DM on the surface of B cells and immature dendritic cells
    • Arndt SO, et al. Functional HLA-DM on the surface of B cells and immature dendritic cells. EMBO J 2000;19:1241–1251.
    • (2000) EMBO J , vol.19 , pp. 1241-1251
    • Arndt, S.O.1
  • 132
    • 0035879199 scopus 로고    scopus 로고
    • Cutting edge: editing of recycling class II: peptide complexes by HLA-DM
    • Pathak SS, Lich JD, Blum JS. Cutting edge: editing of recycling class II: peptide complexes by HLA-DM. J Immunol 2001;167:632–635.
    • (2001) J Immunol , vol.167 , pp. 632-635
    • Pathak, S.S.1    Lich, J.D.2    Blum, J.S.3
  • 133
    • 70349119901 scopus 로고    scopus 로고
    • In vivo enhancement of peptide display by MHC class II molecules with small molecule catalysts of peptide exchange
    • Call MJ, et al. In vivo enhancement of peptide display by MHC class II molecules with small molecule catalysts of peptide exchange. J Immunol 2009;182:6342–6352.
    • (2009) J Immunol , vol.182 , pp. 6342-6352
    • Call, M.J.1
  • 134
    • 0026505030 scopus 로고
    • Irreversible association of peptides with class II MHC molecules in living cells
    • 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
  • 135
    • 70349117004 scopus 로고    scopus 로고
    • Enhancement of tumour-specific immune responses in vivo by ‘MHC loading-enhancer’ (MLE)
    • Dickhaut K, et al. Enhancement of tumour-specific immune responses in vivo by ‘MHC loading-enhancer’ (MLE). PLoS ONE 2009;4:e6811.
    • (2009) PLoS ONE , vol.4
    • Dickhaut, K.1
  • 137
    • 33646360828 scopus 로고    scopus 로고
    • Noble metals strip peptides from class II MHC proteins
    • De Wall SL, et al. Noble metals strip peptides from class II MHC proteins. Nat Chem Biol 2006;2:197–201.
    • (2006) Nat Chem Biol , vol.2 , pp. 197-201
    • De Wall, S.L.1
  • 138
    • 33646038285 scopus 로고    scopus 로고
    • Small molecules that enhance the catalytic efficiency of HLA-DM
    • Nicholson MJ, et al. Small molecules that enhance the catalytic efficiency of HLA-DM. J Immunol 2006;176:4208–4220.
    • (2006) J Immunol , vol.176 , pp. 4208-4220
    • Nicholson, M.J.1
  • 139
    • 77949315137 scopus 로고    scopus 로고
    • Cutting edge: HLA-DM-mediated peptide exchange functions normally on MHC class II-peptide complexes that have been weakened by elimination of a conserved hydrogen bond
    • Ferrante A, Gorski J. Cutting edge: HLA-DM-mediated peptide exchange functions normally on MHC class II-peptide complexes that have been weakened by elimination of a conserved hydrogen bond. J Immunol 2010;184:1153–1158.
    • (2010) J Immunol , vol.184 , pp. 1153-1158
    • Ferrante, A.1    Gorski, J.2
  • 140
    • 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
    • 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
  • 141
    • 84947930848 scopus 로고    scopus 로고
    • Structural insights into HLA-DM mediated MHC II peptide exchange
    • Painter CA, Stern LJ. Structural insights into HLA-DM mediated MHC II peptide exchange. Curr Topics Biochem Res 2011;13:39–55.
    • (2011) Curr Topics Biochem Res , vol.13 , pp. 39-55
    • Painter, C.A.1    Stern, L.J.2
  • 142
    • 84871595445 scopus 로고    scopus 로고
    • Crystal structure of the HLA-DM–HLA-DR1 complex defines mechanisms for rapid peptide selection
    • Pos W, et al. Crystal structure of the HLA-DM–HLA-DR1 complex defines mechanisms for rapid peptide selection. Cell 2012;151:1557–1568.
    • (2012) Cell , vol.151 , pp. 1557-1568
    • Pos, W.1
  • 143
    • 84884269811 scopus 로고    scopus 로고
    • Development of the schedule for multiple parallel “difficult” Peptide synthesis on pins
    • Kolesanova EF, Sanzhakov MA, Kharybin ON. Development of the schedule for multiple parallel “difficult” Peptide synthesis on pins. Int J Pept 2013;2013:197317.
    • (2013) Int J Pept , vol.2013 , pp. 197317
    • Kolesanova, E.F.1    Sanzhakov, M.A.2    Kharybin, O.N.3
  • 144
    • 84880790787 scopus 로고    scopus 로고
    • Disruption of hydrogen bonds between major histocompatibility complex class II and the peptide N-terminus is not sufficient to form a human leukocyte antigen-DM receptive state of major histocompatibility complex class II
    • Schulze MS, Anders AK, Sethi DK, Call MJ. Disruption of hydrogen bonds between major histocompatibility complex class II and the peptide N-terminus is not sufficient to form a human leukocyte antigen-DM receptive state of major histocompatibility complex class II. PLoS ONE 2013;8:e69228.
    • (2013) PLoS ONE , vol.8
    • Schulze, M.S.1    Anders, A.K.2    Sethi, D.K.3    Call, M.J.4
  • 145
    • 0034684671 scopus 로고    scopus 로고
    • HLA-DM recognizes the flexible conformation of major histocompatibility complex class II
    • Chou C-L, Sadegh-Nasseri S. HLA-DM recognizes the flexible conformation of major histocompatibility complex class II. J Exp Med 2000;192:1697–1706.
    • (2000) J Exp Med , vol.192 , pp. 1697-1706
    • Chou, C.-L.1    Sadegh-Nasseri, S.2
  • 146
    • 0030458137 scopus 로고    scopus 로고
    • HLA-DM interactions with intermediates in HLA-DR maturation and a role for HLA-DM in stabilizing empty HLA-DR molecules
    • Denzin LK, Hammond C, Cresswell P. HLA-DM interactions with intermediates in HLA-DR maturation and a role for HLA-DM in stabilizing empty HLA-DR molecules. J Exp Med 1996;184:2153–2166.
    • (1996) J Exp Med , vol.184 , pp. 2153-2166
    • Denzin, L.K.1    Hammond, C.2    Cresswell, P.3
  • 147
  • 148
    • 0030978530 scopus 로고    scopus 로고
    • HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH
    • Kropshofer H, Arndt SO, Moldenhauer G, Hämmerling GJ, Vogt AB. HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH. Immunity 1997;6:293–302.
    • (1997) Immunity , vol.6 , pp. 293-302
    • Kropshofer, H.1    Arndt, S.O.2    Moldenhauer, G.3    Hämmerling, G.J.4    Vogt, A.B.5
  • 149
    • 0025895264 scopus 로고
    • Critical role for the Val/Gly86 HLA-DR beta dimorphism in autoantigen presentation to human T cells
    • Ong B, et al. Critical role for the Val/Gly86 HLA-DR beta dimorphism in autoantigen presentation to human T cells. Proc Natl Acad Sci USA 1991;88:7343–7347.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7343-7347
    • Ong, B.1
  • 150
    • 78651242465 scopus 로고    scopus 로고
    • Molecular and structural determinants of adamantyl susceptibility to HLA-DRs allelic variants: an in silico approach to understand the mechanism of MLEs
    • Zaheer Ul H, Khan W. Molecular and structural determinants of adamantyl susceptibility to HLA-DRs allelic variants: an in silico approach to understand the mechanism of MLEs. J Comput Aided Mol Des 2011;25:81–101.
    • (2011) J Comput Aided Mol Des , vol.25 , pp. 81-101
    • Zaheer Ul, H.1    Khan, W.2
  • 152
    • 0032080385 scopus 로고    scopus 로고
    • Enhancement of tumor outgrowth through CTL tolerization after peptide vaccination is avoided by peptide presentation on dendritic cells
    • Toes RE, et al. Enhancement of tumor outgrowth through CTL tolerization after peptide vaccination is avoided by peptide presentation on dendritic cells. J Immunol 1998;160:4449–4456.
    • (1998) J Immunol , vol.160 , pp. 4449-4456
    • Toes, R.E.1
  • 154
    • 2442484053 scopus 로고    scopus 로고
    • + regulatory T cells for immunologic self-tolerance and negative control of immune responses
    • + regulatory T cells for immunologic self-tolerance and negative control of immune responses. Annu Rev Immunol 2004;22:531–562.
    • (2004) Annu Rev Immunol , vol.22 , pp. 531-562
    • Sakaguchi, S.1
  • 155
    • 28044454553 scopus 로고    scopus 로고
    • Current strategies for the development of peptide-based anti-cancer therapeutics
    • Borghouts C, Kunz C, Groner B. Current strategies for the development of peptide-based anti-cancer therapeutics. J Pept Sci 2005;11:713–726.
    • (2005) J Pept Sci , vol.11 , pp. 713-726
    • Borghouts, C.1    Kunz, C.2    Groner, B.3
  • 156
    • 84868019079 scopus 로고    scopus 로고
    • Making peptides at large scale
    • Thayer A. Making peptides at large scale. Chem Eng News 2011;89:81–85.
    • (2011) Chem Eng News , vol.89 , pp. 81-85
    • Thayer, A.1
  • 159
    • 34247169514 scopus 로고    scopus 로고
    • Vaccine adjuvants revisited
    • Aguilar J, Rodriguez E. Vaccine adjuvants revisited. Vaccine 2007;25:3752–3762.
    • (2007) Vaccine , vol.25 , pp. 3752-3762
    • Aguilar, J.1    Rodriguez, E.2
  • 160
    • 34447639113 scopus 로고    scopus 로고
    • Single administration of low dose cyclophosphamide augments the antitumor effect of dendritic cell vaccine
    • Liu J-Y, et al. Single administration of low dose cyclophosphamide augments the antitumor effect of dendritic cell vaccine. Cancer Immunol Immunother 2007;56:1597–1604.
    • (2007) Cancer Immunol Immunother , vol.56 , pp. 1597-1604
    • Liu, J.-Y.1
  • 161
    • 84960474644 scopus 로고    scopus 로고
    • Safety and immunogenicity of a human papillomavirus peptide vaccine (CIGB-228) in women with high-grade cervical intraepithelial neoplasia: first-in-human. Proof-of-concept trial
    • Solares AM, et al. Safety and immunogenicity of a human papillomavirus peptide vaccine (CIGB-228) in women with high-grade cervical intraepithelial neoplasia: first-in-human. Proof-of-concept trial. ISRN Obstet Gynecol 2011;2011:292951.
    • (2011) ISRN Obstet Gynecol , vol.2011 , pp. 292951
    • Solares, A.M.1
  • 162
    • 77949653002 scopus 로고    scopus 로고
    • Interferon-gamma induction correlates with protection by DNA vaccine expressing E2 glycoprotein against classical swine fever virus infection in domestic pigs
    • Tarradas J, et al. Interferon-gamma induction correlates with protection by DNA vaccine expressing E2 glycoprotein against classical swine fever virus infection in domestic pigs. Vet Microbiol 2010;142:51–58.
    • (2010) Vet Microbiol , vol.142 , pp. 51-58
    • Tarradas, J.1
  • 163
    • 78649476854 scopus 로고    scopus 로고
    • Conserved epitopes of influenza A virus inducing protective immunity and their prospects for universal vaccine development
    • Staneková Z, Vareckova E. Conserved epitopes of influenza A virus inducing protective immunity and their prospects for universal vaccine development. Virol J 2010;7:351.
    • (2010) Virol J , vol.7 , pp. 351
    • Staneková, Z.1    Vareckova, E.2
  • 164
    • 78649845405 scopus 로고    scopus 로고
    • A synthetic peptide vaccine directed against the 2β2–2β3 loop of domain 2 of protective antigen protects rabbits from inhalation anthrax
    • Oscherwitz J, Yu F, Cease KB. A synthetic peptide vaccine directed against the 2β2–2β3 loop of domain 2 of protective antigen protects rabbits from inhalation anthrax. J Immunol 2010;185:3661–3668.
    • (2010) J Immunol , vol.185 , pp. 3661-3668
    • Oscherwitz, J.1    Yu, F.2    Cease, K.B.3
  • 165
    • 34250827428 scopus 로고    scopus 로고
    • Safety and clinical outcome of experimental challenge of human volunteers with Plasmodium falciparum-infected mosquitoes: an update
    • Epstein JE, et al. Safety and clinical outcome of experimental challenge of human volunteers with Plasmodium falciparum-infected mosquitoes: an update. J Infect Dis 2007;196:145–154.
    • (2007) J Infect Dis , vol.196 , pp. 145-154
    • Epstein, J.E.1
  • 167
    • 33845247353 scopus 로고    scopus 로고
    • Telomerase peptide vaccination of patients with non-resectable pancreatic cancer: a dose escalating phase I/II study
    • Bernhardt S, et al. Telomerase peptide vaccination of patients with non-resectable pancreatic cancer: a dose escalating phase I/II study. Br J Cancer 2006;95:1474–1482.
    • (2006) Br J Cancer , vol.95 , pp. 1474-1482
    • Bernhardt, S.1
  • 168
    • 79960329487 scopus 로고    scopus 로고
    • Telomerase peptide vaccination combined with temozolomide: a clinical trial in stage IV melanoma patients
    • Kyte JA, Gaudernack G, Dueland S, Trachsel S, Julsrud L, Aamdal S. Telomerase peptide vaccination combined with temozolomide: a clinical trial in stage IV melanoma patients. Clin Cancer Res 2011;17:4568–4580.
    • (2011) Clin Cancer Res , vol.17 , pp. 4568-4580
    • Kyte, J.A.1    Gaudernack, G.2    Dueland, S.3    Trachsel, S.4    Julsrud, L.5    Aamdal, S.6
  • 169
    • 33745638729 scopus 로고    scopus 로고
    • Telomerase peptide vaccination: a phase I/II study in patients with non-small cell lung cancer
    • Brunsvig PF, et al. Telomerase peptide vaccination: a phase I/II study in patients with non-small cell lung cancer. Cancer Immunol Immunother 2006;55:1553–1564.
    • (2006) Cancer Immunol Immunother , vol.55 , pp. 1553-1564
    • Brunsvig, P.F.1
  • 170
    • 77649148760 scopus 로고    scopus 로고
    • + T-cell responses in patients with advanced HCC
    • + T-cell responses in patients with advanced HCC. J Immunother 2010;33:211–218.
    • (2010) J Immunother , vol.33 , pp. 211-218
    • Greten, T.F.1
  • 171
    • 67649598300 scopus 로고    scopus 로고
    • Cancer vaccination with telomerase peptide GV1001
    • Kyte JA. Cancer vaccination with telomerase peptide GV1001. Expert Opin Investig Drugs 2009;18:687–694.
    • (2009) Expert Opin Investig Drugs , vol.18 , pp. 687-694
    • Kyte, J.A.1
  • 172
    • 84855746005 scopus 로고    scopus 로고
    • Oral delivery of curcumin bound to chitosan nanoparticles cured Plasmodium yoelii infected mice
    • Akhtar F, Rizvi MMA, Kar SK. Oral delivery of curcumin bound to chitosan nanoparticles cured Plasmodium yoelii infected mice. Biotechnol Adv 2012;30:310–320.
    • (2012) Biotechnol Adv , vol.30 , pp. 310-320
    • Akhtar, F.1    Rizvi, M.M.A.2    Kar, S.K.3
  • 173
    • 71149112331 scopus 로고    scopus 로고
    • Binding of prostate-specific membrane antigen to dendritic cells: a critical step in vaccine preparation
    • Garetto S, Sizzano F, Brusa D, Tizzani A, Malavasi F, Matera L. Binding of prostate-specific membrane antigen to dendritic cells: a critical step in vaccine preparation. Cytotherapy 2009;11:1090–1100.
    • (2009) Cytotherapy , vol.11 , pp. 1090-1100
    • Garetto, S.1    Sizzano, F.2    Brusa, D.3    Tizzani, A.4    Malavasi, F.5    Matera, L.6
  • 174
    • 84859435256 scopus 로고    scopus 로고
    • Carcinoembryonic antigen (CEA) as tumor marker in lung cancer
    • Grunnet M, Sorensen J. Carcinoembryonic antigen (CEA) as tumor marker in lung cancer. Lung Cancer 2012;76:138–143.
    • (2012) Lung Cancer , vol.76 , pp. 138-143
    • Grunnet, M.1    Sorensen, J.2
  • 175
    • 84355166378 scopus 로고    scopus 로고
    • Focus and breadth of cellular immune responses elicited by a heterologous insert prime-boost vaccine regimen in rhesus monkeys
    • Kaufman DR, Li F, Cruz AN, Self SG, Barouch DH. Focus and breadth of cellular immune responses elicited by a heterologous insert prime-boost vaccine regimen in rhesus monkeys. Vaccine 2012;30:506–509.
    • (2012) Vaccine , vol.30 , pp. 506-509
    • Kaufman, D.R.1    Li, F.2    Cruz, A.N.3    Self, S.G.4    Barouch, D.H.5
  • 176
  • 177
    • 84867982523 scopus 로고    scopus 로고
    • Adjuvant vaccination with melanoma antigen-pulsed dendritic cells in stage III melanoma patients
    • Markowicz S, et al. Adjuvant vaccination with melanoma antigen-pulsed dendritic cells in stage III melanoma patients. Med Oncol 2012;29:2966–2977.
    • (2012) Med Oncol , vol.29 , pp. 2966-2977
    • Markowicz, S.1
  • 178
    • 0033813525 scopus 로고    scopus 로고
    • A phase I trial of a human papillomavirus (HPV) peptide vaccine for women with high-grade cervical and vulvar intraepithelial neoplasia who are HPV 16 positive
    • Muderspach L, et al. A phase I trial of a human papillomavirus (HPV) peptide vaccine for women with high-grade cervical and vulvar intraepithelial neoplasia who are HPV 16 positive. Clin Cancer Res 2000;6:3406–3416.
    • (2000) Clin Cancer Res , vol.6 , pp. 3406-3416
    • Muderspach, L.1
  • 179
    • 35348839053 scopus 로고    scopus 로고
    • GV-1001, an injectable telomerase peptide vaccine for the treatment of solid cancers
    • Nava-Parada P, Emens LA. GV-1001, an injectable telomerase peptide vaccine for the treatment of solid cancers. Curr Opin Mol Ther 2007;9:490–497.
    • (2007) Curr Opin Mol Ther , vol.9 , pp. 490-497
    • Nava-Parada, P.1    Emens, L.A.2
  • 180
    • 79960330731 scopus 로고    scopus 로고
    • A novel method for the simultaneous quantification of phenotypic resistance to maturation, protease, reverse transcriptase, and integrase HIV inhibitors based on 3′ Gag (p2/p7/p1/p6)/PR/RT/INT-recombinant viruses: a useful tool in the multi-target era of antiretroviral therapy
    • AAC. 00396-00311
    • Weber J, et al. A novel method for the simultaneous quantification of phenotypic resistance to maturation, protease, reverse transcriptase, and integrase HIV inhibitors based on 3′ Gag (p2/p7/p1/p6)/PR/RT/INT-recombinant viruses: a useful tool in the multi-target era of antiretroviral therapy. Antimicrob Agents Chemother 2011;55:3729–3742. AAC. 00396-00311.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 3729-3742
    • Weber, J.1
  • 181
    • 84872263479 scopus 로고    scopus 로고
    • Next-generation peptide vaccines for advanced cancer
    • Yamada A, Sasada T, Noguchi M, Itoh K. Next-generation peptide vaccines for advanced cancer. Cancer Sci 2013;104:15–21.
    • (2013) Cancer Sci , vol.104 , pp. 15-21
    • Yamada, A.1    Sasada, T.2    Noguchi, M.3    Itoh, K.4
  • 182
    • 23344445706 scopus 로고    scopus 로고
    • MUC1 peptide vaccination in patients with advanced pancreas or biliary tract cancer
    • Yamamoto K, et al. MUC1 peptide vaccination in patients with advanced pancreas or biliary tract cancer. Anticancer Res 2005;25:3575–3579.
    • (2005) Anticancer Res , vol.25 , pp. 3575-3579
    • Yamamoto, K.1
  • 183
    • 79954889432 scopus 로고    scopus 로고
    • Dendritic cell-directed lentivector vaccine induces antigen-specific immune responses against murine melanoma
    • Yang H, Hu B, Xiao L, Wang P. Dendritic cell-directed lentivector vaccine induces antigen-specific immune responses against murine melanoma. Cancer Gene Ther 2011;18:370–380.
    • (2011) Cancer Gene Ther , vol.18 , pp. 370-380
    • Yang, H.1    Hu, B.2    Xiao, L.3    Wang, P.4
  • 184
    • 84920723279 scopus 로고    scopus 로고
    • A cyclic peptide accelerates the loading of peptide antigens in major histocompatibility complex class II molecules
    • Afridi S, et al. A cyclic peptide accelerates the loading of peptide antigens in major histocompatibility complex class II molecules. Biochem Biophys Res Commun 2015;456:774–779.
    • (2015) Biochem Biophys Res Commun , vol.456 , pp. 774-779
    • Afridi, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.