메뉴 건너뛰기




Volumn 8, Issue 8, 2013, Pages

Molecular dynamics simulations to provide insights into epitopes coupled to the soluble and membrane-bound MHC-II complexes

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; HETERODIMER; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; HLA ANTIGEN CLASS 2; PEPTIDE; PROTEIN BINDING; WATER;

EID: 84901193849     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0072575     Document Type: Article
Times cited : (30)

References (64)
  • 1
    • 17644370329 scopus 로고    scopus 로고
    • Cell biology of antigen processing in vitro and in vivo
    • Trombetta ES, Mellman I (2005) Cell biology of antigen processing in vitro and in vivo. Annu Rev Immunol 23: 975-1028
    • (2005) Annu Rev Immunol , vol.23 , pp. 975-1028
    • Trombetta, E.S.1    Mellman, I.2
  • 2
    • 0028922319 scopus 로고
    • Chemistry of peptides associated with MHCclass i and class II molecules
    • Rammensee HG (1995) Chemistry of peptides associated with MHCclass I and class II molecules. Curr Opin Immunol 7: 85-96
    • (1995) Curr Opin Immunol , vol.7 , pp. 85-96
    • Rammensee, H.G.1
  • 4
    • 30044446973 scopus 로고    scopus 로고
    • The wide diversity and complexity of peptides bound to class II MHC molecules
    • Suri A, Lovitch SB, Unanue ER (2006) The wide diversity and complexity of peptides bound to class II MHC molecules. Curr Opin Immunol 18: 70-77
    • (2006) Curr Opin Immunol , vol.18 , pp. 70-77
    • Suri, A.1    Lovitch, S.B.2    Unanue, E.R.3
  • 5
    • 0028773294 scopus 로고
    • Antigenic peptide binding by class i and class II histocompatibility proteins
    • Wiley DC
    • Stern LJ, Wiley DC (1994) Antigenic peptide binding by class I and class II histocompatibility proteins. Structure 2: 245-251
    • (1994) Structure , vol.2 , pp. 245-251
    • Stern, L.J.1
  • 6
    • 0035338992 scopus 로고    scopus 로고
    • Naturally processed HLAclass II peptides reveal highly conserved immunogenic flanking region sequence preferences that reflect antigen processing rather than peptide-MHC interactions
    • Godkin AJ, Smith KJ, Willis A, Tejada-Simon MV, Zhang J, et al. (2001) Naturally processed HLAclass II peptides reveal highly conserved immunogenic flanking region sequence preferences that reflect antigen processing rather than peptide-MHC interactions. J Immunol 166: 6720-6727
    • (2001) J Immunol , vol.166 , pp. 6720-6727
    • Godkin, A.J.1    Smith, K.J.2    Willis, A.3    Tejada-Simon, M.V.4    Zhang, J.5
  • 7
    • 26244451774 scopus 로고    scopus 로고
    • Conformational isomers of a peptide-class II major histocompatibility complex
    • Lovitch SB, Unanue ER (2005) Conformational isomers of a peptide-class II major histocompatibility complex. Immunol Rev 207: 293-313
    • (2005) Immunol Rev , vol.207 , pp. 293-313
    • Lovitch, S.B.1    Unanue, E.R.2
  • 9
    • 0347926117 scopus 로고    scopus 로고
    • Formation of two peptide/MHC II isomers is catalyzed differentially by HLA-DM
    • Belmares MP, Busch R, Mellins ED, McConnell HM (2003) Formation of two peptide/MHC II isomers is catalyzed differentially by HLA-DM. Biochemistry 42: 838-847
    • (2003) Biochemistry , vol.42 , pp. 838-847
    • Belmares, M.P.1    Busch, R.2    Mellins, E.D.3    McConnell, H.M.4
  • 10
    • 0033548189 scopus 로고    scopus 로고
    • Conformational isomers of a class II MHC-peptide complex in solution
    • Schmitt L, Boniface JJ, Davis MM, McConnell HM (1999) Conformational isomers of a class II MHC-peptide complex in solution. J Mol Biol 286: 207-218
    • (1999) J Mol Biol , vol.286 , pp. 207-218
    • Schmitt, L.1    Boniface, J.J.2    Davis, M.M.3    McConnell, H.M.4
  • 11
    • 26244456282 scopus 로고    scopus 로고
    • Recognition of open conformers of classical MHC by chaperones and monoclonal antibodies
    • Hansen TH, Lybarger L, Yu L, Mitaksov V, Fremont DH (2005) Recognition of open conformers of classical MHC by chaperones and monoclonal antibodies. Immunol Rev 207: 100-111
    • (2005) Immunol Rev , vol.207 , pp. 100-111
    • Hansen, T.H.1    Lybarger, L.2    Yu, L.3    Mitaksov, V.4    Fremont, D.H.5
  • 12
    • 0033522437 scopus 로고    scopus 로고
    • A conformational change in the human major histocompatibility complex protein HLA-DR1 induced by peptide binding
    • Zarutskie JA, Sato AK, Rushe MM, Chan IC, Lomakin A, et al. (1999) A conformational change in the human major histocompatibility complex protein HLA-DR1 induced by peptide binding. Biochemistry 38: 5878-5887
    • (1999) Biochemistry , vol.38 , pp. 5878-5887
    • Zarutskie, J.A.1    Sato, A.K.2    Rushe, M.M.3    Chan, I.C.4    Lomakin, A.5
  • 13
    • 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, Zarutskie JA, Rushe MM, Lomakin A, Natarajan SK, et al. (2000) Determinants of the peptide-induced conformational change in the human class II major histocompatibility complex protein HLA-DR1. J Biol Chem 275: 2165-2173
    • (2000) J Biol Chem , vol.275 , pp. 2165-2173
    • Sato, A.K.1    Zarutskie, J.A.2    Rushe, M.M.3    Lomakin, A.4    Natarajan, S.K.5
  • 14
    • 0029782111 scopus 로고    scopus 로고
    • Structures of an MHC class II molecule with covalently bound single peptides
    • Hendrickson WA, Marrack P, Kappler J
    • Fremont DH, Hendrickson WA, Marrack P, Kappler J (1996) Structures of an MHC class II molecule with covalently bound single peptides. Science 272: 1001-1004
    • (1996) Science , vol.272 , pp. 1001-1004
    • Fremont, D.H.1
  • 15
    • 0030069683 scopus 로고    scopus 로고
    • Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides
    • Jardetzky TS, Brown JH, Gorga JC, Stern LJ, Urban RG, et al. (1996) Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides. Proc Natl Acad Sci USA 93: 734-738
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 734-738
    • Jardetzky, T.S.1    Brown, J.H.2    Gorga, J.C.3    Stern, L.J.4    Urban, R.G.5
  • 16
    • 0028348369 scopus 로고
    • Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
    • Stern LJ, Brown JH, Jardetzky TS, Gorga JC, Urban RG, et al. (1994) Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 368: 215-221
    • (1994) Nature , vol.368 , pp. 215-221
    • Stern, L.J.1    Brown, J.H.2    Jardetzky, T.S.3    Gorga, J.C.4    Urban, R.G.5
  • 17
    • 0033662436 scopus 로고    scopus 로고
    • Structural basis of peptide binding and presentation by the type i diabetes-Associated MHC class II molecule of NOD mice
    • Latek RR, Suri A, Petzold SJ, Nelson CA, Kanagawa O, et al. (2000) Structural basis of peptide binding and presentation by the type I diabetes-Associated MHC class II molecule of NOD mice. Immunity 12: 699-710
    • (2000) Immunity , vol.12 , pp. 699-710
    • Latek, R.R.1    Suri, A.2    Petzold, S.J.3    Nelson, C.A.4    Kanagawa, O.5
  • 18
    • 34249803281 scopus 로고    scopus 로고
    • Cooperativity of hydrophobic anchor interactions: Evidence for epitope selection by MHC class II as a folding process
    • Ferrante A, Gorski J (2007) Cooperativity of hydrophobic anchor interactions: evidence for epitope selection by MHC class II as a folding process. J Immunol 178:7181-7189
    • (2007) J Immunol , vol.178 , pp. 7181-7189
    • Ferrante, A.1    Gorski, J.2
  • 19
    • 0028135684 scopus 로고
    • Molecular dynamics simulation of MHC-peptide complexes as a tool for predicting potential T-cell epitopes
    • Rognan D, Scapozza L, Folkers G, Daser A (1994) Molecular dynamics simulation of MHC-peptide complexes as a tool for predicting potential T-cell epitopes. Biochemistry 33: 11476-11485
    • (1994) Biochemistry , vol.33 , pp. 11476-11485
    • Rognan, D.1    Scapozza, L.2    Folkers, G.3    Daser, A.4
  • 20
    • 0030746962 scopus 로고    scopus 로고
    • A model of water structure inside the HLA-A2 peptide binding groove
    • Meng WS, von Grafenstein H, Haworth IS (1997) A model of water structure inside the HLA-A2 peptide binding groove. Int Immunol 9: 1339-1346
    • (1997) Int Immunol , vol.9 , pp. 1339-1346
    • Meng, W.S.1    Von Grafenstein, H.2    Haworth, I.S.3
  • 21
    • 49649086640 scopus 로고    scopus 로고
    • Analysis of key parameters for molecular dynamics of pMHC molecules
    • Omasits U, Knapp B, Neumann M, Steinhauser O, Stockinger H, et al. (2008) Analysis of key parameters for molecular dynamics of pMHC molecules. Mol Simul 34:781-793
    • (2008) Mol Simul , vol.34 , pp. 781-793
    • Omasits, U.1    Knapp, B.2    Neumann, M.3    Steinhauser, O.4    Stockinger, H.5
  • 22
    • 5044232231 scopus 로고    scopus 로고
    • Conformational flexibility of the MHC class i a1-A2 domain in peptide bound and free states: A molecular dynamics simulation study
    • Springer S
    • Zacharias M, Springer S (2004) Conformational flexibility of the MHC class I a1-A2 domain in peptide bound and free states: A molecular dynamics simulation study. Biophys J 87: 2203-2214
    • (2004) Biophys J , vol.87 , pp. 2203-2214
    • Zacharias, M.1
  • 23
    • 8344225257 scopus 로고    scopus 로고
    • Large-scale molecular dynamics simulations of HLA-A 0201 complexed with a tumor-specific antigenic peptide Can the a3 and b2m domains be neglected?
    • Wan S, Coveney P, Flower DR (2004) Large-scale molecular dynamics simulations of HLA-A0201 complexed with a tumor-specific antigenic peptide: Can the a3 and b2m domains be neglected? J Comput Chem 25: 1803-1813
    • (2004) J Comput Chem , vol.25 , pp. 1803-1813
    • Wan, S.1    Coveney, P.2    Flower, D.R.3
  • 24
    • 64149087447 scopus 로고    scopus 로고
    • 3-Layer-based analysis of peptide-MHC interaction in silico prediction, peptide binding affinity and T cell activation in a relevant allergen-specific model
    • Knapp B, Omasits U, Bohle B, Maillere B, Ebner C, Schreiner W, et al. (2009) 3-Layer-based analysis of peptide-MHC interaction: In silico prediction, peptide binding affinity and T cell activation in a relevant allergen-specific model. Mol Immunol 46: 1839-1844
    • (2009) Mol Immunol , vol.46 , pp. 1839-1844
    • Knapp, B.1    Omasits, U.2    Bohle, B.3    Maillere, B.4    Ebner, C.5    Schreiner, W.6
  • 25
    • 37349112664 scopus 로고    scopus 로고
    • Toward an atomistic understanding of the immune synapse: Large-scale molecular dynamics simulation of a membraneembedded TCR-pMHC-CD4 complex
    • Wan S, Flower DR, Coveney P (2008) Toward an atomistic understanding of the immune synapse: large-scale molecular dynamics simulation of a membraneembedded TCR-pMHC-CD4 complex. Mol Immunol 45: 1221-1230
    • (2008) Mol Immunol , vol.45 , pp. 1221-1230
    • Wan, S.1    Flower, D.R.2    Coveney, P.3
  • 26
    • 84876414055 scopus 로고    scopus 로고
    • Theoretical analysis of the neuraminidase epitope of the Mexican A H1N1 influenza strain, and experimental studies on its interaction with rabbit and human hosts
    • Loyola PK, Campos-Rodr?guez R, Bello M, Rojas-Hernandez S, Zimic M, et al. (2013) Theoretical analysis of the neuraminidase epitope of the Mexican A H1N1 influenza strain, and experimental studies on its interaction with rabbit and human hosts. Immunol Res 56: 44-60
    • (2013) Immunol Res , vol.56 , pp. 44-60
    • Loyola, P.K.1    Campos-Rodrguez, R.2    Bello, M.3    Rojas-Hernandez, S.4    Zimic, M.5
  • 27
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Yang Z (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9:40
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Yang, Z.1
  • 28
    • 77957963055 scopus 로고    scopus 로고
    • Achieving reliability and high accuracy in automated protein docking: Cluspro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19
    • Kozakov D, Hall DR, Beglov D, Brenke R, Comeau SR, et al. (2010) Achieving reliability and high accuracy in automated protein docking: Cluspro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19. Proteins 78: 3124-30
    • (2010) Proteins , vol.78 , pp. 3124-3130
    • Kozakov, D.1    Hall, D.R.2    Beglov, D.3    Brenke, R.4    Comeau, S.R.5
  • 29
    • 0345832301 scopus 로고    scopus 로고
    • ClusPro: An automated docking and discrimination method for the prediction of protein complexes
    • Comeau SR, Gatchell DW, Vajda S, Camacho CJ (2004) ClusPro: an automated docking and discrimination method for the prediction of protein complexes. Bioinformatics 20: 45-50
    • (2004) Bioinformatics , vol.20 , pp. 45-50
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 30
    • 64549106038 scopus 로고    scopus 로고
    • Convergence and combination of methods in protein-protein docking
    • A. Vajda S, Kozakov D (2009) Convergence and combination of methods in protein-protein docking. Curr Opin Struct Biol 19: 164-70
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 164-170
    • Vajda S, A.1    Kozakov, D.2
  • 31
    • 77954293798 scopus 로고    scopus 로고
    • CPHmodels-3.0 - Remote homology modeling using structure guided sequence profiles
    • Nielsen M, Lundegaard C, Lund O, Petersen TN (2010) CPHmodels-3.0 - Remote homology modeling using structure guided sequence profiles. Nucleic Acids Research 38: 576-81
    • (2010) Nucleic Acids Research , vol.38 , pp. 576-581
    • Nielsen, M.1    Lundegaard, C.2    Lund, O.3    Petersen, T.N.4
  • 32
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25:3389-3402
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 33
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol.234(3):779-815
    • (1993) J Mol Biol , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 35
    • 0036169191 scopus 로고    scopus 로고
    • Modeling MHC class II molecules and their bound peptides as expressed at the cell surface
    • Simon A, Simon I, Rajnavolgyi E (2002) Modeling MHC class II molecules and their bound peptides as expressed at the cell surface. Mol Immunol 38: 681-7
    • (2002) Mol Immunol , vol.38 , pp. 681-687
    • Simon, A.1    Simon, I.2    Rajnavolgyi, E.3
  • 37
    • 0026505030 scopus 로고
    • Irreversible association of peptide with class II MHC molecules in living cells
    • Lazavecchia AA, Reid PA, Watts RC (1992) Irreversible association of peptide with class II MHC molecules in living cells. Nature 357: 249-251
    • (1992) Nature , vol.357 , pp. 249-251
    • Lazavecchia, A.A.1    Reid, P.A.2    Watts, R.C.3
  • 38
    • 0023115557 scopus 로고
    • The relation between major histocompatibility complex (MHC) restriction and the capacity of to bind immunogenic peptides
    • Buus S, Sette A, Colon SM, Miles C, Grey HM (1987) The relation between major histocompatibility complex (MHC) restriction and the capacity of to bind immunogenic peptides. Science 235: 1353-1358
    • (1987) Science , vol.235 , pp. 1353-1358
    • Buus, S.1    Sette, A.2    Colon, S.M.3    Miles, C.4    Grey, H.M.5
  • 39
    • 77954256616 scopus 로고    scopus 로고
    • Gmembed. Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation
    • Wolf MG, Hoefling M, Aponte-Santamar?a C, Grubmuller H, Groenhof G (2010) gmembed. Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation. J Comput Chem 31: 2169-2174
    • (2010) J Comput Chem , vol.31 , pp. 2169-2174
    • Wolf, M.G.1    Hoefling, M.2    Aponte-Santamara, C.3    Grubmuller Groenhof H, G.4
  • 40
    • 0029633168 scopus 로고
    • GROMACS A message-passing parallel molecular dynamics implementation
    • Berendsen HJC, van der Spoel D, van Drunen R (1995) GROMACS. A message-passing parallel molecular dynamics implementation. Comput Phys Commun 91: 43-56
    • (1995) Comput Phys Commun , vol.91 , pp. 43-56
    • Hjc, B.1    Van Der Spoel, D.2    Van Drunen, R.3
  • 42
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • Oostenbrink C, Villa A, Mark AE, van Gunsteren WF (2004) A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6. J Comput Chem 25: 1656-1676
    • (2004) J Comput Chem , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 44
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log (N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L (1993) Particle mesh Ewald: An Nlog (N) method for Ewald sums in large systems. J Chem Phys 98: 10089-10092
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 45
    • 33750587438 scopus 로고
    • Molecular dynamics with coupling to an external bath
    • Berendsen HJC, Postma JPM, Di Nola A, Haak JR (1984) Molecular dynamics with coupling to an external bath. J Chem Phys 81: 3684-3690
    • (1984) J Chem Phys , vol.81 , pp. 3684-3690
    • Hjc, B.1    Jpm, P.2    Di Nola, A.3    Haak, J.R.4
  • 46
    • 0032534843 scopus 로고    scopus 로고
    • Lipid properties and the orientation of aromatic residues in OmpF, influenza M2, and alamethicin systems: Molecular dynamics simulations
    • Tieleman DP, Forrest LR, Sansom MS, Berendsen HJ (1998) Lipid properties and the orientation of aromatic residues in OmpF, influenza M2, and alamethicin systems: molecular dynamics simulations. Biochemistry 50: 17554-61
    • (1998) Biochemistry , vol.50 , pp. 17554-17561
    • Tieleman, D.P.1    Forrest, L.R.2    Sansom, M.S.3    Berendsen, H.J.4
  • 47
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess B, Bekker H, Berendsen HJC, Fraaije JGEM (1997) LINCS: a linear constraint solver for molecular simulations. J Comput Chem 18: 1463-1472
    • (1997) J Comput Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Hjc, B.3    Jgem, F.4
  • 48
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure and constant temperature
    • Berger O, Edholm O, Jahnig F (1997) Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure and constant temperature. Biophys J 72: 2002-2013
    • (1997) Biophys J , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 49
    • 0031880829 scopus 로고    scopus 로고
    • Adhesion forces of lipids in a phospholipid membrane studied by molecular dynamics simulations
    • Marrink SJ, Berger O, Tieleman DP, Jahnig F (1998) Adhesion forces of lipids in a phospholipid membrane studied by molecular dynamics simulations. Biophys J 74: 931-943
    • (1998) Biophys J , vol.74 , pp. 931-943
    • Marrink, S.J.1    Berger, O.2    Tieleman, D.P.3    Jahnig, F.4
  • 50
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thornton JM (1995) LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Prot Eng 8: 127-134
    • (1995) Prot Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 52
    • 0026088251 scopus 로고
    • Formation of a nine-subunit complex by HLA class II glycoproteins and the invariant chain
    • Roche PA, Marks MS, Cresswell P (1991) Formation of a nine-subunit complex by HLA class II glycoproteins and the invariant chain. Nature 354: 392-394
    • (1991) Nature , vol.354 , pp. 392-394
    • Roche, P.A.1    Marks, M.S.2    Cresswell, P.3
  • 53
    • 0026509280 scopus 로고
    • Assembly and transport properties of invariant chain trimers and HLA-DR-invariant chain complexes
    • Lamb CA, Cresswell P (1992) Assembly and transport properties of invariant chain trimers and HLA-DR-invariant chain complexes. J Immunol 148: 3478-3482
    • (1992) J Immunol , vol.148 , pp. 3478-3482
    • Lamb, C.A.1    Cresswell, P.2
  • 54
    • 0025202076 scopus 로고
    • MHC class II-Associated invariant chain contains a sorting signal for endosomal compartments
    • Bakke O, Dobberstein B (1990) MHC class II-Associated invariant chain contains a sorting signal for endosomal compartments. Cell 63: 707-716
    • (1990) Cell , vol.63 , pp. 707-716
    • Bakke, O.1    Dobberstein, B.2
  • 55
    • 0037196549 scopus 로고    scopus 로고
    • Multiple roles of the invariant chain in MHC class II function
    • Stumptner-Cuvelette P, Benaroch P (2002) Multiple roles of the invariant chain in MHC class II function. Biochim. Biophys Acta 1542: 1-13
    • (2002) Biochim. Biophys Acta , vol.1542 , pp. 1-13
    • Stumptner-Cuvelette, P.1    Benaroch, P.2
  • 56
    • 84860343209 scopus 로고    scopus 로고
    • Expression, purification and assembly of soluble multimeric MHC class II-invariant chain complexes
    • Majera D, Kristan KC, Neefjes J, Turk D, Mihelic M (2012) Expression, purification and assembly of soluble multimeric MHC class II-invariant chain complexes. FEBS Lett 586: 1318-24
    • (2012) FEBS Lett , vol.586 , pp. 1318-1324
    • Majera, D.1    Kristan, K.C.2    Neefjes, J.3    Turk, D.4    Mihelic, M.5
  • 58
    • 78650895128 scopus 로고    scopus 로고
    • Towards universal structure-based prediction of class II MHC epitopes for diverse allotypes
    • Bordner AJ (2010) Towards universal structure-based prediction of class II MHC epitopes for diverse allotypes. PLoS One 5:e14383
    • (2010) PLoS One , vol.5 , pp. e14383
    • Bordner, A.J.1
  • 60
    • 0028823585 scopus 로고
    • The structure of an intermediate in class II MHC maturation: CLIP bound to HLADR3
    • Wiley DC
    • Ghosh P, Amaya M, Mellins E, Wiley DC (1995) The structure of an intermediate in class II MHC maturation: CLIP bound to HLADR3. Nature 378: 457-462
    • (1995) Nature , vol.378 , pp. 457-462
    • Ghosh, P.1    Amaya, M.2    Mellins, E.3
  • 61
    • 0031572833 scopus 로고    scopus 로고
    • The class II MHC protein HLA-DR1 in complex with an endogenous peptide: Implications for the structural basis of the specificity of peptide binding
    • Murthy VL, Stern LJ (1997) The class II MHC protein HLA-DR1 in complex with an endogenous peptide: implications for the structural basis of the specificity of peptide binding. Structure 5: 1385-96
    • (1997) Structure , vol.5 , pp. 1385-1396
    • Murthy, V.L.1    Stern, L.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.