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Volumn 112, Issue 1, 2015, Pages 202-207

Dipeptides catalyze rapid peptide exchange on MHC class I molecules

Author keywords

Dipeptides; Immunotherapy; MHC tetramers; Peptide exchange; Tapasin

Indexed keywords

DIPEPTIDE; MAJOR HISTOCOMPATIBILITY COMPLEX CLASS I PROTEIN; MONOMER; POLYMER; PROTEIN; TAPASIN; TETRAMER; UNCLASSIFIED DRUG; CYCLOHEXYLALANINE; EPITOPE; HLA ANTIGEN CLASS 1; PHENYLALANINE;

EID: 84920393219     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1418690112     Document Type: Article
Times cited : (45)

References (30)
  • 1
    • 0028943275 scopus 로고
    • The three-dimensional structure of peptide-MHC complexes
    • Madden DR (1995) The three-dimensional structure of peptide-MHC complexes. Annu Rev Immunol 13:587-622.
    • (1995) Annu Rev Immunol , vol.13 , pp. 587-622
    • Madden, D.R.1
  • 2
    • 33749528390 scopus 로고    scopus 로고
    • Confronting complexity: Real-world immunodominance in antiviral CD8+ T cell responses
    • Yewdell JW (2006) Confronting complexity: Real-world immunodominance in antiviral CD8+ T cell responses. Immunity 25(4):533-543.
    • (2006) Immunity , vol.25 , Issue.4 , pp. 533-543
    • Yewdell, J.W.1
  • 3
    • 26244451375 scopus 로고    scopus 로고
    • The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex
    • Elliott T, Williams A (2005) The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex. Immunol Rev 207:89-99.
    • (2005) Immunol Rev , vol.207 , pp. 89-99
    • Elliott, T.1    Williams, A.2
  • 4
    • 84880756901 scopus 로고    scopus 로고
    • The MHC I loading complex: A multitasking machinery in adaptive immunity
    • Hulpke S, Tampé R (2013) The MHC I loading complex: A multitasking machinery in adaptive immunity. Trends Biochem Sci 38(8):412-420.
    • (2013) Trends Biochem Sci , vol.38 , Issue.8 , pp. 412-420
    • Hulpke, S.1    Tampé, R.2
  • 5
    • 84884296628 scopus 로고    scopus 로고
    • Dipeptides promote folding and peptide binding of MHC class I molecules
    • Saini SK, et al. (2013) Dipeptides promote folding and peptide binding of MHC class I molecules. Proc Natl Acad Sci USA 110(38):15383-15388.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.38 , pp. 15383-15388
    • Saini, S.K.1
  • 6
    • 46349107222 scopus 로고    scopus 로고
    • Anchor side chains of short peptide fragments trigger ligand-exchange of class II MHC molecules
    • Gupta S, et al. (2008) Anchor side chains of short peptide fragments trigger ligand-exchange of class II MHC molecules. PLoS ONE 3(3):e1814.
    • (2008) PLoS ONE , vol.3 , Issue.3 , pp. e1814
    • Gupta, S.1
  • 7
    • 38949197822 scopus 로고    scopus 로고
    • Short peptide sequences mimic HLA-DM functions
    • Chou CL, et al. (2008) Short peptide sequences mimic HLA-DM functions. Mol Immunol 45(7):1935-1943.
    • (2008) Mol Immunol , vol.45 , Issue.7 , pp. 1935-1943
    • Chou, C.L.1
  • 8
    • 84873305369 scopus 로고    scopus 로고
    • Not all empty MHC class I molecules are molten globules: Tryptophan fluorescence reveals a two-step mechanism of thermal denaturation
    • Saini SK, et al. (2013) Not all empty MHC class I molecules are molten globules: Tryptophan fluorescence reveals a two-step mechanism of thermal denaturation. Mol Immunol 54(3-4):386-396.
    • (2013) Mol Immunol , vol.54 , Issue.3-4 , pp. 386-396
    • Saini, S.K.1
  • 9
    • 75549084463 scopus 로고    scopus 로고
    • The immune epitope database 2.0
    • Vita R, et al. (2010) The immune epitope database 2.0. Nucleic Acids Res 38(Database issue):D854-D862.
    • (2010) Nucleic Acids Res , vol.38 , Issue.DATABASE ISSUE , pp. D854-D862
    • Vita, R.1
  • 10
    • 0035993241 scopus 로고    scopus 로고
    • Establishment of a quantitative ELISA capable of determining peptide - MHC class I interaction
    • Sylvester-Hvid C, et al. (2002) Establishment of a quantitative ELISA capable of determining peptide - MHC class I interaction. Tissue Antigens 59(4):251-258.
    • (2002) Tissue Antigens , vol.59 , Issue.4 , pp. 251-258
    • Sylvester-Hvid, C.1
  • 11
    • 0025076114 scopus 로고
    • Empty MHC class I molecules come out in the cold
    • Ljunggren HG, et al. (1990) Empty MHC class I molecules come out in the cold. Nature 346(6283):476-480.
    • (1990) Nature , vol.346 , Issue.6283 , pp. 476-480
    • Ljunggren, H.G.1
  • 12
    • 0028224014 scopus 로고
    • LacZ inducible, antigen/MHC-specific T cell hybrids
    • Sanderson S, Shastri N (1994) LacZ inducible, antigen/MHC-specific T cell hybrids. Int Immunol 6(3):369-376.
    • (1994) Int Immunol , vol.6 , Issue.3 , pp. 369-376
    • Sanderson, S.1    Shastri, N.2
  • 13
    • 0029743737 scopus 로고    scopus 로고
    • Phenotypic analysis of antigen-specific T lymphocytes
    • Altman JD, et al. (1996) Phenotypic analysis of antigen-specific T lymphocytes. Science 274(5284):94-96.
    • (1996) Science , vol.274 , Issue.5284 , pp. 94-96
    • Altman, J.D.1
  • 14
    • 34347266953 scopus 로고    scopus 로고
    • Generation of peptide-MHC class I complexes through UV-mediated ligand exchange
    • Rodenko B, et al. (2006) Generation of peptide-MHC class I complexes through UV-mediated ligand exchange. Nat Protoc 1(3):1120-1132.
    • (2006) Nat Protoc , vol.1 , Issue.3 , pp. 1120-1132
    • Rodenko, B.1
  • 15
    • 69349092258 scopus 로고    scopus 로고
    • Class I major histocompatibility complexes loaded by a periodate trigger
    • Rodenko B, et al. (2009) Class I major histocompatibility complexes loaded by a periodate trigger. J Am Chem Soc 131(34):12305-12313.
    • (2009) J Am Chem Soc , vol.131 , Issue.34 , pp. 12305-12313
    • Rodenko, B.1
  • 16
    • 5044224594 scopus 로고    scopus 로고
    • Tapasin and other chaperones: Models of the MHC class I loading complex
    • Wright CA, Kozik P, Zacharias M, Springer S (2004) Tapasin and other chaperones: Models of the MHC class I loading complex. Biol Chem 385(9):763-778.
    • (2004) Biol Chem , vol.385 , Issue.9 , pp. 763-778
    • Wright, C.A.1    Kozik, P.2    Zacharias, M.3    Springer, S.4
  • 17
    • 0036230677 scopus 로고    scopus 로고
    • Optimization of the MHC class I peptide cargo is dependent on tapasin
    • Williams AP, Peh CA, Purcell AW, McCluskey J, Elliott T (2002) Optimization of the MHC class I peptide cargo is dependent on tapasin. Immunity 16(4):509-520.
    • (2002) Immunity , vol.16 , Issue.4 , pp. 509-520
    • Williams, A.P.1    Peh, C.A.2    Purcell, A.W.3    McCluskey, J.4    Elliott, T.5
  • 18
    • 77956297939 scopus 로고    scopus 로고
    • The cell biology of major histocompatibility complex class I assembly: Towards a molecular understanding
    • Van Hateren A, et al. (2010) The cell biology of major histocompatibility complex class I assembly: Towards a molecular understanding. Tissue Antigens 76(4):259-275.
    • (2010) Tissue Antigens , vol.76 , Issue.4 , pp. 259-275
    • Van Hateren, A.1
  • 19
    • 34547121970 scopus 로고    scopus 로고
    • Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer
    • Wearsch PA, Cresswell P (2007) Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer. Nat Immunol 8(8):873-881.
    • (2007) Nat Immunol , vol.8 , Issue.8 , pp. 873-881
    • Wearsch, P.A.1    Cresswell, P.2
  • 20
    • 33947606283 scopus 로고    scopus 로고
    • Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection
    • Chen M, Bouvier M(2007) Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection. EMBO J 26(6):1681-1690.
    • (2007) EMBO J , vol.26 , Issue.6 , pp. 1681-1690
    • Chen, M.1    Bouvier, M.2
  • 21
    • 74249105478 scopus 로고    scopus 로고
    • Tapasin edits peptides on MHC class I molecules by accelerating peptide exchange
    • Praveen PV, Yaneva R, Kalbacher H, Springer S (2010) Tapasin edits peptides on MHC class I molecules by accelerating peptide exchange. Eur J Immunol 40(1):214-224.
    • (2010) Eur J Immunol , vol.40 , Issue.1 , pp. 214-224
    • Praveen, P.V.1    Yaneva, R.2    Kalbacher, H.3    Springer, S.4
  • 22
    • 58149215628 scopus 로고    scopus 로고
    • Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer
    • Dong G, Wearsch PA, Peaper DR, Cresswell P, Reinisch KM (2009) Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer. Immunity 30(1):21-32.
    • (2009) Immunity , vol.30 , Issue.1 , pp. 21-32
    • Dong, G.1    Wearsch, P.A.2    Peaper, D.R.3    Cresswell, P.4    Reinisch, K.M.5
  • 23
    • 84871595445 scopus 로고    scopus 로고
    • Crystal structure of the HLA-DM-HLA-DR1 complex defines mechanisms for rapid peptide selection
    • Pos W, et al. (2012) Crystal structure of the HLA-DM-HLA-DR1 complex defines mechanisms for rapid peptide selection. Cell 151(7):1557-1568.
    • (2012) Cell , vol.151 , Issue.7 , pp. 1557-1568
    • Pos, W.1
  • 24
    • 33646038285 scopus 로고    scopus 로고
    • Small molecules that enhance the catalytic efficiency of HLA-DM
    • Nicholson MJ, et al. (2006) Small molecules that enhance the catalytic efficiency of HLA-DM. J Immunol 176(7):4208-4220.
    • (2006) J Immunol , vol.176 , Issue.7 , pp. 4208-4220
    • Nicholson, M.J.1
  • 25
    • 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 (2010) Peptide binding to MHC class I and II proteins: New avenues from new methods. Mol Immunol 47(4):649-657.
    • (2010) Mol Immunol , vol.47 , Issue.4 , pp. 649-657
    • Yaneva, R.1    Schneeweiss, C.2    Zacharias, M.3    Springer, S.4
  • 26
    • 84893833939 scopus 로고    scopus 로고
    • Beyond model antigens: High-dimensional methods for the analysis of antigen-specific T cells
    • Newell EW, Davis MM (2014) Beyond model antigens: High-dimensional methods for the analysis of antigen-specific T cells. Nat Biotechnol 32(2):149-157.
    • (2014) Nat Biotechnol , vol.32 , Issue.2 , pp. 149-157
    • Newell, E.W.1    Davis, M.M.2
  • 27
    • 84880721353 scopus 로고    scopus 로고
    • Dendritic-cell-based therapeutic cancer vaccines
    • Palucka K, Banchereau J (2013) Dendritic-cell-based therapeutic cancer vaccines. Immunity 39(1):38-48.
    • (2013) Immunity , vol.39 , Issue.1 , pp. 38-48
    • Palucka, K.1    Banchereau, J.2
  • 28
    • 0026529908 scopus 로고
    • HLA-A2-peptide complexes: Refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides
    • Garboczi DN, Hung DT, Wiley DC (1992) HLA-A2-peptide complexes: Refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides. Proc Natl Acad Sci USA 89(8):3429-3433.
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.8 , pp. 3429-3433
    • Garboczi, D.N.1    Hung, D.T.2    Wiley, D.C.3
  • 29
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink MR (1994) The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys J 66(2 Pt 1):482-501.
    • (1994) Biophys J , vol.66 , Issue.2 , pp. 482-501
    • Eftink, M.R.1
  • 30
    • 0026639652 scopus 로고
    • Detection of rare antigen-presenting cells by the lacZ T-cell activation assay suggests an expression cloning strategy for T-cell antigens
    • Karttunen J, Sanderson S, Shastri N (1992) Detection of rare antigen-presenting cells by the lacZ T-cell activation assay suggests an expression cloning strategy for T-cell antigens. Proc Natl Acad Sci USA 89(13):6020-6024.
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.13 , pp. 6020-6024
    • Karttunen, J.1    Sanderson, S.2    Shastri, N.3


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