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Volumn 109, Issue 12, 2012, Pages 4580-4585

Promiscuous binding of extracellular peptides to cell surface class I MHC protein

Author keywords

[No Author keywords available]

Indexed keywords

EXTRACELLULAR PEPTIDE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PEPTIDE; UNCLASSIFIED DRUG;

EID: 84863350387     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1201586109     Document Type: Article
Times cited : (39)

References (39)
  • 1
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M (2011) Molecular chaperones in protein folding and proteostasis. Nature 475:324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 2
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • DOI 10.1093/emboj/16.7.1501
    • Rüdiger S, Germeroth L, Schneider-Mergener J, Bukau B (1997) Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J 16:1501-1507. (Pubitemid 27151945)
    • (1997) EMBO Journal , vol.16 , Issue.7 , pp. 1501-1507
    • Rudiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 3
    • 0025855156 scopus 로고
    • Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
    • Falk K, Rötzschke O, Stevanović S, Jung G, Rammensee HG (1991) Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 351:290-296. (Pubitemid 21896578)
    • (1991) Nature , vol.351 , Issue.6324 , pp. 290-296
    • Falk, K.1    Rotzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.-G.5
  • 4
    • 0029902364 scopus 로고    scopus 로고
    • Self-MHC-restricted peptides recognized by an alloreactive T lymphocyte clone
    • Udaka K, Wiesmüller KH, Kienle S, Jung G, Walden P (1996) Self-MHC-restricted peptides recognized by an alloreactive T lymphocyte clone. J Immunol 157:670-678. (Pubitemid 26231370)
    • (1996) Journal of Immunology , vol.157 , Issue.2 , pp. 670-678
    • Udaka, K.1    Wiesmuller, K.-H.2    Kienle, S.3    Jung, G.4    Walden, P.5
  • 6
    • 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 25:533-543.
    • (2006) Immunity , vol.25 , pp. 533-543
    • Yewdell, J.W.1
  • 7
    • 0035525290 scopus 로고    scopus 로고
    • Cross-presentation in viral immunity and self-tolerance
    • Heath WR, Carbone FR (2001) Cross-presentation in viral immunity and self-tolerance. Nat Rev Immunol 1:126-134. (Pubitemid 33741966)
    • (2001) Nature Reviews Immunology , vol.1 , Issue.2 , pp. 126-134
    • Heath, W.R.1    Carbone, F.R.2
  • 9
    • 77949872804 scopus 로고    scopus 로고
    • Unique autoreactive T cells recognize insulin peptides generated within the islets of Langerhans in autoimmune diabetes
    • Mohan JF, et al. (2010) Unique autoreactive T cells recognize insulin peptides generated within the islets of Langerhans in autoimmune diabetes. Nat Immunol 11:350-354.
    • (2010) Nat Immunol , vol.11 , pp. 350-354
    • Mohan, J.F.1
  • 10
    • 0346521283 scopus 로고    scopus 로고
    • Making sense of mass destruction: Quantitating MHC class I antigen presentation
    • Yewdell JW, Reits E, Neefjes J (2003) Making sense of mass destruction: Quantitating MHC class I antigen presentation. Nat Rev Immunol 3:952-961. (Pubitemid 37521537)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.12 , pp. 952-961
    • Yewdell, J.W.1    Reits, E.2    Neefjes, J.3
  • 11
    • 56949107069 scopus 로고    scopus 로고
    • The quality control of MHC class I peptide loading
    • Wearsch PA, Cresswell P (2008) The quality control of MHC class I peptide loading. Curr Opin Cell Biol 20:624-631.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 624-631
    • Wearsch, P.A.1    Cresswell, P.2
  • 12
    • 0035501063 scopus 로고    scopus 로고
    • Stability of surface H-2K(b), H-2D(b), and peptide-receptive H-2K(b) on splenocytes
    • Su RC, Miller RG (2001) Stability of surface H-2K(b), H-2D(b), and peptide-receptive H-2K(b) on splenocytes. J Immunol 167:4869-4877.
    • (2001) J Immunol , vol.167 , pp. 4869-4877
    • Su, R.C.1    Miller, R.G.2
  • 13
    • 0038670730 scopus 로고    scopus 로고
    • Thermodynamic and kinetic analysis of a peptide-class I MHC interaction highlights the noncovalent nature and conformational dynamics of the class I heterotrimer
    • DOI 10.1021/bi034077m
    • Binz AK, Rodriguez RC, Biddison WE, Baker BM (2003) Thermodynamic and kinetic analysis of a peptide-class I MHC interaction highlights the noncovalent nature and conformational dynamics of the class I heterotrimer. Biochemistry 42:4954-4961. (Pubitemid 36532048)
    • (2003) Biochemistry , vol.42 , Issue.17 , pp. 4954-4961
    • Binz, A.-K.1    Rodriguez, R.C.2    Biddison, W.E.3    Baker, B.M.4
  • 14
    • 0030446828 scopus 로고    scopus 로고
    • Peptide interaction with a class I major histocompatibility complex-encoded molecule: Allosteric control of the ternary complex stability
    • Gakamsky DM, Bjorkman PJ, Pecht I (1996) Peptide interaction with a class I major histocompatibility complex-encoded molecule: Allosteric control of the ternary complex stability. Biochemistry 35:14841-14848.
    • (1996) Biochemistry , vol.35 , pp. 14841-14848
    • Gakamsky, D.M.1    Bjorkman, P.J.2    Pecht, I.3
  • 15
    • 0033554405 scopus 로고    scopus 로고
    • An allosteric mechanism controls antigen presentation by the H-2K(b) complex
    • Gakamsky DM, et al. (1999) An allosteric mechanism controls antigen presentation by the H-2K(b) complex. Biochemistry 38:12165-12173.
    • (1999) Biochemistry , vol.38 , pp. 12165-12173
    • Gakamsky, D.M.1
  • 16
    • 0025006862 scopus 로고
    • Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro
    • Schumacher TN, et al. (1990) Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro. Cell 62:563-567.
    • (1990) Cell , vol.62 , pp. 563-567
    • Schumacher, T.N.1
  • 17
    • 0027074320 scopus 로고
    • Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule
    • Fahnestock ML, Tamir I, Narhi L, Bjorkman PJ (1992) Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule. Science 258:1658-1662. (Pubitemid 23012440)
    • (1992) Science , vol.258 , Issue.5088 , pp. 1658-1662
    • Fahnestock, M.L.1    Tamir, I.2    Narhi, L.3    Bjorkman, P.J.4
  • 18
    • 0023785318 scopus 로고
    • Selective expression of an antigen receptor on CD8-bearing T lymphocytes in transgenic mice
    • Sha WC, et al. (1988) Selective expression of an antigen receptor on CD8-bearing T lymphocytes in transgenic mice. Nature 335:271-274.
    • (1988) Nature , vol.335 , pp. 271-274
    • Sha, W.C.1
  • 20
    • 33846248827 scopus 로고    scopus 로고
    • Cellular uptake followed by class I MHC presentation of some exogenous peptides contributes to T cell stimulatory capacity
    • DOI 10.1016/j.molimm.2006.11.016, PII S0161589006006924
    • Brophy SE, Jones LL, Holler PD, Kranz DM (2007) Cellular uptake followed by class I MHC presentation of some exogenous peptides contributes to T cell stimulatory capacity. Mol Immunol 44:2184-2194. (Pubitemid 46097122)
    • (2007) Molecular Immunology , vol.44 , Issue.9 , pp. 2184-2194
    • Brophy, S.E.1    Jones, L.L.2    Holler, P.D.3    Kranz, D.M.4
  • 21
    • 0027105145 scopus 로고
    • In vitro peptide binding to soluble empty class I major histocompatibility complex molecules isolated from transfected Drosophila melanogaster cells
    • Matsumura M, Saito Y, Jackson MR, Song ES, Peterson PA (1992) In vitro peptide binding to soluble empty class I major histocompatibility complex molecules isolated from transfected Drosophila melanogaster cells. J Biol Chem 267:23589-23595. (Pubitemid 23088159)
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.33 , pp. 23589-23595
    • Matsumura, M.1    Saito, Y.2    Jackson, M.R.3    Song, E.S.4    Peterson, P.A.5
  • 22
    • 0027983589 scopus 로고
    • Determinant selection of major histocompatibility complex class I-restricted antigenic peptides is explained by class I-peptide affinity and is strongly influenced by nondominant anchor residues
    • Chen W, Khilko S, Fecondo J, Margulies DH, McCluskey J (1994) Determinant selection of major histocompatibility complex class I-restricted antigenic peptides is explained by class I-peptide affinity and is strongly influenced by nondominant anchor residues. J Exp Med 180:1471-1483.
    • (1994) J Exp Med , vol.180 , pp. 1471-1483
    • Chen, W.1    Khilko, S.2    Fecondo, J.3    Margulies, D.H.4    McCluskey, J.5
  • 23
    • 0020170182 scopus 로고
    • Localization of allodeterminants on H-2Kb antigens determined with monoclonal antibodies and H-2 mutant mice
    • Hämmerling GJ, Rüsch E, Tada N, Kimura S, Hämmerling U (1982) Localization of allodeterminants on H-2Kb antigens determined with monoclonal antibodies and H-2 mutant mice. Proc Natl Acad Sci USA 79:4737-4741.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4737-4741
    • Hämmerling, G.J.1    Rüsch, E.2    Tada, N.3    Kimura, S.4    Hämmerling, U.5
  • 24
    • 79960951687 scopus 로고    scopus 로고
    • Cellular uptake mechanisms and toxicity of quantum dots in dendritic cells
    • Zhang LW, Bäumer W, Monteiro-Riviere NA (2011) Cellular uptake mechanisms and toxicity of quantum dots in dendritic cells. Nanomedicine (Lond) 6:777-791.
    • (2011) Nanomedicine (Lond) , vol.6 , pp. 777-791
    • Zhang, L.W.1    Bäumer, W.2    Monteiro-Riviere, N.A.3
  • 25
    • 59449094834 scopus 로고    scopus 로고
    • NetMHCpan, a method for MHC class I binding prediction beyond humans
    • Hoof I, et al. (2009) NetMHCpan, a method for MHC class I binding prediction beyond humans. Immunogenetics 61:1-13.
    • (2009) Immunogenetics , vol.61 , pp. 1-13
    • Hoof, I.1
  • 26
    • 77952742298 scopus 로고    scopus 로고
    • Effects of thymic selection of the T-cell repertoire on HLA class I-associated control of HIV infection
    • Kosmrlj A, et al. (2010) Effects of thymic selection of the T-cell repertoire on HLA class I-associated control of HIV infection. Nature 465:350-354.
    • (2010) Nature , vol.465 , pp. 350-354
    • Kosmrlj, A.1
  • 28
    • 4444301196 scopus 로고    scopus 로고
    • Phylogenetic profiling of the Arabidopsis thaliana proteome: What proteins distinguish plants from other organisms?
    • Gutiérrez RA, Green PJ, Keegstra K, Ohlrogge JB (2004) Phylogenetic profiling of the Arabidopsis thaliana proteome: What proteins distinguish plants from other organisms? Genome Biol 5:R53.
    • (2004) Genome Biol , vol.5
    • Gutiérrez, R.A.1    Green, P.J.2    Keegstra, K.3    Ohlrogge, J.B.4
  • 29
    • 0028410566 scopus 로고
    • Kinetics and affinity of reactions between an antigen-specific T cell receptor and peptide-MHC complexes
    • Sykulev Y, et al. (1994) Kinetics and affinity of reactions between an antigen-specific T cell receptor and peptide-MHC complexes. Immunity 1:15-22.
    • (1994) Immunity , vol.1 , pp. 15-22
    • Sykulev, Y.1
  • 30
    • 0028169020 scopus 로고
    • A cytotoxic T lymphocyte clone can recognize the same naturally occurring self peptide in association with a self and nonself class I MHC protein
    • Dutz JP, Tsomides TJ, Kageyama S, Rasmussen MH, Eisen HN (1994) A cytotoxic T lymphocyte clone can recognize the same naturally occurring self peptide in association with a self and nonself class I MHC protein. Mol Immunol 31:967-975.
    • (1994) Mol Immunol , vol.31 , pp. 967-975
    • Dutz, J.P.1    Tsomides, T.J.2    Kageyama, S.3    Rasmussen, M.H.4    Eisen, H.N.5
  • 33
    • 0345516047 scopus 로고    scopus 로고
    • b upon peptide binding
    • DOI 10.1021/bi9717441
    • Springer S, Doring K, Skipper JC, Townsend AR, Cerundolo V (1998) Fast association rates suggest a conformational change in the MHC class I molecule H-2Db upon peptide binding. Biochemistry 37:3001-3012. (Pubitemid 28145753)
    • (1998) Biochemistry , vol.37 , Issue.9 , pp. 3001-3012
    • Springer, S.1    Doring, K.2    Skipper, J.C.A.3    Townsend, A.R.M.4    Cerundolo, V.5
  • 34
    • 0032780521 scopus 로고    scopus 로고
    • Distance estimates from paramagnetic enhancements of nuclear relaxation in linear and flexible model peptides
    • Jacob J, Baker B, Bryant RG, Cafiso DS (1999) Distance estimates from paramagnetic enhancements of nuclear relaxation in linear and flexible model peptides. Biophys J 77:1086-1092. (Pubitemid 29362478)
    • (1999) Biophysical Journal , vol.77 , Issue.2 , pp. 1086-1092
    • Jacob, J.1    Baker, B.2    Bryant, R.G.3    Cafiso, D.S.4
  • 35
    • 81155132239 scopus 로고    scopus 로고
    • Loss of T cell antigen recognition arising from changes in peptide and major histocompatibility complex protein flexibility: Implications for vaccine design
    • Insaidoo FK, et al. (2011) Loss of T cell antigen recognition arising from changes in peptide and major histocompatibility complex protein flexibility: Implications for vaccine design. J Biol Chem 286:40163-40173.
    • (2011) J Biol Chem , vol.286 , pp. 40163-40173
    • Insaidoo, F.K.1
  • 36
    • 79959334212 scopus 로고    scopus 로고
    • Systematic identification of immunodominant CD8+ T-cell responses to influenza A virus in HLA-A2 individuals
    • Wu C, et al. (2011) Systematic identification of immunodominant CD8+ T-cell responses to influenza A virus in HLA-A2 individuals. Proc Natl Acad Sci USA 108:9178-9183.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 9178-9183
    • Wu, C.1
  • 39
    • 0030849769 scopus 로고    scopus 로고
    • Localization, quantitation, and in situ detection of specific peptide- MHC class I complexes using a monoclonal antibody
    • DOI 10.1016/S1074-7613(00)80447-1
    • Porgador A, Yewdell JW, Deng Y, Bennink JR, Germain RN (1997) Localization, quantitation, and in situ detection of specific peptide-MHC class I complexes using a monoclonal antibody. Immunity 6:715-726. (Pubitemid 27305734)
    • (1997) Immunity , vol.6 , Issue.6 , pp. 715-726
    • Porgador, A.1    Yewdell, J.W.2    Deng, Y.3    Bennink, J.R.4    Germain, R.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.