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Pamer EG, Cresswell P. Mechanisms of MHC class I-restricted antigen processing. Annu Rev Immunol. 15:1998;. in press.
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Pamer, E.G.1
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Cloning and functional characterization of a subunit of the transporter associated with antigen processing
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Li, S.1
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5
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0030865333
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A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes
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Ortmann B, Copeman J, Lehner PJ, Sadasivan B, Herberg JA, Grandea AG, Riddell SR, Tampe R, Spies T, Trowsdale J, Cresswell P. A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes. Science. 277:1997;1306-1309.
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Ortmann, B.1
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Grandea, A.G.6
Riddell, S.R.7
Tampe, R.8
Spies, T.9
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6
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0028943275
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The three-dimensional structure of peptide-MHC complexes
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Madden DR. The three-dimensional structure of peptide-MHC complexes. Annu Rev Immunol. 13:1995;587-622.
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Madden, D.R.1
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7
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0025855156
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Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
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Falk, K.1
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8
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0028344533
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Structure of peptides associated with class I and class II molecules
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Engelhard VH. Structure of peptides associated with class I and class II molecules. Annu Rev Immunol. 12:1994;181-207.
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Engelhard, V.H.1
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0029888847
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Needles in haystacks. Identifying specific peptide antigens for T-cells
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Shastri N. Needles in haystacks. Identifying specific peptide antigens for T-cells. Curr Opin Immunol. 8:1996;271-277.
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Shastri, N.1
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12
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+ cytotoxic lymphocytes in association with a class I MHC protein
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+ cytotoxic lymphocytes in association with a class I MHC protein. Cell. 69:1992;989-998.
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Udaka, K.1
Tsomides, T.J.2
Eisen, H.N.3
-
13
-
-
0030588548
-
+ T-cells can recognize unusual, rare and unique processed peptide/MHC complexes
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of outstanding interest. This report, together with [14], demonstrate examples of naturally processed peptides that do not conform to the consensus motifs and are expressed at less than 50 copies/cell.
-
+ T-cells can recognize unusual, rare and unique processed peptide/MHC complexes. J Immunol. 157:1996;4464-4473 This report, together with [14], demonstrate examples of naturally processed peptides that do not conform to the consensus motifs and are expressed at less than 50 copies/cell.
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J Immunol
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Malarkannan, S.1
Gonzalez, F.2
Nguyen, V.3
Adair, G.4
Shastri, N.5
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14
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-
0030715545
-
Minors held by majors. The H13 minor histocompatibility locus defined as a peptide/MHC class I complex
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of outstanding interest. This report, together with [13], demonstrates examples of naturally processed peptides that do not conform to the consensus motifs and are expressed at less than 50 copies/cell.
-
of outstanding interest Mendoza L, Paz P, Zuberi AR, Christianson G, Roopenian DC, Shastri N. Minors held by majors. The H13 minor histocompatibility locus defined as a peptide/MHC class I complex. Immunity. 7:1997;461-472 This report, together with [13], demonstrates examples of naturally processed peptides that do not conform to the consensus motifs and are expressed at less than 50 copies/cell.
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(1997)
Immunity
, vol.7
, pp. 461-472
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Mendoza, L.1
Paz, P.2
Zuberi, A.R.3
Christianson, G.4
Roopenian, D.C.5
Shastri, N.6
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16
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0030176270
-
Evidence that a single peptide-MHC complex on a target cell can elicit a cytolytic T cell response
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Sykulev Y, Joo M, Vturina I, Tsomides TJ, Eisen HN. Evidence that a single peptide-MHC complex on a target cell can elicit a cytolytic T cell response. Immunity. 4:1996;565-571.
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Immunity
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Sykulev, Y.1
Joo, M.2
Vturina, I.3
Tsomides, T.J.4
Eisen, H.N.5
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17
-
-
0001433072
-
An HLA-A2 restricted tyrosinase antigen on melanoma cells results from post-translational modification and suggests a distinct antigen processing pathway for membrane proteins
-
of outstanding interest. This, together with [18], reports on examples of post-translationally modified naturally processed peptides analyzed by innovative mass spectrometry methods.
-
of outstanding interest Skipper JCA, Hendrickson RC, Gulden PH, Brichard V, Van Pel A, Chen Y, Shabanowitz J, Wolfel T, Slingluff CL, Boon T, et al. An HLA-A2 restricted tyrosinase antigen on melanoma cells results from post-translational modification and suggests a distinct antigen processing pathway for membrane proteins. J Exp Med. 183:1996;527-534 This, together with [18], reports on examples of post-translationally modified naturally processed peptides analyzed by innovative mass spectrometry methods.
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(1996)
J Exp Med
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-
Skipper, J.C.A.1
Hendrickson, R.C.2
Gulden, P.H.3
Brichard, V.4
Van Pel, A.5
Chen, Y.6
Shabanowitz, J.7
Wolfel, T.8
Slingluff, C.L.9
Boon, T.10
-
18
-
-
0030615171
-
The HLA-A*0201-Restricted H-Y antigen contains a posttranslationally modified cysteine that significantly affects T cell recognition
-
of outstanding interest. This, together with [17], reports on examples of post-translationally modified naturally processed peptides analyzed by innovative mass spectrometry methods.
-
of outstanding interest Meadows L, Wang W, den Haan JMM, Blokland E, Reinhardus C, Drijfhout JW, Shabanowitz J, Pierce R, Agulnik AI, Bishop CE, et al. The HLA-A*0201-Restricted H-Y antigen contains a posttranslationally modified cysteine that significantly affects T cell recognition. Immunity. 6:1997;273-281 This, together with [17], reports on examples of post-translationally modified naturally processed peptides analyzed by innovative mass spectrometry methods.
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(1997)
Immunity
, vol.6
, pp. 273-281
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Meadows, L.1
Wang, W.2
Den Haan, J.M.M.3
Blokland, E.4
Reinhardus, C.5
Drijfhout, J.W.6
Shabanowitz, J.7
Pierce, R.8
Agulnik, A.I.9
Bishop, C.E.10
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19
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-
0026507564
-
Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry
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Hunt DF, Henderson RA, Shabanowitz J, Sakaguchi K, Michel H, Sevilir N, Cox AL, Appella E, Engelhard VH. Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry. Science. 255:1992;1261-1263.
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Hunt, D.F.1
Henderson, R.A.2
Shabanowitz, J.3
Sakaguchi, K.4
Michel, H.5
Sevilir, N.6
Cox, A.L.7
Appella, E.8
Engelhard, V.H.9
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20
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-
0028304337
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Identification of a peptide recognized by five melanoma-specific human cytoxic T cell lines
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Cox AL, Skipper J, Chen Y, Henderson RA, Darrow TL, Shabanowitz J, Engelhard VH, Hunt DF, Slingluff CL Jr. Identification of a peptide recognized by five melanoma-specific human cytoxic T cell lines. Science. 264:1994;716-719.
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Cox, A.L.1
Skipper, J.2
Chen, Y.3
Henderson, R.A.4
Darrow, T.L.5
Shabanowitz, J.6
Engelhard, V.H.7
Hunt, D.F.8
Slingluff C.L., Jr.9
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21
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0028501143
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Efficiency of MHC class I antigen processing: A quantitative analysis
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Villanueva MS, Fischer P, Feen K, Pamer EG. Efficiency of MHC class I antigen processing: A quantitative analysis. Immunity. 1:1994;479-489.
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(1994)
Immunity
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Villanueva, M.S.1
Fischer, P.2
Feen, K.3
Pamer, E.G.4
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22
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0031569179
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MHC class I-associated peptides produced from endogenous gene products with vastly different efficiencies
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Anton LC, Yewdell JW, Bennink JR. MHC class I-associated peptides produced from endogenous gene products with vastly different efficiencies. J Immunol. 158:1997;2535-2542.
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J Immunol
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Anton, L.C.1
Yewdell, J.W.2
Bennink, J.R.3
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23
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0029003999
-
Inhibition of antigen processing by the internal repeat region of the Epstein-Barr virus nuclear antigen-1
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Levitskaya J, Coram M, Levitsky V, Imreh S, Steigerwald-Mullen PM, Klein G, Kurilla MG, Masucci MG. Inhibition of antigen processing by the internal repeat region of the Epstein-Barr virus nuclear antigen-1. Nature. 375:1995;685-688.
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Levitskaya, J.1
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Imreh, S.4
Steigerwald-Mullen, P.M.5
Klein, G.6
Kurilla, M.G.7
Masucci, M.G.8
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24
-
-
0029805272
-
Cytomegalovirus selectively blocks antigen processing and presentation of its immediate-early gene product
-
of special interest. In this report, and in [25], the authors show that certain viral proteins are exempt from the endogenous antigen-processing pathway. The EBNA1 protein is instead processed by the exogenous MHC class I-processing pathway.
-
of special interest Gilbert MJ, Riddell SR, Plachter B, Greenberg PD. Cytomegalovirus selectively blocks antigen processing and presentation of its immediate-early gene product. Nature. 383:1996;720-722 In this report, and in [25], the authors show that certain viral proteins are exempt from the endogenous antigen-processing pathway. The EBNA1 protein is instead processed by the exogenous MHC class I-processing pathway.
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(1996)
Nature
, vol.383
, pp. 720-722
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Gilbert, M.J.1
Riddell, S.R.2
Plachter, B.3
Greenberg, P.D.4
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25
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-
0031414705
-
Human CD8(+) T cell responses to EBV EBNA1: HLA class I presentation of the (Gly-Ala)-containing protein requires exogenous processing
-
of special interest. In this report, and in [24], the authors show that certain viral proteins are exempt from the endogenous antigen-processing pathway. The EBNA1 protein is instead processed by the exogenous MHC class I-processing pathway.
-
of special interest Blake N, Lee S, Redchenko I, Thomas W, Steven N, Leese A, SteigerwaldMullen P, Kurilla MG, Frappier L, Rickinson A. Human CD8(+) T cell responses to EBV EBNA1: HLA class I presentation of the (Gly-Ala)-containing protein requires exogenous processing. Immunity. 7:1997;791-802 In this report, and in [24], the authors show that certain viral proteins are exempt from the endogenous antigen-processing pathway. The EBNA1 protein is instead processed by the exogenous MHC class I-processing pathway.
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(1997)
Immunity
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, pp. 791-802
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Blake, N.1
Lee, S.2
Redchenko, I.3
Thomas, W.4
Steven, N.5
Leese, A.6
Steigerwaldmullen, P.7
Kurilla, M.G.8
Frappier, L.9
Rickinson, A.10
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26
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0023821578
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Introduction of soluble protein into the class I pathway of antigen processing and presentation
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Moore MW, Carbone FR, Bevan MJ. Introduction of soluble protein into the class I pathway of antigen processing and presentation. Cell. 54:1988;777-785.
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Moore, M.W.1
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27
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0030749118
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MHC class I antigen processing of Listeria monocytogenes proteins: Implications for dominant and subdominant CTL responses
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Pamer EG, Sijts AJAM, Villanueva MS, Busch DH, Vijh S. MHC class I antigen processing of Listeria monocytogenes proteins: Implications for dominant and subdominant CTL responses. Immunol Rev. 158:1997;129-136.
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Busch, D.H.4
Vijh, S.5
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28
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0029550235
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Class I MHC presentation of exogenous soluble antigen via macropinocytosis in bone marrow macrophages
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Norbury CC, Hewlett LJ, Prescott AR, Shastri N, Watts C. Class I MHC presentation of exogenous soluble antigen via macropinocytosis in bone marrow macrophages. Immunity. 3:1995;783-791.
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MHC Class I-restricted CTL responses to exogenous antigens
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Jondal M, Schirmbeck R, Reimann J. MHC Class I-restricted CTL responses to exogenous antigens. Immunity. 5:1996;295-302.
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Jondal, M.1
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30
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0029867486
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Interleukin 3 enhances CTL development and class I re-presentation of exogenous antigen by tumor-infiltrating antigen presenting cells
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Pulaski BA, Yeh K-Y, Shastri N, Maltby KM, Penny DP, Lord EM, Frelinger J. Interleukin 3 enhances CTL development and class I re-presentation of exogenous antigen by tumor-infiltrating antigen presenting cells. Proc Natl Acad Sci USA. 93:1996;3669-3674.
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Pulaski, B.A.1
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Maltby, K.M.4
Penny, D.P.5
Lord, E.M.6
Frelinger, J.7
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31
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0029993103
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Roles of proteasomes, transporter for antigen presentation (TAP), and beta-2-microglobulin in the processing of bacterial or particulate antigens via an alternate class I MHC processing pathway
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Song R, Harding CV. Roles of proteasomes, transporter for antigen presentation (TAP), and beta-2-microglobulin in the processing of bacterial or particulate antigens via an alternate class I MHC processing pathway. J Immunol. 156:1996;4182-4190.
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Song, R.1
Harding, C.V.2
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33
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0029125899
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A mutated intron sequence codes for an antigenic peptide recognized by cytolytic T lymphocytes on a human melanoma
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Coulie PG, Lehmann F, Lethe B, Heman J, Lurquin C, Andrawiss M, Boon T. A mutated intron sequence codes for an antigenic peptide recognized by cytolytic T lymphocytes on a human melanoma. Proc Natl Acad Sci USA. 92:1995;7976-7980.
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Coulie, P.G.1
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Lethe, B.3
Heman, J.4
Lurquin, C.5
Andrawiss, M.6
Boon, T.7
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35
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0029854328
-
Ribosomal scanning past the primary initiation codon as a mechanism for expression of CTL epitopes encoded in alternative reading frames
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of outstanding interest. This report, together with [36-39], shows that cryptic translation products are presented by MHC class I molecules and are capable of eliciting cytotoxic T lymphocyte-mediated immune responses.
-
of outstanding interest Bullock TNJ, Eisenlohr LC. Ribosomal scanning past the primary initiation codon as a mechanism for expression of CTL epitopes encoded in alternative reading frames. J Exp Med. 184:1996;1319-1329 This report, together with [36-39], shows that cryptic translation products are presented by MHC class I molecules and are capable of eliciting cytotoxic T lymphocyte-mediated immune responses.
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(1996)
J Exp Med
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Bullock, T.N.J.1
Eisenlohr, L.C.2
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36
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-
0029924928
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Recognition of out-of-frame major histocompatibility complex class I-restricted epitopes in vivo
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of outstanding interest. This report, together with [35,37 - 39], shows that cryptic translation products are presented by MHC class I molecules and are capable of eliciting cytotoxic T lymphocyte-mediated immune responses.
-
of outstanding interest Elliott T, Bodmer H, Townsend A. Recognition of out-of-frame major histocompatibility complex class I-restricted epitopes in vivo. Eur J Immunol. 26:1996;1175-1179 This report, together with [35,37 - 39], shows that cryptic translation products are presented by MHC class I molecules and are capable of eliciting cytotoxic T lymphocyte-mediated immune responses.
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(1996)
Eur J Immunol
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, pp. 1175-1179
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Elliott, T.1
Bodmer, H.2
Townsend, A.3
-
37
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-
0029862690
-
Utilization of an alternative open reading frame of a normal gene in generating a novel human cancer antigen
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of outstanding interest. This report, together with [35,36,38,39], shows that cryptic translation products are presented by MHC class I molecules and are capable of eliciting cytotoxic T lymphocyte-mediated immune responses.
-
of outstanding interest Wang R-F, Parkhurst MR, Kawakami Y, Robbins PF, Rosenberg SA. Utilization of an alternative open reading frame of a normal gene in generating a novel human cancer antigen. J Exp Med. 183:1996;1131-1140 This report, together with [35,36,38,39], shows that cryptic translation products are presented by MHC class I molecules and are capable of eliciting cytotoxic T lymphocyte-mediated immune responses.
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(1996)
J Exp Med
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Wang R-F1
Parkhurst, M.R.2
Kawakami, Y.3
Robbins, P.F.4
Rosenberg, S.A.5
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38
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-
0030763646
-
Initiation codon scanthrough versus termination codon readthrough demonstrates strong potential for major histocompatibility complex class I-restricted cryptic epitope expression
-
of outstanding interest. This report, together with [35-37,39], shows that cryptic translation products are presented by MHC class I molecules are capable of eliciting cytotoxic T lymphocyte-mediated immune responses.
-
of outstanding interest Bullock TNJ, Patterson AE, Franlin LL, Notidis E, Eisenlohr LC. Initiation codon scanthrough versus termination codon readthrough demonstrates strong potential for major histocompatibility complex class I-restricted cryptic epitope expression. J Exp Med. 186:1997;1051-1058 This report, together with [35-37,39], shows that cryptic translation products are presented by MHC class I molecules are capable of eliciting cytotoxic T lymphocyte-mediated immune responses.
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(1997)
J Exp Med
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Bullock, T.N.J.1
Patterson, A.E.2
Franlin, L.L.3
Notidis, E.4
Eisenlohr, L.C.5
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39
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-
0031882090
-
An alternative translational reading frame encodes an immunodominant retroviral CTL determinant expressed by an immunodeficiency-causing retrovirus
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of outstanding interest. This report, together with [35-38], shows that cryptic translation products are presented by MHC class I molecules and are capable of eliciting cytotoxic T lymphocyte-mediated immune responses.
-
of outstanding interest Mayrand SM, Schwarz DA, Green WR. An alternative translational reading frame encodes an immunodominant retroviral CTL determinant expressed by an immunodeficiency-causing retrovirus. J Immunol. 160:1998;39-50 This report, together with [35-38], shows that cryptic translation products are presented by MHC class I molecules and are capable of eliciting cytotoxic T lymphocyte-mediated immune responses.
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J Immunol
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Mayrand, S.M.1
Schwarz, D.A.2
Green, W.R.3
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40
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0028893927
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Major histocompatibility class I molecules can present cryptic translation products to T-cells
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Shastri N, Nguyen V, Gonzalez F. Major histocompatibility class I molecules can present cryptic translation products to T-cells. J Biol Chem. 270:1995;1088-1091.
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Shastri, N.1
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Gonzalez, F.3
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41
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0030239693
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Defective ribosomal products (DRIPs): A major source of antigenic peptides for MHC class I molecules?
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of outstanding interest. This proposes an interesting hypothesis for explaining the origin of naturally processed peptides from errors in translation.
-
of outstanding interest Yewdell JW, Anton LC, Bennink JR. Defective ribosomal products (DRIPs): a major source of antigenic peptides for MHC class I molecules? J Immunol. 157:1996;1823-1826 This proposes an interesting hypothesis for explaining the origin of naturally processed peptides from errors in translation.
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Yewdell, J.W.1
Anton, L.C.2
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How selective is the transporter associated with antigen processing?
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Androlowicz MJ, Cresswell P. How selective is the transporter associated with antigen processing? Immunity. 5:1996;1-5.
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Androlowicz, M.J.1
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43
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0025879780
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Endogenously synthesized peptide with an endoplasmic reticulum signal sequence sensitizes antigen processing mutant cells to class I-restricted cell-mediated lysis
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Anderson K, Cresswell P, Gammon M, Hermes J, Williamson A, Zweerink H. Endogenously synthesized peptide with an endoplasmic reticulum signal sequence sensitizes antigen processing mutant cells to class I-restricted cell-mediated lysis. J Exp Med. 174:1991;489-492.
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Trimming of antigenic peptides in an early secretory compartment
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Snyder HL, Yewdell JW, Bennink JR. Trimming of antigenic peptides in an early secretory compartment. J Exp Med. 180:1994;2389-2393.
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Elliott T, Willis A, Cerundolo V, Townsend A. Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum. J Exp Med. 181:1995;1481-1491.
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46
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0027237066
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Transporter-Independent Processing of HIV-1 Envelope Protein for Recognition by CD8-Positive T Cells
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Hammond SA, Bollinger RC, Tobery TW, Siliciano RF. Transporter-Independent Processing of HIV-1 Envelope Protein for Recognition by CD8-Positive T Cells. Nature. 364:1993;158-161.
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Nature
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Hammond, S.A.1
Bollinger, R.C.2
Tobery, T.W.3
Siliciano, R.F.4
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47
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0029811941
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Transporter (TAP)-independent processing of a multiple membrane-spanning protein, the Epstein-Barr virus latent membrane protein 2
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Lee SP, Thomas WA, Blake NW, Rickinson AB. Transporter (TAP)-independent processing of a multiple membrane-spanning protein, the Epstein-Barr virus latent membrane protein 2. Eur J Immunol. 26:1996;1875-1883.
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Lee, S.P.1
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Rickinson, A.B.4
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48
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1842290406
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Introduction of a glycosylation site into a secreted protein provides evidence for an alternative antigen processing pathway: Transport of precursors of major histocompatibility complex class I-restricted peptides from the endoplasmic reticulum to the cytosol
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of outstanding interest. This, together with [49], demonstrates a novel mechanism for retrieval and degradation of endoplasmic reticulum proteins in the cytosol. These may serve as possible source of antigenic peptides derived from precursors normally present in membrane-bound subcellular compartments.
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of outstanding interest Bacik I, Snyder HL, Anton LC, Russ G, Chen W, Bennink JR, Urge L, Otvos L, Dudkowska B, Eisenlohr L, Yewdell JW. Introduction of a glycosylation site into a secreted protein provides evidence for an alternative antigen processing pathway: Transport of precursors of major histocompatibility complex class I-restricted peptides from the endoplasmic reticulum to the cytosol. J Exp Med. 186:1997;479-487 This, together with [49], demonstrates a novel mechanism for retrieval and degradation of endoplasmic reticulum proteins in the cytosol. These may serve as possible source of antigenic peptides derived from precursors normally present in membrane-bound subcellular compartments.
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J Exp Med
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Bacik, I.1
Snyder, H.L.2
Anton, L.C.3
Russ, G.4
Chen, W.5
Bennink, J.R.6
Urge, L.7
Otvos, L.8
Dudkowska, B.9
Eisenlohr, L.10
Yewdell, J.W.11
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49
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0029915568
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The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
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of special interest. This, together with [48], demonstrates a novel mechanism for retrieval and degradation of endoplasmic reticulum proteins in the cytosol. These may serve as possible source of antigenic peptides derived from precursors normally present in membrane-bound subcellular compartments.
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of special interest Wiertz EJHJ, Jones TR, Sun L, Bogyo M, Gueze HJ, Ploegh HL. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell. 84:1996;769-779 This, together with [48], demonstrates a novel mechanism for retrieval and degradation of endoplasmic reticulum proteins in the cytosol. These may serve as possible source of antigenic peptides derived from precursors normally present in membrane-bound subcellular compartments.
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Cell
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Wiertz, E.J.H.J.1
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Ploegh, H.L.6
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50
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MHC class I-restricted processing of transmembrane proteins. Mechanism and biological significance
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Siliciano RF, Soloski MJ. MHC class I-restricted processing of transmembrane proteins. Mechanism and biological significance. J Immunol. 155:1995;1-5.
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Siliciano, R.F.1
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51
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0030068265
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Class I-restricted presentation of an HIV-1 gp41 epitope containing an N-linked glycosylation site: Implications for the mechanism of processing of viral envelope proteins
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Ferris RL, Buck C, Hammond SA, Woods AS, Cotter RJ, Takiguchi M, Igarashi Y, Ichikawa Y, Siliciano RF. Class I-restricted presentation of an HIV-1 gp41 epitope containing an N-linked glycosylation site: Implications for the mechanism of processing of viral envelope proteins. J Immunol. 156:1996;834-840.
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J Immunol
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Ferris, R.L.1
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Hammond, S.A.3
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Cotter, R.J.5
Takiguchi, M.6
Igarashi, Y.7
Ichikawa, Y.8
Siliciano, R.F.9
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52
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0027263157
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A role for the ubiquitin-dependent proteolytic pathway in MHC class I restricted antigen presentation
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Michalek MT, Grant EP, Gramm C, Goldberg AL, Rock KL. A role for the ubiquitin-dependent proteolytic pathway in MHC class I restricted antigen presentation. Nature. 363:1993;552-554.
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Nature
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Michalek, M.T.1
Grant, E.P.2
Gramm, C.3
Goldberg, A.L.4
Rock, K.L.5
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53
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0028872334
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Presentation of endogenous and exogenous antigens is not affected by inactivation of E1 ubiquitin-activating enzyme in temperature-sensitive cell lines
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Cox JH, Galardy P, Bennink JR, Yewdell JW. Presentation of endogenous and exogenous antigens is not affected by inactivation of E1 ubiquitin-activating enzyme in temperature-sensitive cell lines. J Immunol. 154:1995;511-519.
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J Immunol
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Cox, J.H.1
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Bennink, J.R.3
Yewdell, J.W.4
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54
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0030240571
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Generation of naturally processed peptide/MHC class I complexes is independent of the stability of endogenously synthesized precursors
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of outstanding interest. This describes the unexpected finding that presentation of endogenously synthesized proteins does not correlate with protein stability.
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of outstanding interest Goth S, Nguyen V, Shastri N. Generation of naturally processed peptide/MHC class I complexes is independent of the stability of endogenously synthesized precursors. J Immunol. 157:1996;1894-1904 This describes the unexpected finding that presentation of endogenously synthesized proteins does not correlate with protein stability.
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J Immunol
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Goth, S.1
Nguyen, V.2
Shastri, N.3
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55
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0029120173
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Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation
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Grant EP, Michalek MT, Goldberg AL, Rock KL. Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation. J Immunol. 155:1995;3750-3758.
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J Immunol
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Grant, E.P.1
Michalek, M.T.2
Goldberg, A.L.3
Rock, K.L.4
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56
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0030040594
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CTL epitope generation is tightly linked to cellular proteolysis of a Listeria monocytogenes antigen
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Sijts AJ, Villanueva MS, Pamer EG. CTL epitope generation is tightly linked to cellular proteolysis of a Listeria monocytogenes antigen. J Immunol. 156:1996;1497-1503.
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Sijts, A.J.1
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Pamer, E.G.3
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57
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0028941532
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Presentation without processing of endogenous precursors in the MHC class I presentation pathway
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Buchholz D, Scott P, Shastri N. Presentation without processing of endogenous precursors in the MHC class I presentation pathway. J Biol Chem. 270:1995;6515-6522.
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Buchholz, D.1
Scott, P.2
Shastri, N.3
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58
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0027980319
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Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
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Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 78:1994;761-771.
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Rock, K.L.1
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Clark, K.4
Stein, R.5
Dick, L.6
Hwang, D.7
Goldberg, A.L.8
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59
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0027489488
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Identification of T-cell epitopes: Rapid isolation of class I-presented peptides from viable cells by mild acid elution
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Storkus WJ, Zeh HJ III, Salter RD, Lotze MT. Identification of T-cell epitopes: rapid isolation of class I-presented peptides from viable cells by mild acid elution. J Immunother. 14:1993;94-103.
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Storkus, W.J.1
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Salter, R.D.3
Lotze, M.T.4
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60
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0031570893
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The generation of MHC Class I-associated peptides is only partially inhibited by proteasome inhibitors: Involvement of nonproteasomal cytosolic proteases in antigen processing?
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Vinitsky A, Anton LC, Snyder HL, Orlowski M, Bennink JR, Yewdell JW. The generation of MHC Class I-associated peptides is only partially inhibited by proteasome inhibitors: involvement of nonproteasomal cytosolic proteases in antigen processing? J Immunol. 159:1997;554-564.
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J Immunol
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Vinitsky, A.1
Anton, L.C.2
Snyder, H.L.3
Orlowski, M.4
Bennink, J.R.5
Yewdell, J.W.6
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61
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0025900181
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Efficient processing of an antigenic sequence for presentation by MHC class I molecules depends upon its neighboring residues in the protein
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Del Val M, Schlicht H-J, Ruppert T, Reddehase MJ, Koszinowski UH. Efficient processing of an antigenic sequence for presentation by MHC class I molecules depends upon its neighboring residues in the protein. Cell. 66:1991;1145-1153.
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Del Val, M.1
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62
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0026599764
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Flanking sequences influence the presentation of an endogenously synthesized peptide to cytotoxic T lymphocytes
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Eisenlohr LC, Yewdell JW, Bennink JR. Flanking sequences influence the presentation of an endogenously synthesized peptide to cytotoxic T lymphocytes. J Exp Med. 175:1992;481-487.
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Eisenlohr, L.C.1
Yewdell, J.W.2
Bennink, J.R.3
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63
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0028793597
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Presentation of endogenous peptide-MHC class I complexes is profoundly influenced by specific C-terminal flanking residues
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Shastri N, Serwold T, Gonzalez F. Presentation of endogenous peptide-MHC class I complexes is profoundly influenced by specific C-terminal flanking residues. J Immunol. 155:1995;4339-4346.
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Shastri, N.1
Serwold, T.2
Gonzalez, F.3
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64
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0031114456
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Point mutation flanking a CTL epitope ablates in vitro and in vivo recognition of a full-length viral protein
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Yellen-Shaw AJ, Wherry EJ, Dubois GC, Eisenlohr LC. Point mutation flanking a CTL epitope ablates in vitro and in vivo recognition of a full-length viral protein. J Immunol. 158:1997;3227-3234.
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Yellen-Shaw, A.J.1
Wherry, E.J.2
Dubois, G.C.3
Eisenlohr, L.C.4
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65
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0028968217
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Contribution of proteasome-mediated proteolysis to the hierarchy of epitopes presented by major histocompatibility complex class I molecules
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Niedermann G, Butz S, Ihlenfeldt HG, Grimm R, Lucchiari M, Hoschutzky H, Jung G, Maier B, Eichmann K. Contribution of proteasome-mediated proteolysis to the hierarchy of epitopes presented by major histocompatibility complex class I molecules. Immunity. 2:1995;289-299.
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Niedermann, G.1
Butz, S.2
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Grimm, R.4
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Hoschutzky, H.6
Jung, G.7
Maier, B.8
Eichmann, K.9
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66
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0030602834
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Coordinated dual cleavages induced by the proteasome regulator PA28 lead to dominant MHC ligands
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Dick TP, Ruppert T, Groettrup M, Kloetzel PM, Kuehn L, Koszinowski UH, Stevanovic S, Schild H, Rammensee HG. Coordinated dual cleavages induced by the proteasome regulator PA28 lead to dominant MHC ligands. Cell. 86:1996;253-262.
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Cell
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Dick, T.P.1
Ruppert, T.2
Groettrup, M.3
Kloetzel, P.M.4
Kuehn, L.5
Koszinowski, U.H.6
Stevanovic, S.7
Schild, H.8
Rammensee, H.G.9
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67
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16044372545
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A single residue exchange within a viral CTL epitope alters proteasome-mediated degradation resulting in lack of antigen presentation
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Ossendorp F, Eggers M, Neisig A, Ruppert T, Groettrup M, Sijts A, Mengede E, Kloetzel PM, Neefjes J, Koszinowski U, Melief C. A single residue exchange within a viral CTL epitope alters proteasome-mediated degradation resulting in lack of antigen presentation. Immunity. 5:1996;115-124.
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Immunity
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Ossendorp, F.1
Eggers, M.2
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Ruppert, T.4
Groettrup, M.5
Sijts, A.6
Mengede, E.7
Kloetzel, P.M.8
Neefjes, J.9
Koszinowski, U.10
Melief, C.11
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68
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0028829908
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Major differences in transporter associated with antigen presentation (TAP)-dependent translocation of MHC class I-presentable peptides and the effect of flanking sequences
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Neisig A, Roelse J, Sijts AJAM, Ossendorp F, Feltkamp MCW, Kast WM, Melief CJM, Neefjes JJ. Major differences in transporter associated with antigen presentation (TAP)-dependent translocation of MHC class I-presentable peptides and the effect of flanking sequences. J Immunol. 154:1995;1273-1279.
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J Immunol
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Neisig, A.1
Roelse, J.2
Sijts, A.J.A.M.3
Ossendorp, F.4
Feltkamp, M.C.W.5
Kast, W.M.6
Melief, C.J.M.7
Neefjes, J.J.8
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69
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0030886208
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Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide
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of special interest. This work leads to the suggestion that mechanism for proteolytic cleavage of the amino- or the carboxy-terminal flanking residues may differ with regard to the requirement for the proteosome.
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of special interest Craiu A, Akopian T, Goldberg A, Rock KL. Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide. Proc Natl Acad Sci USA. 94:1997;10850-10855 This work leads to the suggestion that mechanism for proteolytic cleavage of the amino- or the carboxy-terminal flanking residues may differ with regard to the requirement for the proteosome.
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(1997)
Proc Natl Acad Sci USA
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Craiu, A.1
Akopian, T.2
Goldberg, A.3
Rock, K.L.4
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70
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0025155682
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Cellular peptide composition governed by major histocompatibility complex class I molecules
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Falk K, Rstzschke O, Rammensee H-G. Cellular peptide composition governed by major histocompatibility complex class I molecules. Nature. 348:1990;248-251.
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Nature
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Falk, K.1
Rstzschke, O.2
Rammensee H-G3
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71
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0028889987
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The role of MHC class I molecules in the generation of endogenous peptide/MHC complexes
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Malarkannan S, Goth S, Buchholz DR, Shastri N. The role of MHC class I molecules in the generation of endogenous peptide/MHC complexes. J Immunol. 154:1995;585-598.
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(1995)
J Immunol
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Malarkannan, S.1
Goth, S.2
Buchholz, D.R.3
Shastri, N.4
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72
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0028793597
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Presentation of endogenous peptide/MHC class I complexes is profoundly influenced by specific C-terminal flanking residues
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Shastri N, Serwold T, Gonzalez F. Presentation of endogenous peptide/MHC class I complexes is profoundly influenced by specific C-terminal flanking residues. J Immunol. 155:1995;4339-4346.
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(1995)
J Immunol
, vol.155
, pp. 4339-4346
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Shastri, N.1
Serwold, T.2
Gonzalez, F.3
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73
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0345416155
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Do MHCI molecules select peptides from a random or a nonrandom pool?
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Serwold T, Gonzalez F, Shastri N. Do MHCI molecules select peptides from a random or a nonrandom pool? J Allerg Clin Immunol. 99:1997;S253.
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(1997)
J Allerg Clin Immunol
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Serwold, T.1
Gonzalez, F.2
Shastri, N.3
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74
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0029127770
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Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96
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Arnold D, Faath S, Rammensee HG, Schild H. Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96. J Exp Med. 182:1995;885-889.
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(1995)
J Exp Med
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Arnold, D.1
Faath, S.2
Rammensee, H.G.3
Schild, H.4
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75
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0028979675
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A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
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Suto R, Srivastava PK. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science. 269:1995;1585-1588.
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(1995)
Science
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Suto, R.1
Srivastava, P.K.2
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76
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0030820099
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Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations
-
of outstanding interest. This report, together with [77], demonstrates that gp96-associated peptides can elicit protective anti-tumor responses and that the presence of some of these peptides is transporter associated with antigen processing (TAP) dependent.
-
of outstanding interest Tamura Y, Peng P, Liu K, Daou M, Srivastava PK. Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations. Science. 278:1997;117-120 This report, together with [77], demonstrates that gp96-associated peptides can elicit protective anti-tumor responses and that the presence of some of these peptides is transporter associated with antigen processing (TAP) dependent.
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(1997)
Science
, vol.278
, pp. 117-120
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-
Tamura, Y.1
Peng, P.2
Liu, K.3
Daou, M.4
Srivastava, P.K.5
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77
-
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0030800342
-
Influences of transporter associated with antigen processing (TAP) on the repertoire of peptides associated with the endoplasmic reticulum-resident stress protein gp96
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of outstanding interest. This report, together with [76], demonstrates that gp96-associated peptides can elicit protective anti-tumor responses and that the presence of some of these peptides is transporter associated with antigen processing (TAP) dependent.
-
of outstanding interest Arnold D, Wahl C, Faath S, Rammensee HG, Schild H. Influences of transporter associated with antigen processing (TAP) on the repertoire of peptides associated with the endoplasmic reticulum-resident stress protein gp96. J Exp Med. 186:1997;461-466 This report, together with [76], demonstrates that gp96-associated peptides can elicit protective anti-tumor responses and that the presence of some of these peptides is transporter associated with antigen processing (TAP) dependent.
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(1997)
J Exp Med
, vol.186
, pp. 461-466
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-
Arnold, D.1
Wahl, C.2
Faath, S.3
Rammensee, H.G.4
Schild, H.5
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78
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0029892849
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Isolation of an immunodominant viral peptide that is endogenously bound to the stress protein GP96-GRP94
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of special interest. This first report containing biochemical evidence that gp96 is bound to a known naturally processed antigenic peptide.
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of special interest Nieland TJF, Agnes MC, Tan A, Monnee-Van Muijen M, Koning F, Kruisbeek AM, Van Bleek GM. Isolation of an immunodominant viral peptide that is endogenously bound to the stress protein GP96-GRP94. Proc Natl Acad Sci USA. 93:1996;6135-6139 This first report containing biochemical evidence that gp96 is bound to a known naturally processed antigenic peptide.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 6135-6139
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-
Nieland, T.J.F.1
Agnes, M.C.2
Tan, A.3
Monnee-Van Muijen, M.4
Koning, F.5
Kruisbeek, A.M.6
Van Bleek, G.M.7
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