Coping with loss of perfection in the MHC class I peptide repertoire.
暂无分享,去创建一个
[1] Simon C. Potter,et al. Association scan of 14,500 nonsynonymous SNPs in four diseases identifies autoimmunity variants , 2007, Nature Genetics.
[2] K. Rock,et al. Analysis of the Role of Bleomycin Hydrolase in Antigen Presentation and the Generation of CD8 T Cell Responses1 , 2007, The Journal of Immunology.
[3] M. Bevan,et al. Effector and memory CTL differentiation. , 2007, Annual review of immunology.
[4] P. van Endert,et al. The Role of Endoplasmic Reticulum-Associated Aminopeptidase 1 in Immunity to Infection and in Cross-Presentation1 , 2007, The Journal of Immunology.
[5] Nicholas A Williamson,et al. A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule , 2007, Nature Immunology.
[6] N. Shastri,et al. In the absence of aminopeptidase ERAAP, MHC class I molecules present many unstable and highly immunogenic peptides , 2007, Nature Immunology.
[7] L. C. Antón,et al. Need for Tripeptidyl-peptidase II in Major Histocompatibility Complex Class I Viral Antigen Processing when Proteasomes are Detrimental* , 2006, Journal of Biological Chemistry.
[8] N. Shastri,et al. ERAAP synergizes with MHC class I molecules to make the final cut in the antigenic peptide precursors in the endoplasmic reticulum. , 2006, Immunity.
[9] A. Goldberg,et al. Tripeptidyl Peptidase II Is the Major Peptidase Needed to Trim Long Antigenic Precursors, but Is Not Required for Most MHC Class I Antigen Presentation1 , 2006, The Journal of Immunology.
[10] K. Rock,et al. Endoplasmic reticulum aminopeptidase 1 (ERAP1) trims MHC class I-presented peptides in vivo and plays an important role in immunodominance. , 2006, Proceedings of the National Academy of Sciences of the United States of America.
[11] N. Shastri,et al. Hsp90alpha chaperones large C-terminally extended proteolytic intermediates in the MHC class I antigen processing pathway. , 2006, Immunity.
[12] S. Ferracuti,et al. Expression of Endoplasmic Reticulum Aminopeptidases in EBV-B Cell Lines from Healthy Donors and in Leukemia/Lymphoma, Carcinoma, and Melanoma Cell Lines1 , 2006, The Journal of Immunology.
[13] Vrajesh V. Parekh,et al. In vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules , 2006, The Journal of experimental medicine.
[14] P. van Endert,et al. A Long N-terminal-extended Nested Set of Abundant and Antigenic Major Histocompatibility Complex Class I Natural Ligands from HIV Envelope Protein* , 2006, Journal of Biological Chemistry.
[15] James McCluskey,et al. Have we cut ourselves too short in mapping CTL epitopes? , 2006, Trends in immunology.
[16] N. Shastri,et al. The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules , 2006, Nature Immunology.
[17] A. Goldberg,et al. The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[18] K. Rock,et al. Leucine Aminopeptidase Is Not Essential for Trimming Peptides in the Cytosol or Generating Epitopes for MHC Class I Antigen Presentation1 , 2005, The Journal of Immunology.
[19] Natalie A Borg,et al. T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I–bound peptide , 2005, Nature Immunology.
[20] N. Shastri,et al. All the peptides that fit: the beginning, the middle, and the end of the MHC class I antigen‐processing pathway , 2005, Immunological reviews.
[21] L. Schomburg,et al. Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum , 2005, Nature Immunology.
[22] M. Probst-Kepper,et al. Conformational Restraints and Flexibility of 14-Meric Peptides in Complex with HLA-B*35011 , 2004, The Journal of Immunology.
[23] Wendy J M van Zuylen,et al. Potent T cell response to a class I‐binding 13‐mer viral epitope and the influence of HLA micropolymorphism in controlling epitope length , 2004, European journal of immunology.
[24] M. Altfeld,et al. Immune Selection for Altered Antigen Processing Leads to Cytotoxic T Lymphocyte Escape in Chronic HIV-1 Infection , 2004, The Journal of experimental medicine.
[25] Jacques Neefjes,et al. A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation. , 2004, Immunity.
[26] Muthuraman Sathiamurthy,et al. Toward a Definition of Self: Proteomic Evaluation of the Class I Peptide Repertoire1 , 2004, The Journal of Immunology.
[27] O. Lund,et al. The Immune Epitope Database and Analysis Resource: From Vision to Blueprint , 2005, PLoS biology.
[28] Jun Kunisawa,et al. The group II chaperonin TRiC protects proteolytic intermediates from degradation in the MHC class I antigen processing pathway. , 2003, Molecular cell.
[29] S. Mizutani,et al. Human Leukocyte-derived Arginine Aminopeptidase , 2003, Journal of Biological Chemistry.
[30] Concepción Marañón,et al. An essential role for tripeptidyl peptidase in the generation of an MHC class I epitope , 2003, Nature Immunology.
[31] S. Mizutani,et al. Human Leukocyte-derived Arginine Aminopeptidase THE THIRD MEMBER OF THE OXYTOCINASE SUBFAMILY OF AMINOPEPTIDASES* , 2003 .
[32] A. Goldberg,et al. The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8–9 residues , 2002, Nature Immunology.
[33] Akira Hattori,et al. An IFN-γ–induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I–presented peptides , 2002, Nature Immunology.
[34] N. Shastri,et al. ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum , 2002, Nature.
[35] N. Shastri,et al. ER aminopeptidases generate a unique pool of peptides for MHC class I molecules , 2001, Nature Immunology.
[36] A. Goldberg,et al. 26S proteasomes and immunoproteasomes produce mainly N‐extended versions of an antigenic peptide , 2001, The EMBO journal.
[37] Hans-Georg Rammensee,et al. Two new proteases in the MHC class I processing pathway , 2000, Nature Immunology.
[38] H. Rammensee,et al. SYFPEITHI: database for MHC ligands and peptide motifs , 1999, Immunogenetics.
[39] W. Baumeister,et al. A giant protease with potential to substitute for some functions of the proteasome. , 1999, Science.
[40] A. Goldberg,et al. Degradation of cell proteins and the generation of MHC class I-presented peptides. , 1999, Annual review of immunology.
[41] M. Bevan,et al. Selecting and maintaining a diverse T-cell repertoire , 1999, Nature.
[42] A. Goldberg,et al. Interferon-γ Can Stimulate Post-proteasomal Trimming of the N Terminus of an Antigenic Peptide by Inducing Leucine Aminopeptidase* , 1998, The Journal of Biological Chemistry.
[43] A Sette,et al. The peptide-binding motif for the human transporter associated with antigen processing , 1995, The Journal of experimental medicine.
[44] M. Feltkamp,et al. Major differences in transporter associated with antigen presentation (TAP)-dependent translocation of MHC class I-presentable peptides and the effect of flanking sequences. , 1995, Journal of immunology.
[45] D. Madden. The three-dimensional structure of peptide-MHC complexes. , 1995, Annual review of immunology.
[46] Edward J. Collins,et al. Three-dimensional structure of a peptide extending from one end of a class I MHC binding site , 1994, Nature.
[47] H. Rammensee,et al. Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules , 1991, Nature.
[48] Hans-Georg Rammensee,et al. Cellular peptide composition governed by major histocompatibility complex class I molecules , 1990, Nature.