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Genomes and Genes | Ian A YorkSummaryAffiliation: University of Massachusetts Medical School Country: USA Publications
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Endoplasmic reticulum aminopeptidase 1 (ERAP1) trims MHC class I-presented peptides in vivo and plays an important role in immunodominanceIan A York
Department of Pathology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA
Proc Natl Acad Sci U S A 103:9202-7. 2006..Moreover, peptide trimming and the resulting abundance of peptide-MHC complexes are dominant factors in establishing immunodominance...
The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residuesIan A York
Department of Pathology, University of Massachusetts Medical Center, Worcester, MA 01655, USA
Nat Immunol 3:1177-84. 2002..However, after interferon-gamma treatment, which causes proteasomes to produce more NH2-extended antigenic precursors, ERAP1 increased the supply of peptides for MHC class I antigen presentation...- A mutant cell with a novel defect in MHC class I quality controlIan A York
Department of Pathology, University of Massachusetts Medical Center, Worcester, 01655, USA
J Immunol 174:6839-46. 2005..The 4S8.12 cells provide strong genetic evidence for a novel component in the MHC class I pathway. This as-yet unidentified gene is important in early assembly of primate, but not mouse, MHC class I complexes... - Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentationIan A York
Department of Pathology, University of Massachusetts Medical School, Worcester, MA 01655, USA
J Immunol 177:1434-43. 2006..Moreover, these findings reveal that three sequential proteolytic steps (by proteasomes, TPPII, and then ER aminopepsidase 1) are required for the generation of a subset of epitopes... - Puromycin-sensitive aminopeptidase limits MHC class I presentation in dendritic cells but does not affect CD8 T cell responses during viral infectionsCharles F Towne
Department of Pathology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA
J Immunol 180:1704-12. 2008.... - Characterizing the specificity and cooperation of aminopeptidases in the cytosol and endoplasmic reticulum during MHC class I antigen presentationArron Hearn
Department of Pathology, University of Massachusetts Medical School, Worcester, MA 01655, USA
J Immunol 184:4725-32. 2010..Because N-terminal trimming has different specificity in the cytosol and ER, the cleavage of peptides in both of these compartments serves to broaden the repertoire of sequences that are presented... - Analysis of the role of bleomycin hydrolase in antigen presentation and the generation of CD8 T cell responsesCharles F Towne
Department of Pathology, University of Massachusetts Medical School, Worcester, MA 01655, USA
J Immunol 178:6923-30. 2007..Therefore, BH does influence presentation of some Ags, although its role is largely redundant with other aminopeptidases... 
Analysis of the role of tripeptidyl peptidase II in MHC class I antigen presentation in vivoMasahiro Kawahara
Department of Pathology, University of Massachusetts Medical School, Worcester, MA 01655, USA
J Immunol 183:6069-77. 2009....- The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentationIan A York
Department of Pathology, University of Massachusetts Medical School, Worcester, MA 01655, USA
Immunity 18:429-40. 2003..TOP therefore plays an important role in vivo in degrading peptides released by proteasomes and is a significant factor limiting the extent of antigen presentation... - Leucine aminopeptidase is not essential for trimming peptides in the cytosol or generating epitopes for MHC class I antigen presentationCharles F Towne
Department of Pathology, University of Massachusetts Medical School, Worcester, MA 01655, USA
J Immunol 175:6605-14. 2005..These data demonstrate that LAP is not an essential enzyme for generating most MHC class I-presented peptides and reveal redundancy in the function of cellular aminopeptidases... - The specificity of trimming of MHC class I-presented peptides in the endoplasmic reticulumArron Hearn
Department of Pathology, University of Massachusetts Medical School, Worcester, MA 01655, USA
J Immunol 183:5526-36. 2009..These data define key determinants in the specificity of Ag processing... - Post-proteasomal antigen processing for major histocompatibility complex class I presentationKenneth L Rock
Department of Pathology, University of Massachusetts Medical Center, Worcester, MA 01655, USA
Nat Immunol 5:670-7. 2004..Thus, the extent of antigen presentation depends on the balance between several proteolytic processes that may generate or destroy epitopes... - Structural basis for antigenic peptide precursor processing by the endoplasmic reticulum aminopeptidase ERAP1Tina T Nguyen
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA
Nat Struct Mol Biol 18:604-13. 2011..ERAP1's unique structural elements suggest how a generic aminopeptidase structure has been adapted for the specialized function of trimming antigenic precursors... - Protein degradation and the generation of MHC class I-presented peptidesKenneth L Rock
Department of Pathology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA
Adv Immunol 80:1-70. 2002.... - An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptidesTomo Saric
Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA
Nat Immunol 3:1169-76. 2002..Like other proteins involved in antigen presentation, ERAP1 is induced by interferon-gamma. When overexpressed in vivo, we found that ERAP1 stimulates the processing and presentation of an antigenic precursor in the ER...