{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,11]],"date-time":"2026-10-11T11:32:01Z","timestamp":1791718321346,"version":"4.3.4"},"reference-count":74,"publisher":"Oxford University Press (OUP)","issue":"10","license":[{"start":{"date-parts":[[2017,5,1]],"date-time":"2017-05-01T00:00:00Z","timestamp":1493596800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2017,5,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>CD8+ T cell immunosurveillance is based on recognizing oligopeptides presented by MHC class I molecules. Despite decades of study, the importance of protein ubiquitylation to peptide generation remains uncertain. In this study, we examined the ability of MLN7243, a recently described ubiquitin-activating enzyme E1 inhibitor, to block overall cytosolic peptide generation and generation of specific peptides from vaccinia- and influenza A virus\u2013encoded proteins. We show that MLN7243 rapidly inhibits ubiquitylation in a variety of cell lines and can profoundly reduce the generation of cytosolic peptides. Kinetic analysis of specific peptide generation reveals that ubiquitylation of defective ribosomal products is rate limiting in generating class I peptide complexes. More generally, our findings demonstrate that the requirement for ubiquitylation in MHC class I\u2013restricted Ag processing varies with class I allomorph, cell type, source protein, and peptide context. Thus, ubiquitin-dependent and -independent pathways robustly contribute to MHC class I\u2013based immunosurveillance.<\/jats:p>","DOI":"10.4049\/jimmunol.1602122","type":"journal-article","created":{"date-parts":[[2017,4,1]],"date-time":"2017-04-01T00:40:32Z","timestamp":1491007232000},"page":"3835-3845","source":"Crossref","is-referenced-by-count":46,"title":["Varied Role of Ubiquitylation in Generating MHC Class I Peptide Ligands"],"prefix":"10.1093","volume":"198","author":[{"given":"Jiajie","family":"Wei","sequence":"first","affiliation":[{"name":"Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health , Bethesda, MD 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1163-9902","authenticated-orcid":false,"given":"Damien","family":"Zanker","sequence":"additional","affiliation":[{"name":"T Cell Laboratory, School of Molecular Science, La Trobe University , Bundoora, Victoria 3086,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6925-3829","authenticated-orcid":false,"given":"Anthony R","family":"Di Carluccio","sequence":"additional","affiliation":[{"name":"T Cell Laboratory, School of Molecular Science, La Trobe University , Bundoora, Victoria 3086,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7777-5574","authenticated-orcid":false,"given":"Margery G","family":"Smelkinson","sequence":"additional","affiliation":[{"name":"Biological Imaging Section, Research Technologies Branch, National Institute of Allergy and Infectious Diseases, National Institutes of Health , Bethesda, MD 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazuyo","family":"Takeda","sequence":"additional","affiliation":[{"name":"Microscopy and Imaging Core Facility, Center for Biologics Evaluation and Research, Food and Drug Administration , Silver Spring, MD 20993"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mina O","family":"Seedhom","sequence":"additional","affiliation":[{"name":"Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health , Bethesda, MD 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Devin","family":"Dersh","sequence":"additional","affiliation":[{"name":"Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health , Bethesda, MD 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James S","family":"Gibbs","sequence":"additional","affiliation":[{"name":"Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health , Bethesda, MD 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5121-7208","authenticated-orcid":false,"given":"Ning","family":"Yang","sequence":"additional","affiliation":[{"name":"Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health , Bethesda, MD 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ajit","family":"Jadhav","sequence":"additional","affiliation":[{"name":"Chemical Genomics Center, National Center for Advancing Translational Sciences, National Institutes of Health , Rockville, MD 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5221-9771","authenticated-orcid":false,"given":"Weisan","family":"Chen","sequence":"additional","affiliation":[{"name":"T Cell Laboratory, School of Molecular Science, La Trobe University , Bundoora, Victoria 3086,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2123-6189","authenticated-orcid":false,"given":"Jonathan W","family":"Yewdell","sequence":"additional","affiliation":[{"name":"Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health , Bethesda, MD 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2017,5,15]]},"reference":[{"key":"2025030615143834900_r1","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1189\/jlb.1113599","article-title":"Translating DRiPs: MHC class I immunosurveillance of pathogens and tumors","volume":"95","author":"Ant\u00f3n","year":"2014","journal-title":"J. Leukoc. Biol."},{"key":"2025030615143834900_r2","doi-asserted-by":"crossref","first-page":"E1591","DOI":"10.1073\/pnas.1321902111","article-title":"The nature and extent of contributions by defective ribosome products to the HLA peptidome","volume":"111","author":"Bourdetsky","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2025030615143834900_r3","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.coi.2016.03.007","article-title":"Immunology by numbers: quantitation of antigen presentation completes the quantitative milieu of systems immunology!","volume":"40","author":"Purcell","year":"2016","journal-title":"Curr. Opin. Immunol."},{"key":"2025030615143834900_r4","doi-asserted-by":"crossref","first-page":"52","DOI":"10.4049\/jimmunol.1300802","article-title":"Mixed proteasomes function to increase viral peptide diversity and broaden antiviral CD8+ T cell responses","volume":"191","author":"Zanker","year":"2013","journal-title":"J. Immunol."},{"key":"2025030615143834900_r5","doi-asserted-by":"crossref","first-page":"e1003129","DOI":"10.1371\/journal.ppat.1003129","article-title":"Kinetics of antigen expression and epitope presentation during virus infection","volume":"9","author":"Croft","year":"2013","journal-title":"PLoS Pathog."},{"key":"2025030615143834900_r6","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1515\/hsz-2014-0320","article-title":"The transporter associated with antigen processing: a key player in adaptive immunity","volume":"396","author":"Eggensperger","year":"2015","journal-title":"Biol. Chem."},{"key":"2025030615143834900_r7","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1152\/physrev.00027.2001","article-title":"The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction","volume":"82","author":"Glickman","year":"2002","journal-title":"Physiol. Rev."},{"key":"2025030615143834900_r8","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/j.tcb.2015.03.002","article-title":"The demographics of the ubiquitin system","volume":"25","author":"Clague","year":"2015","journal-title":"Trends Cell Biol."},{"key":"2025030615143834900_r9","first-page":"153","article-title":"Ubiquitin-independent degradation of proteins by the proteasome","volume":"1786","author":"Jariel-Encontre","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"2025030615143834900_r10","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.mam.2016.05.001","article-title":"Degradation of oxidized proteins by the proteasome: distinguishing between the 20S, 26S, and immunoproteasome proteolytic pathways","volume":"50","author":"Raynes","year":"2016","journal-title":"Mol. Aspects Med."},{"key":"2025030615143834900_r11","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/S0161-5890(02)00096-2","article-title":"Insights into antigen processing gained by direct analysis of the naturally processed class I MHC associated peptide repertoire","volume":"39","author":"Engelhard","year":"2002","journal-title":"Mol. Immunol."},{"key":"2025030615143834900_r12","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/S0161-5890(02)00101-3","article-title":"Antigen degradation or presentation by MHC class I molecules via classical and non-classical pathways","volume":"39","author":"Gromm\u00e9","year":"2002","journal-title":"Mol. Immunol."},{"key":"2025030615143834900_r13","doi-asserted-by":"crossref","first-page":"554","DOI":"10.4049\/jimmunol.159.2.554","article-title":"The generation of MHC class I-associated peptides is only partially inhibited by proteasome inhibitors: involvement of nonproteasomal cytosolic proteases in antigen processing?","volume":"159","author":"Vinitsky","year":"1997","journal-title":"J. Immunol."},{"key":"2025030615143834900_r14","doi-asserted-by":"crossref","first-page":"1904","DOI":"10.4049\/jimmunol.1003411","article-title":"Cutting edge: selective role of ubiquitin in MHC class I antigen presentation","volume":"186","author":"Huang","year":"2011","journal-title":"J. Immunol."},{"key":"2025030615143834900_r15","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1074\/jbc.M509126200","article-title":"Characterization of rapidly degraded polypeptides in mammalian cells reveals a novel layer of nascent protein quality control","volume":"281","author":"Qian","year":"2006","journal-title":"J. Biol. Chem."},{"key":"2025030615143834900_r16","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/S0959-8049(14)70703-8","article-title":"577 Characterization of the cellular mechanism of action of the first in class investigational inhibitor of the ubiquitin activating enzyme, MLN7243","volume":"50","author":"Milhollen","year":"2014","journal-title":"Eur. J. Cancer"},{"key":"2025030615143834900_r17","doi-asserted-by":"crossref","first-page":"2065","DOI":"10.4049\/jimmunol.1003096","article-title":"Distinct pathways generate peptides from defective ribosomal products for CD8+ T cell immunosurveillance","volume":"186","author":"Dolan","year":"2011","journal-title":"J. Immunol."},{"key":"2025030615143834900_r18","doi-asserted-by":"crossref","first-page":"9178","DOI":"10.1073\/pnas.1105624108","article-title":"Systematic identification of immunodominant CD8+ T-cell responses to influenza A virus in HLA-A2 individuals","volume":"108","author":"Wu","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2025030615143834900_r19","doi-asserted-by":"crossref","first-page":"16431","DOI":"10.1074\/jbc.M115.658062","article-title":"Ubiquitous autofragmentation of fluorescent proteins creates abundant defective ribosomal products (DRiPs) for immunosurveillance","volume":"290","author":"Wei","year":"2015","journal-title":"J. Biol. Chem."},{"key":"2025030615143834900_r20","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.jim.2012.10.012","article-title":"An optimized method for establishing high purity murine CD8+ T cell cultures","volume":"387","author":"Zanker","year":"2013","journal-title":"J. Immunol. Methods"},{"key":"2025030615143834900_r21","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1038\/icb.2012.78","article-title":"Nucleoprotein of influenza A virus is a major target of immunodominant CD8+ T-cell responses","volume":"91","author":"Grant","year":"2013","journal-title":"Immunol. Cell Biol."},{"key":"2025030615143834900_r22","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/0014-5793(94)00647-4","article-title":"Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins","volume":"349","author":"Fujimuro","year":"1994","journal-title":"FEBS Lett."},{"key":"2025030615143834900_r23","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/0022-1759(87)90175-X","article-title":"A simple method to eliminate the antigenicity of surface class I MHC molecules from the membrane of viable cells by acid treatment at pH 3","volume":"100","author":"Sugawara","year":"1987","journal-title":"J. Immunol. Methods"},{"key":"2025030615143834900_r24","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1016\/0161-5890(93)90037-C","article-title":"Dissociation of \u03b22-microglobulin is responsible for selective reduction of HLA class I antigenicity following acid treatment of cells","volume":"30","author":"Polakova","year":"1993","journal-title":"Mol. Immunol."},{"key":"2025030615143834900_r25","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1038\/346476a0","article-title":"Empty MHC class I molecules come out in the cold","volume":"346","author":"Ljunggren","year":"1990","journal-title":"Nature"},{"key":"2025030615143834900_r26","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S1074-7613(95)80014-X","article-title":"Effect of TAP on the generation and intracellular trafficking of peptide-receptive major histocompatibility complex class I molecules","volume":"2","author":"Day","year":"1995","journal-title":"Immunity"},{"key":"2025030615143834900_r27","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1038\/35008103","article-title":"The major substrates for TAP in vivo are derived from newly synthesized proteins","volume":"404","author":"Reits","year":"2000","journal-title":"Nature"},{"key":"2025030615143834900_r28","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/S0198-8859(97)00082-7","article-title":"The diversity of antigen-specific TCR repertoires reflects the relative complexity of epitopes recognized","volume":"54","author":"Maryanski","year":"1997","journal-title":"Hum. Immunol."},{"key":"2025030615143834900_r29","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/0092-8674(78)90296-9","article-title":"Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens-new tools for genetic analysis","volume":"14","author":"Barnstable","year":"1978","journal-title":"Cell"},{"key":"2025030615143834900_r30","doi-asserted-by":"crossref","first-page":"2891","DOI":"10.1002\/eji.1830211136","article-title":"Exact prediction of a natural T cell epitope","volume":"21","author":"R\u00f6tzschke","year":"1991","journal-title":"Eur. J. Immunol."},{"key":"2025030615143834900_r31","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1016\/S1074-7613(00)80447-1","article-title":"Localization, quantitation, and in situ detection of specific peptide-MHC class I complexes using a monoclonal antibody","volume":"6","author":"Porgador","year":"1997","journal-title":"Immunity"},{"key":"2025030615143834900_r32","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1126\/science.3018930","article-title":"In vivo half-life of a protein is a function of its amino-terminal residue","volume":"234","author":"Bachmair","year":"1986","journal-title":"Science"},{"key":"2025030615143834900_r33","doi-asserted-by":"crossref","first-page":"7120","DOI":"10.1128\/MCB.25.16.7120-7136.2005","article-title":"A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons","volume":"25","author":"Tasaki","year":"2005","journal-title":"Mol. Cell. Biol."},{"key":"2025030615143834900_r34","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.1084\/jem.168.4.1211","article-title":"Defective presentation to class I-restricted cytotoxic T lymphocytes in vaccinia-infected cells is overcome by enhanced degradation of antigen","volume":"168","author":"Townsend","year":"1988","journal-title":"J. Exp. Med."},{"key":"2025030615143834900_r35","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1016\/S1074-7613(03)00051-7","article-title":"Quantitating protein synthesis, degradation, and endogenous antigen processing","volume":"18","author":"Princiotta","year":"2003","journal-title":"Immunity"},{"key":"2025030615143834900_r36","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1083\/jcb.146.1.113","article-title":"Intracellular localization of proteasomal degradation of a viral antigen","volume":"146","author":"Ant\u00f3n","year":"1999","journal-title":"J. Cell Biol."},{"key":"2025030615143834900_r37","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1084\/jem.186.7.1087","article-title":"Two novel routes of transporter associated with antigen processing (TAP)-independent major histocompatibility complex class I antigen processing","volume":"186","author":"Snyder","year":"1997","journal-title":"J. Exp. Med."},{"issue":"2","key":"2025030615143834900_r38","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.molimm.2015.04.012","article-title":"The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense","volume":"68","author":"Basler","year":"2015","journal-title":"Mol. Immunol."},{"key":"2025030615143834900_r39","doi-asserted-by":"crossref","first-page":"2249","DOI":"10.4049\/jimmunol.176.4.2249","article-title":"Re-evaluating the generation of a \u201cproteasome-independent\u201d MHC class I-restricted CD8 T cell epitope","volume":"176","author":"Wherry","year":"2006","journal-title":"J. Immunol."},{"key":"2025030615143834900_r40","doi-asserted-by":"crossref","first-page":"112","DOI":"10.4049\/jimmunol.161.1.112","article-title":"Proteasomes can either generate or destroy MHC class I epitopes: evidence for nonproteasomal epitope generation in the cytosol","volume":"161","author":"Luckey","year":"1998","journal-title":"J. Immunol."},{"key":"2025030615143834900_r41","doi-asserted-by":"crossref","first-page":"83","DOI":"10.4049\/jimmunol.161.1.83","article-title":"Allelic differences in the relationship between proteasome activity and MHC class I peptide loading","volume":"161","author":"Benham","year":"1998","journal-title":"J. Immunol."},{"key":"2025030615143834900_r42","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1038\/33443","article-title":"A proteolytic system that compensates for loss of proteasome function","volume":"392","author":"Glas","year":"1998","journal-title":"Nature"},{"key":"2025030615143834900_r43","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1073\/pnas.98.2.513","article-title":"Cells adapted to the proteasome inhibitor 4-hydroxy- 5-iodo-3-nitrophenylacetyl-Leu-Leu-leucinal-vinyl sulfone require enzymatically active proteasomes for continued survival","volume":"98","author":"Princiotta","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"2","key":"2025030615143834900_r44","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.molimm.2015.04.014","article-title":"Proteolytic enzymes involved in MHC class I antigen processing: a guerrilla army that partners with the proteasome","volume":"68","author":"L\u00e1zaro","year":"2015","journal-title":"Mol. Immunol."},{"key":"2025030615143834900_r45","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0161-5890(02)00097-4","article-title":"To DRiP or not to DRiP: generating peptide ligands for MHC class I molecules from biosynthesized proteins","volume":"39","author":"Yewdell","year":"2002","journal-title":"Mol. Immunol."},{"key":"2025030615143834900_r46","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1016\/j.it.2006.06.008","article-title":"The DRiP hypothesis decennial: support, controversy, refinement and extension","volume":"27","author":"Yewdell","year":"2006","journal-title":"Trends Immunol."},{"key":"2025030615143834900_r47","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/BF00395854","article-title":"T cell-recognized antigenic peptides derived from the cellular genome are not protein degradation products but can be generated directly by transcription and translation of short subgenic regions. A hypothesis","volume":"29","author":"Boon","year":"1989","journal-title":"Immunogenetics"},{"key":"2025030615143834900_r48","doi-asserted-by":"crossref","first-page":"17951","DOI":"10.1073\/pnas.1309956110","article-title":"Translation of pre-spliced RNAs in the nuclear compartment generates peptides for the MHC class I pathway","volume":"110","author":"Apcher","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2025030615143834900_r49","doi-asserted-by":"crossref","first-page":"303","DOI":"10.4049\/jimmunol.159.1.303","article-title":"The intronic region of an incompletely spliced gp100 gene transcript encodes an epitope recognized by melanoma-reactive tumor-infiltrating lymphocytes","volume":"159","author":"Robbins","year":"1997","journal-title":"J. Immunol."},{"key":"2025030615143834900_r50","doi-asserted-by":"crossref","first-page":"1139","DOI":"10.1126\/science.1061216","article-title":"Coupled transcription and translation within nuclei of mammalian cells","volume":"293","author":"Iborra","year":"2001","journal-title":"Science"},{"key":"2025030615143834900_r51","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1083\/jcb.201112145","article-title":"Nuclear translation visualized by ribosome-bound nascent chain puromycylation","volume":"197","author":"David","year":"2012","journal-title":"J. Cell Biol."},{"key":"2025030615143834900_r52","doi-asserted-by":"crossref","first-page":"6728","DOI":"10.4049\/jimmunol.1002543","article-title":"RNA polymerase II inhibitors dissociate antigenic peptide generation from normal viral protein synthesis: a role for nuclear translation in defective ribosomal product synthesis?","volume":"185","author":"Dolan","year":"2010","journal-title":"J. Immunol."},{"key":"2025030615143834900_r53","doi-asserted-by":"crossref","first-page":"11572","DOI":"10.1073\/pnas.1104104108","article-title":"Major source of antigenic peptides for the MHC class I pathway is produced during the pioneer round of mRNA translation","volume":"108","author":"Apcher","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2025030615143834900_r54","doi-asserted-by":"crossref","first-page":"1719","DOI":"10.1126\/science.1220270","article-title":"Leucine-tRNA initiates at CUG start codons for protein synthesis and presentation by MHC class I","volume":"336","author":"Starck","year":"2012","journal-title":"Science"},{"key":"2025030615143834900_r55","doi-asserted-by":"crossref","first-page":"e366","DOI":"10.1371\/journal.pbio.0020366","article-title":"Unanticipated antigens: translation initiation at CUG with leucine","volume":"2","author":"Schwab","year":"2004","journal-title":"PLoS Biol."},{"key":"2025030615143834900_r56","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1084\/jem.186.7.1051","article-title":"Initiation codon scanthrough versus termination codon readthrough demonstrates strong potential for major histocompatibility complex class I-restricted cryptic epitope expression","volume":"186","author":"Bullock","year":"1997","journal-title":"J. Exp. Med."},{"key":"2025030615143834900_r57","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1084\/jem.184.4.1319","article-title":"Ribosomal scanning past the primary initiation codon as a mechanism for expression of CTL epitopes encoded in alternative reading frames","volume":"184","author":"Bullock","year":"1996","journal-title":"J. Exp. Med."},{"key":"2025030615143834900_r58","doi-asserted-by":"crossref","first-page":"2697","DOI":"10.4049\/jimmunol.147.8.2697","article-title":"A frameshift mutation at the NH2 terminus of the nucleoprotein gene does not affect generation of cytotoxic T lymphocyte epitopes","volume":"147","author":"Fetten","year":"1991","journal-title":"J. Immunol."},{"key":"2025030615143834900_r59","doi-asserted-by":"crossref","first-page":"6928","DOI":"10.4049\/jimmunol.176.11.6928","article-title":"Epitopes derived by incidental translational frameshifting give rise to a protective CTL response","volume":"176","author":"Zook","year":"2006","journal-title":"J. Immunol."},{"key":"2025030615143834900_r60","doi-asserted-by":"crossref","first-page":"5070","DOI":"10.4049\/jimmunol.164.10.5070","article-title":"Sequential cleavage by metallopeptidases and proteasomes is involved in processing HIV-1 ENV epitope for endogenous MHC class I antigen presentation","volume":"164","author":"L\u00f3pez","year":"2000","journal-title":"J. Immunol."},{"key":"2025030615143834900_r61","doi-asserted-by":"crossref","first-page":"36474","DOI":"10.1074\/jbc.M105517200","article-title":"MHC class I-presented peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase","volume":"276","author":"Saric","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2025030615143834900_r62","doi-asserted-by":"crossref","first-page":"18734","DOI":"10.1074\/jbc.273.30.18734","article-title":"Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase","volume":"273","author":"Beninga","year":"1998","journal-title":"J. Biol. Chem."},{"key":"2025030615143834900_r63","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1038\/80852","article-title":"Two new proteases in the MHC class I processing pathway","volume":"1","author":"Stoltze","year":"2000","journal-title":"Nat. Immunol."},{"key":"2025030615143834900_r64","doi-asserted-by":"crossref","first-page":"9002","DOI":"10.1074\/jbc.272.14.9002","article-title":"Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70","volume":"272","author":"Bercovich","year":"1997","journal-title":"J. Biol. Chem."},{"key":"2025030615143834900_r65","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1038\/360597a0","article-title":"Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination","volume":"360","author":"Murakami","year":"1992","journal-title":"Nature"},{"key":"2025030615143834900_r66","doi-asserted-by":"crossref","first-page":"8805","DOI":"10.1074\/jbc.M115.705178","article-title":"Major histocompatibility complex (MHC) class I processing of the NY-ESO-1 antigen is regulated by Rpn10 and Rpn13 proteins and immunoproteasomes following non-lysine ubiquitination","volume":"291","author":"Golnik","year":"2016","journal-title":"J. Biol. Chem."},{"key":"2025030615143834900_r67","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1002\/eji.201444830","article-title":"Polyubiquitination of lysine-48 is an essential but indirect signal for MHC class I antigen processing","volume":"45","author":"Fiebiger","year":"2015","journal-title":"Eur. J. Immunol."},{"key":"2025030615143834900_r68","doi-asserted-by":"crossref","first-page":"e67796","DOI":"10.1371\/journal.pone.0067796","article-title":"MHC class I antigen presentation of DRiP-derived peptides from a model antigen is not dependent on the AAA ATPase p97","volume":"8","author":"Palmer","year":"2013","journal-title":"PLoS One"},{"key":"2025030615143834900_r69","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1083\/jcb.200908092","article-title":"BAG-6 is essential for selective elimination of defective proteasomal substrates","volume":"190","author":"Minami","year":"2010","journal-title":"J. Cell Biol."},{"key":"2025030615143834900_r70","first-page":"271","article-title":"Quantitating defective ribosome products","volume":"301","author":"Qian","year":"2005","journal-title":"Methods Mol. Biol."},{"key":"2025030615143834900_r71","doi-asserted-by":"crossref","first-page":"617","DOI":"10.4049\/jimmunol.157.2.617","article-title":"Chemical denaturation and modification of ovalbumin alters its dependence on ubiquitin conjugation for class I antigen presentation","volume":"157","author":"Michalek","year":"1996","journal-title":"J. Immunol."},{"key":"2025030615143834900_r72","doi-asserted-by":"crossref","first-page":"3750","DOI":"10.4049\/jimmunol.155.8.3750","article-title":"Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation","volume":"155","author":"Grant","year":"1995","journal-title":"J. Immunol."},{"key":"2025030615143834900_r73","doi-asserted-by":"crossref","first-page":"511","DOI":"10.4049\/jimmunol.154.2.511","article-title":"Presentation of endogenous and exogenous antigens is not affected by inactivation of E1 ubiquitin-activating enzyme in temperature-sensitive cell lines","volume":"154","author":"Cox","year":"1995","journal-title":"J. Immunol."},{"key":"2025030615143834900_r74","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1038\/363552a0","article-title":"A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation","volume":"363","author":"Michalek","year":"1993","journal-title":"Nature"}],"container-title":["The Journal of Immunology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/jimmunol\/article-pdf\/198\/10\/3835\/61452464\/1602122.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/jimmunol\/article-pdf\/198\/10\/3835\/61452464\/1602122.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,3,6]],"date-time":"2025-03-06T17:34:08Z","timestamp":1741282448000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/jimmunol\/article\/198\/10\/3835\/7956594"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,5]]},"references-count":74,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2017,5,15]]}},"URL":"https:\/\/doi.org\/10.4049\/jimmunol.1602122","relation":{},"ISSN":["0022-1767","1550-6606"],"issn-type":[{"value":"0022-1767","type":"print"},{"value":"1550-6606","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2017,5]]},"published":{"date-parts":[[2017,5]]}}}