{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T13:23:57Z","timestamp":1789133037603,"version":"build-2803163510"},"reference-count":36,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2018,2,1]],"date-time":"2018-02-01T00:00:00Z","timestamp":1517443200000},"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":[[2018,2,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Infected or transformed cells must present peptides derived from endogenous proteins on MHC class I molecules to be recognized and targeted for elimination by Ag-specific cytotoxic T cells. In the first step of peptide generation, proteins are degraded by the proteasome. In this study, we investigated the role of the ubiquitin-specific protease 14 (Usp14), a proteasome-associated deubiquitinase, in direct Ag presentation using a ligand-stabilized model protein expressed as a self-antigen. Chemical inhibition of Usp14 diminished direct presentation of the model antigenic peptide, and the effect was especially pronounced when presentation was restricted to the defective ribosomal product (DRiP) form of the protein. Additionally, presentation specifically from DRiP Ags was diminished by expression of a catalytically inactive form of Usp14. Usp14 inhibition did not appreciably alter protein synthesis and only partially delayed protein degradation as measured by a slight increase in the half-life of the model protein when its degradation was induced. Taken together, these data indicate that functional Usp14 enhances direct Ag presentation, preferentially of DRiP-derived peptides, suggesting that the processing of DRiPs is in some ways different from other forms of Ag.<\/jats:p>","DOI":"10.4049\/jimmunol.1700273","type":"journal-article","created":{"date-parts":[[2017,12,27]],"date-time":"2017-12-27T15:52:17Z","timestamp":1514389937000},"page":"928-936","source":"Crossref","is-referenced-by-count":16,"title":["Inhibition of the Deubiquitinase Usp14 Diminishes Direct MHC Class I Antigen Presentation"],"prefix":"10.1093","volume":"200","author":[{"given":"Amy L","family":"Palmer","sequence":"first","affiliation":[{"name":"Department of Biomedical Sciences, College of Veterinary Medicine, Oregon State University , Corvallis, OR 97331"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Annemieke","family":"de Jong","sequence":"additional","affiliation":[{"name":"Division of Cell Biology II, Netherlands Cancer Institute , 1066 CX Amsterdam,","place":["the Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yves","family":"Leestemaker","sequence":"additional","affiliation":[{"name":"Division of Cell Biology II, Netherlands Cancer Institute , 1066 CX Amsterdam,","place":["the Netherlands"]},{"name":"Department of Chemical Immunology, Leiden University Medical Center , 2333 ZC Leiden,","place":["the Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul P","family":"Geurink","sequence":"additional","affiliation":[{"name":"Division of Cell Biology II, Netherlands Cancer Institute , 1066 CX Amsterdam,","place":["the Netherlands"]},{"name":"Department of Chemical Immunology, Leiden University Medical Center , 2333 ZC Leiden,","place":["the Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruud H","family":"Wijdeven","sequence":"additional","affiliation":[{"name":"Division of Cell Biology II, Netherlands Cancer Institute , 1066 CX Amsterdam,","place":["the Netherlands"]},{"name":"Department of Chemical Immunology, Leiden University Medical Center , 2333 ZC Leiden,","place":["the Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0068-054X","authenticated-orcid":false,"given":"Huib","family":"Ovaa","sequence":"additional","affiliation":[{"name":"Division of Cell Biology II, Netherlands Cancer Institute , 1066 CX Amsterdam,","place":["the Netherlands"]},{"name":"Department of Chemical Immunology, Leiden University Medical Center , 2333 ZC Leiden,","place":["the Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian P","family":"Dolan","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences, College of Veterinary Medicine, Oregon State University , Corvallis, OR 97331"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2018,2,1]]},"reference":[{"key":"2025030610013124500_r1","doi-asserted-by":"crossref","first-page":"1553","DOI":"10.1007\/s00018-011-0662-1","article-title":"Post-proteasomal and proteasome-independent generation of MHC class I ligands","volume":"68","author":"van Endert","year":"2011","journal-title":"Cell. 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