Learning from the Proteasome How To Fine-Tune Cancer Immunotherapy

Vigneron, Nathalie; Abi Habib, Joanna; Van den Eynde, Benoit J.

doi:10.1016/j.trecan.2017.07.007

Cited by 33Immunotherapy and Immune ResponsesCancer Immunotherapy and Biomarkersvaccines and immunoinformatics approaches

Learning from the Proteasome How To Fine-Tune Cancer Immunotherapy

Vigneron, Nathalie, Abi Habib, Joanna, Van den Eynde, Benoit J.·2017·Trends in Cancer

DOI 10.1016/j.trecan.2017.07.007

Open this paper in CoChat — free account

Abstract

Cancer immunotherapy has recently emerged as a forefront strategy to fight cancer. Key players in antitumor responses are CD8+ cytolytic T lymphocytes (CTLs) that can detect tumor cells that carry antigens, in other words, small peptides bound to surface major histocompatibility complex (MHC) class I molecules. The success and safety of cancer immunotherapy strategies depends on the nature of the antigens recognized by the targeted T cells, their strict tumor specificity, and whether tumors and antigen-presenting cells can efficiently process the peptide. We review here the nature of the tumor antigens and their potential for the development of immunotherapeutic strategies. We also discuss the importance of proteasome in the production of these peptides in the context of immunotherapy and therapeutic cancer vaccines.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.trecan.2017.07.007

Cites

94 of 94 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

The greater hydrophobicity of bacterial peptides might make them preferable for antigen presentation and T cell recognition.
“a property that might make these peptides preferable for antigen presentation16 and recognition by T cells17”
From Identification of bacteria-derived HLA-bound peptides in melanoma (2021) · cites this paper as [16]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Safety, activity, and immune correlates of anti–PD-1 antibody in cancer
Topalian, S. L., Hodi, F. S., Brahmer, J. R., Gettinger, S. N., Smith, D. C., McDermott, D. F., Powderly, J. D., Carvajal, R. D., Sosman, J. A., Atkins, M. B., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1200690 · Cited by 12,628 · see citing works
PD-1 Blockade in Tumors with Mismatch-Repair Deficiency
Le, D. T., Uram, J. N., Wang, H., Bartlett, B. R., Kemberling, H., Eyring, A. D., Skora, A. D., Luber, B. S., Azad, N. S., Laheru, D., et al. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1500596 · Cited by 9,377 · see citing works
Mutational landscape determines sensitivity to PD-1 blockade in non–small cell lung cancer
Rizvi, N. A., Hellmann, M. D., Snyder, A., Kvistborg, P., Makarov, V., Havel, J. J., Lee, W., Yuan, J., Wong, P., Ho, T. S., et al. (2015) · Science · doi:10.1126/science.aaa1348 · Cited by 7,802 · see citing works
Genomic correlates of response to CTLA-4 blockade in metastatic melanoma
Van Allen, E. M., Miao, D., Schilling, B., Shukla, S. A., Blank, C., Zimmer, L., Sucker, A., Hillen, U., Geukes Foppen, M. H., Goldinger, S. M., et al. (2015) · Science · doi:10.1126/science.aad0095 · Cited by 2,839 · see citing works
Case Report of a Serious Adverse Event Following the Administration of T Cells Transduced With a Chimeric Antigen Receptor Recognizing ERBB2
Morgan, R. A., Yang, J. C.-H., Kitano, M., Dudley, M. E., Laurençot, C. M., & Rosenberg, S. A. (2010) · Molecular Therapy · doi:10.1038/mt.2010.24 · Cited by 2,542 · see citing works
Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules.
Rock, K. L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., & Goldberg, A. L. (1994) · Cell · doi:10.1016/s0092-8674(94)90462-6 · Cited by 2,524 · see citing works
Use of Tumor-Infiltrating Lymphocytes and Interleukin-2 in the Immunotherapy of Patients with Metastatic Melanoma
Rosenberg, S. A., Packard, B. S., Aebersold, P. M., Solomon, D., Topalian, S. L., Toy, S. T., Simon, P., Lotze, M. T., Yang, J. C., Seipp, C. A., et al. (1988) · New England Journal of Medicine · doi:10.1056/nejm198812223192527 · Cited by 2,389 · see citing works
Structure of 20S proteasome from yeast at 2.4Å resolution
Groll, M., Ditzel, L., Löwe, J., Stock, D., Bochtler, M., Bartunik, H. D., & Huber, R. (1997) · Nature · doi:10.1038/386463a0 · Cited by 2,265 · see citing works
Crystal Structure of the 20 S Proteasome from the Archaeon T. acidophilum at 3.4 Å Resolution
Löwe, J., Stock, D., Jap, B. K., Zwickl, P., Baumeister, W. P., & Huber, R. (1995) · Science · doi:10.1126/science.7725097 · Cited by 1,527 · see citing works
Gene therapy with human and mouse T-cell receptors mediates cancer regression and targets normal tissues expressing cognate antigen
Johnson, L. A., Morgan, R. A., Dudley, M. E., Cassard, L., Yang, J. C.-H., Hughes, M. S., Kammula, U. S., Royal, R. E., Sherry, R. M., Wunderlich, J. R., et al. (2009) · Blood · doi:10.1182/blood-2009-03-211714 · Cited by 1,421 · see citing works
The carcinoembryonic antigen (CEA) family: structures, suggested functions and expression in normal and malignant tissues
Hammarström, S. (1999) · Seminars in Cancer Biology · doi:10.1006/scbi.1998.0119 · Cited by 1,303 · see citing works
Ipilimumab monotherapy in patients with pretreated advanced melanoma: a randomised, double-blind, multicentre, phase 2, dose-ranging study
Wolchok, J. D., Neyns, B., Linette, G., Negrier, S., Lutzky, J., Thomas, L., Waterfield, W., Schadendorf, D., Smylie, M., Guthrie, T., et al. (2010) · The Lancet Oncology · doi:10.1016/s1470-2045(09)70334-1 · Cited by 1,195 · see citing works
Cardiovascular toxicity and titin cross-reactivity of affinity-enhanced T cells in myeloma and melanoma
Linette, G. P., Stadtmauer, E. A., Maus, M. V., Rapoport, A. P., Levine, B. L., Emery, L., Litzky, L. A., Bagg, A., Carreno, B. M., Cimino, P. J., et al. (2013) · Blood · doi:10.1182/blood-2013-03-490565 · Cited by 1,183 · see citing works
Cancer Regression and Neurological Toxicity Following Anti-MAGE-A3 TCR Gene Therapy
Morgan, R. A., Chinnasamy, N., Abate‐Daga, D., Gros, A., Robbins, P. F., Zheng, Z., Dudley, M. E., Feldman, S. A., Yang, J. C., Sherry, R. M., et al. (2013) · Journal of Immunotherapy · doi:10.1097/cji.0b013e3182829903 · Cited by 1,155 · see citing works
Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
Obeng, E. A., Carlson, L. M., Gutman, D. M., Harrington, W. J., Lee, K. P., & Boise, L. (2006) · Blood · doi:10.1182/blood-2005-08-3531 · Cited by 1,147 · see citing works
Tumour antigens recognized by T lymphocytes: at the core of cancer immunotherapy
Coulie, P. G., den Eynde, B. J. V., van der Bruggen, P., & Boon, T. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3670 · Cited by 1,142 · see citing works
Vaccination against HPV-16 Oncoproteins for Vulvar Intraepithelial Neoplasia
Kenter, G. G., Welters, M. J. P., Valentijn, A. R. P. M., Löwik, M. J. G., der Meer, D. M. A. B.-V., Vloon, A. P. G., Essahsah, F., Fathers, L. M., Offringa, R., Drijfhout, J. W., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0810097 · Cited by 1,101 · see citing works
Mining exomic sequencing data to identify mutated antigens recognized by adoptively transferred tumor-reactive T cells
Robbins, P. F., Lu, Y., El‐Gamil, M., Li, Y. F., Gross, C. A., Gartner, J. J., Lin, J., Teer, J. K., Cliften, P. F., Tycksen, E., et al. (2013) · Nature Medicine · doi:10.1038/nm.3161 · Cited by 1,074 · see citing works
T Cells Targeting Carcinoembryonic Antigen Can Mediate Regression of Metastatic Colorectal Cancer but Induce Severe Transient Colitis
Parkhurst, M. R., Yang, J. C.-H., Langan, R. C., Dudley, M. E., Nathan, D.-A. N., Feldman, S. A., Davis, J. L., Morgan, R. A., Merino, M. J., Sherry, R. M., et al. (2010) · Molecular Therapy · doi:10.1038/mt.2010.272 · Cited by 1,025 · see citing works
Treatment of Metastatic Renal Cell Carcinoma With Autologous T-Lymphocytes Genetically Retargeted Against Carbonic Anhydrase IX: First Clinical Experience
Lamers, C. H. J., Sleijfer, S., Vulto, A. G., Kruit, W. H. J., Kliffen, M., Debets, R., Gratama, J. W., Stoter, G., & Oosterwijk, E. (2006) · Journal of Clinical Oncology · doi:10.1200/jco.2006.05.9964 · Cited by 915 · see citing works
Evolution of Neoantigen Landscape during Immune Checkpoint Blockade in Non–Small Cell Lung Cancer
Anagnostou, V., Smith, K. N., Forde, P. M., Niknafs, N., Bhattacharya, R., White, J. R., Zhang, T., Adleff, V., Phallen, J. A., Wali, N., et al. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-0828 · Cited by 898 · see citing works
Adoptive immunotherapy for cancer: building on success
Gattinoni, L., Powell, D. J., Rosenberg, S. A., & Restifo, N. P. (2006) · Nature reviews. Immunology · doi:10.1038/nri1842 · Cited by 841 · see citing works
Tumor Exome Analysis Reveals Neoantigen-Specific T-Cell Reactivity in an Ipilimumab-Responsive Melanoma
van Rooij, N., van Buuren, M. M., Philips, D., Velds, A., Toebes, M., Heemskerk, B., van Dijk, L. J. A., Behjati, S., Hilkmann, H., el Atmioui, D., et al. (2013) · Journal of Clinical Oncology · doi:10.1200/jco.2012.47.7521 · Cited by 798 · see citing works
Tryptophan Catabolism in Cancer: Beyond IDO and Tryptophan Depletion
Platten, M., Wick, W., & den Eynde, B. J. V. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-0569 · Cited by 708 · see citing works
Identification of a Titin-Derived HLA-A1–Presented Peptide as a Cross-Reactive Target for Engineered MAGE A3–Directed T Cells
Cameron, B., Gerry, A. B., Dukes, J. D., Harper, J. V., Kannan, V., Bianchi, F., Grand, F., Brewer, J. E., Gupta, M., Plesa, G., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3006034 · Cited by 685 · see citing works
Proteasome from Thermoplasma acidophilum : a Threonine Protease
Seemüller, E., Lupas, A. N., Stock, D., Löwe, J., Huber, R., & Baumeister, W. P. (1995) · Science · doi:10.1126/science.7725107 · Cited by 634 · see citing works
A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis
Muchamuel, T., Basler, M., Aujay, M. A., Suzuki, É., Kalim, K. W., Lauer, C., Sylvain, C., Ring, E. R., Shields, J., Jiang, J., et al. (2009) · Nature Medicine · doi:10.1038/nm.1978 · Cited by 603 · see citing works
Regulation of CD8 + T Cell Development by Thymus-Specific Proteasomes
Murata, S., Sasaki, K., Kishimoto, T., Niwa, S., Hayashi, H., Takahama, Y., & Tanaka, K. (2007) · Science · doi:10.1126/science.1141915 · Cited by 584 · see citing works
γ-Interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
Gaczynska, M. E., Rock, K. L., & Goldberg, A. L. (1993) · Nature · doi:10.1038/365264a0 · Cited by 571 · see citing works
Immuno- and Constitutive Proteasome Crystal Structures Reveal Differences in Substrate and Inhibitor Specificity
Huber, E. M., Basler, M., Schwab, R., Heinemeyer, W., Kirk, C. J., Groettrup, M., & Groll, M. (2012) · Cell · doi:10.1016/j.cell.2011.12.030 · Cited by 485 · see citing works
The response of autologous T cells to a human melanoma is dominated by mutated neoantigens
Lennerz, V., Fatho, M., Gentilini, C., Frye, R. A., Lifke, A., Ferel, D., Wölfel, C., Huber, C., & Wölfel, T. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500090102 · Cited by 458 · see citing works
MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
Driscoll, J. J., Brown, M. G., Finley, D. J., & Monaco, J. J. (1993) · Nature · doi:10.1038/365262a0 · Cited by 448 · see citing works
Processing of Some Antigens by the Standard Proteasome but Not by the Immunoproteasome Results in Poor Presentation by Dendritic Cells
Morel, S., Lévy, F., Burlet‐Schiltz, O., Brasseur, F., Probst‐Kepper, M., Peitrequin, A.-L., Monsarrat, B., Velthoven, R. V., Cerottini, J., Boon, T., et al. (2000) · Immunity · doi:10.1016/s1074-7613(00)80163-6 · Cited by 415 · see citing works
Mechanism of Gate Opening in the 20S Proteasome by the Proteasomal ATPases
Rabl, J., Smith, D. M., Yu, Y., Chang, S., Goldberg, A. L., & Cheng, Y. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.004 · Cited by 383 · see citing works
Isolation of neoantigen-specific T cells from tumor and peripheral lymphocytes
Cohen, C. J., Gartner, J. J., Horovitz‐Fried, M., Shamalov, K., Trebska-McGowan, K., Bliskovsky, V. V., Parkhurst, M. R., Ankri, C., Prickett, T. D., Crystal, J. S., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci82416 · Cited by 374 · see citing works
Induction of Tumor-Specific CD4+ and CD8+ T-Cell Immunity in Cervical Cancer Patients by a Human Papillomavirus Type 16 E6 and E7 Long Peptides Vaccine
Welters, M. J. P., Kenter, G. G., Piersma, S. J., Vloon, A. P. G., Löwik, M. J. G., der Meer, D. M. A. B.-V., Drijfhout, J. W., Valentijn, A. R. P. M., Wafelman, A. R., Oostendorp, J., et al. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-1880 · Cited by 374 · see citing works
A large fraction of HLA class I ligands are proteasome-generated spliced peptides
Liepe, J., Marino, F., Sidney, J., Jekő, A., Bunting, D. E., Sette, A., Kloetzel, P. M., Stumpf, M. P. H., Heck, A. J. R., & Mishto, M. (2016) · Science · doi:10.1126/science.aaf4384 · Cited by 368 · see citing works
Landscape of immunogenic tumor antigens in successful immunotherapy of virally-induced epithelial cancer
Stevanović, S., Pasetto, A., Helman, S. R., Gartner, J. J., Prickett, T. D., Howie, B., Robins, H., Robbins, P., Klebanoff, C., Rosenberg, S., et al. (2017) · Science · doi:10.1126/science.aak9510 · Cited by 364 · see citing works
Medullary Epithelial Cells of the Human Thymus Express a Highly Diverse Selection of Tissue-specific Genes Colocalized in Chromosomal Clusters
Gotter, J., Brors, B., Hergenhahn, M., & Kyewski, B. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20031677 · Cited by 363 · see citing works
Immune recognition of a human renal cancer antigen through post-translational protein splicing
Hanada, K., Yewdell, J. W., & Yang, J. C.-H. (2004) · Nature · doi:10.1038/nature02240 · Cited by 337 · see citing works
Vitiligo in Patients with Melanoma
Rosenberg, S. A., & White, D. E. (1996) · Journal of Immunotherapy · doi:10.1097/00002371-199601000-00009 · Cited by 331 · see citing works
An Antigenic Peptide Produced by Peptide Splicing in the Proteasome
Vigneron, N., Stroobant, V., Chapiro, J., Ooms, A., Degiovanni, G., Morel, S., van der Bruggen, P., Boon, T., & den Eynde, B. J. V. (2004) · Science · doi:10.1126/science.1095522 · Cited by 329 · see citing works
Self-citation
Bortezomib Inhibits PKR-Like Endoplasmic Reticulum (ER) Kinase and Induces Apoptosis via ER Stress in Human Pancreatic Cancer Cells
Nawrocki, S. T., Carew, J. S., Dunner, K., Boise, L., Chiao, P. J., Huang, P., Abbruzzese, J. L., & McConkey, D. J. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-2394 · Cited by 326 · see citing works
A role for the ubiquitin-dependent proteolytic pathway in MHC class l-restricted antigen presentation
Michalek, M. T., Grant, E. P., Gramm, C. F., Goldberg, A. L., & Rock, K. L. (1993) · Nature · doi:10.1038/363552a0 · Cited by 321 · see citing works
Mice completely lacking immunoproteasomes show major changes in antigen presentation
Kincaid, E., Che, J. W., York, I. A., Escobar, H., Reyes‐Vargas, E., Delgado, J. C., Welsh, R. M., Karow, M. L., Murphy, A. J., Valenzuela, D. M., et al. (2011) · Nature Immunology · doi:10.1038/ni.2203 · Cited by 291 · see citing works
Programmed death-1 pathway in cancer and autoimmunity
Pedoeem, A., Azoulay‐Alfaguter, I., Strazza, M., Silverman, G. J., & Mor, A. (2014) · Clinical Immunology · doi:10.1016/j.clim.2014.04.010 · Cited by 269 · see citing works
Human Tumor Antigens and Cancer Immunotherapy
Vigneron, N. (2015) · BioMed Research International · doi:10.1155/2015/948501 · Cited by 227 · see citing works
Self-citation
Two abundant proteasome subtypes that uniquely process some antigens presented by HLA class I molecules
Guillaume, B., Chapiro, J., Stroobant, V., Colau, D., Holle, B. V., Parvizi, G. K., Bousquet, M., Théate, I., Parmentier, N., & den Eynde, B. J. V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009778107 · Cited by 218 · see citing works
Vaccination during myeloid cell depletion by cancer chemotherapy fosters robust T cell responses
Welters, M. J. P., van der Sluis, T. C., van Meir, H., Loof, N. M., van Ham, V. J., van Duikeren, S., Santegoets, S. J. A. M., Arens, R., de Kam, M. L., Cohen, A. F., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aad8307 · Cited by 216 · see citing works
Thymoproteasome Shapes Immunocompetent Repertoire of CD8+ T Cells
Nitta, T., Murata, S., Sasaki, K., Fujii, H., Ripen, A. M., Ishimaru, N., Koyasu, S., Tanaka, K., & Takahama, Y. (2010) · Immunity · doi:10.1016/j.immuni.2009.10.009 · Cited by 213 · see citing works
Targeted inhibition of the immunoproteasome is a potent strategy against models of multiple myeloma that overcomes resistance to conventional drugs and nonspecific proteasome inhibitors
Kuhn, D. J., Hunsucker, S. A., Chen, Q., Voorhees, P. M., Orłowski, M., & Orlowski, R. Z. (2008) · Blood · doi:10.1182/blood-2008-07-171637 · Cited by 207 · see citing works
Immunoproteasome deficiency is a feature of non-small cell lung cancer with a mesenchymal phenotype and is associated with a poor outcome
Tripathi, S. C., Peters, H. L., Taguchi, A., Katayama, H., Wang, H., Momin, A. A., Jolly, M. K., Çeliktaş, M., Rodriguez‐Canales, J., Liu, H., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1521812113 · Cited by 203 · see citing works
An Antigen Produced by Splicing of Noncontiguous Peptides in the Reverse Order
Warren, E. H., Vigneron, N., Gavin, M. A., Coulie, P. G., Stroobant, V., Dalet, A., Tykodi, S. S., Xuereb, S. M., Mito, J. K., Riddell, S. R., et al. (2006) · Science · doi:10.1126/science.1130660 · Cited by 201 · see citing works
Self-citation
HPV16 synthetic long peptide (HPV16-SLP) vaccination therapy of patients with advanced or recurrent HPV16-induced gynecological carcinoma, a phase II trial
van Poelgeest, M. I. E., Welters, M. J. P., van Esch, E. M. G., Stynenbosch, L. F. M., Kerpershoek, G., van Meerten, E. L. V. P., van den Hende, M., Löwik, M. J. G., der Meer, D. M. A. B.-V., Fathers, L. M., et al. (2013) · Journal of Translational Medicine · doi:10.1186/1479-5876-11-88 · Cited by 194 · see citing works
The Human Vaccines Project: A roadmap for cancer vaccine development
Romero, P. J., Banchereau, J., Bhardwaj, N., Cockett, M. I., Disis, M. L., Dranoff, G., Gilboa, E., Hammond, S. A., Hershberg, R. D., Korman, A. J., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf0685 · Cited by 194 · see citing works
Different proteasome subtypes in a single tissue exhibit different enzymatic properties 1 1Edited by R. Huber
Dahlmann, B., Ruppert, T., Kuehn, L., Merforth, S., & Kloetzel, P. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4185 · Cited by 193 · see citing works
Database of T cell-defined human tumor antigens: the 2013 update.
Vigneron, N., Stroobant, V., den Eynde, B. J. V., & van der Bruggen, P. (2013) · Europe PMC (PubMed Central) · Cited by 191 · see citing works
Self-citation
Isolation of T-Cell Receptors Specifically Reactive with Mutated Tumor-Associated Antigens from Tumor-Infiltrating Lymphocytes Based on CD137 Expression
Parkhurst, M. R., Gros, A., Pasetto, A., Prickett, T. D., Crystal, J. S., Robbins, P. F., & Rosenberg, S. A. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-2680 · Cited by 182 · see citing works
Antigen Spreading Contributes to MAGE Vaccination-Induced Regression of Melanoma Metastases
Corbière, V., Chapiro, J., Stroobant, V., Ma, W., Lurquin, C., Lethé, B., van Baren, N., den Eynde, B. J. V., Boon, T., & Coulie, P. G. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-2693 · Cited by 176 · see citing works
Destructive Cleavage of Antigenic Peptides Either by the Immunoproteasome or by the Standard Proteasome Results in Differential Antigen Presentation
Chapiro, J., Claverol, S., Piette, F., Ma, W., Stroobant, V., Guillaume, B., Gairin, J.-E., Morel, S., Burlet‐Schiltz, O., Monsarrat, B., et al. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.2.1053 · Cited by 159 · see citing works
Efficient Generation of a Hepatitis B Virus Cytotoxic T Lymphocyte Epitope Requires the Structural Features of Immunoproteasomes
Sijts, A. J. A. M., Ruppert, T., Rehermann, B., Schmidt, M., Koszinowski, U. H., & Kloetzel, P. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.191.3.503 · Cited by 153 · see citing works
Use of HLA peptidomics and whole exome sequencing to identify human immunogenic neo-antigens
Kalaora, S., Barnea, E., Merhavi-Shoham, E., Qutob, N., Teer, J. K., Shimony, N., Schachter, J., Rosenberg, S. A., Besser, M. J., Admon, A., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.6960 · Cited by 148 · see citing works
Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation
Grant, E. P., Michalek, M. T., Goldberg, A. L., & Rock, K. L. (1995) · The Journal of Immunology · doi:10.4049/jimmunol.155.8.3750 · Cited by 142 · see citing works
Purification and characterization of a protein inhibitor of the 20S proteasome (macropain)
Chu-Ping, M., Slaughter, C. A., & Demartino, G. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90218-3 · Cited by 142 · see citing works
An antigenic peptide produced by reverse splicing and double asparagine deamidation
Dalet, A., Robbins, P. F., Stroobant, V., Vigneron, N., Li, Y. F., El‐Gamil, M., Hanada, K., Yang, J. C.-H., Rosenberg, S. A., & den Eynde, B. J. V. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1101892108 · Cited by 128 · see citing works
Self-citation
Durable Complete Response from Metastatic Melanoma after Transfer of Autologous T Cells Recognizing 10 Mutated Tumor Antigens
Prickett, T. D., Crystal, J. S., Cohen, C. J., Pasetto, A., Parkhurst, M. R., Gartner, J. J., Yao, X., Wang, R., Gros, A., Li, Y. F., et al. (2016) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-15-0215 · Cited by 126 · see citing works
The proteasome‐specific inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells
Cerundolo, V., Benham, A. M., Braud, V. M., Mukherjee, S., Gould, K. G., Macino, B., Neefjes, J., & Townsend, A. (1997) · European Journal of Immunology · doi:10.1002/eji.1830270148 · Cited by 122 · see citing works
The Production of a New MAGE-3 Peptide Presented to Cytolytic T Lymphocytes by HLA-B40 Requires the Immunoproteasome
Schultz, E. S., Chapiro, J., Lurquin, C., Claverol, S., Burlet‐Schiltz, O., Warnier, G., Russo, V. E. A., Morel, S., Lévy, F., Boon, T., et al. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20011974 · Cited by 122 · see citing works
LMP2-Specific Inhibitors: Chemical Genetic Tools for Proteasome Biology
Ho, Y. K., Bargagna‐Mohan, P., Wehenkel, M., Mohan, R., & Kim, K. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.03.008 · Cited by 114 · see citing works
A Conserved F Box Regulatory Complex Controls Proteasome Activity in Drosophila
Bader, M., Benjamin, S., Wapinski, O. L., Smith, D. M., Goldberg, A. L., & Steller, H. (2011) · Cell · doi:10.1016/j.cell.2011.03.021 · Cited by 111 · see citing works
Expression of immunoproteasome genes is regulated by cell-intrinsic and –extrinsic factors in human cancers
Rouette, A., Trofimov, A., Haberl, D., Boucher, G., Lavallée, V., D’Angelo, G., Hébert, J., Sauvageau, G., Lemieux, S., & Perreault, C. (2016) · Scientific Reports · doi:10.1038/srep34019 · Cited by 102 · see citing works
Proteasomes generate spliced epitopes by two different mechanisms and as efficiently as non-spliced epitopes
Ebstein, F., Textoris‐Taube, K., Keller, C., Golnik, R., Vigneron, N., den Eynde, B. J. V., Schuler‐Thurner, B., Schadendorf, D., Lorenz, F. K. M., Uckert, W., et al. (2016) · Scientific Reports · doi:10.1038/srep24032 · Cited by 100 · see citing works
Self-citation
Expression of the proteasome activator PA28 rescues the presentation of a cytotoxic T lymphocyte epitope on melanoma cells.
Sun, Y., Sijts, A. J. A. M., Song, M., Janek, K., Nussbaum, A. K., Kral, S., Schirle, M., Stevanović, S., Paschen, A., Schild, H., et al. (2002) · PubMed · Cited by 96 · see citing works
Deletion of Immunoproteasome Subunits Imprints on the Transcriptome and Has a Broad Impact on Peptides Presented by Major Histocompatibility Complex I molecules
de Verteuil, D. A., Muratore‐Schroeder, T. L., Granados, D. P., Fortier, M., Hardy, M., Bramoullé, A., Caron, É., Vincent, K., Mader, S., Lemieux, S., et al. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900566-mcp200 · Cited by 94 · see citing works
Proteasome Subtypes and Regulators in the Processing of Antigenic Peptides Presented by Class I Molecules of the Major Histocompatibility Complex
Vigneron, N., & den Eynde, B. V. (2014) · Biomolecules · doi:10.3390/biom4040994 · Cited by 91 · see citing works
Self-citation
Twelve-year survival and immune correlates in dendritic cell–vaccinated melanoma patients
Groß, S., Erdmann, M., Haendle, I., Voland, S., Berger, T. G., Schultz, E. S., Strasser, E. F., Dankerl, P., Janka, R., Schliep, S., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.91438 · Cited by 87 · see citing works
Splicing of Distant Peptide Fragments Occurs in the Proteasome by Transpeptidation and Produces the Spliced Antigenic Peptide Derived from Fibroblast Growth Factor-5
Dalet, A., Vigneron, N., Stroobant, V., Hanada, K., & den Eynde, B. J. V. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0901277 · Cited by 86 · see citing works
Self-citation
Analysis of the Processing of Seven Human Tumor Antigens by Intermediate Proteasomes
Guillaume, B., Stroobant, V., Bousquet, M., Colau, D., Chapiro, J., Parmentier, N., Dalet, A., & den Eynde, B. J. V. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1103213 · Cited by 79 · see citing works
Driving Forces of Proteasome-catalyzed Peptide Splicing in Yeast and Humans
Mishto, M., Goede, A., Textoris‐Taube, K., Keller, C., Janek, K., Henklein, P., Niewienda, A., Kloß, A., Gohlke, S., Dahlmann, B., et al. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.020164 · Cited by 78 · see citing works
Molecular and Cellular Roles of PI31 (PSMF1) Protein in Regulation of Proteasome Function
Li, X., Thompson, D., Kumar, B., & Demartino, G. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.561183 · Cited by 74 · see citing works
A Spliced Antigenic Peptide Comprising a Single Spliced Amino Acid Is Produced in the Proteasome by Reverse Splicing of a Longer Peptide Fragment followed by Trimming
Michaux, A., Larrieu, P., Stroobant, V., Fonteneau, J., Jotereau, F., den Eynde, B. J. V., Moreau‐Aubry, A., & Vigneron, N. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302032 · Cited by 72 · see citing works
Self-citation
Melanoma immunotherapy using mature DCs expressing the constitutive proteasome
Dannull, J., Haley, N. R., Archer, G. E., Nair, S. K., Boczkowski, D., Harper, M., de Rosa, N., Pickett, N., Mosca, P. J., Burchette, J. L., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67544 · Cited by 69 · see citing works
Processing of Tumor-Associated Antigen by the Proteasomes of Dendritic Cells ControlsIn vivoT-Cell Responses
Chapatte, L., Ayyoub, M., Morel, S., Peitrequin, A.-L., Lévy, N., Servis, C., den Eynde, B. J. V., Valmori, D., & Lévy, F. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4310 · Cited by 65 · see citing works
Comparative Prime-Boost Vaccinations Using Semliki Forest Virus, Adenovirus, and ALVAC Vectors Demonstrate Differences in the Generation of a Protective Central Memory CTL Response against the P815 Tumor
Näslund, T. I., Uyttenhove, C., Nordström, E. K. L., Colau, D., Warnier, G., Jondal, M., den Eynde, B. J. V., & Liljeström, P. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.11.6761 · Cited by 65 · see citing works
Differences in the production of spliced antigenic peptides by the standard proteasome and the immunoproteasome
Dalet, A., Stroobant, V., Vigneron, N., & den Eynde, B. J. V. (2010) · European Journal of Immunology · doi:10.1002/eji.201040750 · Cited by 63 · see citing works
Self-citation
The proteasome immunosubunits, PA28 and ER‐aminopeptidase 1 protect melanoma cells from efficient MART‐126‐35‐specific T‐cell recognition
Keller, M., Ebstein, F., Bürger, E., Textoris‐Taube, K., Gorny, X., Urban, S., Zhao, F., Dannenberg, T., Sucker, A., Keller, C., et al. (2015) · European Journal of Immunology · doi:10.1002/eji.201445243 · Cited by 54 · see citing works
Long-term follow-up of patients treated by adoptive transfer of melanoma tumor-infiltrating lymphocytes as adjuvant therapy for stage III melanoma
Khammari, A., Nguyen, J., Pandolfino, M. C., Quereux, G., Brocard, A., Bercegeay, S., Cassidanius, A., Lemarre, P., Volteau, C., Labarrière, N., et al. (2007) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-007-0340-1 · Cited by 52 · see citing works
Role of peptide processing predictions in T cell epitope identification: contribution of different prediction programs
Calis, J. J. A., Reinink, P., Keller, C., Kloetzel, P. M., & Keşmir, C. (2014) · Immunogenetics · doi:10.1007/s00251-014-0815-0 · Cited by 48 · see citing works
Insights into the processing of MHC class I ligands gained from the study of human tumor epitopes
Vigneron, N., & den Eynde, B. J. V. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0658-x · Cited by 41 · see citing works
Self-citation
Mismatch in epitope specificities between IFNγ inflamed and uninflamed conditions leads to escape from T lymphocyte killing in melanoma
Woods, K., Knights, A. J., Anaka, M., Schittenhelm, R. B., Purcell, A. W., Behren, A., & Cebon, J. S. (2016) · Journal for ImmunoTherapy of Cancer · doi:10.1186/s40425-016-0111-7 · Cited by 28 · see citing works
Shared mechanisms in stemness and carcinogenesis: lessons from oncogenic viruses
Iacovides, D. C., Michael, S., Achilleos, C., & Strati, K. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00066 · Cited by 21 · see citing works
Production of a Specific Major Histocompatibility Complex Class I-restricted Epitope by Ubiquitin-dependent Degradation of Modified Ovalbumin in Lymphocyte Lysate
Ben-Shahar, S., Cassouto, B., Novak, L., Porgador, A., & Reiss, Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.34.21060 · Cited by 19 · see citing works
Polyubiquitination of lysine‐48 is an essential but indirect signal for MHC class I antigen processing
Fiebiger, B. M., Pfister, H., Behrends, U., & Mautner, J. (2014) · European Journal of Immunology · doi:10.1002/eji.201444830 · Cited by 11 · see citing works
The capture proteasome assay: A method to measure proteasome activity in vitro
Vigneron, N., Habib, J. A., & den Eynde, B. J. V. (2015) · Analytical Biochemistry · doi:10.1016/j.ab.2015.04.019 · Cited by 10 · see citing works
Self-citation

Flagged first, then by citations

2 of the 96 references couldn’t be matched to a known paper.

Sorted by citations

Identification of bacteria-derived HLA-bound peptides in melanoma
Kalaora, S., Nagler, A., Nejman, D., Alon, M., Barbolin, C., Barnea, E., Ketelaars, S. L. C., Cheng, K., Vervier, K., Shental, N., et al. (2021) · Nature · doi:10.1038/s41586-021-03368-8 · Cited by 457 · see citing works
Immunoproteasome expression is associated with better prognosis and response to checkpoint therapies in melanoma
Kalaora, S., Lee, J. S., Barnea, E., Levy, R., Greenberg, P., Alon, M., Yagel, G., Eli, G. B., Oren, R., Peri, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14639-9 · Cited by 153 · see citing works
Mechanisms of resistance to immune checkpoint inhibitors in melanoma: What we have to overcome?
Ziogas, D. C., Theocharopoulos, C., Koutouratsas, T., Haanen, J. B. A. G., & Gogas, H. J. (2022) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2022.102499 · Cited by 119 · see citing works
Proteasomes and Several Aspects of Their Heterogeneity Relevant to Cancer
Morozov, A. V., & Карпов, В. Л. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00761 · Cited by 111 · see citing works
Functional Differences between Proteasome Subtypes
Habib, J. A., Lesenfants, J., Vigneron, N., & den Eynde, B. J. V. (2022) · Cells · doi:10.3390/cells11030421 · Cited by 88 · see citing works
Self-citation
FAK suppresses antigen processing and presentation to promote immune evasion in pancreatic cancer
Canel, M., Sławińska, A., Lonergan, D. W., Kallor, A. A., Upstill‐Goddard, R., Davidson, C., von Kriegsheim, A., Biankin, A. V., Byron, A., Alfaro, J. A., et al. (2023) · Gut · doi:10.1136/gutjnl-2022-327927 · Cited by 81 · see citing works
On the Role of the Immunoproteasome in Protein Homeostasis
Basler, M., & Groettrup, M. (2021) · Cells · doi:10.3390/cells10113216 · Cited by 72 · see citing works
The emerging role for Cullin 4 family of E3 ligases in tumorigenesis
Cheng, J., Guo, J., North, B. J., Tao, K., Zhou, P., & Wei, W. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.11.007 · Cited by 69 · see citing works
Islet stress, degradation and autoimmunity
Thomaidou, S., Zaldumbide, A., & Roep, B. O. (2018) · Diabetes Obesity and Metabolism · doi:10.1111/dom.13387 · Cited by 47 · see citing works
Recent insights how combined inhibition of immuno/proteasome subunits enables therapeutic efficacy
Basler, M., & Groettrup, M. (2020) · Genes and Immunity · doi:10.1038/s41435-020-00109-1 · Cited by 40 · see citing works
Targeting an alternate Wilms’ tumor antigen 1 peptide bypasses immunoproteasome dependency
Lahman, M. C., Schmitt, T. M., Paulson, K. G., Vigneron, N., Buenrostro, D., Wagener, F. D., Voillet, V., Martin, L., Gottardo, R., Bielas, J. H., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abg8070 · Cited by 40 · see citing works
Self-citation
The dichotomous role of immunoproteasome in cancer: Friend or foe?
Chen, B., Zhu, H., Yang, B. Y., & Cao, J. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.11.005 · Cited by 36 · see citing works
Genetically modified immune cells targeting tumor antigens
Poorebrahim, M., Abazari, M. F., Sadeghi, S., Mahmoudi, R., Kheirollahi, A., Askari, H., Wickström, S. L., Poortahmasebi, V., Lundqvist, A., Kiessling, R. W., et al. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107603 · Cited by 35 · see citing works
The biogenesis of the immunopeptidome
Admon, A. (2023) · Seminars in Immunology · doi:10.1016/j.smim.2023.101766 · Cited by 27 · see citing works
A synthetic DNA template for fast manufacturing of versatile single epitope mRNA
de Mey, W., Schrijver, P. D., Autaers, D., Pfitzer, L., Fant, B., Locy, H., Esprit, A., Lybaert, L., Bogaert, C., Verdonck, M., et al. (2022) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2022.08.021 · Cited by 28 · see citing works
At the Cutting Edge against Cancer: A Perspective on Immunoproteasome and Immune Checkpoints Modulation as a Potential Therapeutic Intervention
Tundo, G. R., Sbardella, D., Oddone, F., Kudriaeva, A. A., Lacal, P. M., Belogurov, A. A., Graziani, G., & Marini, S. (2021) · Cancers · doi:10.3390/cancers13194852 · Cited by 24 · see citing works
RNA in Cancer Immunotherapy: Unlocking the Potential of the Immune System
de Mey, W., Esprit, A., Thielemans, K., Breckpot, K., & Franceschini, L. (2022) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-21-3304 · Cited by 25 · see citing works
Pro- and Antitumorigenic Capacity of Immunoproteasomes in Shaping the Tumor Microenvironment
Leister, H., Luu, M., Staudenraus, D., Krol, A. L., Mollenkopf, H., Sharma, A., Schmerer, N., Schulte, L. N., Bertrams, W., Schmeck, B., et al. (2021) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-20-0492 · Cited by 24 · see citing works
Identification of PSMB9 and CXCL13 as Immune-related Diagnostic Markers for Rheumatoid Arthritis by Machine Learning
Li, Z. Y., Chen, Y., Maimaiti, Z., Xu, C., Fu, J. Q., Deng, T., Hao, L., & Chen, J. (2022) · Current Pharmaceutical Design · doi:10.2174/1381612828666220831085608 · Cited by 21 · see citing works
Driving neoantigen-based cancer vaccines for personalized immunotherapy into clinic: A burdensome journey to promising land
Yu, G., He, X., Li, X., & Wu, Y. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113464 · Cited by 20 · see citing works
The Effect of Interferons on Presentation of Defective Ribosomal Products as HLA Peptides
Komov, L., Kadosh, D. M., Barnea, E., & Admon, A. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100105 · Cited by 16 · see citing works
Unraveling UPR-mediated intercellular crosstalk: Implications for immunotherapy resistance mechanisms
Si, L., Zhou, Q., Zhao, R., Xie, L., Cao, W., & Feng, Y. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.217613 · Cited by 14 · see citing works
DHDH-mediated D-xylose metabolism induces immune evasion in triple-negative breast cancer
Wu, H., Gong, Y., Ling, Y.-X., Wu, S., Ji, P., Zhao, Q., He, L., Shao, Z., Jiang, Y., & Liu, G. (2024) · Med · doi:10.1016/j.medj.2024.10.012 · Cited by 11 · see citing works
The Novel HDAC Inhibitor OBP-801 Promotes MHC Class I Presentation Through LMP2 Upregulation, Enhancing the PD-1-Targeting Therapy in Clear Cell Renal Cell Carcinoma
Narukawa, T., Yasuda, S., Horinaka, M., Taniguchi, K., Tsujikawa, T., Morita, M., Ukimura, O., & Sakai, T. (2024) · Cancers · doi:10.3390/cancers16234058 · Cited by 9 · see citing works
Harnessing microbial antigens as cancer antigens: a promising avenue for cancer immunotherapy
Zhang, T., Zhang, X., Chen, J., Zhang, X., & Zhang, Y. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1411490 · Cited by 7 · see citing works
Evolution by innovation as a driving force to improve TCR-T therapies
Schendel, D. J. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1216829 · Cited by 6 · see citing works
Myelin Basic Protein Fragmentation by Engineered Human Proteasomes with Different Catalytic Phenotypes Revealed Direct Peptide Ligands of MS-Associated and Protective HLA Class I Molecules
Saratov, G. A., Vladimirov, V. I., Novoselov, A. L., Ziganshin, R., Chen, G., Baymukhametov, T. N., Konevega, A. L., Belogurov, A. A., & Kudriaeva, A. A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032091 · Cited by 3 · see citing works
Multikinase inhibitors modulate non-constitutive proteasome expression in colorectal cancer cells
Burov, A. V., Grigorieva, E., Lebedev, T. D., Vedernikova, V., Попенко, В. И., Astakhova, T., Leonova, O. G., Spirin, P., Prassolov, V., Карпов, В. Л., et al. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1351641 · Cited by 4 · see citing works
Association of Proteasome Activity and Pool Heterogeneity with Markers Determining the Molecular Subtypes of Breast Cancer
Кондакова, И. В., Sereda, E. E., Александровна, С. Е., Vtorushin, S. V., Vedernikova, V., Burov, A. V., Spirin, P., Prassolov, V., Lebedev, T. D., Morozov, A. V., et al. (2025) · Cancers · doi:10.3390/cancers17010159 · Cited by 4 · see citing works
Intratumor injection of BCG Ag85A high-affinity peptides enhanced anti-tumor efficacy in PPD-positive melanoma
Qin, L., Zhang, G., Wu, Y., Yang, Y., & Zou, Z. (2024) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-024-03693-7 · Cited by 2 · see citing works
Protein Degradation and the Lysosomal System
Kaushik, S., & Cuervo, A. M. (2020) · Wiley eBooks · doi:10.1002/9781119436812.ch11 · Cited by 1 · see citing works
Faculty Opinions recommendation of Immunoproteasome expression is associated with better prognosis and response to checkpoint therapies in melanoma.
Endert, P. V. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.737378954.793571888
Échapper à la mort cellulaire dans le cancer : mitophagie et régulation de la mort indépendante des caspases
Villa, E. (2017) · theses.fr (ABES) · doi:10.70675/f0d1579dzdd47z4ac8z82abz4e3b85a0100b

Identification d'antigènes tumoraux d’intérêt pour l'immunothérapie spécifique au cancer
den Eynde, B. J. V. (2001) · DIAL (Catholic University of Leuven)
MM-210 Targeting Proteasome-Dependent Antigen Presentation to Enhance T Cell–Mediated Tumor Killing
Kim, B., Ignatz-Hoover, J. J., Malek, E., Murphy, E., & Driscoll, J. J. (2022) · Clinical Lymphoma Myeloma & Leukemia · doi:10.1016/s2152-2650(22)01605-6
[Discovery of the splicing of peptides by the proteasome and study of preclinical models of anticancer immunotherapy].
den Eynde, B. J. V. (2007) · PubMed · Cited by 1 · see citing works
Synthetic antigenic peptides as a new strategy for immunotherapy of cancer.
Appella, E., Loftus, D. J., Sakaguchi, K., Sette, A., & Celis, E. (1995) · PubMed · Cited by 12 · see citing works
A MAGE‐C2 antigenic peptide processed by the immunoproteasome is recognized by cytolytic T cells isolated from a melanoma patient after successful immunotherapy
Ma, W., Vigneron, N., Chapiro, J., Stroobant, V., Germeau, C., Boon, T., Coulie, P. G., & den Eynde, B. J. V. (2011) · International Journal of Cancer · doi:10.1002/ijc.25911 · Cited by 39 · see citing works
Self-citation

Authors: Vigneron, N., Abi Habib, J., & Van den Eynde, B. J.
Affiliations: Ludwig Cancer Research (BE)
Corresponding author: Vigneron, Nathalie
ORCID: Vigneron, Nathalie
Venue: Trends in Cancer
Publisher: Elsevier BV
Published: 2017-10
Volume: 3
Issue: 10
Pages: 726-741
ISSN: 2405-8025 (ISSN-L)
2405-8033
DOI: 10.1016/j.trecan.2017.07.007
OpenAlex: W2748923852
Cited by: 33
References: 96
Citations by year: 2025: 2 · 2024: 5 · 2023: 4 · 2022: 8 · 2021: 5 · 2020: 5 · 2019: 1 · 2018: 2 · 2017: 1
FWCI: 0.25
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in cancer (publishedVersion)
PubMed (publishedVersion)
Digital Access to Libraries (submittedVersion)
Funders: Fonds National de la Recherche Scientifique (7455115F)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
Health Sciences › Medicine › Oncology › Cancer Immunotherapy and Biomarkers
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
Keywords: proteasome, cancer immunotherapy, tumor antigens, cytotoxic T lymphocytes, MHC class I, antigen processing, peptide presentation, therapeutic cancer vaccines, tumor specificity
MeSH terms: Animals, Antigens, Neoplasm, HLA Antigens, Humans, Immunotherapy, Neoplasms, T-Lymphocyte Subsets, Antigen Presentation, CD8-Positive T-Lymphocytes, Proteasome Endopeptidase Complex

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Learning from the Proteasome How To Fine-Tune Cancer Immunotherapy

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks