Present yourself! by MHC class I and MHC class II molecules

Neoantigens in cancer immunotherapy

Schumacher, T. N., & Schreiber, R. D. (2015) · Science · doi:10.1126/science.aaa4971 · Cited by 4,783 · see citing works

Genetic Basis for Clinical Response to CTLA-4 Blockade in Melanoma

Snyder, A., Makarov, V., Merghoub, T., Yuan, J., Zaretsky, J. M., Desrichard, A., Walsh, L. A., Postow, M. A., Wong, P., Ho, T. S., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1406498 · Cited by 4,286 · 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

Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules

Falk, K., Rötzschke, O., Stevanovié, S., Jung, G., & Rammensee, H. (1991) · Nature · doi:10.1038/351290a0 · Cited by 2,412 · see citing works

The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens

Bjorkman, P. J., Saper, M. A., Samraoui, B., Bennett, W. S., Strominger, J. L., & Wiley, D. C. (1987) · Nature · doi:10.1038/329512a0 · Cited by 2,377 · see citing works

Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1

Brown, J. H., Jardetzky, T. S., Gorga, J. C., Stern, L. J., Urban, R. G., Strominger, J. L., & Wiley, D. C. (1993) · Nature · doi:10.1038/364033a0 · Cited by 2,377 · see citing works

SYFPEITHI: database for MHC ligands and peptide motifs

Rammensee, H., Bachmann, J., Emmerich, N., Bachor, O. A., & Stevanović, S. (1999) · Immunogenetics · doi:10.1007/s002510050595 · Cited by 2,316 · see citing works

Towards a systems understanding of MHC class I and MHC class II antigen presentation

Neefjes, J., Jongsma, M. L. M., Paul, P., & Bakke, O. (2011) · Nature Reviews Immunology · doi:10.1038/nri3084 · Cited by 2,044 · see citing works

Cross-presentation by dendritic cells

Joffre, O. P., Segura, É., Savina, A., & Amigorena, S. (2012) · Nature reviews. Immunology · doi:10.1038/nri3254 · Cited by 1,646 · see citing works

Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide

Stern, L. J., Brown, J. H., Jardetzky, T. S., Gorga, J. C., Urban, R. G., Strominger, J. L., & Wiley, D. C. (1994) · Nature · doi:10.1038/368215a0 · Cited by 1,556 · see citing works

New insights into cancer immunoediting and its three component phases--elimination, equilibrium and escape

Mittal, D., Gubin, M. M., Schreiber, R. D., & Smyth, M. J. (2014) · Current Opinion in Immunology · doi:10.1016/j.coi.2014.01.004 · Cited by 1,471 · see citing works

Inflammatory stimuli induce accumulation of MHC class II complexes on dendritic cells

Cella, M., Engering, A. J., Pinet, V., Pieters, J., & Lanzavecchia, A. (1997) · Nature · doi:10.1038/42030 · Cited by 1,123 · see citing works

Cross-priming for a secondary cytotoxic response to minor H antigens with H-2 congenic cells which do not cross-react in the cytotoxic assay.

Bevan, M. J. (1976) · The Journal of Experimental Medicine · doi:10.1084/jem.143.5.1283 · Cited by 962 · see citing works

Origin and evolution of the adaptive immune system: genetic events and selective pressures

Flajnik, M. F., & Kasahara, M. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2703 · Cited by 929 · see citing works

A Phagosome-to-Cytosol Pathway for Exogenous Antigens Presented on MHC Class I Molecules

Kovacsovics-Bankowski, M., & Rock, K. L. (1995) · Science · doi:10.1126/science.7809629 · Cited by 884 · see citing works

Viral Strategies of Immune Evasion

Ploegh, H. L. (1998) · Science · doi:10.1126/science.280.5361.248 · Cited by 786 · see citing works

ER–phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells

Guermonprez, P., Saveanu, L., Kleijmeer, M. J., Davoust, J. M., Endert, P. V., & Amigorena, S. (2003) · Nature · doi:10.1038/nature01911 · Cited by 753 · see citing works

Developmental regulation of MHC class II transport in mouse dendritic cells

Pierre, P., Turley, S. J., Gatti, E., Hull, M. J., Meltzer, J., Mirza, A., Inaba, K., Steinman, R. M., & Mellman, I. (1997) · Nature · doi:10.1038/42039 · Cited by 746 · see citing works

HLA-DM induces clip dissociation from MHC class II αβ dimers and facilitates peptide loading

Denzin, L. K., & Cresswell, P. (1995) · Cell · doi:10.1016/0092-8674(95)90061-6 · Cited by 689 · see citing works

The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2

Madden, D. (1993) · Cell · doi:10.1016/0092-8674(93)90490-h · Cited by 676 · see citing works

ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum

Serwold, T. F., Gonzãlez, F., Kim, J. S., Jacob, R. J., & Shastri, N. (2002) · Nature · doi:10.1038/nature01074 · Cited by 631 · see citing works

Defining the Role of the MHC in Autoimmunity: A Review and Pooled Analysis

Fernando, M. M. A., Stevens, C. R., Walsh, E. C., Jager, P. L. D., Goyette, P., Plenge, R. M., Vyse, T. J., & Rioux, J. D. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000024 · Cited by 603 · see citing works

Efficient major histocompatibility complex class I presentation of exogenous antigen upon phagocytosis by macrophages.

Kovacsovics-Bankowski, M., Clark, K., D, B. B. M., & Rock, K. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.4942 · Cited by 590 · see citing works

The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3

Ghosh, P., Amaya, M., Mellins, E., et al. (1995) · Nature · doi:10.1038/378457a0 · Cited by 580 · 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

Decrease in macrophage antigen catabolism caused by ammonia and chloroquine is associated with inhibition of antigen presentation to T cells.

Ziegler, H. K., & Unanue, E. R. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.1.175 · Cited by 570 · see citing works

An IFN-γ–induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I–presented peptides

Šarić, T., Chang, S., Hattori, A., York, I. A., Markant, S. L., Rock, K. L., Tsujimoto, M., & Goldberg, A. L. (2002) · Nature Immunology · doi:10.1038/ni859 · Cited by 532 · see citing works

Quantitating Protein Synthesis, Degradation, and Endogenous Antigen Processing

Princiotta, M. F., Finzi, D., Qian, S.-B., Gibbs, J., Schuchmann, S., Buttgereit, F., Bennink, J. R., & Yewdell, J. W. (2003) · Immunity · doi:10.1016/s1074-7613(03)00051-7 · Cited by 521 · see citing works

The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8–9 residues

York, I. A., Chang, S., Šarić, T., Keys, J. A., Favreau, J., Goldberg, A. L., & Rock, K. L. (2002) · Nature Immunology · doi:10.1038/ni860 · Cited by 514 · see citing works

MHC class I antigens, immune surveillance, and tumor immune escape

Garcia-Lora, A. M., Algarra, I., & Garrido, F. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10290 · Cited by 502 · see citing works

Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum

Saveanu, L., Carroll, O., Lindo, V., Del Val, M., Lopez, D., Lepelletier, Y., Greer, F., Schomburg, L., Fruci, D., Niedermann, G., et al. (2005) · Nature Immunology · doi:10.1038/ni1208 · Cited by 481 · see citing works

Making sense of mass destruction: quantitating MHC class I antigen presentation

Yewdell, J. W., Reits, E. A., & Neefjes, J. (2003) · Nature reviews. Immunology · doi:10.1038/nri1250 · Cited by 447 · see citing works

Cross-presentation by intercellular peptide transfer through gap junctions

Neijssen, J., Herberts, C. A., Drijfhout, J. W., et al. (2005) · Nature · doi:10.1038/nature03290 · Cited by 446 · see citing works

Cross-priming in health and disease

Kurts, C., Robinson, B. W. S., & Knolle, P. A. (2010) · Nature reviews. Immunology · doi:10.1038/nri2780 · Cited by 427 · see citing works

T-cell engagement of dendritic cells rapidly rearranges MHC class II transport

Boes, M. L., Černý, J., Massol, R., den Brouw, M. O., Kirchhausen, T. L., Chen, J., & Ploegh, H. L. (2002) · Nature · doi:10.1038/nature01004 · Cited by 416 · see citing works

The major substrates for TAP in vivo are derived from newly synthesized proteins

Reits, E. A., Vos, J. C., Grommé, M., et al. (2000) · Nature · doi:10.1038/35008103 · Cited by 415 · see citing works

Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro

Schumacher, T. N., Heemels, M.-T., Neefjes, J., Kast, W. M., Melief, C. J. M., & Ploegh, H. L. (1990) · Cell · doi:10.1016/0092-8674(90)90020-f · Cited by 410 · see citing works

Assembly and function of the two ABC transporter proteins encoded in the human major histocompatibility complex

Kelly, A. P., Powis, S. H., Kerr, L. A., Mockridge, I., Elliott, T. J., Bastin, J. M., Uchańska‐Ziegler, B., Ziegler, A., Trowsdale, J., & Townsend, A. (1992) · Nature · doi:10.1038/355641a0 · Cited by 405 · see citing works

Important Role of Cathepsin S in Generating Peptides for TAP-Independent MHC Class I Crosspresentation In Vivo

Shen, L., Sigal, L. J., Boes, M. L., & Rock, K. L. (2004) · Immunity · doi:10.1016/j.immuni.2004.07.004 · Cited by 391 · see citing works

Discrete Cleavage Motifs of Constitutive and Immunoproteasomes Revealed by Quantitative Analysis of Cleavage Products

Toes, R. E. M., Nussbaum, A. K., Degermann, S., Schirle, M., Emmerich, N., Kraft, M., Laplace, C., Zwinderman, A. H., Dick, T. P., Müller, J., et al. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.194.1.1 · Cited by 371 · see citing works

Proteasome inhibition interferes with Gag polyprotein processing, release, and maturation of HIV-1 and HIV-2

Schubert, U., Ott, D. E., Chertova, E. N., Welker, R., Tessmer, U., Princiotta, M. F., Bennink, J. R., Kräusslich, H., & Yewdell, J. W. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.24.13057 · Cited by 339 · see citing works

Presentation of Exogenous Antigen with Class I Major Histocompatibility Complex Molecules

Rock, K. L., Gamble, S., & Rothstein, L. (1990) · Science · doi:10.1126/science.2392683 · Cited by 335 · see citing works

The nature of the MHC class I peptide loading complex

Cresswell, P., Bangia, N., Dick, T. P., & Diedrich, G. (1999) · Immunological Reviews · doi:10.1111/j.1600-065x.1999.tb01353.x · Cited by 332 · see citing works

TLR Signals Induce Phagosomal MHC-I Delivery from the Endosomal Recycling Compartment to Allow Cross-Presentation

Nair-Gupta, P., Baccarini, A., Tung, N., Seyffer, F., Florey, O., Huang, Y., Banerjee, M., Overholtzer, M., Roche, P. A., Tampé, R., et al. (2014) · Cell · doi:10.1016/j.cell.2014.04.054 · Cited by 327 · see citing works

The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a “molecular ruler” mechanism

Chang, S., Momburg, F., Bhutani, N., & Goldberg, A. L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500721102 · Cited by 322 · 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

Genetics of Type 1 Diabetes

Steck, A. K., & Rewers, M. (2011) · Clinical Chemistry · doi:10.1373/clinchem.2010.148221 · Cited by 315 · see citing works

Myelin autoreactivity in multiple sclerosis: recognition of myelin basic protein in the context of HLA-DR2 products by T lymphocytes of multiple-sclerosis patients and healthy donors.

Pette, M., Fujita, K., Wilkinson, D., Altmann, D. M., Trowsdale, J., Giegerich, G., Hinkkanen, A., Epplen, J. T., Kappos, L., & Wekerle, H. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.20.7968 · Cited by 307 · see citing works

Peptide Diffusion, Protection, and Degradation in Nuclear and Cytoplasmic Compartments before Antigen Presentation by MHC Class I

Reits, E. A., Griekspoor, A., Neijssen, J., Groothuis, T. A., Jalink, K., van Veelen, P. A., Janssen, H., Calafat, J., Drijfhout, J. W., & Neefjes, J. (2003) · Immunity · doi:10.1016/s1074-7613(02)00511-3 · Cited by 299 · see citing works

Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer

Dong, G., Wearsch, P. A., Peaper, D. R., Cresswell, P., & Reinisch, K. M. (2009) · Immunity · doi:10.1016/j.immuni.2008.10.018 · Cited by 293 · see citing works

Recycling MHC class I molecules and endosomal peptide loading

Grommé, M., UytdeHaag, F. G. C. M., Janssen, H., Calafat, J., van Binnendijk, R. S., Kenter, M. J. H., Tulp, A., Verwoerd, D., & Neefjes, J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10326 · Cited by 289 · see citing works

Reorganization of multivesicular bodies regulates MHC class II antigen presentation by dendritic cells

Kleijmeer, M. J., Ramm, G., Schuurhuis, D. H., Griffith, J. M., Rescigno, M., Ricciardi‐Castagnoli, P., Rudensky, A. Y., OSSENDORP, F. A., Melief, C. J. M., Stoorvogel, W., et al. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200103071 · Cited by 288 · see citing works

IRAP Identifies an Endosomal Compartment Required for MHC Class I Cross-Presentation

Saveanu, L., Carroll, O., Weimershaus, M., Guermonprez, P., Firat, E., Lindo, V., Greer, F. M., Davoust, J. M., Kratzer, R., Keller, S. R., et al. (2009) · Science · doi:10.1126/science.1172845 · Cited by 273 · see citing works

Defective Antigen Processing in GILT-Free Mice

Marić, M., Arunachalam, B., Phan, U., et al. (2001) · Science · doi:10.1126/science.1065500 · Cited by 272 · see citing works

Variations in MHC Class II Antigen Processing and Presentation in Health and Disease

Unanue, E. R., Türk, V., & Neefjes, J. (2016) · Annual Review of Immunology · doi:10.1146/annurev-immunol-041015-055420 · Cited by 269 · see citing works

Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer

Wearsch, P. A., & Cresswell, P. (2007) · Nature Immunology · doi:10.1038/ni1485 · Cited by 255 · see citing works

Reversible epigenetic down-regulation of MHC molecules by devil facial tumour disease illustrates immune escape by a contagious cancer

Siddle, H. V. T., Kreiss, A., Tovar, C., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1219920110 · Cited by 248 · see citing works

An ER-Associated Pathway Defines Endosomal Architecture for Controlled Cargo Transport

Jongsma, M. L. M., Berlin, I., Wijdeven, R. H. M., Janssen, L., Janssen, G. M. C., Garstka, M. A., Janssen, H., Mensink, M., van Veelen, P. A., Spaapen, R. M., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.078 · Cited by 237 · see citing works

The Evolving Role of Immune Checkpoint Inhibitors in Cancer Treatment

Pennock, G. K., & Chow, L. Q. M. (2015) · The Oncologist · doi:10.1634/theoncologist.2014-0422 · Cited by 236 · see citing works

Negative Regulation by HLA-DO of MHC Class II-Restricted Antigen Processing

Denzin, L. K., Sant’Angelo, D. B., Hammond, C., Surman, M. J., & Cresswell, P. (1997) · Science · doi:10.1126/science.278.5335.106 · Cited by 234 · see citing works

Pool sequencing of natural HLA-DR, DQ, and DP ligands reveals detailed peptide motifs, constraints of processing, and general rules

Falk, K., R�tzschke, O., Stevanov�c, S., Jung, G., & Rammensee, H. (1994) · Immunogenetics · doi:10.1007/bf00188785 · Cited by 228 · see citing works

Allele and locus‐specific differences in cell surface expression and the association of HLA class I heavy chain with β2‐microglobulin: differential effects of inhibition of glycosylation on class I subunit association

Neefjes, J., & Ploegh, H. L. (1988) · European Journal of Immunology · doi:10.1002/eji.1830180522 · Cited by 226 · see citing works

Bacteria-Induced Gap Junctions in Tumors Favor Antigen Cross-Presentation and Antitumor Immunity

Saccheri, F., Pozzi, C., Avogadri, F., Barozzi, S., Faretta, M., Fusi, P. A., & Rescigno, M. (2010) · Science Translational Medicine · doi:10.1126/scitranslmed.3000739 · Cited by 218 · see citing works

Peptide-induced conformational change of the class I heavy chain

Elliott, T. J., Cerundolo, V., Elvin, J. G., et al. (1991) · Nature · doi:10.1038/351402a0 · Cited by 217 · see citing works

Direct vesicular transport of MHC class II molecules from lysosomal structures to the cell surface.

Wubbolts, R., Fernandez‐Borja, M., Oomen, L. C. J. M., Verwoerd, D., Janssen, H., Calafat, J., Tulp, A., Dusseljee, S., & Neefjes, J. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.135.3.611 · Cited by 213 · see citing works

Phosphorylated Peptides Are Naturally Processed and Presented by Major Histocompatibility Complex Class I Molecules in Vivo

Zarling, A. L., Ficarro, S. B., White, F. M., Shabanowitz, J., Hunt, D. F., & Engelhard, V. H. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.12.1755 · Cited by 213 · see citing works

Structural basis for antigenic peptide precursor processing by the endoplasmic reticulum aminopeptidase ERAP1

Nguyen, T. T.-T. N., Chang, S., Evnouchidou, I., York, I. A., Zikos, C. C., Rock, K. L., Goldberg, A. L., Stratikos, E., & Stern, L. J. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2021 · Cited by 202 · see citing works

Dendritic Cells Regulate Exposure of MHC Class II at Their Plasma Membrane by Oligoubiquitination

van Niel, G., Wubbolts, R., ten Broeke, T., Buschow, S. I., OSSENDORP, F. A., Melief, C. J. M., Raposo, G., van Balkom, B. W. M., & Stoorvogel, W. (2006) · Immunity · doi:10.1016/j.immuni.2006.11.001 · Cited by 195 · see citing works

CD4 T cell traffic control:in vivo evidence that ligation of OX40 on CD4 T cells by OX40-ligand expressed on dendritic cells leads to the accumulation of CD4 T cells in B follicles

Brocker, T., Gulbranson‐Judge, A., Flynn, S., Riedinger, M., Raykundalia, C., & Lane, P. J. L. (1999) · European Journal of Immunology · doi:10.1002/(sici)1521-4141(199905)29:05 · Cited by 186 · see citing works

A Single Residue Exchange Within a Viral CTL Epitope Alters Proteasome-Mediated Degradation Resulting in Lack of Antigen Presentation

OSSENDORP, F. A., Eggers, M., Neisig, A., Ruppert, T., Groettrup, M., Sijts, A. J. A. M., Mengedé, E., Kloetzel, P., Neefjes, J., Koszinowski, U. H., et al. (1996) · Immunity · doi:10.1016/s1074-7613(00)80488-4 · Cited by 179 · see citing works

Crystal Structure of the HLA-DM–HLA-DR1 Complex Defines Mechanisms for Rapid Peptide Selection

Pos, W., Sethi, D. K., Call, M. J., Schulze, M. E. D., Anders, A.-K., Pyrdol, J. W., & Wucherpfennig, K. W. (2012) · Cell · doi:10.1016/j.cell.2012.11.025 · Cited by 174 · see citing works

A third interferon‐γ‐induced subunit exchange in the 20S proteasome

Groettrup, M., Kraft, R., Kostka, S., et al. (1996) · European Journal of Immunology · doi:10.1002/eji.1830260421 · Cited by 170 · see citing works

Interleukin‐10‐induced MARCH1 mediates intracellular sequestration of MHC class II in monocytes

Thibodeau, J., Bourgeois‐Daigneault, M., Huppé, G., Tremblay, J., Aumont, A., Houde, M., Bartee, E., Brunet, A., Gauvreau, M., Gassart, A. D., et al. (2008) · European Journal of Immunology · doi:10.1002/eji.200737902 · Cited by 166 · see citing works

HLA‐DO is a lysosomal resident which requires association with HLA‐DM for efficient intracellular transport.

Liljedahl, M., Kuwana, T., Fung‐Leung, W., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00862.x · Cited by 163 · see citing works

HLA-DO is a negative modulator of HLA-DM-mediated MHC class II peptide loading

van Ham, S. M., Tjin, E. P. M., Lillemeier, B. F., et al. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00414-3 · Cited by 163 · see citing works

DRiPs solidify: progress in understanding endogenous MHC class I antigen processing

Yewdell, J. W. (2011) · Trends in Immunology · doi:10.1016/j.it.2011.08.001 · Cited by 161 · see citing works

Bound Water Structure and Polymorphic Amino Acids Act Together to Allow the Binding of Different Peptides to MHC Class I HLA-B53

Smith, K. J., Reid, S. W., Harlos, K., McMichael, A. J., Stuart, D. I., Bell, J. I., & Jones, E. Y. (1996) · Immunity · doi:10.1016/s1074-7613(00)80430-6 · Cited by 159 · see citing works

Phosphorylation-dependent interaction between antigenic peptides and MHC class I: a molecular basis for the presentation of transformed self

Mohammed, F., Cobbold, M., Zarling, A. L., Salim, M., Barrett-Wilt, G. A., Shabanowitz, J., Hunt, D. F., Engelhard, V. H., & Willcox, B. E. (2008) · Nature Immunology · doi:10.1038/ni.1660 · Cited by 155 · see citing works

A Genome-wide Multidimensional RNAi Screen Reveals Pathways Controlling MHC Class II Antigen Presentation

Paul, P., van den Hoorn, T., Jongsma, M. L. M., Bakker, M. J., Hengeveld, R. C. C., Janssen, L., Cresswell, P., Egan, D. A., van Ham, S. M., ten Brinke, A., et al. (2011) · Cell · doi:10.1016/j.cell.2011.03.023 · Cited by 155 · see citing works

NetMHCIIpan-2.0 - Improved pan-specific HLA-DR predictions using a novel concurrent alignment and weight optimization training procedure

Nielsen, M., Justesen, S. F. L., Lund, O., Lundegaard, C., & Buus, S. (2010) · Immunome Research · doi:10.1186/1745-7580-6-9 · Cited by 154 · see citing works

Is Mate Choice in Humans MHC-Dependent?

Chaix, R., Cao, C., & Donnelly, P. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000184 · Cited by 154 · see citing works

Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling.

Roelse, J., Grommé, M., Momburg, F., Hämmerling, G. J., & Neefjes, J. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.180.5.1591 · Cited by 153 · see citing works

The Structure of HLA-DM, the Peptide Exchange Catalyst that Loads Antigen onto Class II MHC Molecules during Antigen Presentation

Mosyak, L., Zaller, D. M., & Wiley, D. C. (1998) · Immunity · doi:10.1016/s1074-7613(00)80620-2 · Cited by 151 · see citing works

A cytosolic pathway for MHC class II–restricted antigen processing that is proteasome and TAP dependent

Tewari, M. K., Sinnathamby, G., Rajagopal, D., & Eisenlohr, L. C. (2005) · Nature Immunology · doi:10.1038/ni1171 · Cited by 149 · see citing works

Discovery of a Potent, Selective, and Orally Active Proteasome Inhibitor for the Treatment of Cancer

Dorsey, B. D., Iqbal, M. A., Chatterjee, S., Menta, E., Bernardini, R., Bernareggi, A., Cassarà, P. G., D’Arasmo, G., Ferretti, E., Munari, S. D., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm7010589 · Cited by 149 · see citing works

Fcγ Receptors and Cross-Presentation in Dendritic Cells

Amigorena, S. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20011925 · Cited by 126 · see citing works

Tapasin-related protein TAPBPR is an additional component of the MHC class I presentation pathway

Boyle, L. H., Hermann, C., Boname, J. M., Porter, K. M., Patel, P. A., Burr, M. L., Duncan, L. M., Harbour, M. E., Rhodes, D. A., Skjødt, K., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222342110 · Cited by 125 · see citing works

HLA-DO acts as a substrate mimic to inhibit HLA-DM by a competitive mechanism

Guce, A. I., Mortimer, S. E., Yoon, T., et al. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2460 · Cited by 121 · see citing works

Celiac disease and transglutaminase 2: a model for posttranslational modification of antigens and HLA association in the pathogenesis of autoimmune disorders

Sollid, L. M., & Jabrì, B. (2011) · Current Opinion in Immunology · doi:10.1016/j.coi.2011.08.006 · Cited by 121 · see citing works

Spatial Separation of HLA-DM/HLA-DR Interactions within MIIC and Phagosome-Induced Immune Escape

Zwart, W. T., Griekspoor, A., Kuijl, C. P., Marsman, M., van Rheenen, J., Janssen, H., Calafat, J., van Ham, S. M., Janssen, L., van Lith, M., et al. (2005) · Immunity · doi:10.1016/j.immuni.2005.01.006 · Cited by 117 · see citing works

Phosphorylated Peptides Can Be Transported by TAP Molecules, Presented by Class I MHC Molecules, and Recognized by Phosphopeptide-Specific CTL

Andersen, M. H., Bonfill, J. E., Neisig, A., Arsequell, G., Søndergaard, I., Neefjes, J., Zeuthen, J., Elliott, T. J., & Haurum, J. S. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.7.3812 · Cited by 117 · see citing works

Cross-Presentation in Mouse and Human Dendritic Cells

Segura, É., & Amigorena, S. (2015) · Advances in immunology · doi:10.1016/bs.ai.2015.03.002 · Cited by 117 · see citing works

The role of CTLA-4 in induction and maintenance of peripheral T cell tolerance

Eagar, T. N., Karandikar, N. J., Bluestone, J. A., & Miller, S. D. (2002) · European Journal of Immunology · doi:10.1002/1521-4141(200204)32:4 · Cited by 108 · see citing works

Presentation of Cytosolic Glycosylated Peptides by Human Class I Major Histocompatibility Complex Molecules in Vivo

Haurum, J. S., Høier, I. B., Arsequell, G., Neisig, A., Valencia, G., Zeuthen, J., Neefjes, J., & Elliott, T. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.1.145 · Cited by 106 · see citing works

THE GENETICS OF PROTEASOMES AND ANTIGEN PROCESSING

Monaco, J. J., & Nandi, D. (1995) · Annual Review of Genetics · doi:10.1146/annurev.ge.29.120195.003501 · Cited by 106 · see citing works

The antigenic landscape of multiple myeloma: mass spectrometry (re)defines targets for T-cell–based immunotherapy

Walz, S., Stickel, J. S., Kowalewski, D. J., Schuster, H., Weisel, K. C., Backert, L., Kahn, S., Nelde, A., Bilich, T., Handel, M., et al. (2015) · Blood · doi:10.1182/blood-2015-04-640532 · Cited by 105 · see citing works

The first step of peptide selection in antigen presentation by MHC class I molecules

Garstka, M. A., Fish, A., Celie, P. H. N., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1416543112 · Cited by 103 · see citing works

Crystal Structure of the Stress-Inducible Human Heat Shock Protein 70 Substrate-Binding Domain in Complex with Peptide Substrate

Zhang, P., Leu, J. I.-J., Murphy, M. E., George, D. L., & Marmorstein, R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103518 · Cited by 99 · see citing works

TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst

Hermann, C., van Hateren, A., Trautwein, N., Neerincx, A., Duriez, P. J., Stevanović, S., Trowsdale, J., Deane, J. E., Elliott, T. J., & Boyle, L. H. (2015) · eLife · doi:10.7554/elife.09617 · Cited by 95 · see citing works

Interaction of TAPBPR, a tapasin homolog, with MHC-I molecules promotes peptide editing

Morozov, G. I., Zhao, H., Mage, M. G., Boyd, L. F., Jiang, J., Dolan, M. A., Venna, R., Norcross, M. A., McMurtrey, C., Hildebrand, W. H., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519894113 · Cited by 95 · see citing works

MHC class I-presented peptides and the DRiP hypothesis

Rock, K., Farfán-Arribas, D. J., Colbert, J. D., & Goldberg, A. (2014) · Trends in immunology · doi:10.1016/j.it.2014.01.002 · Cited by 93 · see citing works

The luminal part of the murine cytomegalovirus glycoprotein gp40 catalyzes the retention of MHC class I molecules

Ziegler, H., Muranyi, W., Burgert, H.-G., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.5.870 · Cited by 92 · see citing works

MHC class I and class II structures

Jones, E. Y. (1997) · Current Opinion in Immunology · doi:10.1016/s0952-7915(97)80162-8 · Cited by 90 · see citing works

Crystal Structure of Mouse H2-M

Fremont, D. H., Crawford, F., Marrack, P., et al. (1998) · Immunity · doi:10.1016/s1074-7613(00)80621-4 · Cited by 88 · see citing works

Post-translationally modified T cell epitopes: immune recognition and immunotherapy

Petersen, J., Purcell, A. W., & Rossjohn, J. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0526-4 · Cited by 82 · see citing works

Lessons from the bare lymphocyte syndrome: molecular mechanisms regulating MHC class II expression

Waldburger, J., Masternak, K., Mühlethaler‐Mottet, A., Villard, J., Peretti, M., LeibundGut‐Landmann, S., & Reith, W. (2000) · Immunological Reviews · doi:10.1034/j.1600-065x.2000.17813.x · Cited by 81 · see citing works

Experimental infections of humans with wild-type adenoviruses and with replication-competent adenovirus vectors: replication, safety, and transmission

Lichtenstein, D. L., & Wold, W. S. M. (2004) · Cancer Gene Therapy · doi:10.1038/sj.cgt.7700765 · Cited by 77 · see citing works

The wide diversity and complexity of peptides bound to class II MHC molecules.

Suri, A., Lovitch, S., & Unanue, E. (2006) · Current Opinion in Immunology · doi:10.1016/j.coi.2005.11.002 · Cited by 75 · see citing works

Targeted regulation of self-peptide presentation prevents type I diabetes in mice without disrupting general immunocompetence.

Yi, W., Seth, N., Martillotti, T., Wucherpfennig, K., Sant'Angelo, D., & Denzin, L. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40220 · Cited by 74 · see citing works

Exclusive expression of proteasome subunit β5t in the human thymic cortex

Tomaru, U., Ishizu, A., Murata, S., Miyatake, Y., Suzuki, S., Takahashi, S., Kazamaki, T., Ohara, J., Baba, T., Iwasaki, S., et al. (2009) · Blood · doi:10.1182/blood-2008-11-187633 · Cited by 70 · see citing works

Inhibition of cell surface MHC class II expression by Salmonella

Mitchell, E., Mastroeni, P., Kelly, A. P., & Trowsdale, J. (2004) · European Journal of Immunology · doi:10.1002/eji.200425314 · Cited by 67 · see citing works

Definition of Proteasomal Peptide Splicing Rules for High-Efficiency Spliced Peptide Presentation by MHC Class I Molecules

Berkers, C. R., de Jong, A., Schuurman, K. G., et al. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402455 · Cited by 67 · see citing works

Characterization of major histocompatibility complex class I and class II genes from the Tasmanian devil (Sarcophilus harrisii)

Siddle, H. V. T., Sanderson, C., & Belov, K. (2007) · Immunogenetics · doi:10.1007/s00251-007-0238-2 · Cited by 63 · see citing works

Cross-presentation by dendritic cells from live cells induces protective immune responses in vivo

Matheoud, D., Perié, L., Hoeffel, G., Vimeux, L., Parent, I., Marañón, C., Bourdoncle, P., Rénia, L., Prévost‐Blondel, A., Lucas, B., et al. (2010) · Blood · doi:10.1182/blood-2009-11-255935 · Cited by 61 · see citing works

Presentation by Recycling MHC Class II Molecules of an Influenza Hemagglutinin-Derived Epitope That Is Revealed in the Early Endosome by Acidification

Sinnathamby, G., & Eisenlohr, L. C. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.7.3504 · Cited by 61 · see citing works

Specialized proteasome subunits have an essential role in the thymic selection of CD8+ T cells

Kincaid, E., Murata, S., Tanaka, K., et al. (2016) · Nature Immunology · doi:10.1038/ni.3480 · Cited by 59 · see citing works

Identification of Natural MHC Class II Presented Phosphopeptides and Tumor-Derived MHC Class I Phospholigands

Meyer, V. S., Drews, O., Günder, M., Hennenlotter, J., Rammensee, H., & Stevanović, S. (2009) · Journal of Proteome Research · doi:10.1021/pr800937k · Cited by 56 · see citing works

Unraveling the Evolution of the Atlantic Cod’s (Gadus morhua L.) Alternative Immune Strategy

Malmstrøm, M., Jentoft, S., Gregers, T. F., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0074004 · Cited by 51 · see citing works

The rational design of TAP inhibitors using peptide substrate modifications and peptidomimetics

Grommé, M., van der Valk, R., Sliedregt, K., et al. (1997) · European Journal of Immunology · doi:10.1002/eji.1830270415 · Cited by 50 · see citing works

Class-switched anti-insulin antibodies originate from unconventional antigen presentation in multiple lymphoid sites

Wan, X., Thomas, J. W., & Unanue, E. R. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20151869 · Cited by 47 · see citing works

The ins-and-outs of endosomal antigens for cross-presentation

Schuette, V., & Burgdorf, S. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2013.11.001 · Cited by 41 · see citing works

Contribution du système immunitaire à l’efficacité des chimiothérapies anticancéreuses

Zitvogel, L., Tesnière, A., Apétoh, L., Ghiringhelli, F., & Kroemer, G. (2008) · Bulletin de l Académie Nationale de Médecine · doi:10.1016/s0001-4079(19)32694-9 · Cited by 39 · see citing works

The Varicellovirus-Encoded TAP Inhibitor UL49.5 Regulates the Presentation of CTL Epitopes by Qa-1b1

van Hall, T., Laban, S., Koppers‐Lalic, D., Koch, J., Precup, C., Asmawidjaja, P. S., Offringa, R., & Wiertz, E. J. H. J. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.2.657 · Cited by 38 · see citing works

Invariant chain–MHC class II complexes: always odd and never invariant

Cresswell, P., & Roche, P. A. (2014) · Immunology and Cell Biology · doi:10.1038/icb.2014.36 · Cited by 26 · see citing works

Alternative Ii-independent antigen-processing pathway in leukemic blasts involves TAP-dependent peptide loading of HLA class II complexes

van Luijn, M. V., Chamuleau, M., Ressing, M., Wiertz, E., Ostrand-Rosenberg, S., Souwer, Y., Zevenbergen, A., Ossenkoppele, G., van de Loosdrecht, A. A., & van Ham, S. M. (2010) · Cancer Immunology and Immunotherapy · doi:10.1007/s00262-010-0908-z · Cited by 18 · see citing works

Correction: Unraveling the Evolution of the Atlantic Cod’s (Gadus morhua L.) Alternative Immune Strategy

̧m, M. M., Jentoft, S., Gregers, T. F., et al. (2013) · PLoS ONE · doi:10.1371/annotation/18b70612-fd3d-46ce-a04b-652d18c82d5b · Cited by 14 · see citing works

Bypassing checkpoints, overcoming resistance, and honing in on new targets

Smit, E. F., & Baas, P. (2015) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2015.223 · Cited by 11 · see citing works

Quantifying how MHC polymorphism prevents pathogens from adapting to the antigen presentation pathway

Schmid, B. V., Keşmir, C., & de Boer, R. J. (2010) · Epidemics · doi:10.1016/j.epidem.2010.05.003 · Cited by 7 · see citing works

Y in X priming

Amigorena, S. (2003) · Nature Immunology · doi:10.1038/ni1103-1047 · Cited by 6 · see citing works

Trafficking and Assembly of MHC Molecules: How Viruses Elude the Immune SystemPreprint

Ploegh, H. L. (1995) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1995.060.01.030 · Cited by 6 · see citing works

COVID-19 vaccines: The status and perspectives in delivery points of view

Chung, J. Y., Thone, M. N., & Kwon, Y. J. (2021) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.12.011 · Cited by 375 · see citing works

Exploring immunotherapy in colorectal cancer

Weng, J., Li, S., Zhu, Z., Liu, Q., Zhang, R., Yang, Y., & Li, X. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01294-4 · Cited by 355 · see citing works

Metal Drugs and the Anticancer Immune Response

Englinger, B., Pirker, C., Heffeter, P., Terenzi, A., Kowol, C. R., Keppler, B. K., & Berger, W. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00396 · Cited by 355 · see citing works

Radiation therapy and anti-tumor immunity: exposing immunogenic mutations to the immune system

Lhuillier, C., Rudqvist, N.-P., Elemento, O., Formenti, S. C., & Demaria, S. (2019) · Genome Medicine · doi:10.1186/s13073-019-0653-7 · Cited by 276 · see citing works

Targeting MHC-I molecules for cancer: function, mechanism, and therapeutic prospects

Wu, X., Li, T., Jiang, R., Yang, X., Guo, H., & Yang, R. (2023) · Molecular Cancer · doi:10.1186/s12943-023-01899-4 · Cited by 223 · see citing works

Technological advances in cancer immunity: from immunogenomics to single‐cell analysis and artificial intelligence

Xu, Y., Su, G.-H., Ma, D., Xiao, Y., Shao, Z.-M., & Jiang, Y.-Z. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00729-7 · Cited by 163 · see citing works

Hydrogel scaffold encapsulating MSC-Exos and ZIF-8 promotes bone regeneration via coordinating osteogenesis and immunomodulation

Si, Y., Li, X., Dong, S., Gao, X., Zhu, Y., Mo, L., Wang, Z., Wang, S., & Zhang, C. (2025) · Bioactive Materials · doi:10.1016/j.bioactmat.2025.08.026 · Cited by 17 · see citing works

Organoid transcriptomics identifies IFIT-associated immune modulation during cryptotanshinone treatment for cancer

Yang, M., Li, S., Li, R., Dong, Y., Zhou, M., Zhao, J., Liu, M., & Tan, R. (2026) · New Biotechnology · doi:10.1016/j.nbt.2026.05.006

Organoid-Based Transcriptomics Indicate IFIT-Associated Immune Modulation during Cryptotanshinone Treatment in Bladder Cancer

Yang, M., Li, R., Dong, Y., Zhou, M., Zhao, J., Liu, M., & Tan, R. (2026) · doi:10.64898/2026.01.28.702456

Principles of MHC class I-mediated antigen presentation and T cell selection.

Ljunggren, H., & Thorpe, C. J. (1996) · PubMed · Cited by 9 · see citing works

Electroporation of exogenous antigen into the cytosol for antigen processing and class I major histocompatibility complex (MHC) presentation: weak base amines and hypothermia (18°C) inhibit the class I MHC processing pathway

Harding, C. V. (1992) · European Journal of Immunology · doi:10.1002/eji.1830220728 · Cited by 37 · see citing works

HLA-DM and the MHC class II antigen presentation pathway

Jensen, P. E., Weber, D. A., Thayer, W. P., et al. (1999) · Immunologic Research · doi:10.1007/bf02790403 · Cited by 47 · see citing works

Intracellular transport of MHC class II molecules

Neefjes, J., & Ploegh, H. L. (1992) · Immunology Today · doi:10.1016/0167-5699(92)90123-o · Cited by 215 · see citing works

Mechanisms of MHC class I‐restricted antigen processing and cross‐presentation

Cresswell, P., Ackerman, A. L., Giodini, A., Peaper, D. R., & Wearsch, P. A. (2005) · Immunological Reviews · doi:10.1111/j.0105-2896.2005.00316.x · Cited by 435 · see citing works