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

Radiation modulates the peptide repertoire, enhances MHC class I expression, and induces successful antitumor immunotherapy

Reits, E. A., Hodge, J. W., Herberts, C. A., Groothuis, T. A., Chakraborty, M., K.Wansley, E., Camphausen, K., Luiten, R. M., de Ru, A. H., Neijssen, J., et al. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20052494 · Cited by 1,737 · see citing works

Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function

Säftig, P., & Klumperman, J. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2745 · Cited by 1,702 · see citing works

Rapid degradation of a large fraction of newly synthesized proteins by proteasomes

Schubert, U., Antón, L. C., Gibbs, J. S., Norbury, C. C., Yewdell, J. W., & Bennink, J. R. (2000) · Nature · doi:10.1038/35008096 · Cited by 1,536 · see citing works

The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins

Raiborg, C., & Stenmark, H. (2009) · Nature · doi:10.1038/nature07961 · Cited by 1,408 · 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

Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility

Evans, D. M., Spencer, C. C. A., Pointon, J. J., Su, Z., Harvey, D., Kochan, G. T., Oppermann, U. C. T., Dilthey, A., Pirinen, M., Stone, M., et al. (2011) · Nature Genetics · doi:10.1038/ng.873 · Cited by 895 · see citing works

AAA+ Proteases: ATP-Fueled Machines of Protein Destruction

Sauer, R. T., & Baker, T. A. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060408-172623 · Cited by 763 · 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

Activation of Lysosomal Function During Dendritic Cell Maturation

Trombetta, E. S., Ebersold, M. W., Garrett, W. S., Pypaert, M., & Mellman, I. (2003) · Science · doi:10.1126/science.1080106 · Cited by 740 · see citing works

Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7–RILP–p150Glued and late endosome positioning

Rocha, N., Kuijl, C. P., van der Kant, R., Janssen, L., Houben, D., Janssen, H., Zwart, W. T., & Neefjes, J. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200811005 · Cited by 705 · see citing works

The known unknowns of antigen processing and presentation

Vyas, J., van der Veen, A. G., & Ploegh, H. (2008) · Nature reviews. Immunology · doi:10.1038/nri2368 · Cited by 703 · see citing works

Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments

Peters, P. J., Neefjes, J., Oorschot, V. M. J., Ploegh, H. L., & Geuze, H. J. (1991) · Nature · doi:10.1038/349669a0 · Cited by 658 · 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

Immunoproteasomes Preserve Protein Homeostasis upon Interferon-Induced Oxidative Stress

Seifert, U., Biały, Ł. P., Ebstein, F., Bech‐Otschir, D., Beling, A., Schröter, F., Prozorovski, T., Lange, N., Steffen, J., Rieger, M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.07.036 · Cited by 554 · 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

Expression of MHC class II molecules in different cellular and functional compartments is controlled by differential usage of multiple promoters of the transactivator CIITA

Mühlethaler‐Mottet, A., Otten, L., Steimle, V., & Mach, B. (1997) · The EMBO Journal · doi:10.1093/emboj/16.10.2851 · Cited by 507 · 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

Widespread RNA and DNA Sequence Differences in the Human Transcriptome

Li, M., Wang, I. X., Li, Y., Bruzel, A., Richards, A. L., Toung, J. M., & Cheung, V. G. (2011) · Science · doi:10.1126/science.1207018 · Cited by 463 · see citing works

Regulation of MHC class II gene expression by the class II transactivator

Reith, W., LeibundGut‐Landmann, S., & Waldburger, J. (2005) · Nature reviews. Immunology · doi:10.1038/nri1708 · Cited by 463 · 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

The biosynthetic pathway of MHC class II but not class I molecules intersects the endocytic route

Neefjes, J., Stollorz, V., Peters, P. J., Geuze, H. J., & Ploegh, H. L. (1990) · Cell · doi:10.1016/0092-8674(90)90224-3 · Cited by 440 · 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

The CD19/CD21 signal transducing complex of human B lymphocytes includes the target of antiproliferative antibody-1 and Leu-13 molecules

Bradbury, L. E., Kansas, G. S., Levy, S., et al. (1992) · The Journal of Immunology · doi:10.4049/jimmunol.149.9.2841 · Cited by 407 · see citing works

Mice lacking the MHC class II-associated invariant chain

Viville, S., Neefjes, J., Lotteau, V., Dierich, A., LeMeur, M., Ploegh, H. L., Benoist, C. O., & Mathis, D. J. (1993) · Cell · doi:10.1016/0092-8674(93)90081-z · Cited by 374 · 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

Modeling the MHC class I pathway by combining predictions of proteasomal cleavage,TAP transport and MHC class I binding

Tenzer, S., Peters, B., Bulik, S., Schoor, O., Lemmel, C., Schatz, M., Kloetzel, P. M., Rammensee, H., Schild, H., & Holzhütter, H. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-4528-2 · Cited by 350 · see citing works

The lysosomal cysteine proteases in MHC class II antigen presentation

Hsing, L. C., & Rudensky, A. Y. (2005) · Immunological Reviews · doi:10.1111/j.0105-2896.2005.00310.x · Cited by 349 · see citing works

Innate immune and chemically triggered oxidative stress modifies translational fidelity

Netzer, N., Goodenbour, J. M., David, A., Dittmar, K. A., Jones, R. B., Schneider, J. R., Boone, D. L., Eves, E. M., Rosner, M. R., Gibbs, J. S., et al. (2009) · Nature · doi:10.1038/nature08576 · Cited by 349 · see citing works

Protein degradation and the generation of MHC class I-presented peptides

Rock, K. L., York, I. A., Šarić, T., & Goldberg, A. L. (2002) · Advances in immunology · doi:10.1016/s0065-2776(02)80012-8 · Cited by 337 · 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

26S proteasomes and immunoproteasomes produce mainly N‐extended versions of an antigenic peptide

Cascio, P., Hilton, C., Kisselev, A. F., Rock, K. L., & Goldberg, A. L. (2001) · The EMBO Journal · doi:10.1093/emboj/20.10.2357 · Cited by 330 · 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

Defective major histocompatibility complex class II assembly, transport, peptide acquisition, and CD4+ T cell selection in mice lacking invariant chain expression.

Bikoff, E. K., Huang, L., Episkopou, V., et al. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.177.6.1699 · Cited by 327 · see citing works

Differential microRNA regulation of HLA-C expression and its association with HIV control

Kulkarni, S., Savan, R., Qi, Y., Gao, X., Yuki, Y., Bass, S. E., Martin, M. P., Hunt, P. W., Deeks, S. G., Telenti, A., et al. (2011) · Nature · doi:10.1038/nature09914 · Cited by 325 · see citing works

Downregulation of Major Histocompatibility Complex Class I by Human Ubiquitin Ligases Related to Viral Immune Evasion Proteins

Bartee, E., Mansouri, M., Nerenberg, B. T. H., Gouveia, K., & Früh, K. (2004) · Journal of Virology · doi:10.1128/jvi.78.3.1109-1120.2004 · Cited by 325 · 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

Interleukin-10 Down-Regulates MHC Class II αβ Peptide Complexes at the Plasma Membrane of Monocytes by Affecting Arrival and Recycling

Koppelman, B., Neefjes, J., de Vries, J. E., & Malefyt, R. D. W. (1997) · Immunity · doi:10.1016/s1074-7613(00)80404-5 · 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

Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome

Hughes, E., Hammond, C., & Cresswell, P. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.5.1896 · Cited by 299 · 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

The role of the proteasome in the generation of MHC class I ligands and immune responses

Sijts, A. J. A. M., & Kloetzel, P. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0657-y · Cited by 286 · see citing works

Editing of the HLA‐DR‐peptide repertoire by HLA‐DM.

Kropshofer, H., Vogt, A. B., Moldenhauer, G., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01002.x · Cited by 274 · see citing works

Protein targeting and degradation are coupled for elimination of mislocalized proteins

Hessa, T., Sharma, A., Mariappan, M., Eshleman, H. D., Gutierrez, E., & Hegde, R. S. (2011) · Nature · doi:10.1038/nature10181 · Cited by 272 · see citing works

Antigen presentation by interferon-gamma-treated endothelial cells and fibroblasts: differential ability to function as antigen-presenting cells despite comparable Ia expression.

Geppert, T. D., & Lipsky, P. E. (1985) · The Journal of Immunology · doi:10.4049/jimmunol.135.6.3750 · Cited by 271 · see citing works

Surface expression of MHC class II in dendritic cells is controlled by regulated ubiquitination

Shin, J., Ebersold, M. W., Pypaert, M., Delamarre, L., Hartley, A., & Mellman, I. (2006) · Nature · doi:10.1038/nature05261 · Cited by 262 · see citing works

A Major Role for TPPII in Trimming Proteasomal Degradation Products for MHC Class I Antigen Presentation

Reits, E. A., Neijssen, J., Herberts, C. A., Benckhuijsen, W. E., Janssen, L., Drijfhout, J. W., & Neefjes, J. (2004) · Immunity · doi:10.1016/s1074-7613(04)00074-3 · Cited by 261 · see citing works

Intracellular MHC class II molecules promote TLR-triggered innate immune responses by maintaining activation of the kinase Btk

Liu, X., Zhan, Z., Li, D., Xu, L., Ma, F., Zhang, P., Yao, H., & Cao, X. (2011) · Nature Immunology · doi:10.1038/ni.2015 · Cited by 261 · see citing works

MHC class II stabilization at the surface of human dendritic cells is the result of maturation-dependent MARCH I down-regulation

Gassart, A. D., Camosseto, V., Thibodeau, J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708874105 · Cited by 259 · see citing works

MHC Class II Engagement by Its Ligand LAG-3 (CD223) Contributes to Melanoma Resistance to Apoptosis

Hémon, P., Jean‐Louis, F., Ramgolam, K., Brignone, C., Viguier, M. A., Bachelez, H., Triebel, F., Charron, D. J., Aoudjit, F., Al‐Daccak, R., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002050 · Cited by 253 · see citing works

HLA-B27–Restricted Antigen Presentation in the Absence of Tapasin Reveals Polymorphism in Mechanisms of HLA Class I Peptide Loading

Peh, C. A., Burrows, S. R., Barnden, M., Khanna, R., Cresswell, P., Moss, D. J., & McCluskey, J. (1998) · Immunity · doi:10.1016/s1074-7613(00)80558-0 · Cited by 252 · see citing works

Two new proteases in the MHC class I processing pathway

Stoltze, L., Schirle, M., Schwarz, G., et al. (2000) · Nature Immunology · doi:10.1038/80852 · Cited by 251 · see citing works

Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII

Kloetzel, P. M. (2004) · Nature Immunology · doi:10.1038/ni1090 · Cited by 243 · see citing works

Accumulation of HLA-DM, a regulator of antigen presentation, in MHC class II compartments

Sanderson, F., Kleijmeer, M. J., Kelly, A. P., Verwoerd, D., Tulp, A., Neefjes, J., Geuze, H. J., & Trowsdale, J. (1994) · Science · doi:10.1126/science.7985027 · Cited by 242 · see citing works

CD83 increases MHC II and CD86 on dendritic cells by opposing IL-10–driven MARCH1-mediated ubiquitination and degradation

Tze, L. E., Horikawa, K., Domaschenz, H., Howard, D. R., Roots, C. M., Rigby, R. J., Way, D. A., Ohmura‐Hoshino, M., Ishido, S., Andoniou, C. E., et al. (2011) · The Journal of Experimental Medicine · doi:10.1084/jem.20092203 · Cited by 232 · 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

Regulation of MHC Class II Expression and Antigen Processing in Murine and Human Mesenchymal Stromal Cells by IFN-γ, TGF-β, and Cell Density

Romieu, R., François, M., Boivin, M., Stagg, J., & Galipeau, J. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.3.1549 · Cited by 221 · see citing works

In the absence of aminopeptidase ERAAP, MHC class I molecules present many unstable and highly immunogenic peptides

Hammer, G. E., Gonzãlez, F., James, E., Nolla, H. A., & Shastri, N. (2006) · Nature Immunology · doi:10.1038/ni1409 · Cited by 219 · 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

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

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

The quality control of MHC class I peptide loading

Wearsch, P. A., & Cresswell, P. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.09.005 · Cited by 203 · 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

Additive Contribution of HLA Class I Alleles in the Immune Control of HIV-1 Infection

Leslie, A. J., Matthews, P. C., Listgarten, J., et al. (2010) · Journal of Virology · doi:10.1128/jvi.00320-10 · Cited by 187 · see citing works

Allele-specific differences in the interaction of MHC class I molecules with transporters associated with antigen processing

Neisig, A., Wubbolts, R., Zang, X., et al. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.156.9.3196 · Cited by 170 · see citing works

Major source of antigenic peptides for the MHC class I pathway is produced during the pioneer round of mRNA translation

Apcher, S., Daskalogianni, C., Lejeune, F., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1104104108 · Cited by 169 · 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

MHC class II expression by the gut epithelium

Bland, P. W. (1988) · Immunology Today · doi:10.1016/0167-5699(88)91293-5 · Cited by 164 · see citing works

Redox Regulation Facilitates Optimal Peptide Selection by MHC Class I during Antigen Processing

Park, B., Lee, S., Kim, E., et al. (2006) · Cell · doi:10.1016/j.cell.2006.08.041 · Cited by 157 · see citing works

The Cytosolic Endopeptidase, Thimet Oligopeptidase, Destroys Antigenic Peptides and Limits the Extent of MHC Class I Antigen Presentation

York, I. A., Mo, A. X. Y., Lemerise, K., Zeng, W., Shen, Y., Abraham, C. R., Šarić, T., Goldberg, A. L., & Rock, K. L. (2003) · Immunity · doi:10.1016/s1074-7613(03)00058-x · 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

Export of Antigenic Peptides from the Endoplasmic Reticulum Intersects with Retrograde Protein Translocation through the Sec61p Channel

Koopmann, J., Albring, J. C., Huter, E. N., Bulbuc, N., Spee, P., Neefjes, J., Hämmerling, G. J., & Momburg, F. (2000) · Immunity · doi:10.1016/s1074-7613(00)00013-3 · Cited by 153 · 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

Differences in the risk of celiac disease associated with HLA-DQ2.5 or HLA-DQ2.2 are related to sustained gluten antigen presentation

Fallang, L.-E., Bergseng, E., Hotta, K., et al. (2009) · Nature Immunology · doi:10.1038/ni.1780 · Cited by 152 · 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

MHC class II signaling in antigen-presenting cells

Al‐Daccak, R., Mooney, N., & Charron, D. J. (2003) · Current Opinion in Immunology · doi:10.1016/j.coi.2003.11.006 · Cited by 148 · see citing works

Autophagy and adaptive immunity

Crotzer, V. L., & Blum, J. (2010) · Immunology · doi:10.1111/j.1365-2567.2010.03321.x · Cited by 145 · see citing works

Therapeutic vaccination against human papilloma virus induced malignancies

van der Burg, S. H., & Melief, C. J. M. (2011) · Current Opinion in Immunology · doi:10.1016/j.coi.2010.12.010 · Cited by 131 · see citing works

Involvement of clathrin and AP-2 in the trafficking of MHC class II molecules to antigen-processing compartments

McCormick, P. J., Martina, J. A., & Bonifacino, J. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502206102 · Cited by 131 · see citing works

Major histocompatibility complex class I binding predictions as a tool in epitope discovery

Lundegaard, C., Lund, O., Buus, S., & Nielsen, M. (2010) · Immunology · doi:10.1111/j.1365-2567.2010.03300.x · Cited by 128 · see citing works

Efficient Internalization of MHC I Requires Lysine‐11 and Lysine‐63 Mixed Linkage Polyubiquitin Chains

Boname, J. M., Thomas, M., Stagg, H. R., Xu, P., Peng, J., & Lehner, P. J. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.01011.x · Cited by 128 · 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

Reduced Cell Surface Expression of HLA-C Molecules Correlates with Restricted Peptide Binding and Stable TAP Interaction

Neisig, A., Melief, C. J. M., & Neefjes, J. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.1.171 · Cited by 126 · see citing works

A Caspase-Independent Pathway of MHC Class II Antigen-Mediated Apoptosis of Human B Lymphocytes

Drénou, B., Blancheteau, V., Burgess, D. H., et al. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.8.4115 · Cited by 119 · see citing works

ABC proteins in antigen translocation and viral inhibition

Parcej, D. N., & Tampé, R. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.410 · Cited by 119 · see citing works

Diversity of Endogenous Epitopes Bound to MHC Class II Molecules Limited by Invariant Chain

Bodmer, H. C., Viville, S., Benoist, C. O., et al. (1994) · Science · doi:10.1126/science.7510069 · Cited by 117 · 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

The actin-based motor protein myosin II regulates MHC class II trafficking and BCR-driven antigen presentation

Vascotto, F., Lankar, D., Faure-André, G., Vargas, P., Diaz, J., Roux, D. L., Yuseff, M.-I., Sibarita, J., Boes, M. L., Raposo, G., et al. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611147 · Cited by 115 · see citing works

Ubiquitination regulates MHC class II-peptide complex retention and degradation in dendritic cells

Walseng, E., Furuta, K., Bosch, B., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010990107 · Cited by 113 · see citing works

Tapasin Is a Facilitator, Not an Editor, of Class I MHC Peptide Binding

Zarling, A. L., Luckey, C. J., Marto, J. A., et al. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.10.5287 · Cited by 111 · see citing works

The low-affinity receptor for IgE (CD23) on B lymphocytes is spatially associated with HLA-DR antigens.

Bonnefoy, J. Y., Guillot, O., Spits, H., et al. (1988) · The Journal of Experimental Medicine · doi:10.1084/jem.167.1.57 · Cited by 110 · see citing works

TCR-Induced Transmembrane Signaling by Peptide/MHC Class II Via Associated Ig-α/β Dimers

Lang, P., Stolpa, J. C., Freiberg, B. A., et al. (2001) · Science · doi:10.1126/science.291.5508.1537 · Cited by 109 · see citing works

Antigen processing by nardilysin and thimet oligopeptidase generates cytotoxic T cell epitopes

Kessler, J. H., Khan, S., Seifert, U., Gall, S. L., Chow, K. M., Paschen, A., Bres-Vloemans, S. A., de Ru, A., van Montfoort, N., Franken, K. L. M. C., et al. (2010) · Nature Immunology · doi:10.1038/ni.1974 · Cited by 109 · see citing works

Enhancement of CIITA transcriptional function by ubiquitin

Greer, S. F., Zika, E., Conti, B. J., Zhu, X.-S., & Ting, J. P.-Y. (2003) · Nature Immunology · doi:10.1038/ni985 · Cited by 105 · see citing works

AP2 Clathrin Adaptor Complex, but Not AP1, Controls the Access of the Major Histocompatibility Complex (MHC) Class II to Endosomes

Dugast, M., Toussaint, H., Dousset, C., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501357200 · Cited by 105 · see citing works

Regulation of major histocompatibility complex class II genes

Choi, N. M., Majumder, P., & Boss, J. M. (2010) · Current Opinion in Immunology · doi:10.1016/j.coi.2010.09.007 · Cited by 105 · see citing works

The Leucine-based Sorting Motifs in the Cytoplasmic Domain of the Invariant Chain Are Recognized by the Clathrin Adaptors AP1 and AP2 and their Medium Chains

Hofmann, M. W., Höning, S., Rodionov, D., Dobberstein, B., FIGURA, K. V., & Bakke, O. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.51.36153 · Cited by 103 · see citing works

Viral evasion of T cell immunity: ancient mechanisms offering new applications.

Horst, D., Verweij, M., Davison, A., Ressing, M., & Wiertz, E. (2011) · Current Opinion in Immunology · doi:10.1016/j.coi.2010.11.005 · Cited by 102 · see citing works

HLA-DM captures partially empty HLA-DR molecules for catalyzed removal of peptide

Anders, A.-K., Call, M. J., Schulze, M. E. D., et al. (2010) · Nature Immunology · doi:10.1038/ni.1967 · Cited by 102 · see citing works

Cutting Edge: Neosynthesis Is Required for the Presentation of a T Cell Epitope from a Long-Lived Viral Protein

Khan, S., de Giuli, R., Schmidtke, G., et al. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.9.4801 · Cited by 102 · see citing works

Endoplasmic Reticulum Aminopeptidase Associated with Antigen Processing Defines the Composition and Structure of MHC Class I Peptide Repertoire in Normal and Virus-Infected Cells

Blanchard, N., Kanaseki, T., Escobar, H., Delebecque, F., Nagarajan, N. A., Reyes‐Vargas, E., Crockett, D. K., Raulet, D. H., Delgado, J. C., & Shastri, N. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903712 · Cited by 99 · see citing works

Essential glycan-dependent interactions optimize MHC class I peptide loading

Wearsch, P. A., Peaper, D. R., & Cresswell, P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102524108 · Cited by 99 · see citing works

Calreticulin‐dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules

Howe, C. M., Garstka, M. A., Al-Balushi, M. S., Ghanem, E., Antoniou, A. N., Fritzsche, S., Jankevicius, G., Kontouli, N., Schneeweiß, C., Williams, A. P., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.296 · Cited by 97 · see citing works

Accessory molecules for MHC class II peptide loading

Busch, R., Doebele, R. C., Patil, N. S., Pashine, A., & Mellins, E. (2000) · Current Opinion in Immunology · doi:10.1016/s0952-7915(99)00057-6 · Cited by 96 · see citing works

Association of distinct tetraspanins with MHC class II molecules at different subcellular locations in human immature dendritic cells

Engering, A. J., & Pieters, J. (2001) · International Immunology · doi:10.1093/intimm/13.2.127 · Cited by 96 · see citing works

Tripeptidyl Peptidase II Is the Major Peptidase Needed to Trim Long Antigenic Precursors, but Is Not Required for Most MHC Class I Antigen Presentation

York, I. A., Bhutani, N., Zendzian, S., Goldberg, A. L., & Rock, K. L. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.3.1434 · Cited by 95 · see citing works

Antigen Presentation and MHC Class II Expression by Human Esophageal Epithelial Cells

Mulder, D. J., Pooni, A., Mak, N., et al. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.10.027 · Cited by 89 · see citing works

MHC II and the Endocytic Pathway: Regulation by Invariant Chain

Landsverk, O. J. B., Bakke, O., & Gregers, T. F. (2009) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.2009.02301.x · Cited by 88 · see citing works

Statins Affect Cell-Surface Expression of Major Histocompatibility Complex Class II Molecules by Disrupting Cholesterol-Containing Microdomains

Kuipers, H. F., Biesta, P. J., Groothuis, T. A., Neefjes, J., Mommaas, A. M., & van den Elsen, P. J. (2005) · Human Immunology · doi:10.1016/j.humimm.2005.04.004 · Cited by 87 · see citing works

Puromycin‐sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation

Bhutani, N., Venkatraman, P., & Goldberg, A. L. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601592 · Cited by 87 · see citing works

HLA genomics in the third millennium

Trowsdale, J. (2005) · Current Opinion in Immunology · doi:10.1016/j.coi.2005.07.015 · Cited by 79 · see citing works

Involvement of caspase-cleaved and intact adaptor protein 1 complex in endosomal remodeling in maturing dendritic cells

Santambrogio, L., Potolicchio, I., Fessler, S. P., et al. (2005) · Nature Immunology · doi:10.1038/ni1250 · Cited by 78 · see citing works

A Universal Approach to Eliminate Antigenic Properties of Alpha-Gliadin Peptides in Celiac Disease

Mitea, C., Salentijn, E. M. J., van Veelen, P. A., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015637 · Cited by 78 · see citing works

Therapeutic dosing of an orally active, selective cathepsin S inhibitor suppresses disease in models of autoimmunity

Baugh, M. D., Black, D., Westwood, P., et al. (2011) · Journal of Autoimmunity · doi:10.1016/j.jaut.2011.01.003 · Cited by 75 · see citing works

Right place, right time, right peptide: DO keeps DM focused

Denzin, L. K., Fallas, J. L., Prendes, M. J., & Yi, W. (2005) · Immunological Reviews · doi:10.1111/j.0105-2896.2005.00302.x · Cited by 73 · see citing works

Upregulation of cathepsin S in psoriatic keratinocytes

Schönefuß, A., Wendt, W., Schattling, B., Schulten, R., Hoffmann, K. H., Stüecker, M., Tigges, C., Lübbert, H., & Stichel, C. C. (2009) · Experimental Dermatology · doi:10.1111/j.1600-0625.2009.00990.x · Cited by 71 · see citing works

Direct Antigen Presentation and Gap Junction Mediated Cross-Presentation during Apoptosis

Pang, B., Neijssen, J., Qiao, X., Janssen, L., Janssen, H., Lippuner, C., & Neefjes, J. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900861 · Cited by 71 · see citing works

Compartmentalized MHC class I antigen processing enhances immunosurveillance by circumventing the law of mass action

Lev, A., Princiotta, M. F., Zanker, D. J., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910997107 · Cited by 65 · see citing works

A reductionist cell-free major histocompatibility complex class II antigen processing system identifies immunodominant epitopes

Hartman, I. Z., Kim, A., Cotter, R. J., et al. (2010) · Nature Medicine · doi:10.1038/nm.2248 · Cited by 65 · see citing works

The Exception that Reinforces the Rule: Crosspriming by Cytosolic Peptides that Escape Degradation

Lev, A., Takeda, K., Zanker, D. J., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.04.015 · Cited by 64 · see citing works

Distinct Pathways Generate Peptides from Defective Ribosomal Products for CD8+ T Cell Immunosurveillance

Dolan, B. P., Li, L., Veltri, C. A., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003096 · Cited by 63 · see citing works

Positive Regulatory Domain I (PRDM1) and IRF8/PU.1 Counter-regulate MHC Class II Transactivator (CIITA) Expression during Dendritic Cell Maturation

Smith, M. A., Wright, G. M., Wu, J., Tailor, P. B., Ozato, K., Chen, X., Wei, S., Piskurich, J. F., Ting, J. P. ‐., & Wright, K. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.165431 · Cited by 63 · see citing works

Production of an antigenic peptide by insulin-degrading enzyme

Parmentier, N., Stroobant, V., Colau, D., de Diesbach, P., Morel, S., Chapiro, J., Endert, P. V., & den Eynde, B. J. V. (2010) · Nature Immunology · doi:10.1038/ni.1862 · Cited by 63 · see citing works

LAMP‐2‐deficient human B cells exhibit altered MHC class II presentation of exogenous antigens

Crotzer, V. L., Glosson, N. L., Zhou, D., et al. (2010) · Immunology · doi:10.1111/j.1365-2567.2010.03309.x · Cited by 60 · see citing works

Combining radiation and immunotherapy for synergistic antitumor therapy.

Ferrara, T. A., Hodge, J. W., & Gulley, J. L. (2009) · PubMed · Cited by 57 · see citing works

Complexity, contradictions, and conundrums: studying post‐proteasomal proteolysis in HLA class I antigen presentation

Saveanu, L., Carroll, O., Hassainya, Y., & Endert, P. V. (2005) · Immunological Reviews · doi:10.1111/j.0105-2896.2005.00313.x · Cited by 56 · see citing works

Cutting Edge: MHC Class II Expression by Pulmonary Nonhematopoietic Cells Plays a Critical Role in Controlling Local Inflammatory Responses

Kreisel, D., Richardson, S. B., Li, W., Lin, X., Kornfeld, C. G., Sugimoto, S., Hsieh, C., Gelman, A. E., & Krupnick, A. S. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000971 · Cited by 55 · see citing works

Regulation of cell-surface major histocompatibility complex class I expression by the endopeptidase EC3.4.24.15 (thimet oligopeptidase)

Kim, S. I., Pabon, A., Swanson, T. A., et al. (2003) · Biochemical Journal · doi:10.1042/bj20030490 · Cited by 53 · see citing works

The MHC class II-associated invariant chain: a molecule with multiple roles in MHC class II biosynthesis and antigen presentation to CD4+ T cells.

Bertolino, P., & Rabourdin-Combe, C. (1996) · PubMed · Cited by 52 · see citing works

Viral Alteration of Cellular Translational Machinery Increases Defective Ribosomal Products

Berglund, P., Finzi, D., Bennink, J. R., et al. (2007) · Journal of Virology · doi:10.1128/jvi.00137-07 · Cited by 51 · see citing works

Expression of Angiotensin-converting Enzyme Changes Major Histocompatibility Complex Class I Peptide Presentation by Modifying C Termini of Peptide Precursors

Shen, X. Z., Lukacher, A. E., Billet, S., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709574200 · Cited by 50 · see citing works

Insights into MHC class I antigen processing gained from large-scale analysis of class I ligands

Mester, G., Hoffmann, V., & Stevanović, S. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0659-9 · Cited by 47 · see citing works

The Cytoplasmic Tail of Invariant Chain Regulates Endosome Fusion and Morphology

Nordeng, T. W., Gregers, T. F., Kongsvik, T. L., Méresse, S., Gorvel, J., Jourdan, F. L., Motta, A., & Bakke, O. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-10-0478 · Cited by 45 · see citing works

Phosphorylation of class II transactivator regulates its interaction ability and transactivation function

Sisk, T. J. (2003) · International Immunology · doi:10.1093/intimm/dxg116 · Cited by 44 · see citing works

The fate of the three subunits of major histocompatibility complex class I molecules

Neefjes, J., Smit, L., Gehrmann, M., et al. (1992) · European Journal of Immunology · doi:10.1002/eji.1830220639 · Cited by 43 · see citing works

Cutting Edge: HLA-B27 Acquires Many N-Terminal Dibasic Peptides: Coupling Cytosolic Peptide Stability to Antigen Presentation

Herberts, C. A., Neijssen, J., de Haan, J., et al. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.5.2697 · Cited by 42 · see citing works

Analysis of the Role of Tripeptidyl Peptidase II in MHC Class I Antigen Presentation In Vivo

Kawahara, M., York, I. A., Hearn, A. R., Farfán-Arribas, D. J., & Rock, K. L. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803564 · Cited by 41 · see citing works

Uniquely Conformed Peptide-Containing β2-Microglobulin- Free Heavy Chains of HLA-B2705 on the Cell Surface

Malik, P., Klimovitsky, P., Deng, L., et al. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.8.4379 · Cited by 39 · see citing works

Serine Residues 286, 288, and 293 within the CIITA: A Mechanism for Down-Regulating CIITA Activity through Phosphorylation

Greer, S. F., Harton, J. A., Linhoff, M. W., Janczak, C. A., Ting, J. P. ‐., & Cressman, D. E. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.1.376 · Cited by 35 · see citing works

Both treated and untreated tumors are eliminated by short hairpin RNA-based induction of target-specific immune responses

Gu, W., Cochrane, M., Leggatt, G. R., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812085106 · Cited by 31 · see citing works

Invariant chain increases the half‐life of MHC II by delaying endosomal maturation

Landsverk, O. J. B., Barois, N., Gregers, T. F., & Bakke, O. (2010) · Immunology and Cell Biology · doi:10.1038/icb.2010.143 · Cited by 29 · see citing works

Anti-Ia-reactive cells in mycosis fungoides: a study of skin biopsies, single epidermal cells and circulating T lymphocytes

Tjernlund, U., Scheynius, A., Kabelitz, D., et al. (1981) · Acta Dermato Venereologica · doi:10.2340/0001555561291301 · Cited by 29 · see citing works

Phosphorylation and Ubiquitination of Degron Proximal Residues Are Essential for Class II Transactivator (CIITA) Transactivation and Major Histocompatibility Class II Expression

Bhat, K. P., Truax, A. D., & Greer, S. F. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.127746 · Cited by 28 · see citing works

Endosomally Stored MHC Class II Does Not Contribute to Antigen Presentation by Dendritic Cells at Inflammatory Conditions

ten Broeke, T., van Niel, G., Wauben, M. H. M., et al. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01212.x · Cited by 22 · see citing works

Ubiquitin-Dependent Control of Class II MHC Localization Is Dispensable for Antigen Presentation and Antibody Production

McGehee, A. M., Strijbis, K., Guillén, E., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018817 · Cited by 21 · see citing works

Class I HLA Folding and Antigen Presentation in β2-Microglobulin-Defective Daudi Cells

Martayan, A., Sibilio, L., Tremante, E., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0802316 · Cited by 20 · see citing works

Nardilysin Cleaves Peptides at Monobasic Sites

Chow, K. M., Oakley, O. R., Goodman, J. P., Ma, Z., Juliano, M. A., Juliano, L., & Hersh, L. B. (2003) · Biochemistry · doi:10.1021/bi027178d · Cited by 19 · see citing works

Studies on the Subsite Specificity of Rat Nardilysin (N-Arginine Dibasic Convertase)

Chow, K. M., Csuhai, É., Juliano, M. A., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909020199 · Cited by 19 · see citing works

Presentation of Type B Peptide–MHC Complexes from Hen Egg White Lysozyme by TLR Ligands and Type I IFNs Independent of H2-DM Regulation

Strong, B., & Unanue, E. R. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100152 · Cited by 18 · see citing works

New lane in the information highway: alternative reading frame peptides elicit T cells with potent antiretrovirus activity

Yewdell, J. W., & Hickman, H. D. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20071986 · Cited by 14 · see citing works

Metachromasia of 3-amino-9-ethylcarbazole (AEC) and its prevention in immunoperoxidase techniques

Koretz, K., Leman, J., Brandt, I., et al. (1987) · Histochemistry and Cell Biology · doi:10.1007/bf00500619 · Cited by 13 · see citing works

Localization of the conformational alteration of MHC molecules induced by the association of mouse class I heavy chain with a xenogeneic β2-microglobulin

Rocca, A., Opolski, A., Samaan, A., et al. (1992) · Molecular Immunology · doi:10.1016/0161-5890(92)90005-i · Cited by 10 · see citing works

Molecular definitions of autophagy and related processes

Galluzzi, L., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cecconi, F., Choi, A. M., Chu, C. T., Codogno, P., Colombo, M. I., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796697 · Cited by 1,646 · see citing works

Recent advances in 2D and 3D in vitro systems using primary hepatocytes, alternative hepatocyte sources and non-parenchymal liver cells and their use in investigating mechanisms of hepatotoxicity, cell signaling and ADME

Godoy, P., Hewitt, N. J., Albrecht, U., Andersen, M. E., Ansari, N., Bhattacharya, S., Bode, J. G., Bolleyn, J., Borner, C., Böttger, J., et al. (2013) · Archives of Toxicology · doi:10.1007/s00204-013-1078-5 · Cited by 1,280 · see citing works

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

Rock, K. L., Reits, E., & Neefjes, J. (2016) · Trends in Immunology · doi:10.1016/j.it.2016.08.010 · Cited by 814 · see citing works

Single-nucleus transcriptome analysis reveals dysregulation of angiogenic endothelial cells and neuroprotective glia in Alzheimer’s disease

Lau, S.-F., Cao, H., Fu, A. K. Y., & Ip, N. Y. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2008762117 · Cited by 476 · 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

Evolutionary insights into host–pathogen interactions from mammalian sequence data

Sironi, M., Cagliani, R., Forni, D., & Clerici, M. (2015) · Nature Reviews Genetics · doi:10.1038/nrg3905 · Cited by 302 · see citing works

Emerging roles of innate and adaptive immunity in Alzheimer’s disease

Chen, X., & Holtzman, D. M. (2022) · Immunity · doi:10.1016/j.immuni.2022.10.016 · Cited by 297 · 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

LAG-3 inhibits the activation of CD4+ T cells that recognize stable pMHCII through its conformation-dependent recognition of pMHCII

Maruhashi, T., Okazaki, I.-M., Sugiura, D., Takahashi, S., Maeda, T. K., Shimizu, K., & Okazaki, T. (2018) · Nature Immunology · doi:10.1038/s41590-018-0217-9 · Cited by 275 · see citing works

Prevalence of Pre-existing Antibodies to CRISPR-Associated Nuclease Cas9 in the USA Population

Simhadri, V. L., McGill, J., McMahon, S., Wang, J., Jiang, H., & Sauna, Z. E. (2018) · Molecular Therapy - Methods & Clinical Development · doi:10.1016/j.omtm.2018.06.006 · Cited by 241 · see citing works

Immune checkpoint inhibitor–associated myocarditis: manifestations and mechanisms

Moslehi, J., Lichtman, A. H., Sharpe, A. H., Galluzzi, L., & Kitsis, R. N. (2021) · Journal of Clinical Investigation · doi:10.1172/jci145186 · Cited by 237 · see citing works

Antigen processing and presentation

(2019) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2019.07.005 · Cited by 194 · 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

Immunological Mechanisms Underneath the Efficacy of Cancer Therapy

Galluzzi, L., Zitvogel, L., & Kroemer, G. (2016) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-16-0197 · Cited by 175 · see citing works

Monitoring immune modulation by nutrition in the general population: identifying and substantiating effects on human health

Albers, R., Bourdet-Sicard, R., Braun, D., Calder, P. C., Herz, U., Lambert, C., Lenoir-Wijnkoop, I., Méheust, A., Ouwehand, A., Phothirath, P., et al. (2013) · British Journal of Nutrition · doi:10.1017/s0007114513001505 · Cited by 150 · see citing works

Profiling SARS-CoV-2 HLA-I peptidome reveals T cell epitopes from out-of-frame ORFs

Weingarten-Gabbay, S., Klaeger, S., Sarkizova, S., Pearlman, L. R., Chen, D.-Y., Gallagher, K. M. E., Bauer, M. R., Taylor, H. B., Dunn, W. A., Tarr, C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.05.046 · Cited by 147 · see citing works

Modulation of gastrointestinal barrier and nutrient transport function in farm animals by natural plant bioactive compounds–a comprehensive review

Patra, A. K., Amasheh, S., & Aschenbach, J. R. (2019) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2018.1486284 · Cited by 130 · see citing works

T-cell agonists in cancer immunotherapy

Choi, Y., Shi, Y., Haymaker, C. L., Naing, A., Ciliberto, G., & Hajjar, J. (2020) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2020-000966 · Cited by 119 · see citing works

Interactions between cancer stem cells, immune system and some environmental components: Friends or foes?

Vahidian, F., Duijf, P. H. G., Safarzadeh, E., Derakhshani, A., Baghbanzadeh, A., & Baradaran, B. (2019) · Immunology Letters · doi:10.1016/j.imlet.2019.03.004 · Cited by 75 · see citing works

Polysaccharide A from the capsule of Bacteroides fragilis induces clonal CD4+ T cell expansion

Johnson, J. L., Jones, M. B., & Cobb, B. A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.621771 · Cited by 74 · see citing works

The major histocompatibility complex and autism spectrum disorder

Needleman, L. A., & McAllister, A. K. (2012) · Developmental Neurobiology · doi:10.1002/dneu.22046 · Cited by 66 · see citing works

Dendritic cells as cancer therapeutics

Bryant, C. E., Sutherland, S., Kong, B., Papadimitrious, M. S., Fromm, P. D., & Hart, D. N. J. (2019) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2018.02.015 · Cited by 61 · see citing works

Delivery strategies for CRISPR/Cas genome editing tool for retinal dystrophies: Challenges and opportunities

Lohia, A., Sahel, D. K., Salman, M., Singh, V., Mariappan, I., Mittal, A., & Chitkara, D. (2022) · Asian Journal of Pharmaceutical Sciences · doi:10.1016/j.ajps.2022.02.001 · Cited by 33 · see citing works

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

Molecular Mechanisms of Viral Immune Evasion Proteins to Inhibit MHC Class I Antigen Processing and Presentation

Zhou, F. (2009) · International Reviews of Immunology · doi:10.1080/08830180903013034 · Cited by 16 · 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

The ins and outs of MHC class II-mediated antigen processing and presentation

Roche, P. A., & Furuta, K. (2015) · Nature reviews. Immunology · doi:10.1038/nri3818 · Cited by 1,207 · see citing works

Monitoring Antigen Processing for MHC Presentation via Macroautophagy.

Gannagé, M., Silva, R. D. D., & Münz, C. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9450-2_25 · Cited by 2 · see citing works