Indoleamine 2,3 dioxygenase and metabolic control of immune responses

From inflammation to sickness and depression: when the immune system subjugates the brain

Dantzer, R., O'Connor, J. C., Freund, G. G., Johnson, R. W., & Kelley, K. W. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2297 · Cited by 7,395

Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase

Uyttenhove, C., Pilotte, L., Théate, I., Stroobant, V., Colau, D., Parmentier, N., Boon, T., & Van den Eynde, B. J. (2003) · Nature Medicine · doi:10.1038/nm934 · Cited by 2,305

An endogenous tumour-promoting ligand of the human aryl hydrocarbon receptor

Opitz, C. A., Litzenburger, U. M., Sahm, F., Ott, M., Tritschler, I., Trump, S., Schumacher, T., Jestaedt, L., Schrenk, D., Weller, M., et al. (2011) · Nature · doi:10.1038/nature10491 · Cited by 1,898

An Interaction between Kynurenine and the Aryl Hydrocarbon Receptor Can Generate Regulatory T Cells

Mezrich, J. D., Fechner, J. H., Zhang, X., Johnson, B. P., Burlingham, W. J., & Bradfield, C. A. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903670 · Cited by 1,667

Modulation of tryptophan catabolism by regulatory T cells

Fallarino, F., Grohmann, U., Hwang, K. W., Orabona, C., Vacca, C., Bianchi, R., Belladonna, M. L., Fioretti, M. C., Alegre, M., & Puccetti, P. (2003) · Nature Immunology · doi:10.1038/ni1003 · Cited by 1,375

Coping with stress: eIF2 kinases and translational control

Wek, R. C., Jiang, H.-Y., & Anthony, T. G. (2005) · Biochemical Society Transactions · doi:10.1042/bst0340007 · Cited by 1,353

GCN2 Kinase in T Cells Mediates Proliferative Arrest and Anergy Induction in Response to Indoleamine 2,3-Dioxygenase

Munn, D. H., Sharma, M. D., Baban, B., Harding, H. P., Zhang, Y., Ron, D., & Mellor, A. L. (2005) · Immunity · doi:10.1016/j.immuni.2005.03.013 · Cited by 1,309

The Combined Effects of Tryptophan Starvation and Tryptophan Catabolites Down-Regulate T Cell Receptor ζ-Chain and Induce a Regulatory Phenotype in Naive T Cells

Fallarino, F., Grohmann, U., You, S., McGrath, B. C., Cavener, D. R., Vacca, C., Orabona, C., Bianchi, R., Belladonna, M. L., Volpi, C., et al. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.11.6752 · Cited by 1,078

Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy

Muller, A. J., DuHadaway, J. B., Donover, P. S., Sutanto-Ward, E., & Prendergast, G. C. (2005) · Nature Medicine · doi:10.1038/nm1196 · Cited by 1,064

Relationship between interferon‐γ, indoleamine 2,3‐dioxygenase, and tryptophan catabolism

Taylor, M. W., & Feng, G. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.11.1907934 · Cited by 1,060

L-arginine availability regulates T-lymphocyte cell-cycle progression.

Rodriguez, P. C., Quiceno, D. G., & Ochoa, A. C. (2007) · Blood · doi:10.1182/blood-2006-06-031856 · Cited by 926

Expression of indoleamine 2,3-dioxygenase by plasmacytoid dendritic cells in tumor-draining lymph nodes

Munn, D. H., Sharma, M. D., Hou, D., Baban, B., Lee, J. R., Antonia, S. J., Messina, J. L., Chandler, P., Koni, P. A., & Mellor, A. L. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21583 · Cited by 852

Regulation of Immune Responses by mTOR

Powell, J. D., Pollizzi, K. N., Heikamp, E. B., & Horton, M. R. (2012) · Annual Review of Immunology · doi:10.1146/annurev-immunol-020711-075024 · Cited by 836

Plasmacytoid dendritic cells from mouse tumor-draining lymph nodes directly activate mature Tregs via indoleamine 2,3-dioxygenase

Sharma, M. D., Baban, B., Chandler, P., Hou, D., Singh, N., Yagita∥, H., Azuma, M., Blazar, B. R., Mellor, A. L., & Munn, D. H. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31911 · Cited by 791

Indoleamine 2,3-dioxygenase is a signaling protein in long-term tolerance by dendritic cells

Pallotta, M. T., Orabona, C., Volpi, C., Vacca, C., Belladonna, M. L., Bianchi, R., Servillo, G., Brunacci, C., Calvitti, M., Bicciato, S., et al. (2011) · Nature Immunology · doi:10.1038/ni.2077 · Cited by 737

Aryl hydrocarbon receptor negatively regulates dendritic cell immunogenicity via a kynurenine-dependent mechanism

Nguyen, N. T., Kimura, A., Nakahama, T., Chinen, I., Masuda, K., Nohara, K., Fujii‐Kuriyama, Y., & Kishimoto, T. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014465107 · Cited by 702

Kynurenine Pathway Metabolites in Humans: Disease and Healthy States

Chen, Y., & Guillemin, G. J. (2009) · International Journal of Tryptophan Research · doi:10.4137/ijtr.s2097 · Cited by 642

ATF4-dependent transcription mediates signaling of amino acid limitation

Kilberg, M. S., Shan, J., & Su, N. Y. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.05.008 · Cited by 614

Reversal of tumoral immune resistance by inhibition of tryptophan 2,3-dioxygenase

Pilotte, L., Larrieu, P., Stroobant, V., Colau, D., Dolušić, E., Frédérick, R., Plaen, E. D., Uyttenhove, C., Wouters, J., Masereel, B., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113873109 · Cited by 582

Selective inhibition of IDO1 effectively regulates mediators of antitumor immunity

Liu, X., Shin, N., Koblish, H. K., Yang, G., Wang, Q., Wang, K., Leffet, L., Hansbury, M., Thomas, B. A., Rupar, M. J., et al. (2010) · Blood · doi:10.1182/blood-2009-09-246124 · Cited by 559

Imatinib potentiates antitumor T cell responses in gastrointestinal stromal tumor through the inhibition of Ido

Balachandran, V. P., Cavnar, M. J., Zeng, S., Bamboat, Z. M., Ocuin, L. M., Obaid, H., Sorenson, E. C., Popow, R., Ariyan, C. E., Rossi, F., et al. (2011) · Nature Medicine · doi:10.1038/nm.2438 · Cited by 541

Tryptophan Catabolism by Indoleamine 2,3-Dioxygenase 1 Alters the Balance of T H 17 to Regulatory T Cells in HIV Disease

Favre, D., Mold, J. E., Hunt, P. W., Kanwar, B., Loke, P., Seu, L., Barbour, J. D., Lowe, M. M., Jayawardene, A., Aweeka, F. T., et al. (2010) · Science Translational Medicine · doi:10.1126/scitranslmed.3000632 · Cited by 539

Defective tryptophan catabolism underlies inflammation in mouse chronic granulomatous disease

Romani, L., Fallarino, F., De Luca, A., Montagnoli, C., D’Angelo, C., Zelante, T., Vacca, C., Bistoni, F., Fioretti, M. C., Grohmann, U., et al. (2008) · Nature · doi:10.1038/nature06471 · Cited by 535

A prospective phase II trial exploring the association between tumor microenvironment biomarkers and clinical activity of ipilimumab in advanced melanoma

Hamid, O., Schmidt, H., Nissan, A., Ridolfi, L., Aamdal, S., Hansson, J., Guida, M., Hyams, D. M., Gómez, H., Bastholt, L., et al. (2011) · Journal of Translational Medicine · doi:10.1186/1479-5876-9-204 · Cited by 534

Induction of Lymphoidlike Stroma and Immune Escape by Tumors That Express the Chemokine CCL21

Shields, J. D., Kourtis, I. C., Tomei, A. A., Roberts, J., & Swartz, M. A. (2010) · Science · doi:10.1126/science.1185837 · Cited by 530

Novel Tryptophan Catabolic Enzyme IDO2 Is the Preferred Biochemical Target of the Antitumor Indoleamine 2,3-Dioxygenase Inhibitory Compound d -1-Methyl-Tryptophan

Metz, R. A., DuHadaway, J. B., Kamasani, U. R., Laury‐Kleintop, L. D., Muller, A. J., & Prendergast, G. C. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1872 · Cited by 482

The Indoleamine 2,3-Dioxygenase Pathway Is Essential for Human Plasmacytoid Dendritic Cell-Induced Adaptive T Regulatory Cell Generation

Chen, W., Liang, X., Peterson, A. J., Munn, D. H., & Blazar, B. R. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.8.5396 · Cited by 472

Halofuginone Inhibits T H 17 Cell Differentiation by Activating the Amino Acid Starvation Response

Sundrud, M. S., Koralov, S. B., Feuerer, M., Calado, D. P., Kozhaya, A. E., Rhule-Smith, A., Lefebvre, R. E., Unutmaz, D., Mazitschek, R., Waldner, H., et al. (2009) · Science · doi:10.1126/science.1172638 · Cited by 447

Kynurenine is an endothelium-derived relaxing factor produced during inflammation

Wang, Y., Liu, H., McKenzie, G. A., Witting, P. K., Stasch, J., Hahn, M. G., Changsirivathanathamrong, D., Wu, B. J., Ball, H. J., Thomas, S. R., et al. (2010) · Nature Medicine · doi:10.1038/nm.2092 · Cited by 446

Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice

Ball, H. J., Sánchez-Pérez, Á., Weiser, S., Austin, C., Astelbauer, F., Miu, J., McQuillan, J. A., Stocker, R., Jermiin, L. S., & Hunt, N. H. (2007) · Gene · doi:10.1016/j.gene.2007.04.010 · Cited by 445

Metabolic pathways in T cell fate and function

Gerriets, V. A., & Rathmell, J. C. (2012) · Trends in Immunology · doi:10.1016/j.it.2012.01.010 · Cited by 444

Indoleamine 2,3-dioxygenase controls conversion of Foxp3+ Tregs to TH17-like cells in tumor-draining lymph nodes

Sharma, M. D., Hou, D., Liu, Y., Koni, P. A., Metz, R. A., Chandler, P., Mellor, A. L., He, Y., & Munn, D. H. (2009) · Blood · doi:10.1182/blood-2008-12-195354 · Cited by 406

Halofuginone and other febrifugine derivatives inhibit prolyl-tRNA synthetase

Keller, T. L., Zocco, D., Sundrud, M. S., Hendrick, M., Edenius, M., Yum, J., Kim, Y. J., Lee, H., Cortese, J. F., Wirth, D. F., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.790 · Cited by 398

Gut CD103 + dendritic cells express indoleamine 2,3-dioxygenase which influences T regulatory/T effector cell balance and oral tolerance induction

Matteoli, G., Mazzini, E., Iliev, I. D., Mileti, E., Fallarino, F., Puccetti, P., Chieppa, M., & Rescigno, M. (2010) · Gut · doi:10.1136/gut.2009.185108 · Cited by 377

Revving the Engine: Signal Transduction Fuels T Cell Activation

Jones, R. G., & Thompson, C. B. (2007) · Immunity · doi:10.1016/j.immuni.2007.07.008 · Cited by 349

Infectious tolerance via the consumption of essential amino acids and mTOR signaling

Cobbold, S. P., Adams, E., Farquhar, C. A., Nolan, K. F., Howie, D., Lui, K. O., Fairchild, P. J., Mellor, A. L., Ron, D., & Waldmann, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903919106 · Cited by 344

Brain indoleamine 2,3-dioxygenase contributes to the comorbidity of pain and depression

Kim, H., Chen, L. L., Lim, G., Sung, B., Wang, S., McCabe, M. F., Rusanescu, G., Yang, L., Tian, Y., & Mao, J. (2012) · Journal of Clinical Investigation · doi:10.1172/jci61884 · Cited by 329

Infected site-restricted Foxp3+ natural regulatory T cells are specific for microbial antigens

Suffia, I., Reckling, S. K., Piccirillo, C. A., Goldszmid, R. S., & Belkaid, Y. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20052056 · Cited by 311

Induction of IDO by Bacille Calmette-Guérin Is Responsible for Development of Murine Depressive-Like Behavior

O’Connor, J. C., Lawson, M. A., André, C., Briley, E. M., Szegedi, S. S., Lestage, J., Castanon, N., Herkenham, M. A., Dantzer, R., & Kelley, K. W. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0802722 · Cited by 305

IDO1 and IDO2 are expressed in human tumors: levo- but not dextro-1-methyl tryptophan inhibits tryptophan catabolism

Löb, S., Königsrainer, A., Zieker, D., Brücher, B. L. D. M., Rammensee, H., Opelz, G., & Terness, P. (2008) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-008-0513-6 · Cited by 305

HIV-activated human plasmacytoid DCs induce Tregs through an indoleamine 2,3-dioxygenase–dependent mechanism

Manches, O., Munn, D. H., Fallahi, A., Lifson, J. D., Chaperot, L., Plumas, J., & Bhardwaj, N. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34823 · Cited by 247

Interferon-γ-Responsive Nonhematopoietic Cells Regulate the Immune Response to Mycobacterium tuberculosis

Desvignes, L., & Ernst, J. (2009) · Immunity · doi:10.1016/j.immuni.2009.10.007 · Cited by 245

Transcription factor Foxo3 controls the magnitude of T cell immune responses by modulating the function of dendritic cells

Dejean, A. S., Beisner, D. R., Ch’en, I. L., Kerdiles, Y. M., Babour, A., Arden, K. C., Castrillón, D. H., DePinho, R. A., & Hedrick, S. Μ. (2009) · Nature Immunology · doi:10.1038/ni.1729 · Cited by 238

SOCS3 drives proteasomal degradation of indoleamine 2,3-dioxygenase (IDO) and antagonizes IDO-dependent tolerogenesis

Orabona, C., Pallotta, M. T., Volpi, C., Fallarino, F., Vacca, C., Bianchi, R., Belladonna, M. L., Fioretti, M. C., Grohmann, U., & Puccetti, P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810278105 · Cited by 214

Tolerance to apoptotic cells is regulated by indoleamine 2,3-dioxygenase

Ravishankar, B., Liu, H., Shinde, R. S., Chandler, P., Baban, B., Tanaka, M., Munn, D. H., Mellor, A. L., Karlsson, M. C. I., & McGaha, T. L. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117736109 · Cited by 201

CD40Ig treatment results in allograft acceptance mediated by CD8+CD45RClow T cells, IFN-γ, and indoleamine 2,3-dioxygenase

Guillonneau, C., Hill, M., Hubert, F., Chiffoleau, E., Hervé, C., Li, X., Heslan, M., Usal, C., Tesson, L., Ménoret, S., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci28801 · Cited by 198

External influences on the immune system via activation of the aryl hydrocarbon receptor

Stockinger, B., Hirota, K., Duarte, J. H., & Veldhoen, M. (2011) · Seminars in Immunology · doi:10.1016/j.smim.2011.01.008 · Cited by 190

Toward the identification of a tolerogenic signature in IDO-competent dendritic cells

Orabona, C., Puccetti, P., Vacca, C., Bicciato, S., Luchini, A., Fallarino, F., Bianchi, R., Velardi, E., Perruccio, K., Velardi, A., et al. (2005) · Blood · doi:10.1182/blood-2005-10-4077 · Cited by 188

Studying the immunosuppressive role of indoleamine 2,3-dioxygenase: tryptophan metabolites suppress rat allogeneic T-cell responses in vitro and in vivo

Bauer, T. M., Jiga, L. P., Chuang, J.-J., Randazzo, M., Opelz, G., & Terness, P. (2004) · Transplant International · doi:10.1111/j.1432-2277.2004.00031.x · Cited by 181

Reprogrammed Foxp3+ Regulatory T Cells Provide Essential Help to Support Cross-presentation and CD8+ T Cell Priming in Naive Mice

Sharma, M. D., Hou, D., Baban, B., Koni, P. A., He, Y., Chandler, P., Blazar, B. R., Mellor, A. L., & Munn, D. H. (2010) · Immunity · doi:10.1016/j.immuni.2010.11.022 · Cited by 174

Inducing CTLA-4–Dependent Immune Regulation by Selective CD28 Blockade Promotes Regulatory T Cells in Organ Transplantation

Poirier, N., Azimzadeh, A. M., Zhang, T., Dilek, N., Mary, C., Nguyen, B., Tillou, X., Wu, G., Reneaudin, K., Hervouet, J., et al. (2010) · Science Translational Medicine · doi:10.1126/scitranslmed.3000116 · Cited by 173

Regulation of indoleamine 2,3-dioxygenase and tryptophanyl-tRNA-synthetase by CTLA-4-Fc in human CD4+ T cells

Boasso, A., Herbeuval, J., Hardy, A. W., Winkler, C., & Shearer, G. M. (2004) · Blood · doi:10.1182/blood-2004-06-2089 · Cited by 171

Indoleamine 2,3-dioxygenase is a critical regulator of acute graft-versus-host disease lethality

Jasperson, L. K., Bucher, C. M., Panoskaltsis‐Mortari, A., Taylor, P. A., Mellor, A. L., Munn, D. H., & Blazar, B. R. (2007) · Blood · doi:10.1182/blood-2007-06-096081 · Cited by 145

Blocking IDO activity to enhance anti-tumor immunity

Munn, D. H. (2012) · Frontiers in Bioscience-Elite · doi:10.2741/e414 · Cited by 136

CDllc+ cells modulate pulmonary immune responses by production of indoleamine 2,3-dioxygenase.

Swanson, K., Zheng, Y., Heidler, K., Mizobuchi, T., & Wilkes, D. (2004) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2003-0268oc · Cited by 129

IL-17 and Therapeutic Kynurenines in Pathogenic Inflammation to Fungi

Romani, L. R., Zelante, T., LUCA, A. D., Fallarino, F., & Puccetti, P. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.8.5157 · Cited by 123

Mechanism and Localization of CD8 Regulatory T Cells in a Heart Transplant Model of Tolerance

Li, X. L., Ménoret, S., Bézie, S., Caron, L., Chabannes, D., Hill, M., Halary, F. A., Angin, M., Heslan, M., Usal, C., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000120 · Cited by 123

Blockade of Indoleamine 2,3-Dioxygenase Protects Mice against Lipopolysaccharide-Induced Endotoxin Shock

Jung, I. D., Lee, M. G., Chang, J. H., Lee, J. S., Jeong, Y.-I., Lee, C. M., Park, W. S., Han, J., Seo, S., Lee, S. Y., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803104 · Cited by 120

Opposing Biological Functions of Tryptophan Catabolizing Enzymes During Intracellular Infection

Divanovic, S., Sawtell, N. M., Trompette, A., Warning, J. I., Dias, A., Cooper, A. M., Yap, G. S., Arditi, M., Shimada, K., DuHadaway, J. B., et al. (2011) · The Journal of Infectious Diseases · doi:10.1093/infdis/jir621 · Cited by 116

Blocking IDO activity to enhance anti-tumor immunity

David, H. M. (2011) · Frontiers in Bioscience-Elite · doi:10.2741/414 · Cited by 114

Influenza‐Induced Expression of Indoleamine 2,3‐Dioxygenase Enhances Interleukin‐10 Production and Bacterial Outgrowth during Secondary Pneumococcal Pneumonia

van der Sluijs, K. F., Nijhuis, M., Levels, J. H. M., Florquin, S., Mellor, A. L., Jansen, H. M., der Poll, T. V., & Lutter, R. (2006) · The Journal of Infectious Diseases · doi:10.1086/498911 · Cited by 111

The roles of mast cells in anticancer immunity

Dalton, D. K., & Noelle, R. J. (2012) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-012-1246-0 · Cited by 97

Reduced Cytotoxic Function of Effector CD8+ T Cells Is Responsible for Indoleamine 2,3-Dioxygenase-Dependent Immune Suppression

Liu, H., Liu, L., Liu, K., Bizargity, P., Hancock, W. W., & Visner, G. A. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900408 · Cited by 94

Toxicology and pharmacokinetics of 1-methyl-d-tryptophan: Absence of toxicity due to saturating absorption

Jia, L., Schweikart, K. M., Tomaszewski, J. E., Page, J. G., Noker, P. E., Buhrow, S. A., Reid, J. M., Ames, M. M., & Munn, D. H. (2007) · Food and Chemical Toxicology · doi:10.1016/j.fct.2007.07.017 · Cited by 93

Cell‐autonomous control of interferon type I expression by indoleamine 2,3‐dioxygenase in regulatory CD19+ dendritic cells

Manlapat, A., Kahler, D. J., Chandler, P., Munn, D. H., & Mellor, A. L. (2007) · European Journal of Immunology · doi:10.1002/eji.200636690 · Cited by 92

Severe Tryptophan Starvation Blocks Onset of Conventional Persistence and Reduces Reactivation of Chlamydia trachomatis

Leonhardt, R. M., Lee, S., Kavathas, P., & Cresswell, P. (2007) · Infection and Immunity · doi:10.1128/iai.00668-07 · Cited by 92

3-Hydroxykynurenine Suppresses CD4 + T-Cell Proliferation, Induces T-Regulatory-Cell Development, and Prolongs Corneal Allograft Survival

Zaher, S. S., Germain, C., Fu, H., Larkin, F., & George, A. J. T. (2011) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.10-5793 · Cited by 89

Orally Administered Eicosapentaenoic Acid Induces Rapid Regression of Atherosclerosis Via Modulating the Phenotype of Dendritic Cells in LDL Receptor-Deficient Mice

Nakajima, K., Yamashita, T., Kita, T., Takeda, M., Sasaki, N., Kasahara, K., Shinohara, M., Rikitake, Y., Ishida, T., Yokoyama, M., et al. (2011) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.111.229443 · Cited by 84

The Absence of IDO Upregulates Type I IFN Production, Resulting in Suppression of Viral Replication in the Retrovirus-Infected Mouse

Hoshi, M., Saito, K., Hara, A., Taguchi, A., Ohtaki, H., Tanaka, R., Fujigaki, H., Osawa, Y., Takemura, M., Matsunami, H., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0901150 · Cited by 83

IDO and Regulatory T Cell Support Are Critical for Cytotoxic T Lymphocyte-Associated Ag-4 Ig-Mediated Long-Term Solid Organ Allograft Survival

Sucher, R., Fischler, K., Oberhuber, R., Kronberger, I. E., Margreiter, C., Öllinger, R., Schneeberger, S., Fuchs, D., Werner, E. R., Watschinger, K., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002777 · Cited by 83

Leishmania major Attenuates Host Immunity by Stimulating Local Indoleamine 2,3-Dioxygenase Expression

Makala, L., Baban, B., Lemos, H. D. P., El‐Awady, A., Chandler, P., Hou, D., Munn, D. H., & Mellor, A. L. (2011) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiq095 · Cited by 82

Activation of indoleamine 2,3-dioxygenase-induced tryptophan degradation in advanced atherosclerotic plaques: Tampere Vascular Study

Niinisalo, P., Oksala, N., Levula, M., Pelto‐Huikko, M., Järvinen, O., Salenius, J., Kytömäki, L., Soini, J. T., Kähönen, M. A. P., Laaksonen, R., et al. (2009) · Annals of Medicine · doi:10.3109/07853890903321559 · Cited by 81

Sleeping Beauty‐based gene therapy with indoleamine 2,3‐dioxygenase inhibits lung allograft fibrosis

Liu, H., Liu, L., Fletcher, B. S., & Visner, G. A. (2006) · The FASEB Journal · doi:10.1096/fj.06-6228fje · Cited by 80

Inflammatory stimuli reduce survival of serotonergic neurons and induce neuronal expression of indoleamine 2,3-dioxygenase in rat dorsal raphe nucleus organotypic brain slices

Hochstrasser, T., Ullrich, C., Sperner‐Unterweger, B., & Humpel, C. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.03.070 · Cited by 80

Human CD 1c ( BDCA ‐1)+ myeloid dendritic cells secrete IL ‐10 and display an immuno‐regulatory phenotype and function in response to E scherichia coli

Kassianos, A. J., Hardy, M. Y., Ju, X., Vijayan, D., Ding, Y., Vulink, A. J. E., McDonald, K. J., Jongbloed, S. L., Wadley, R. B., Wells, C. A., et al. (2012) · European Journal of Immunology · doi:10.1002/eji.201142098 · Cited by 79

Physiologic Control of IDO Competence in Splenic Dendritic Cells

Baban, B., Chandler, P., Johnson, B. A., Huang, L., Li, M., Sharpe, M. L., Francisco, L. M., Sharpe, A. H., Blazar, B. R., Munn, D. H., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100276 · Cited by 70

Development of Murine Lupus Involves the Combined Genetic Contribution of the SLAM and FcγR Intervals within the Nba2 Autoimmune Susceptibility Locus

Jørgensen, T. N., Alfaro, J., Enriquez, H. L., Jiang, C., Loo, W. M., Atencio, S., Bupp, M. G., Mailloux, C. M., Metzger, T. E., Flannery, S., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901322 · Cited by 68

The kynurenine pathway and quinolinic acid: pivotal roles in HIV associated neurocognitive disorders

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B-lymphoid cells with attributes of dendritic cells regulate T cells via indoleamine 2,3-dioxygenase

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