Reversal of indoleamine 2,3-dioxygenase-mediated cancer immune suppression by systemic kynurenine depletion with a therapeutic enzyme

Over-production of Proteins inEscherichia coli: Mutant Hosts that Allow Synthesis of some Membrane Proteins and Globular Proteins at High Levels

Miroux, B., & Walker, J. E. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0399 · Cited by 1,964 · see citing works

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 · see citing works

Up-Regulation of PD-L1, IDO, and T _regs in the Melanoma Tumor Microenvironment Is Driven by CD8 ⁺ T Cells

Spranger, S., Spaapen, R. M., Zha, Y., Williams, J., Meng, Y., Ha, T. T., & Gajewski, T. F. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3006504 · Cited by 1,677 · see citing works

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 1,617 · see citing works

Kynurenines: Tryptophan’s metabolites in exercise, inflammation, and mental health

Cervenka, I., Agudelo, L. Z., & Ruas, J. L. (2017) · Science · doi:10.1126/science.aaf9794 · Cited by 1,382 · see citing works

Tryptophan-derived Catabolites Are Responsible for Inhibition of T and Natural Killer Cell Proliferation Induced by Indoleamine 2,3-Dioxygenase

Frumento, G., Rotondo, R., Tonetti, M., Damonte, G., Benatti, U., & Ferrara, G. B. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20020121 · Cited by 1,133 · see citing works

Indoleamine 2,3-dioxygenase and tumor-induced tolerance

Munn, D. H., & Mellor, A. L. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31178 · Cited by 1,074 · see citing works

In Situ Cytotoxic and Memory T Cells Predict Outcome in Patients With Early-Stage Colorectal Cancer

Pagès, F., Kirilovsky, A., Mlecnik, B., Asslaber, M., Tosolini, M., Bindea, G., Lagorce, C., Wind, P., Marliot, F., Bruneval, P., et al. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2008.19.6147 · Cited by 953 · see citing works

Inhibition of Allogeneic T Cell Proliferation by Indoleamine 2,3-Dioxygenase–expressing Dendritic Cells

Terness, P., Bauer, T. M., Röse, L., Dufter, C., Watzlik, A., Simon, H., & Opelz, G. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20020052 · Cited by 939 · see citing works

Tryptophan Catabolism in Cancer: Beyond IDO and Tryptophan Depletion

Platten, M., Wick, W., & den Eynde, B. J. V. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-0569 · Cited by 708 · see citing works

Kynurenines in the CNS: recent advances and new questions

Vécsei, L., Szalárdy, L., Fülöp, F., & Toldi, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd3793 · Cited by 641 · see citing works

Indoleamine 2,3-dioxygenase is a critical resistance mechanism in antitumor T cell immunotherapy targeting CTLA-4

Holmgaard, R., Zamarin, D., Munn, D. H., Wolchok, J. D., & Allison, J. P. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20130066 · Cited by 633 · see citing works

Inhibition of Indoleamine 2,3-Dioxygenase in Dendritic Cells by Stereoisomers of 1-Methyl-Tryptophan Correlates with Antitumor Responses

Hou, D., Muller, A. J., Sharma, M. D., DuHadaway, J. B., Banerjee, T., Johnson, M., Mellor, A. L., Prendergast, G. C., & Munn, D. H. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-2925 · Cited by 586 · see citing works

Durable Therapeutic Efficacy Utilizing Combinatorial Blockade against IDO, CTLA-4, and PD-L1 in Mice with Brain Tumors

Wainwright, D. A., Chang, A. L., Dey, M., Balyasnikova, I. V., Kim, C. K., Tobias, A. L., Cheng, Y., Kim, J. W., Qiao, J., Zhang, L., et al. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-0514 · Cited by 571 · see citing works

Discovery of IDO1 Inhibitors: From Bench to Bedside

Prendergast, G. C., Malachowski, W. P., DuHadaway, J. B., & Muller, A. J. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-2285 · Cited by 563 · see citing works

Mechanism of tumor rejection with doublets of CTLA-4, PD-1/PD-L1, or IDO blockade involves restored IL-2 production and proliferation of CD8(+) T cells directly within the tumor microenvironment

Spranger, S., Koblish, H. K., Horton, B., Scherle, P. A., Newton, R., & Gajewski, T. F. (2014) · Journal for ImmunoTherapy of Cancer · doi:10.1186/2051-1426-2-3 · Cited by 552 · see citing works

Targeting the IDO1/TDO2–KYN–AhR Pathway for Cancer Immunotherapy – Challenges and Opportunities

Cheong, J. E., & Sun, L. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.11.007 · Cited by 489 · see citing works

CTLA-4 blockade enhances polyfunctional NY-ESO-1 specific T cell responses in metastatic melanoma patients with clinical benefit

Yuan, J. D., Gnjatic, S., Li, H., Powel, S., Gallardo, H. F., Ritter, E., Ku, G. Y., Jungbluth, A. A., Segal, N. H., Rasalan, T. S., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810114105 · Cited by 346 · see citing works

CTLA-4 blockade in tumor models: an overview of preclinical and translational research.

Grosso, J. F., & Jure‐Kunkel, M. (2013) · Europe PMC (PubMed Central) · Cited by 335 · see citing works

A Relay Pathway between Arginine and Tryptophan Metabolism Confers Immunosuppressive Properties on Dendritic Cells

Mondanelli, G., Bianchi, R., Pallotta, M. T., Orabona, C., Albini, E., Iacono, A., Belladonna, M. L., Vacca, C., Fallarino, F., Macchiarulo, A., et al. (2017) · Immunity · doi:10.1016/j.immuni.2017.01.005 · Cited by 335 · see citing works

Tumor indoleamine 2,3-dioxygenase (IDO) inhibits CD19-CAR T cells and is downregulated by lymphodepleting drugs

Ninomiya, S., Narala, N., Huye, L. E., Yagyu, S., Savoldo, B., Dotti, G., Heslop, H. E., Brenner, M. K., Rooney, C. M., & Ramos, C. A. (2015) · Blood · doi:10.1182/blood-2015-01-621474 · Cited by 317 · see citing works

Molecular mechanisms of acquired resistance to tyrosine kinase targeted therapy

Sierra, J. R., Cepero, V., & Giordano, S. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-75 · Cited by 230 · see citing works

IDO1 Metabolites Activate β-catenin Signaling to Promote Cancer Cell Proliferation and Colon Tumorigenesis in Mice

Thaker, A. I., Rao, M. S., Bishnupuri, K. S., Kerr, T. A., Foster, L. R., Marinshaw, J. M., Newberry, R. D., Stenson, W. F., & Ciorba, M. A. (2013) · Gastroenterology · doi:10.1053/j.gastro.2013.05.002 · Cited by 195 · see citing works

A key in vivo antitumor mechanism of action of natural product-based brassinins is inhibition of indoleamine 2,3-dioxygenase

Banerjee, T., DuHadaway, J. B., Gaspari, P. M., Sutanto‐Ward, E., Munn, D. H., Mellor, A. L., Malachowski, W. P., Prendergast, G. C., & Muller, A. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210939 · Cited by 175 · see citing works

Indoleamine 2,3-dioxygenase 2 (IDO2) and the kynurenine pathway: characteristics and potential roles in health and disease

Fatokun, A. A., Hunt, N. H., & Ball, H. J. (2013) · Amino Acids · doi:10.1007/s00726-013-1602-1 · Cited by 162 · see citing works

Trace derivatives of kynurenine potently activate the aryl hydrocarbon receptor (AHR)

Seok, S.-H., Ma, Z.-X., Feltenberger, J. B., Chen, H., Chen, H., Scarlett, C., Lin, Z., Satyshur, K. A., Cortopassi, M., Jefcoate, C. R., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000631 · Cited by 157 · see citing works

Targeting myeloid-derived suppressor cells with colony stimulating factor-1 receptor blockade can reverse immune resistance to immunotherapy in indoleamine 2,3-dioxygenase-expressing tumors

Holmgaard, R., Zamarin, D., Lesokhin, A. M., Merghoub, T., & Wolchok, J. D. (2016) · EBioMedicine · doi:10.1016/j.ebiom.2016.02.024 · Cited by 146 · see citing works

A community-based study on determinants of circulating markers of cellular immune activation and kynurenines: the Hordaland Health Study

Theofylaktopoulou, D., Midttun, Ø., Ulvik, A., Ueland, P. M., Tell, G. S., Vollset, S. E., Nygard, O. K., & Eussen, S. J. P. M. (2013) · Clinical & Experimental Immunology · doi:10.1111/cei.12092 · Cited by 129 · see citing works

The end of the road for the tryptophan depletion concept in pregnancy and infection

Badawy, A. A.-B., Namboodiri, A. M. A., & Moffett, J. R. (2016) · Clinical Science · doi:10.1042/cs20160153 · Cited by 92 · see citing works

Accumulation of an Endogenous Tryptophan-Derived Metabolite in Colorectal and Breast Cancers

Puccetti, P., Fallarino, F., Italiano, A., Soubeyran, I., MacGrogan, G. M., Debled, M., Velasco, V., Bodet, D., Eimer, S., Veldhoen, M., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0122046 · Cited by 87 · see citing works

Stress Kinase GCN2 Controls the Proliferative Fitness and Trafficking of Cytotoxic T Cells Independent of Environmental Amino Acid Sensing

de Velde, L.-A. V., Guo, X.-Z. J., Barbaric, L., Smith, A. M., Oguin, T. H., Thomas, P. G., & Murray, P. J. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.10.079 · Cited by 82 · see citing works

Possible roles of excess tryptophan metabolites in cancer

Chung, K., & Gadupudi, G. (2011) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20588 · Cited by 79 · see citing works

The stress kinase GCN2 does not mediate suppression of antitumor T cell responses by tryptophan catabolism in experimental melanomas

Sonner, J. K., Deumelandt, K., Ott, M., Thomé, C. M., Rauschenbach, K. J., Schulz, S., Munteanu, B., Mohapatra, S., Adam, I., Hofer, A.-C., et al. (2016) · OncoImmunology · doi:10.1080/2162402x.2016.1240858 · Cited by 64 · see citing works

Indoleamine 2,3-dioxygenase 1 (IDO1) inhibitors activate the aryl hydrocarbon receptor

Moyer, B. J., Rojas, I. Y., Murray, I. A., Lee, S., Hazlett, H. F., Perdew, G. H., & Tomlinson, C. R. (2017) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2017.03.012 · Cited by 64 · see citing works

Structure and mechanism of kynureninase

Phillips, R. S. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.10.020 · Cited by 60 · see citing works

Immunological and Nonimmunological Effects of Indoleamine 2,3-Dioxygenase on Breast Tumor Growth and Spontaneous Metastasis Formation

Levina, V. V., Su, Y., & Gorelik, E. (2012) · Clinical and Developmental Immunology · doi:10.1155/2012/173029 · Cited by 49 · see citing works

IDO1 suppresses inhibitor development in hemophilia A treated with factor VIII

Matino, D., Gargaro, M., Santagostino, E., Minno, M. N. D. D., Castaman, G., Morfini, M., Rocino, A., Mancuso, M. E., Minno, G. D., Coppola, A., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci81859 · Cited by 46 · see citing works

Tumor immunogenicity and responsiveness to cancer vaccine therapy: The state of the art

Schreiber, T. H., Raez, L. E., Rosenblatt, J. D., & Podack, E. R. (2010) · Seminars in Immunology · doi:10.1016/j.smim.2010.02.001 · Cited by 46 · see citing works

Strategies for optimizing the serum persistence of engineered human arginase I for cancer therapy

Stone, E. M., Chantranupong, L., Gonzalez, C., O’Neal, J. F., Rani, M., Berg, C. L. V. D., & Georgiou, G. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2011.09.097 · Cited by 28 · see citing works

Cloning, Sequence, and Expression of Kynureninase fromPseudomonas fluorescens

Koushik, S. V., Sundararaju, B., McGraw, R. A., & Phillips, R. S. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0220 · Cited by 20 · see citing works

Cancer immunoediting and resistance to T cell-based immunotherapy

O’Donnell, J. S., Teng, M. W. L., & Smyth, M. J. (2018) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-018-0142-8 · Cited by 1,759 · see citing works

The aryl hydrocarbon receptor: an environmental sensor integrating immune responses in health and disease

Rothhammer, V., & Quintana, F. J. (2019) · Nature Reviews Immunology · doi:10.1038/s41577-019-0125-8 · Cited by 1,197 · see citing works

Tryptophan metabolism in health and disease

Chen, X., Li, G., Zheng, Q., Gu, X., Shi, Q., Su, Y., Chu, Q., Yuan, X., Bao, Z., Lu, J., et al. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.06.004 · Cited by 1,008 · see citing works

Therapy-Induced Evolution of Human Lung Cancer Revealed by Single-Cell RNA Sequencing

Maynard, A., McCoach, C. E., Rotow, J. K., Harris, L., Haderk, F., Kerr, D. L., Yu, E. A., Schenk, E. L., Tan, W., Zee, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.07.017 · Cited by 697 · see citing works

Advantages of targeting the tumor immune microenvironment over blocking immune checkpoint in cancer immunotherapy

Tang, T., Huang, X., Zhang, G., Hong, Z., Bai, X., & Liang, T. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00449-4 · Cited by 613 · see citing works

Navigating CAR-T cells through the solid-tumour microenvironment

Hou, A. J., Chen, L. C., & Chen, Y. Y. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00189-2 · Cited by 556 · see citing works

Blockade of the AHR restricts a Treg-macrophage suppressive axis induced by L-Kynurenine

Campesato, L. F., Budhu, S., Tchaicha, J. H., Weng, C., Gigoux, M., Cohen, I., Redmond, D., Mangarin, L. M. B., Pourpe, S., Liu, C., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17750-z · Cited by 536 · see citing works

Gut Microbiota-Derived Tryptophan Metabolites Maintain Gut and Systemic Homeostasis

Su, X., Gao, Y., & Yang, R. (2022) · Cells · doi:10.3390/cells11152296 · Cited by 424 · see citing works

Reimagining IDO Pathway Inhibition in Cancer Immunotherapy via Downstream Focus on the Tryptophan–Kynurenine–Aryl Hydrocarbon Axis

Labadie, B. W., Bao, R., & Luke, J. J. (2019) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-2882 · Cited by 413 · see citing works

PD-1/PD-L1 Blockade Therapy in Advanced Non-Small-Cell Lung Cancer: Current Status and Future Directions

Xia, L., Liu, Y., & Wang, Y. (2019) · The Oncologist · doi:10.1634/theoncologist.2019-io-s1-s05 · Cited by 393 · see citing works

Amino acid metabolism in immune cells: essential regulators of the effector functions, and promising opportunities to enhance cancer immunotherapy

Yang, L., Chu, Z., Liu, M., Zou, Q., Li, J., Liu, Q., Wang, Y., Wang, T., Xiang, J., & Wang, B. (2023) · Journal of Hematology & Oncology · doi:10.1186/s13045-023-01453-1 · Cited by 362 · see citing works

Immunometabolic Interplay in the Tumor Microenvironment

Kaymak, I., Williams, K. S., Cantor, J. R., & Jones, R. G. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.09.004 · Cited by 330 · see citing works

Metabolic interventions in the immune response to cancer

O’Sullivan, D., Sanin, D. E., Pearce, E. J., & Pearce, E. L. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0140-9 · Cited by 314 · see citing works

Amino Acids and Their Transporters in T Cell Immunity and Cancer Therapy

Wang, W., & Zou, W. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.09.006 · Cited by 304 · see citing works

The therapeutic potential of targeting tryptophan catabolism in cancer

Opitz, C. A., Somarribas Patterson, L. F., Mohapatra, S. R., Dewi, D. L., Sadik, A., Platten, M., & Trump, S. (2020) · British Journal of Cancer · doi:10.1038/s41416-019-0664-6 · Cited by 300 · see citing works

Immune control by amino acid catabolism during tumorigenesis and therapy

Lemos, H. D. P., Huang, L., Prendergast, G. C., & Mellor, A. L. (2019) · Nature reviews. Cancer · doi:10.1038/s41568-019-0106-z · Cited by 275 · see citing works

Activatable Polymer Nanoenzymes for Photodynamic Immunometabolic Cancer Therapy

Zeng, Z., Zhang, C., Li, J., Cui, D., Jiang, Y., & Pu, K. (2021) · Advanced Materials · doi:10.1002/adma.202007247 · Cited by 276 · see citing works

Inhibiting IDO pathways to treat cancer: lessons from the ECHO-301 trial and beyond

Muller, A. J., Manfredi, M. G., Zakharia, Y., & Prendergast, G. C. (2018) · Seminars in Immunopathology · doi:10.1007/s00281-018-0702-0 · Cited by 265 · see citing works

Immune checkpoint modulators in cancer immunotherapy: recent advances and emerging concepts

Wang, Y., Zhang, H., Liu, C., Wang, Z., Wu, W., Zhang, N., Zhang, L., Hu, J. J., Luo, P., Zhang, J., et al. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01325-0 · Cited by 261 · see citing works

Glioblastoma Therapy: Past, Present and Future

Obrador, E., Moreno-Murciano, P., Oriol‐Caballo, M., López‐Blanch, R., Pineda, B., Gutiérrez-Arroyo, J., Loras, A., Bonet, L. G. G., Martínez‐Cadenas, C., Estrela, J. M., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052529 · Cited by 263 · see citing works

ADORA1 Inhibition Promotes Tumor Immune Evasion by Regulating the ATF3-PD-L1 Axis

Liu, H., Kuang, X., Zhang, Y., Ye, Y., Li, J., Liang, L., Xie, Z., Weng, L., Guo, J., Li, H., et al. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.02.006 · Cited by 227 · see citing works

Advancing to the era of cancer immunotherapy

Wang, Y., Wang, M., Wu, H., & Xu, R. (2021) · 癌症：英文版 · doi:10.1002/cac2.12178 · Cited by 219 · see citing works

USP14 promotes tryptophan metabolism and immune suppression by stabilizing IDO1 in colorectal cancer

Shi, D., Wu, X., Jian, Y., Wang, J., Huang, C., Mo, S., Li, Y., Li, F., Zhang, C., Zhang, D., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33285-x · Cited by 214 · see citing works

Enzyme Therapy: Current Challenges and Future Perspectives

de la Fuente, M., Lombardero, L., Gómez-González, A., Solari, C., Angulo‐Barturen, Í., Acera, A., Vecino, E., Astigarraga, E., & Barreda‐Gómez, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179181 · Cited by 217 · see citing works

Activation of RAS/MAPK pathway confers MCL-1 mediated acquired resistance to BCL-2 inhibitor venetoclax in acute myeloid leukemia

Zhang, Q., Riley-Gillis, B. M., Han, L., Jia, Y., Lodi, A., Zhang, H., Ganesan, S., Pan, R. A., Konoplev, S. N., Sweeney, S., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00870-3 · Cited by 202 · see citing works

Metabolic Modulation of Immunity: A New Concept in Cancer Immunotherapy

Guerra, L., Bonetti, L., & Brenner, D. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107848 · Cited by 186 · see citing works

Molecular mechanisms and therapeutic significance of Tryptophan Metabolism and signaling in cancer

Yan, J. J., Chen, D., Ye, Z., Zhu, X., Li, X., Jiao, H., Duan, M., Zhang, C., Cheng, J., Xu, L., et al. (2024) · Molecular Cancer · doi:10.1186/s12943-024-02164-y · Cited by 184 · see citing works

Aptamer-conjugated nano-liposome for immunogenic chemotherapy with reversal of immunosuppression

Kim, M., Lee, J. S., Kim, W.-Y., Lee, J. H., Jun, B., Kim, K., & Kim, D. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.06.039 · Cited by 178 · see citing works

Is There a Clinical Future for IDO1 Inhibitors After the Failure of Epacadostat in Melanoma?

Van den Eynde, B. J., van Baren, N., & Baurain, J.-F. (2020) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030419-033635 · Cited by 175 · see citing works

Nanomedicine‐Based Immunotherapy for the Treatment of Cancer Metastasis

Zhang, P., Zhai, Y., Cai, Y., Zhao, Y., & Li, Y. (2019) · Advanced Materials · doi:10.1002/adma.201904156 · Cited by 170 · see citing works

Reprogramming the immunosuppressive tumor microenvironment through nanomedicine: an immunometabolism perspective

Liu, J., Bai, Y., Li, Y., Li, X., & Luo, K. (2024) · EBioMedicine · doi:10.1016/j.ebiom.2024.105301 · Cited by 165 · see citing works

High-salt diet mediates interplay between NK cells and gut microbiota to induce potent tumor immunity

Rizvi, Z. A., Dalal, R., Sadhu, S., Kumar, Y., Kumar, S., Gupta, S. K., Tripathy, M. R., Rathore, D. K., & Awasthi, A. (2021) · Science Advances · doi:10.1126/sciadv.abg5016 · Cited by 160 · see citing works

Nanomedicine‐Boosting Tumor Immunogenicity for Enhanced Immunotherapy

Huang, J., Yang, B., Peng, Y., Huang, J., Wong, S. H. D., Bian, L., Zhu, K., Shuai, X., & Han, S. (2021) · Advanced Functional Materials · doi:10.1002/adfm.202011171 · Cited by 157 · see citing works

Engineering Stimuli‐Activatable Boolean Logic Prodrug Nanoparticles for Combination Cancer Immunotherapy

Hou, B., Zhou, L., Wang, H., Saeed, M., Wang, D., Xu, Z., Li, Y., & Yu, H. (2020) · Advanced Materials · doi:10.1002/adma.201907210 · Cited by 152 · see citing works

Tryptophan depletion results in tryptophan-to-phenylalanine substitutants

Pataskar, A., Champagne, J., Nagel, R., Kenski, J. C. N., Laos, M., Michaux, J., Pak, H. S., Bleijerveld, O. B., Mordente, K., Navarro, J. M., et al. (2022) · Nature · doi:10.1038/s41586-022-04499-2 · Cited by 146 · see citing works

Catalytical nano-immunocomplexes for remote-controlled sono-metabolic checkpoint trimodal cancer therapy

Zhang, C., Huang, J., Zeng, Z., He, S., Cheng, P., Li, J., & Pu, K. (2022) · Nature Communications · doi:10.1038/s41467-022-31044-6 · Cited by 151 · see citing works

CRISPR screens in physiologic medium reveal conditionally essential genes in human cells

Rossiter, N. J., Huggler, K. S., Adelmann, C. H., Keys, H. R., Soens, R. W., Sabatini, D. M., & Cantor, J. R. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.02.005 · Cited by 133 · see citing works

Acetate acts as a metabolic immunomodulator by bolstering T-cell effector function and potentiating antitumor immunity in breast cancer

Miller, K. D., O’Connor, S., Pniewski, K. A., Kannan, T., Acosta, R., Mirji, G., Papp, S. B., Hulse, M., Mukha, D., Hlavaty, S. I., et al. (2023) · Nature Cancer · doi:10.1038/s43018-023-00636-6 · Cited by 132 · see citing works

Kynurenine emerges from the shadows – Current knowledge on its fate and function

Marszałek‐Grabska, M., Walczak, K., Gaweł, K., Wicha-Komsta, K., Wnorowska, S., Wnorowski, A., & Turski, W. A. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107845 · Cited by 126 · see citing works

Targeting Tryptophan Catabolism in Cancer Immunotherapy Era: Challenges and Perspectives

Peyraud, F., Guégan, J., Bodet, D., Cousin, S., Bessede, A., & Italiano, A. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.807271 · Cited by 130 · see citing works

Overview of recent advances in liposomal nanoparticle-based cancer immunotherapy

Gao, A., Hu, X., Saeed, M., Chen, B., Li, Y., & Yu, H. (2019) · Acta Pharmacologica Sinica · doi:10.1038/s41401-019-0281-1 · Cited by 125 · see citing works

The path toward using microbial metabolites as therapies

Descamps, H. C., Herrmann, B. I., Wiredu, D., & Thaiss, C. A. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.05.063 · Cited by 121 · see citing works

Immune-checkpoint inhibitor resistance in cancer treatment: Current progress and future directions

Zhang, C., Zhang, C., & Wang, H. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216182 · Cited by 125 · see citing works

Dendritic Cell Vaccines: A Shift from Conventional Approach to New Generations

Lee, K.-W., Yam, J. W. P., & Mao, X. (2023) · Cells · doi:10.3390/cells12172147 · Cited by 124 · see citing works

Exosome-derived miR-142-5p remodels lymphatic vessels and induces IDO to promote immune privilege in the tumour microenvironment

Zhou, C., Zhang, Y., Yan, R.-M., Huang, L., Mellor, A. L., Yang, Y., Chen, X., Wei, W.-F., Wu, X., Yu, L., et al. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00618-6 · Cited by 115 · see citing works

Targeting Dietary and Microbial Tryptophan-Indole Metabolism as Therapeutic Approaches to Colon Cancer

Greathouse, K. L., & Wyatt, M. (2021) · Nutrients · doi:10.3390/nu13041189 · Cited by 111 · see citing works

An in situ hydrogel-mediated chemo-immunometabolic cancer therapy

Wang, B., Chen, J., Caserto, J. S., Wang, X., & Ma, M. (2022) · Nature Communications · doi:10.1038/s41467-022-31579-8 · Cited by 109 · see citing works

m6A methylation: a process reshaping the tumour immune microenvironment and regulating immune evasion

Cao, X., Geng, Q., Fan, D., Wang, Q., Wang, X., Zhang, M., Zhao, L., Jiao, Y., Deng, T., Liu, H., et al. (2023) · Molecular Cancer · doi:10.1186/s12943-022-01704-8 · Cited by 112 · see citing works

Tryptophan and its metabolites in normal physiology and cancer etiology

Perez‐Castro, L., Garcia, R., Venkateswaran, N., Barnes, S. D., & Conacci‐Sorrell, M. (2021) · FEBS Journal · doi:10.1111/febs.16245 · Cited by 104 · see citing works

Uraemic solutes as therapeutic targets in CKD-associated cardiovascular disease

Ravid, J. D., Kamel, M. H., & Chitalia, V. C. (2021) · Nature Reviews Nephrology · doi:10.1038/s41581-021-00408-4 · Cited by 101 · see citing works

The role of AhR in transcriptional regulation of immune cell development and function

Trikha, P., & Lee, D. A. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2019.188335 · Cited by 96 · see citing works

Inflammation in cancer and depression: a starring role for the kynurenine pathway

Sforzini, L., Nettis, M. A., Mondelli, V., & Pariante, C. M. (2019) · Psychopharmacology · doi:10.1007/s00213-019-05200-8 · Cited by 97 · see citing works

Targeting the aryl hydrocarbon receptor (AhR) with BAY 2416964: a selective small molecule inhibitor for cancer immunotherapy

Kober, C., Roewe, J., Schmees, N., Roese, L., Roehn, U., Bader, B., Stoeckigt, D., Prinz, F., Gorjánácz, M., Roider, H. G., et al. (2023) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2023-007495 · Cited by 95 · see citing works

The aryl hydrocarbon receptor: structure, signaling, physiology and pathology

Coumoul, X., Barouki, R., Esser, C., Haarmann‐Stemmann, T., Lawrence, B. P., Lehmann, J., Moura‐Alves, P., Murray, I. A., Opitz, C. A., Perdew, G. H., et al. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02500-8 · Cited by 103 · see citing works

Tryptophan: A Rheostat of Cancer Immune Escape Mediated by Immunosuppressive Enzymes IDO1 and TDO

Kim, M., & Tomek, P. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.636081 · Cited by 89 · see citing works

Molecular and metabolic regulation of immunosuppression in metastatic pancreatic ductal adenocarcinoma

Gautam, S. K., Batra, S. K., & Jain, M. (2023) · Molecular Cancer · doi:10.1186/s12943-023-01813-y · Cited by 88 · see citing works

Noncoding RNAs link metabolic reprogramming to immune microenvironment in cancers

Zhang, Y., Mao, Q., Xia, Q., Cheng, J., Huang, Z., Li, Y., Chen, P., Yang, J., Fan, X., Liang, Y., et al. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01179-y · Cited by 84 · see citing works

Fueling T-cell Antitumor Immunity: Amino Acid Metabolism Revisited

Han, C., Ge, M., Ho, P., & Zhang, L. (2021) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-21-0459 · Cited by 83 · see citing works

Fighting in a wasteland: deleterious metabolites and antitumor immunity

Watson, M. J., & Delgoffe, G. M. (2022) · Journal of Clinical Investigation · doi:10.1172/jci148549 · Cited by 82 · see citing works

Amino acid metabolism reprogramming: shedding new light on T cell anti-tumor immunity

Zheng, Y., Yao, Y., Ge, T., Ge, S., Jia, R., Song, X., & Zhuang, A. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02845-4 · Cited by 86 · see citing works

A Metabolism Toolbox for CAR T Therapy

Xu, X., Gnanaprakasam, J. R., Sherman, J. W., & Wang, R. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00322 · Cited by 81 · see citing works

Programmable prodrug micelle with size-shrinkage and charge-reversal for chemotherapy-improved IDO immunotherapy

Dai, L., Li, X., Yao, M., Niu, P., Yuan, X., Li, K., Chen, M., Fu, Z., Duan, X., Liu, H., et al. (2020) · Biomaterials · doi:10.1016/j.biomaterials.2020.119901 · Cited by 81 · see citing works

Detrimental activation of AhR pathway in cancer: an overview of therapeutic strategies

Leclerc, D., Pires, A. S., Guillemin, G. J., & Gilot, D. (2021) · Current Opinion in Immunology · doi:10.1016/j.coi.2020.12.003 · Cited by 79 · see citing works

Indoleamine 2,3-Dioxygenase 1: A Promising Therapeutic Target in Malignant Tumor

Song, X., Si, Q., Qi, R., Liu, W., Li, M., Guo, M.-Y., Wei, L., & Yao, Z. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.800630 · Cited by 79 · see citing works

Immune checkpoint inhibitors in colorectal cancer: limitation and challenges

Yan, S., Wang, W., Feng, Z., Xue, J., Liang, W., Wu, X., Tan, Z., Zhang, X., Zhang, S., Li, X., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1403533 · Cited by 77 · see citing works

Metabolic checkpoints in immune cell reprogramming: rewiring immunometabolism for cancer therapy

Lv, Y., Li, Z., Liu, S., Zhou, Z., Jinling, S., Ba, Y., Weng, S., Zuo, A., Xu, H. W., Luo, P., et al. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02407-6 · Cited by 83 · see citing works

Inhibition of Tryptophan-Dioxygenase Activity Increases the Antitumor Efficacy of Immune Checkpoint Inhibitors

Schramme, F., Crosignani, S., Frederix, K., Hoffmann, D., Pilotte, L., Stroobant, V., Preillon, J., Driessens, G., & den Eynde, B. J. V. (2019) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-19-0041 · Cited by 71 · see citing works

The Kynurenine Pathway and Indole Pathway in Tryptophan Metabolism Influence Tumor Progression

Lu, Z., Zhang, C., Zhang, J., Su, W., Wang, G., & Wang, Z. (2025) · Cancer Medicine · doi:10.1002/cam4.70703 · Cited by 74 · see citing works

Mechanism of Bazhen decoction in the treatment of colorectal cancer based on network pharmacology, molecular docking, and experimental validation

Lu, S., Sun, X., Zhou, Z., Tang, H., Xiao, R., Lv, Q., Wang, B., Qu, J., Yu, J., Sun, F., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1235575 · Cited by 66 · see citing works

The role of the kynurenine pathway in cardiovascular disease

Yang, Y.-H., Liu, X., Liu, X.-Y., Xie, C.-Y., & Shi, J.-W. (2024) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2024.1406856 · Cited by 60 · see citing works

Immune metabolism in PD-1 blockade-based cancer immunotherapy

Kumar, A., & Chamoto, K. (2020) · International Immunology · doi:10.1093/intimm/dxaa046 · Cited by 63 · see citing works

Tryptophan Metabolites at the Crossroad of Immune-Cell Interaction via the Aryl Hydrocarbon Receptor: Implications for Tumor Immunotherapy

Gargaro, M., Manni, G., Scalisi, G., Puccetti, P., & Fallarino, F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094644 · Cited by 64 · see citing works

Targeting Cancer Cell Ferroptosis to Reverse Immune Checkpoint Inhibitor Therapy Resistance

Deng, J., Zhou, M. L., Liao, T., Kuang, W., Xia, H., Yin, Z., Tan, Q., Li, Y., Song, S., Zhou, E., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.818453 · Cited by 63 · see citing works

Immunosuppressive metabolites in tumoral immune evasion: redundancies, clinical efforts, and pathways forward

Jennings, M. R., Munn, D. H., & Blazeck, J. (2021) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2021-003013 · Cited by 63 · see citing works

Antineoplastic Enzyme as Drug Carrier with Activatable Catalytic Activity for Efficient Combined Therapy

Zhang, Y., Jiang, S., Lin, J., & Huang, P. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202208583 · Cited by 62 · see citing works

Oncogene-dependent sloppiness in mRNA translation

Champagne, J., Pataskar, A., Blommaert, N., Nagel, R., Wernaart, D., Ramalho, S., Kenski, J. C. N., Bleijerveld, O. B., Zaal, E. A., Berkers, C. R., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.09.002 · Cited by 63 · see citing works

Tryptophan 2,3-dioxygenase 2 controls M2 macrophages polarization to promote esophageal squamous cell carcinoma progression via AKT/GSK3β/IL-8 signaling pathway

Zhao, Y., Sun, J., Li, Y., Zhou, X., Zhai, W., Wu, Y., Chen, G., Gou, S., Sui, X., Zhao, W., et al. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.03.009 · Cited by 60 · see citing works

Targeting gut microbiota–derived kynurenine to predict and protect the remodeling of the pressure-overloaded young heart

Shi, B., Zhang, X., Song, Z.-Y., Dai, Z., Luo, K., Chen, B., Zhou, Z., Cui, Y., Feng, B., Zhu, Z., et al. (2023) · Science Advances · doi:10.1126/sciadv.adg7417 · Cited by 60 · see citing works

Leveraging intrinsic flexibility to engineer enhanced enzyme catalytic activity

Karamitros, C. S., Murray, K., Winemiller, B., Lamb, C., Stone, E. M., D’Arcy, S., Johnson, K. A., & Georgiou, G. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2118979119 · Cited by 59 · see citing works

Abrine, an IDO1 inhibitor, suppresses the immune escape and enhances the immunotherapy of anti-PD-1 antibody in hepatocellular carcinoma

Liang, X., Gao, H., Xiao, J. Y., Han, S., He, J., Yuan, R., Yang, S., & Yao, C. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1185985 · Cited by 59 · see citing works

Dual role of interferon-gamma in the response of melanoma patients to immunotherapy with immune checkpoint inhibitors

Wawrzyniak, P., & Hartman, M. L. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02294-x · Cited by 59 · see citing works

The interactive role of inflammatory mediators and metabolic reprogramming in pancreatic cancer

Ohara, Y., Valenzuela, P., & Hussain, S. P. (2022) · Trends in cancer · doi:10.1016/j.trecan.2022.03.004 · Cited by 53 · see citing works

The past, present, and future of enzyme-based therapies

Hennigan, J. N., & Lynch, M. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.09.004 · Cited by 51 · see citing works

Tumor Metabolism-Rewriting Nanomedicines for Cancer Immunotherapy

Dong, X., Xia, S., Du, S., Zhu, M., Lai, X. P., Yao, S. Q., Chen, H., & Fang, C. (2023) · ACS Central Science · doi:10.1021/acscentsci.3c00702 · Cited by 51 · see citing works

How Ah Receptor Ligand Specificity Became Important in Understanding Its Physiological Function

Murray, I. A., & Perdew, G. H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249614 · Cited by 52 · see citing works

Immunometabolism in the Tumor Microenvironment

Roy, D. G., Kaymak, I., Williams, K. S., Ma, E. H., & Jones, R. G. (2020) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030518-055817 · Cited by 48 · see citing works

Targeting metabolic dysfunction of CD8 T cells and natural killer cells in cancer

Viel, S., Vivier, É., Walzer, T., & Marçais, A. (2024) · Nature Reviews Drug Discovery · doi:10.1038/s41573-024-01098-w · Cited by 51 · see citing works

Targeting Metabolism to Control Immune Responses in Cancer and Improve Checkpoint Blockade Immunotherapy

Luby, A., & Alves‐Guerra, M. (2021) · Cancers · doi:10.3390/cancers13235912 · Cited by 47 · see citing works

Targeting Indoleamine Dioxygenase and Tryptophan Dioxygenase in Cancer Immunotherapy: Clinical Progress and Challenges

Peng, X., Zhao, Z., Liu, L., Bai, L., Tong, R., Yang, H., & Zhong, L. (2022) · Drug Design Development and Therapy · doi:10.2147/dddt.s373780 · Cited by 47 · see citing works

Nano-drug delivery systems for T cell-based immunotherapy

Li, R. P., Chen, Z., Li, J., Dai, Z., & Yu, Y. (2022) · Nano Today · doi:10.1016/j.nantod.2022.101621 · Cited by 48 · see citing works

Manipulating the Metabolism to Improve the Efficacy of CAR T-Cell Immunotherapy

Pellegrino, M., Bufalo, F. D., Angelis, B. D., Quintarelli, C., Caruana, I., & de Billy, E. (2020) · Cells · doi:10.3390/cells10010014 · Cited by 46 · see citing works

The Role of Metabolic Enzymes in the Regulation of Inflammation

Godfrey, W. H., & Kornberg, M. D. (2020) · Metabolites · doi:10.3390/metabo10110426 · Cited by 46 · see citing works

Cisplatin Resistance and Redox-Metabolic Vulnerability: A Second Alteration

Wangpaichitr, M., Theodoropoulos, G., Nguyen, D. J. M., Wu, C., Spector, S. A., Feun, L. G., & Savaraj, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147379 · Cited by 44 · see citing works

Bioenzyme-based nanomedicines for enhanced cancer therapy

Ding, M., Zhang, Y., Li, J., & Pu, K. (2022) · Nano Convergence · doi:10.1186/s40580-022-00297-8 · Cited by 44 · see citing works

Metabolites as agents and targets for cancer immunotherapy

Trefny, M. P., Kroemer, G., Zitvogel, L., & Kobold, S. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01227-z · Cited by 48 · see citing works

Discovery of the First Potent IDO1/IDO2 Dual Inhibitors: A Promising Strategy for Cancer Immunotherapy

He, X., He, G., Chu, Z., Wu, H., Wang, J., Ge, Y., Shen, H., Zhang, S., Shan, J., Peng, K., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01305 · Cited by 44 · see citing works

Injectable supramolecular hydrogel co-loading abemaciclib/NLG919 for neoadjuvant immunotherapy of triple-negative breast cancer

Zhu, B., Cai, Y., Zhou, L., Zhao, L., Chen, J., Shan, X., Sun, X., You, Q., Gong, X., Zhang, W., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-55904-z · Cited by 48 · see citing works

Microbial L-asparaginase as a promising enzyme for treatment of various cancers

Darvishi, F., Jahanafrooz, Z., & Mokhtarzadeh, A. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-12086-8 · Cited by 42 · see citing works

Capturing nascent extracellular vesicles by metabolic glycan labeling-assisted microfluidics

Wu, Q., Wang, W., Zhang, C., You, Z., Zeng, Y., Lu, Y., Zhang, S., Li, X., Yang, C. J., & Song, Y. (2023) · Nature Communications · doi:10.1038/s41467-023-42248-9 · Cited by 42 · see citing works

Mutational Activation of the NRF2 Pathway Upregulates Kynureninase Resulting in Tumor Immunosuppression and Poor Outcome in Lung Adenocarcinoma

Fahrmann, J. F., Tanaka, I., Irajizad, E., Mao, X., Dennison, J. B., Murage, E. N., Casabar, J. P., Mayo, J., Peng, Q., Çeliktaş, M., et al. (2022) · Cancers · doi:10.3390/cancers14102543 · Cited by 42 · see citing works

Abstract 3757: Targeting the IDO/TDO pathway through degradation of the immunosuppressive metabolite kynurenine

Coma, S., Cavanaugh, J., Nolan, J., Tchaicha, J. H., McGovern, K., Stone, E. M., Lamb, C., Karamitros, C. S., Blazeck, J., Garrison, K., et al. (2018) · Cancer Research · doi:10.1158/1538-7445.am2018-3757 · Cited by 1 · see citing works

Abstract 5570: A novel approach to targeting the IDO/TDO pathway through degradation of the immunosuppressive metabolite kynurenine

Zhang, M. H., Stone, E. M., Triplett, T., Triplett, K. C., Lamb, C., Karamitros, C. S., Blazeck, J., Georgiou, G., & Manfredi, M. G. (2017) · Cancer Research · doi:10.1158/1538-7445.am2017-5570 · Cited by 7 · see citing works

Abstract 5571: Immune-checkpoint inhibition via enzyme-mediated degradation of kynurenine

Triplett, T., Triplett, K. C., Stone, E. M., Zhang, M. H., Manfredi, M. G., Lamb, C., Tanno, Y., Ehrlich, L. I. R., & Georgiou, G. (2017) · Cancer Research · doi:10.1158/1538-7445.am2017-5571 · Cited by 2 · see citing works

Abstract B008: Treatment of IDO1 and TDO2 positive tumors with a kynurenine-degrading enzyme: A highly differentiated approach from IDO1 inhibition

Coma, S., Cavanaugh, J. D., Nolan, J., Tchaicha, J. H., McGovern, K., Stone, E. M., Blazeck, J., Lamb, C., Georgiou, G., Manfredi, M. G., et al. (2019) · Cancer Immunology Research · doi:10.1158/2326-6074.cricimteatiaacr18-b008

Abstract LB-226: Depletion of kynurenine using an engineered therapeutic enzyme potently inhibits cancer immune checkpoints both as a monotherapy and in combination with anti-PD-1

Stone, E. M., Marshall, N., Donkor, M. K., Triplett, K. C., Blazeck, J., Triplett, T., Ehrlich, L. I. R., & Georgiou, G. (2015) · Cancer Research · doi:10.1158/1538-7445.am2015-lb-226 · Cited by 5 · see citing works