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Article ; Online: Evaluation of Binding Kinetics and Thermodynamics of Antibody-Antigen Interactions and Interactions Involving Complement Proteins.

Rossini, Sofia / Dimitrov, Jordan D

Methods in molecular biology (Clifton, N.J.)

2021 Volume 2227, Page(s) 237–247

Abstract: The study of kinetics and thermodynamics of protein-protein interactions can contribute to assessment of the mechanism of molecular recognition process. These analyses can provide information about conformational changes and noncovalent forces that ... ...

Abstract	The study of kinetics and thermodynamics of protein-protein interactions can contribute to assessment of the mechanism of molecular recognition process. These analyses can provide information about conformational changes and noncovalent forces that influence the initial recognition between proteins and stabilization of the complex. Studying these aspects may lead to a better comprehension of functions of proteins in biological environment and can become useful for the rational modification of some interactions by engineering of one of the implicated partners. Real-time biosensor assays based on surface plasmon resonance have been widely applied for the label-free evaluation of protein-protein interactions, allowing their characterization in term of binding affinity and kinetics. In the present chapter, we provide a protocol for the assessment of interactions involving complement proteins or antibodies, the protagonists of the immune system. We reported guidelines and indications concerning the analysis of the experimental data for the estimation of the kinetic parameters and for the evaluation of activation and equilibrium binding thermodynamics.
MeSH term(s)	Antibodies/chemistry ; Antibodies/metabolism ; Antigen-Antibody Reactions/physiology ; Biophysical Phenomena ; Biosensing Techniques/methods ; Complement System Proteins/metabolism ; Humans ; Immunoglobulins/chemistry ; Immunoglobulins/metabolism ; Kinetics ; Protein Binding ; Proteins/chemistry ; Proteins/immunology ; Proteins/metabolism ; Surface Plasmon Resonance/methods ; Thermodynamics
Chemical Substances	Antibodies ; Immunoglobulins ; Proteins ; Complement System Proteins (9007-36-7)
Language	English
Publishing date	2021-04-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-1016-9_21
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Article ; Online: Polyamines and Kynurenines at the Intersection of Immune Modulation.

Proietti, Elisa / Rossini, Sofia / Grohmann, Ursula / Mondanelli, Giada

Trends in immunology

2020 Volume 41, Issue 11, Page(s) 1037–1050

Abstract: Polyamines (i.e., putrescine, spermidine, and spermine) are bioactive polycations capable of binding nucleic acids and proteins and modulating signaling pathways. Polyamine functions have been studied most extensively in tumors, where they can promote ... ...

Abstract	Polyamines (i.e., putrescine, spermidine, and spermine) are bioactive polycations capable of binding nucleic acids and proteins and modulating signaling pathways. Polyamine functions have been studied most extensively in tumors, where they can promote cell transformation and proliferation. Recently, spermidine was found to exert protective effects in an experimental model of multiple sclerosis (MS) and to confer immunoregulatory properties on dendritic cells (DCs), via the indoleamine 2,3-dioxygenase 1 (IDO1) enzyme. IDO1 converts l-tryptophan into metabolites, collectively known as kynurenines, endowed with several immunoregulatory effects via activation of the arylhydrocarbon receptor (AhR). Because AhR activation increases polyamine production, the emerging scenario has identified polyamines and kynurenines as actors of an immunoregulatory circuitry with potential implications for immunotherapy in autoimmune diseases and cancer.
MeSH term(s)	Animals ; Autoimmune Diseases/immunology ; Disease Models, Animal ; Humans ; Immunomodulation/immunology ; Kynurenine/immunology ; Multiple Sclerosis/enzymology ; Multiple Sclerosis/immunology ; Polyamines/immunology ; Signal Transduction
Chemical Substances	Polyamines ; Kynurenine (343-65-7)
Language	English
Publishing date	2020-10-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2036831-8
ISSN	1471-4981 ; 1471-4906
ISSN (online)	1471-4981
ISSN	1471-4906
DOI	10.1016/j.it.2020.09.007
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Article ; Online: Interaction of clinical-stage antibodies with heme predicts their physiochemical and binding qualities.

Lecerf, Maxime / Kanyavuz, Alexia / Rossini, Sofia / Dimitrov, Jordan D

Communications biology

2021 Volume 4, Issue 1, Page(s) 391

Abstract: Immunoglobulin repertoires contain a fraction of antibodies that recognize low molecular weight compounds, including some enzymes' cofactors, such as heme. Here, by using a set of 113 samples with variable region sequences matching clinical-stage ... ...

Abstract	Immunoglobulin repertoires contain a fraction of antibodies that recognize low molecular weight compounds, including some enzymes' cofactors, such as heme. Here, by using a set of 113 samples with variable region sequences matching clinical-stage antibodies, we demonstrated that a considerable number of these antibodies interact with heme. Antibodies that interact with heme possess specific sequence traits of their antigen-binding regions. Moreover they manifest particular physicochemical and functional qualities i.e. increased hydrophobicity, higher propensity of self-binding, higher intrinsic polyreactivity and reduced expression yields. Thus, interaction with heme is a strong predictor of different molecular and functional qualities of antibodies. Notably, these qualities are of high importance for therapeutic antibodies, as their presence was associated with failure of drug candidates to reach clinic. Our study reveled an important facet of information about relationship sequence-function in antibodies. It also offers a convenient tool for detection of liabilities of therapeutic antibodies.
MeSH term(s)	Antibodies, Monoclonal/metabolism ; Antibody Specificity ; Binding Sites, Antibody ; Epitopes ; Heme/immunology ; Heme/metabolism ; Immunoglobulin Variable Region/metabolism ; Molecular Docking Simulation ; Protein Binding
Chemical Substances	Antibodies, Monoclonal ; Epitopes ; Immunoglobulin Variable Region ; Heme (42VZT0U6YR)
Language	English
Publishing date	2021-03-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-021-01931-7
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Article ; Online: The catalytic inhibitor epacadostat can affect the non-enzymatic function of IDO1.

Panfili, Eleonora / Mondanelli, Giada / Orabona, Ciriana / Gargaro, Marco / Volpi, Claudia / Belladonna, Maria Laura / Rossini, Sofia / Suvieri, Chiara / Pallotta, Maria Teresa

Frontiers in immunology

2023 Volume 14, Page(s) 1134551

Abstract: Indoleamine 2,3-dioxygenase 1 (IDO1) is a tryptophan metabolizing enzyme chronically activated in many cancer patients and its expression and activity correlate with a poor prognosis. In fact, it acts as an immune regulator and contributes to tumor- ... ...

Abstract	Indoleamine 2,3-dioxygenase 1 (IDO1) is a tryptophan metabolizing enzyme chronically activated in many cancer patients and its expression and activity correlate with a poor prognosis. In fact, it acts as an immune regulator and contributes to tumor-induced immunosuppression by determining tryptophan deprivation and producing immunosuppressive metabolites named kynurenines. These findings made IDO1 an attractive target for cancer immunotherapy and small-molecule inhibitors, such as epacadostat, have been developed to block its enzymatic activity. Although epacadostat was effective in preclinical models and in early phase trials, it gave negative results in a metastatic melanoma randomized phase III study to test the benefit of adding epacadostat to the reference pembrolizumab therapy. However, the reason for the epacadostat failure in this clinical trial has never been understood. Our data suggest that a possible explanation of epacadostat ineffectiveness may rely on the ability of this drug to enhance the other IDO1 immunoregulatory mechanism, involving intracellular signaling function. These findings open up a new perspective for IDO1 inhibitors developed as new anticancer drugs, which should be carefully evaluated for their ability to block not only the catalytic but also the signaling activity of IDO1.
MeSH term(s)	Humans ; Tryptophan/metabolism ; Kynurenine/metabolism ; Oximes/pharmacology ; Melanoma
Chemical Substances	Tryptophan (8DUH1N11BX) ; epacadostat (71596A9R13) ; Kynurenine (343-65-7) ; Oximes
Language	English
Publishing date	2023-04-14
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2023.1134551
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Article ; Online: Epacadostat stabilizes the apo-form of IDO1 and signals a pro-tumorigenic pathway in human ovarian cancer cells.

Rossini, Sofia / Ambrosino, Sara / Volpi, Claudia / Belladonna, Maria Laura / Pallotta, Maria Teresa / Panfili, Eleonora / Suvieri, Chiara / Macchiarulo, Antonio / Mondanelli, Giada / Orabona, Ciriana

Frontiers in immunology

2024 Volume 15, Page(s) 1346686

Abstract: The tryptophan-degrading enzyme indoleamine 2,3-dioxygenase 1 (IDO1) is a plastic immune checkpoint molecule that potently orchestrates immune responses within the tumor microenvironment (TME). As a heme-containing protein, IDO1 catalyzes the conversion ... ...

Abstract	The tryptophan-degrading enzyme indoleamine 2,3-dioxygenase 1 (IDO1) is a plastic immune checkpoint molecule that potently orchestrates immune responses within the tumor microenvironment (TME). As a heme-containing protein, IDO1 catalyzes the conversion of the essential amino acid tryptophan into immunoactive metabolites, called kynurenines. By depleting tryptophan and enriching the TME with kynurenines, IDO1 catalytic activity shapes an immunosuppressive TME. Accordingly, the inducible or constitutive IDO1 expression in cancer correlates with a negative prognosis for patients, representing one of the critical tumor-escape mechanisms. However, clinically trialed IDO1 catalytic inhibitors disappointed the expected anti-tumor efficacy. Interestingly, the non-enzymatic apo-form of IDO1 is still active as a transducing protein, capable of promoting an immunoregulatory phenotype in dendritic cells (DCs) as well as a pro-tumorigenic behavior in murine melanoma. Moreover, the IDO1 catalytic inhibitor epacadostat can induce a tolerogenic phenotype in plasmacytoid DCs, overcoming the catalytic inhibition of IDO1. Based on this recent evidence, IDO1 plasticity was investigated in the human ovarian cancer cell line, SKOV-3, that constitutively expresses IDO1 in a dynamic balance between the holo- and apo-protein, and thus potentially endowed with a dual function (i.e., enzymatic and non-enzymatic). Besides inhibiting the catalytic activity, epacadostat persistently stabilizes the apo-form of IDO1 protein, favoring its tyrosine-phosphorylation and promoting its association with the phosphatase SHP-2. In SKOV-3 cells, both these early molecular events activate a signaling pathway transduced by IDO1 apo-protein, which is independent of its catalytic activity and contributes to the tumorigenic phenotype of SKOV-3 cells. Overall, our findings unveiled a new mechanism of action of epacadostat on IDO1 target, repositioning the catalytic inhibitor as a stabilizer of the apo-form of IDO1, still capable of transducing a pro-tumorigenic pathway in SKOV-3 tumor. This mechanism could contribute to clarify the lack of effectiveness of epacadostat in clinical trials and shed light on innovative immunotherapeutic strategies to tackle IDO1 target.
MeSH term(s)	Female ; Humans ; Animals ; Mice ; Tryptophan/metabolism ; Ovarian Neoplasms/drug therapy ; Kynurenine/metabolism ; Sulfonamides ; Enzyme Inhibitors/pharmacology ; Carcinogenesis ; Tumor Microenvironment ; Oximes
Chemical Substances	Tryptophan (8DUH1N11BX) ; epacadostat (71596A9R13) ; Kynurenine (343-65-7) ; Sulfonamides ; Enzyme Inhibitors ; Oximes
Language	English
Publishing date	2024-01-25
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2024.1346686
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Article ; Online: Indoleamine 2,3‐dioxygenase 1 (IDO1): an up‐to‐date overview of an eclectic immunoregulatory enzyme

Pallotta, Maria Teresa / Rossini, Sofia / Suvieri, Chiara / Coletti, Alice / Orabona, Ciriana / Macchiarulo, Antonio / Volpi, Claudia / Grohmann, Ursula

The FEBS Journal. 2022 Oct., v. 289, no. 20 p.6099-6118

2022

Abstract: Indoleamine 2,3‐dioxygenase 1 (IDO1) catalyzes the initial rate‐limiting step in the degradation of the essential amino acid tryptophan along the kynurenine pathway. When discovered more than 50 years ago, IDO1 was thought to be an effector molecule ... ...

Abstract	Indoleamine 2,3‐dioxygenase 1 (IDO1) catalyzes the initial rate‐limiting step in the degradation of the essential amino acid tryptophan along the kynurenine pathway. When discovered more than 50 years ago, IDO1 was thought to be an effector molecule capable of mediating a survival strategy based on the deprivation of bacteria and tumor cells of the essential amino acid tryptophan. Since 1998, when tryptophan catabolism was discovered to be crucially involved in the maintenance of maternal T‐cell tolerance, IDO1 has become the focus of several laboratories around the world. Indeed, IDO1 is now considered as an authentic immune regulator not only in pregnancy, but also in autoimmune diseases, chronic inflammation, and tumor immunity. However, in the last years, a bulk of new information—including structural, biological, and functional evidence—on IDO1 has come to light. For instance, we now know that IDO1 has a peculiar conformational plasticity and, in addition to a complex and highly regulated catalytic activity, is capable of performing a nonenzymic function that reprograms the expression profile of immune cells toward a highly immunoregulatory phenotype. With this state‐of‐the‐art review, we aimed at gathering the most recent information obtained for this eclectic protein as well as at highlighting the major unresolved questions.
Keywords	T-lymphocytes ; catabolism ; catalytic activity ; essential amino acids ; immunomodulation ; indoleamine 2,3-dioxygenase ; inflammation ; kynurenine pathway ; neoplasms ; phenotype ; pregnancy ; reaction kinetics ; tryptophan
Language	English
Dates of publication	2022-10
Size	p. 6099-6118.
Publishing place	John Wiley & Sons, Ltd
Document type	Article ; Online
Note	REVIEW
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.16086
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: V Region of IgG Controls the Molecular Properties of the Binding Site for Neonatal Fc Receptor.

Rossini, Sofia / Noé, Rémi / Daventure, Victoria / Lecerf, Maxime / Justesen, Sune / Dimitrov, Jordan D

Journal of immunology (Baltimore, Md. : 1950)

2020 Volume 205, Issue 10, Page(s) 2850–2860

Abstract: Neonatal Fc receptor (FcRn) has a key role in the homeostasis of IgG. Despite its physiological and clinical importance, the interaction of IgG and FcRn remains not completely comprehended. Thus, IgG molecules with identical constant portions but with ... ...

Abstract	Neonatal Fc receptor (FcRn) has a key role in the homeostasis of IgG. Despite its physiological and clinical importance, the interaction of IgG and FcRn remains not completely comprehended. Thus, IgG molecules with identical constant portions but with minor differences in their V regions have been demonstrated to interact with FcRn with a considerable heterogeneity in the binding affinity. To understand this discrepancy, we dissected the physicochemical mechanism of the interaction of 10 human IgG1 to human FcRn. The interactions of two Abs in the presence of their cognate Ags were also examined. Data from activation and equilibrium thermodynamics analyses as well as pH dependence of the kinetics revealed that the V region of IgG could modulate a degree of conformational changes and binding energy of noncovalent contacts at the FcRn binding interface. These results suggest that the V domains modulate FcRn binding site in Fc by allosteric effects. These findings contribute for a deeper understanding of the mechanism of IgG-FcRn interaction. They might also be of relevance for rational engineering of Abs for optimizing their pharmacokinetic properties.
MeSH term(s)	Allosteric Regulation/immunology ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/metabolism ; Antigens/metabolism ; Binding Sites ; Histocompatibility Antigens Class I/chemistry ; Histocompatibility Antigens Class I/metabolism ; Humans ; Hydrogen-Ion Concentration ; Immunoglobulin G/chemistry ; Immunoglobulin G/metabolism ; Protein Binding/immunology ; Protein Domains/immunology ; Receptors, Fc/chemistry ; Receptors, Fc/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Thermodynamics
Chemical Substances	Antibodies, Monoclonal ; Antigens ; Histocompatibility Antigens Class I ; Immunoglobulin G ; Receptors, Fc ; Recombinant Proteins ; Fc receptor, neonatal (TW3XAW0RCY)
Language	English
Publishing date	2020-10-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.2000732
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Article ; Online: A back-door insight into the modulation of Src kinase activity by the polyamine spermidine.

Rossini, Sofia / Gargaro, Marco / Scalisi, Giulia / Bianconi, Elisa / Ambrosino, Sara / Panfili, Eleonora / Volpi, Claudia / Orabona, Ciriana / Macchiarulo, Antonio / Fallarino, Francesca / Mondanelli, Giada

eLife

2023 Volume 12

Abstract: Src is a protein tyrosine kinase commonly activated downstream of transmembrane receptors and plays key roles in cell growth, migration, and survival signaling pathways. In conventional dendritic cells (cDCs), Src is involved in the activation of the non- ...

Abstract	Src is a protein tyrosine kinase commonly activated downstream of transmembrane receptors and plays key roles in cell growth, migration, and survival signaling pathways. In conventional dendritic cells (cDCs), Src is involved in the activation of the non-enzymatic functions of indoleamine 2,3-dioxygenase 1 (IDO1), an immunoregulatory molecule endowed with both catalytic activity and signal transducing properties. Prompted by the discovery that the metabolite spermidine confers a tolerogenic phenotype on cDCs that is dependent on both the expression of IDO1 and the activity of Src kinase, we here investigated the spermidine mode of action. We found that spermidine directly binds Src in a previously unknown allosteric site located on the backside of the SH2 domain and thus acts as a positive allosteric modulator of the enzyme. Besides confirming that Src phosphorylates IDO1, here we showed that spermidine promotes the protein-protein interaction of Src with IDO1. Overall, this study may pave the way toward the design of allosteric modulators able to switch on/off the Src-mediated pathways, including those involving the immunoregulatory protein IDO1.
MeSH term(s)	src-Family Kinases/metabolism ; Spermidine/pharmacology ; Polyamines ; Phosphorylation ; Signal Transduction ; src Homology Domains
Chemical Substances	src-Family Kinases (EC 2.7.10.2) ; Spermidine (U87FK77H25) ; Polyamines
Language	English
Publishing date	2023-06-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.85872
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Article ; Online: Membrane Localization and Phosphorylation of Indoleamine 2,3-Dioxygenase 2 (IDO2) in A549 Human Lung Adenocarcinoma Cells: First Steps in Exploring Its Signaling Function.

Suvieri, Chiara / De Marchis, Francesca / Mandarano, Martina / Ambrosino, Sara / Rossini, Sofia / Mondanelli, Giada / Gargaro, Marco / Panfili, Eleonora / Orabona, Ciriana / Pallotta, Maria Teresa / Belladonna, Maria Laura / Volpi, Claudia

International journal of molecular sciences

2023 Volume 24, Issue 22

Abstract: Indoleamine 2,3-dioxygenase 2 (IDO2) is a paralog of Indoleamine 2,3-dioxygenase 1 (IDO1), a tryptophan-degrading enzyme producing immunomodulatory molecules. However, the two proteins are unlikely to carry out the same functions. IDO2 shows little or no ...

Abstract	Indoleamine 2,3-dioxygenase 2 (IDO2) is a paralog of Indoleamine 2,3-dioxygenase 1 (IDO1), a tryptophan-degrading enzyme producing immunomodulatory molecules. However, the two proteins are unlikely to carry out the same functions. IDO2 shows little or no tryptophan catabolic activity and exerts contrasting immunomodulatory roles in a context-dependent manner in cancer and autoimmune diseases. The recently described potential non-enzymatic activity of IDO2 has suggested its possible involvement in alternative pathways, resulting in either pro- or anti-inflammatory effects in different models. In a previous study on non-small cell lung cancer (NSCLC) tissues, we found that IDO2 expression revealed at the plasma membrane level of tumor cells was significantly associated with poor prognosis. In this study, the A549 human cell line, basally expressing IDO2, was used as an in vitro model of human lung adenocarcinoma to gain more insights into a possible alternative function of IDO2 different from the catalytic one. In these cells, immunocytochemistry and isopycnic sucrose gradient analyses confirmed the IDO2 protein localization in the cell membrane compartment, and the immunoprecipitation of tyrosine-phosphorylated proteins revealed that kinase activities can target IDO2. The different localization from the cytosolic one and the phosphorylation state are the first indications for the signaling function of IDO2, suggesting that the IDO2 non-enzymatic role in cancer cells is worthy of deeper understanding.
MeSH term(s)	Humans ; Indoleamine-Pyrrole 2,3,-Dioxygenase/metabolism ; Phosphorylation ; Carcinoma, Non-Small-Cell Lung ; Lung Neoplasms ; Tryptophan/metabolism ; Adenocarcinoma of Lung
Chemical Substances	Indoleamine-Pyrrole 2,3,-Dioxygenase ; Tryptophan (8DUH1N11BX)
Language	English
Publishing date	2023-11-12
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms242216236
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Article ; Online: Indoleamine 2,3-dioxygenase 1 (IDO1): an up-to-date overview of an eclectic immunoregulatory enzyme.

Pallotta, Maria Teresa / Rossini, Sofia / Suvieri, Chiara / Coletti, Alice / Orabona, Ciriana / Macchiarulo, Antonio / Volpi, Claudia / Grohmann, Ursula

The FEBS journal

2021 Volume 289, Issue 20, Page(s) 6099–6118

Abstract: Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the initial rate-limiting step in the degradation of the essential amino acid tryptophan along the kynurenine pathway. When discovered more than 50 years ago, IDO1 was thought to be an effector molecule ... ...

Abstract	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the initial rate-limiting step in the degradation of the essential amino acid tryptophan along the kynurenine pathway. When discovered more than 50 years ago, IDO1 was thought to be an effector molecule capable of mediating a survival strategy based on the deprivation of bacteria and tumor cells of the essential amino acid tryptophan. Since 1998, when tryptophan catabolism was discovered to be crucially involved in the maintenance of maternal T-cell tolerance, IDO1 has become the focus of several laboratories around the world. Indeed, IDO1 is now considered as an authentic immune regulator not only in pregnancy, but also in autoimmune diseases, chronic inflammation, and tumor immunity. However, in the last years, a bulk of new information-including structural, biological, and functional evidence-on IDO1 has come to light. For instance, we now know that IDO1 has a peculiar conformational plasticity and, in addition to a complex and highly regulated catalytic activity, is capable of performing a nonenzymic function that reprograms the expression profile of immune cells toward a highly immunoregulatory phenotype. With this state-of-the-art review, we aimed at gathering the most recent information obtained for this eclectic protein as well as at highlighting the major unresolved questions.
MeSH term(s)	Immune Tolerance ; Immunity ; Indoleamine-Pyrrole 2,3,-Dioxygenase/metabolism ; Kynurenine/metabolism ; Tryptophan/metabolism
Chemical Substances	Indoleamine-Pyrrole 2,3,-Dioxygenase ; Kynurenine (343-65-7) ; Tryptophan (8DUH1N11BX)
Language	English
Publishing date	2021-06-30
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.16086
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