Results 201 to 210 of about 18,680 (231)

Mechanism Found for IDO1 Inhibitor Evasion

Cancer Discovery, 2022
Abstract Researchers have pinpointed metabolic alterations that may allow tumors to evade the IDO1 inhibitor epacadostat. Tumor cells enlisted an alternative pathway to break down tryptophan, the target of IDO1, and increased the activity of pathways that generate NAD+. The metabolic changes also suppressed CD8+ T cells.
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The ups, downs and new trends of IDO1 inhibitors

Bioorganic Chemistry, 2021
Cancer immunotherapy has become an emerging driving force in the development of innovative strategies to fight against cancer. Despite the significant clinical benefits that many cancer patients have gained, the generally average response rate of ~ 20% is far behind the expectation for immune checkpoint inhibitors (ICIs).
Shulun, Chen, Jing, Tan, Ao, Zhang
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Abstract B66: Superiority of dual IDO1/TDO2 inhibition versus IDO1 selective inhibition in reducing immunosuppressive KYN levels in tumors co-expressing IDO1 and TDO2

Cancer Immunology Research, 2022
Abstract Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO2) catalyze the oxidation of L-Tryptophan (TRP) leading to the formation of immunosuppressive kynurenine (KYN) pathway metabolites. According to TCGA, a substantial fraction of different tumor types express both IDO1 and TDO2.
Carina Lotz-Jenne, Sylvaine Cren, Christoph Joesch, Sabine Ackerknecht, Jennifer Brandes, Claire Moebs, Dominik Hartl, Felix Hartrampf, Philippe Guerry, Julien Pothier, Alexia Chavanton-Arpel   +10 more
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Abstract 1849: Superiority of dual IDO1/TDO2 inhibition versus IDO1 selective inhibition in reducing immunosuppressive KYN levels in tumors co-expressing IDO1 and TDO2

Cancer Research, 2023
Abstract Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO2) catalyze the oxidation of L-Tryptophan (TRP) leading to the formation of immunosuppressive kynurenine (KYN) pathway metabolites. According to TCGA, a substantial fraction of different tumor types expresses both IDO1 and TDO2.
Carina Lotz-Jenne, Sylvaine Cren, Christoph Joesch, Sabine Ackerknecht, Jennifer Brandes, Claire Moebs, Dominik Hartl, Felix Hartrampf, Philippe Guerry, Julien Pothier, Alexia Chavanton-Arpel   +10 more
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Is IDO1 an adequate target for treatment in glioblastoma?

Journal of Clinical Oncology, 2022
e14039 Background: Glioblastoma (GB) is the most prevalent primary brain tumor in adults. The first-line treatment is based on standard brain surgery and adjuvant radio-chemotherapy. Indoleamine 2,3-dioxygenase 1 (IDO1) is a catabolic enzyme that plays a role in the metabolism of tryptophan (Trp), thereby promoting a state of immunosuppression.
Siancas, CAM, Gonzalez, AH, Domenech, M, Esteve-Codina, A, Arpi, O, Alameda, F, Pineda, E, Chekhun, S, Paradis, AL, Del Barco, S, De la Iglesia, N, Rubio, OG, Mesia, C, Mallo, M, Esteve, A, Carrato, C, Balana, C, Martinez-Garcia, M   +17 more
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IDO1: An important immunotherapy target in cancer treatment

International Immunopharmacology, 2017
Indoleamine 2,3-dioxigenase 1 (IDO1) acts in pathogenic inflammatory processes and engender immune tolerance to tumor antigens. IDO1 can decrease the tryptophan and produce a series of toxic kynurenine metabolites to promote the immune toleration via GCN2 pathway, mTOR pathway, toxic effect of kynurenine and favoring differentiation of Tregs.
Fangxuan, Li, Rupeng, Zhang, Shixia, Li, Juntian, Liu   +3 more
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Alzheimer’s and metabolism wed with IDO1

Science
Kynurenine pathway inhibition reverses deficits in Alzheimer’s mouse ...
Lance A. Johnson, Shannon L. Macauley
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IDO1 expression in glioma molecular subtypes.

Journal of Clinical Oncology, 2018
e14029Background: Indoleamine 2,3-dioxygenase 1 (IDO1), a tryptophan catabolic enzyme is a key mediator of tumor-induced immunosuppression in multiple tumors.
James Snyder, Tathiane M Malta, Houtan Noushmehr   +2 more
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The catalytic inhibitor epacadostat can affect the non-enzymatic function of IDO1

Frontiers in Immunology, 2023
Maria Laura Belladonna, Maria Teresa Pallotta, Giada Mondanelli   +2 more
exaly  

Ido1 induction by human rhinovirus.

We measured total gene expression in human cells following infection separately with two human rhinovirus types: HRV16 and HRV1A. We demonstrate here activation of indoleamine 2,3-dioxygenase 1 encoded by Ido1 in cells following infection with a human rhinovirus.   
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