PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32468023-3 2020 The present study aimed to investigate methods with which to amplify and enhance the antitumor immune response of a DC-based tumor vaccine by silencing the expression of indoleamine 2,3-dioxygenase 2 (IDO2), a tryptophan rate-limiting metabolic enzyme in DCs. Tryptophan 210-220 indoleamine 2,3-dioxygenase 2 Mus musculus 170-199 32468023-8 2020 On the whole, the present study provides evidence that the silencing of the tryptophan rate-limiting metabolic enzyme, IDO2, has the potential to enhance the efficacy of DC-based cancer immunotherapy. Tryptophan 76-86 indoleamine 2,3-dioxygenase 2 Mus musculus 119-123 32752186-2 2020 IDO2 is an isoform of IDO1, recently identified as a catalytic enzyme in the tryptophan-kynurenine pathway, which is expressed in dendritic cells and monocytes. Tryptophan 77-87 indoleamine 2,3-dioxygenase 2 Mus musculus 0-4 30374077-1 2018 Indoleamine 2,3-dioxygenase 2 (Ido2) is a recently identified catalytic enzyme in the tryptophan-kynurenine pathway that is expressed primarily in monocytes and dendritic cells. Tryptophan 86-96 indoleamine 2,3-dioxygenase 2 Mus musculus 0-29 31444833-2 2019 To date, 3 types of tryptophan-metabolizing enzymes have been identified: indoleamine 2,3-dioxygenase 1 and 2 (IDO1 and IDO2) and tryptophan 2,3-dioxygenase 2. Tryptophan 20-30 indoleamine 2,3-dioxygenase 2 Mus musculus 120-124 31444833-4 2019 Recently, IDO2 has been identified as a tryptophan-metabolizing enzyme that is involved in several immune functions and expressed in cancers such as pancreatic cancer. Tryptophan 40-50 indoleamine 2,3-dioxygenase 2 Mus musculus 10-14 31444833-8 2019 Furthermore, Ido2 depletion altered the tumor microenvironment, such as tryptophan accumulation and kynurenine reduction, leading to enhancement of immune cell invasion. Tryptophan 72-82 indoleamine 2,3-dioxygenase 2 Mus musculus 13-17 30403776-2 2019 Tryptophan depletion in pregnancy is facilitated by increased activity of tryptophan-depleting enzymes [i.e. the indolamine-2,3 dioxygenase (IDO)1 and IDO2) in the placenta. Tryptophan 0-10 indoleamine 2,3-dioxygenase 2 Mus musculus 151-155 30403776-2 2019 Tryptophan depletion in pregnancy is facilitated by increased activity of tryptophan-depleting enzymes [i.e. the indolamine-2,3 dioxygenase (IDO)1 and IDO2) in the placenta. Tryptophan 74-84 indoleamine 2,3-dioxygenase 2 Mus musculus 151-155 29241670-2 2018 Induction of immune and stress pathways is accompanied by increased tryptophan entry into the Kynurenine (Kyn) Pathway as governed by the rate-limiting enzymes indoleamine/tryptophan 2,3-dioxygenases (DO"s: Ido1, Ido2, Tdo2). Tryptophan 68-78 indoleamine 2,3-dioxygenase 2 Mus musculus 213-217 29520368-3 2017 Tryptophan entry into this pathway is controlled by rate-limiting indoleamine/tryptophan 2,3-dioxygenases (DOs: Ido1, Ido2, Tdo2). Tryptophan 0-10 indoleamine 2,3-dioxygenase 2 Mus musculus 118-122 29051706-1 2017 Indoleamine 2,3-dioxygenase-2 (IDO2) is 1 of the 3 enzymes that can catalyze the first step in the kynurenine pathway of tryptophan metabolism. Tryptophan 121-131 indoleamine 2,3-dioxygenase 2 Mus musculus 0-29 29051706-1 2017 Indoleamine 2,3-dioxygenase-2 (IDO2) is 1 of the 3 enzymes that can catalyze the first step in the kynurenine pathway of tryptophan metabolism. Tryptophan 121-131 indoleamine 2,3-dioxygenase 2 Mus musculus 31-35 29051706-6 2017 Our analysis, undertaken in Ido2 +/+ and Ido2-/- mice using immunohistochemistry and measurement of tryptophan and kynurenine levels, suggested an even more restricted pattern of tissue expression than previously reported. Tryptophan 100-110 indoleamine 2,3-dioxygenase 2 Mus musculus 41-45 27316339-2 2016 Tissue concentrations of tryptophan are regulated primarily by the enzymes indoleamine 2,3-dioxygenase 1 (IDO1), IDO2 and tryptophan 2,3-dioxygenase (TDO, encoded by TDO2). Tryptophan 25-35 indoleamine 2,3-dioxygenase 2 Mus musculus 113-117 26269528-3 2015 In view of recent observations, and taking into account the differences between human and mouse data that differ in several aspects, in this Cancer Immunology at the Crossroads article, we discuss the role of the three enzymes that have been proposed to control tryptophan catabolism in tumoral immune resistance: indoleamine 2,3-dioxygenase 1 (IDO1), tryptophan 2,3-dioxygenase (TDO), and indoleamine 2,3-dioxygenase 2 (IDO2). Tryptophan 262-272 indoleamine 2,3-dioxygenase 2 Mus musculus 390-419 27058624-1 2016 Indoleamine 2,3-dioxygenase 2 (IDO2) is a newly discovered enzyme that catalyzes the initial and rate-limiting step in the degradation of tryptophan. Tryptophan 138-148 indoleamine 2,3-dioxygenase 2 Mus musculus 0-29 27058624-1 2016 Indoleamine 2,3-dioxygenase 2 (IDO2) is a newly discovered enzyme that catalyzes the initial and rate-limiting step in the degradation of tryptophan. Tryptophan 138-148 indoleamine 2,3-dioxygenase 2 Mus musculus 31-35 26914138-13 2016 We hypothesize that other tryptophan-catabolizing enzymes like IDO2 and tryptophan 2,3-dioxygenase (TDO) might compensate for the lack of IDO1. Tryptophan 26-36 indoleamine 2,3-dioxygenase 2 Mus musculus 63-67 26459907-9 2016 Notably, methionine 385 of IDO-2 was identified to interfere with the entrance of l-tryptophan to the active site of the enzyme, which explains the selectivity of the inhibitors. Tryptophan 82-94 indoleamine 2,3-dioxygenase 2 Mus musculus 27-32 26269528-3 2015 In view of recent observations, and taking into account the differences between human and mouse data that differ in several aspects, in this Cancer Immunology at the Crossroads article, we discuss the role of the three enzymes that have been proposed to control tryptophan catabolism in tumoral immune resistance: indoleamine 2,3-dioxygenase 1 (IDO1), tryptophan 2,3-dioxygenase (TDO), and indoleamine 2,3-dioxygenase 2 (IDO2). Tryptophan 262-272 indoleamine 2,3-dioxygenase 2 Mus musculus 421-425 25408380-1 2015 Ido2 is involved in tryptophan catabolism and immunity, but its physiological functions remain poorly understood. Tryptophan 20-30 indoleamine 2,3-dioxygenase 2 Mus musculus 0-4 24402311-1 2014 IDO2 is implicated in tryptophan catabolism and immunity but its physiological functions are not well established. Tryptophan 22-32 indoleamine 2,3-dioxygenase 2 Mus musculus 0-4 24904580-6 2014 It remains to be evaluated whether other enzymes mediating Trp oxidation, such as indoleamine 2,3-dioxygenase-2, Trp 2,3-dioxygenase, and Trp hydroxylase-1 are of relevance to the biology of the placenta. Tryptophan 59-62 indoleamine 2,3-dioxygenase 2 Mus musculus 82-111 17499941-8 2007 We demonstrate that INDOL1 catalyses the conversion of tryptophan to kynurenine therefore a more appropriate nomenclature for the enzymes might be INDO-1 and INDO-2, or the more commonly-used abbreviations, IDO-1 and IDO-2. Tryptophan 55-65 indoleamine 2,3-dioxygenase 2 Mus musculus 20-26 17499941-8 2007 We demonstrate that INDOL1 catalyses the conversion of tryptophan to kynurenine therefore a more appropriate nomenclature for the enzymes might be INDO-1 and INDO-2, or the more commonly-used abbreviations, IDO-1 and IDO-2. Tryptophan 55-65 indoleamine 2,3-dioxygenase 2 Mus musculus 217-222 34965962-1 2022 IDO2 is one of two closely related tryptophan catabolizing enzymes induced under inflammatory conditions. Tryptophan 35-45 indoleamine 2,3-dioxygenase 2 Mus musculus 0-4 32973768-1 2020 Indoleamine-2,3-dioxygenase (IDO)1 and IDO2 are two closely related tryptophan catabolizing enzymes encoded by linked genes. Tryptophan 68-78 indoleamine 2,3-dioxygenase 2 Mus musculus 39-43