Results 91 to 100 of about 29,794,370 (246)
Indoleamine 2,3-dioxygenase 1 inhibitors in cancer immunotherapy [PDF]
The indoleamine 2,3-dioxygenase (IDO 1) enzyme is expressed in small amounts in most of the mammalian tissues, and its production is detected also in various types of tumours.
Muffová, Barbora
core
Substrate Oxidation by Indoleamine 2,3-Dioxygenase : EVIDENCE FOR A COMMON REACTION MECHANISM
The kynurenine pathway is the major route of l-tryptophan (l-Trp) catabolism in biology, leading ultimately to the formation of NAD(+). The initial and rate-limiting step of the kynurenine pathway involves oxidation of l-Trp to N-formylkynurenine.
M. Lee (6332354) +4 more
core +6 more sources
The Two Sides of Indoleamine 2,3-Dioxygenase 2 (IDO2)
Indoleamine 2,3-dioxygenase 1 (IDO1) and IDO2 originated from gene duplication before vertebrate divergence. While IDO1 has a well-defined role in immune regulation, the biological role of IDO2 remains unclear.
Chiara Suvieri +2 more
doaj +1 more source
Altered Cerebrospinal Fluid Tryptophan–Kynurenine Pathway Metabolism in Multiple System Atrophy
Abstract Background Alterations in tryptophan–kynurenine (TRP‐KYN) metabolism, which is associated with neuroinflammation, remain unclear in multiple system atrophy (MSA). Objective The aim was to investigate cerebrospinal fluid (CSF) TRP metabolites in MSA and their associations with other biomarkers.
Ryunosuke Nagao +8 more
wiley +1 more source
Peptide‐directed nanovehicles enabling tumor‐selective ROS amplification and antitumor immunity
Cancer cells are vulnerable to oxidative stress, yet exploit immune tolerance to escape destruction. In contrast, their metabolic profile is markedly altered to support rapid proliferation, accompanied by elevated production of reactive oxygen species (ROS).
Manuela Calin +3 more
wiley +1 more source
Human placental indoleamine 2,3-dioxygenase: cellular localization and characterization of an enzyme preventing fetal rejection [PDF]
In order to test the hypothesis (Munn, Zhou, Attwood, Bondarev, Conway, Marshall, Brown, Mellor, Science 281 (1998) 1191–1193) that localized placental tryptophan catabolism prevents immune rejection of the mammalian fetus, the cellular localization and ...
Kudo, Yoshiki, Boyd, C.A.R
core +1 more source
Kaempferol modulates the tryptophan metabolism pathway by increasing the abundances of Christensenellaceae R7 group, Bacteroides, and Blautia and reducing that of Rikenellaceae RC9 gut group, thereby significantly increasing the levels of ILA and IAA. This process inhibits the activation of NF‐κB/NLRP3 signaling pathway, reduces pro‐inflammatory factor
Xiangyu Liu +3 more
wiley +1 more source
Decreased tryptophan catabolism by placental indoleamine 2,3-dioxygenase in preeclampsia.
OBJECTIVE: Tryptophan degradation and depletion resulting from activation of indoleamine 2,3-dioxygenase is characteristic of inflammatory reactions and may control their intensity. Normal third-trimester pregnancy is characterized by a maternal systemic
Sargent, IL +5 more
core +1 more source
Imaging mass cytometry shows lupus panniculitis lesions are dominated by cytotoxic and skin‐homing T cells with abundant macrophages and B‐cell aggregates. Spatial neighborhood analysis reveals organized leukocyte architecture, including B‐cell proximity to naïve T cells and M1 macrophages to cytotoxic T cells.
Milad Ameri +11 more
wiley +1 more source
Modulation of indoleamine 2,3-dioxygenase by interferon-gamma in human placental chorionic villi.
The effect of interferon-gamma on indoleamine 2,3-dioxygenase, a tryptophan catabolizing enzyme, was studied in cultured human placental chorionic villi.
Sargent, IL +4 more
core +1 more source

