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Differential expression of CD25 (show IL2RA Proteins) and IDO mRNA with high and low virulence bovine viral diarrhea virus might reflect temporal differences in transcription during the immune response elicited by these viral strains.
IDO may be involved in downregulating immune responses to M. avium subsp. paratuberculosis and other virulent mycobacteria, which may be an example of the pathogen harnessing host immunoregulatory pathways to aid survival.
INDO participates in IFN-gama-induced death of bovine luteal cells, through a mechanism that involves degradation of tryptophan, thereby reducing tryptophan concentrations to a point insufficient to meet luteal cells needs
SIV-infected macaques exhibiting progression to AIDS displayed greater expression of TGF-beta (show TGFB1 Proteins) and indoleamine 2,3 dioxygenase in CD8 (show CD8A Proteins)+ T cells from mesentric lymph nodes.
We discuss how small-molecule inhibitors of the tryptophan (Trp (show TBPL1 Proteins)) catabolic enzyme indoleamine 2,3-dioxygenase (IDO) represent a vanguard of new immunometabolic adjuvants to safely enhance the efficacy of cancer immunotherapy, radiotherapy, or 'immunogenic' chemotherapy by leveraging responses to tumor neoantigens
The role of IDO1-IDO2 (show IDO2 Proteins)-AHR (show AHR Proteins) pathway in the TLR4 (show TLR4 Proteins)-induced tolerogenic phenotype in human dendritic cells has been reported.
High coexpression of cytoplasmic IDO1/COX2 was found to be an independent predictor of poor outcome in colorectal cancer patients.
Report the crystal structures of IDO1 in complex with its substrate, Trp (show TBPL1 Proteins), an inhibitor, epacadostat, and/or an effector, indole ethanol (IDE (show IDE Proteins)). The data reveal structural features of the active site (Sa) critical for substrate activation; in addition, they disclose a new inhibitor-binding mode and a distinct small molecule binding site (Si).
IDO decreased glycolysis and glutaminolysis by activating GCN2K, resulting in activation of AMPactivated protein kinase.
Data suggest that IDO1 is constitutively expressed in insulin (show INS Proteins)-secreting cells from donors without diabetes; IDO1 appears to be down-regulated in insulin (show INS Proteins)-containing beta-cells from double autoantibody-positive donors and donors with recent-onset type 1 diabetes; this study was conducted on donor tissues obtained from cadavers.
Twenty-nine percent (n = 2/7) of the PD-L1 (show CD274 Proteins) positive poorly differentiated thyroid carcinomas also co-expressed IDO1
In non-ST segment elevation myocardial infarction, the tolerogenic mechanism of the immune response related to IDO production by activated monocytes derived dendritic cells is altered, supporting their role in T-cell dysregulation.
These data suggest that the expression of immunosuppressive molecules, including PD-1 (show PDCD1 Proteins) ligands and IDO1, by macrophage/microglia may be involved in immune evasion of lymphoma cells.
Our data demonstrate that high intratumoral IDO1 mRNA levels correlate with a poor glioblastoma (GBM) patient prognosis. It also confirms the positive correlation between increased GBM IDO1 levels and human-infiltrating T cells
The treatment of Salmonella enterica serovar choleraesuis or resveratrol in murine melanoma cells demonstrated the ability of reducing IDO1 production through upregulating Cx43 (show GJA1 Proteins).
Study showed that the knockout of IDO prevented vascular smooth muscle cells apoptosis in AngII -treated Ldlr (show LDLR Proteins)-/- mice fed with HFD, suggesting a detrimental role of IDO in abdominal aortic aneurysm formation.
The KYNurenine pathway of IDO1-mediated Tryptophan metabolism plays a critical role in depressive symptoms associated with IFN-alpha (show IFNA Proteins) therapy.
IDO is a critical regulator of acute pulmonary inflammation .
Data suggest that Indoleamine 2,3-dioxygenase 1 (IDO1) appears to be a potential hallmark of liver lesions, and its deficiency protects mice from CCl4 (show CCL4 Proteins)-induced fibrosis mediated by Th17 cells down-regulation and tryptophan 2,3-dioxygenase (TDO (show TDO2 Proteins)) compensatory increase.
Findings suggest non-redundant neurophysiological roles for indoleamine 2,3-dioxygenase 1, indoleamine 2,3-dioxygenase 2 (show IDO2 Proteins) and tryptophan 2,3-dioxygenase (show TDO2 Proteins) in modulating brain activities and metabolism.
These results show IDO is upregulated with RSV infection and this upregulation likely participates with IFN-gamma (show IFNG Proteins) in inhibition of virus replication and suppression of some host cell responses to infection.
Lipopolysaccharide (LPS (show TLR4 Proteins)) stimulation increased the expression and activity of the immunoregulatory enzyme IDO1 in hepatic stellate cells (HSCs), and LPS (show TLR4 Proteins)/HSCs stimulated aryl hydrocarbon receptor (AhR (show AHR Proteins)) signaling in cocultured regulatory T cells.
this study shows that the presence of IFN-alpha (show IFNA Proteins) at antigen sensitization activates an IDO1/TGF-beta (show TGFB1 Proteins)-dependent anti-inflammatory program that upon antigenic rechallenge prevents inflammation via plasmacytoid dendritic cells
Across strains, networks depicted a predominance of genes under-expressed in microglia relative to macrophages that may be a precursor for the different response of both cell types to challenges. The detected transcriptome differences enhance the understanding of the role of IDO1 in the microglia transcriptome under unchallenged conditions.
This gene encodes indoleamine 2,3-dioxygenase (IDO) - a heme enzyme that catalyzes the first and rate-limiting step in tryptophan catabolism to N-formyl-kynurenine. This enzyme acts on multiple tryptophan substrates including D-tryptophan, L-tryptophan, 5-hydroxy-tryptophan, tryptamine, and serotonin. This enzyme is thought to play a role in a variety of pathophysiological processes such as antimicrobial and antitumor defense, neuropathology, immunoregulation, and antioxidant activity. Through its expression in dendritic cells, monocytes, and macrophages this enzyme modulates T-cell behavior by its peri-cellular catabolization of the essential amino acid tryptophan.
indoleamine-pyrrole 2,3 dioxygenase
, indoleamine 2,3-dioxygenase 2
, putative indoleamine 2,3-dioxygenase
, indoleamine 2,3-dioxygenase 1
, indolamine 2,3 dioxygenase
, indole 2,3-dioxygenase
, indoleamine-pyrrole 2,3-dioxygenase
, indoleamine 23-dioxygenase