GoPubMed Proteins lists recent and important papers and reviews for
proteins. Page last changed on 14 Mar 2013.
Indoleamine 2,3-dioxygenase 1
Indo, indoleamine 2,3-dioxygenase, IDO
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.[provided by RefSeq, Feb 2011] (from
NCBI)
Papers using
Indo
antibodies
To reg or not to reg: that is the question in COPD.
Supplier
In PLoS ONE, 2007
... , the following molecules were added after T cell activation: indoleamine-2,3-dioxygenase-1 (IDO) inhibitor (L-1-methyl-tryptophan, L-1MT - Sigma Aldrich) [1 mM]; inhibitor of ...
MicroRNA-binding viral protein interferes with Arabidopsis development
Supplier
In Nucleic Acids Research, 2004
... This work was supported by the Swiss National Science Foundation, the Indo-Swiss Collaboration in Biotechnology, the Swiss Office for Education and Science as part of the EU Gene Silencing in Transgenic Plants Projects, and by ...
Inhibition of Allogeneic T Cell Proliferation by Indoleamine 2,3-Dioxygenase–expressing Dendritic Cells
Supplier
In The Journal of Experimental Medicine, 1994
... Finally, the linearized recombinant IDO plasmid was transfected by Effectene Transfection Reagent kit (QIAGEN) into adenovirus packaging cells ...
Papers on
Indo
Benznidazole treatment reduces the induction of indoleamine 2, 3-dioxygenase (IDO) enzymatic activity in Chagas disease symptomatic patients.
New
Granada, Spain. In Parasite Immunol, 08 Apr 2013
The enzyme indoleamine 2,3-dioxigenase (IDO) is critical for the regulation of immune responses in pro-tolerogenic APC.
Metabolites of tryptophan catabolism are elevated in sera of patients with myelodysplastic syndromes and inhibit hematopoietic progenitor amplification.
New
Lille, France. In Leuk Res, 28 Mar 2013
Tryptophan catabolism, which is mediated by the enzymes indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO), produces kynurenine.
The ratio between dendritic cells and T cells determines whether prostaglandin E2 has a stimulatory or inhibitory effect.
New
Köln, Germany. In Cell Immunol, 01 Mar 2013
The inhibitory function of PGE2-treated DCs depended primarily on the PGE2-induced induction of indoleamine 2,3-dioxygenase competence.
Remarkable role of indoleamine 2,3-dioxygenase and tryptophan metabolites in infectious diseases: potential role in macrophage-mediated inflammatory diseases.
New
Kyoto, Japan. In Mediators Inflamm, Dec 2012
Indoleamine 2,3-dioxygenase 1 (IDO1), the L-tryptophan-degrading enzyme, plays a key role in the immunomodulatory effects on several types of immune cells.
Projected Near-Future Levels of Temperature and pCO2 Reduce Coral Fertilization Success.
New
Townsville, Australia. In Plos One, Dec 2012
Here we show that increases in temperature (+3°C) and CO (+400 µatm) projected for this century negatively impact fertilization success of a common Indo-Pacific coral species, .
The kynurenine pathway in brain tumor pathogenesis.
Review
New
Sydney, Australia. In Cancer Res, Dec 2012
The enzyme indoleamine 2, 3-dioxygenase (IDO-1) initiates and regulates the first step of the KP in most cells.
Tryptophan catabolism in cancer: beyond IDO and tryptophan depletion.
Review
New
Heidelberg, Germany. In Cancer Res, Dec 2012
It has been proposed that the essential amino acid tryptophan is catabolized in the tumor tissue by the rate-limiting enzyme indoleamine-2,3-dioxygenase (IDO) expressed in tumor cells or antigen-presenting cells.
Jack of all trades: thymosin α1 and its pleiotropy.
Review
New
Perugia, Italy. In Ann N Y Acad Sci, Oct 2012
Additionally, the ability of Tα1 to activate the indoleamine 2,3-dioxygenase enzyme-which confers immune tolerance during transplantation and restrains the vicious circle of chronic inflammation-has been a turning point, suggesting a potential, specific function in immunity.
Opposing biological functions of tryptophan catabolizing enzymes during intracellular infection.
GeneRIF
Cincinnati, United States. In J Infect Dis, 2012
IDO-1 and IDO-2 play biologically important, contradictory roles during intracellular protozoal infection - facilitating (Toxoplasma gondii) or suppressing (Leishmania major) microbial clearance in a pathogen-specific manner.
IDO and regulatory T cell support are critical for cytotoxic T lymphocyte-associated Ag-4 Ig-mediated long-term solid organ allograft survival.
GeneRIF
Innsbruck, Austria. In J Immunol, 2012
CTLA4Ig-induced tolerance to murine cardiac allografts is critically dependent on synergistic cross-linked interplay of IDO and Tregs.
Toll-like receptor-3 ligation-induced indoleamine 2, 3-dioxygenase expression in human trophoblasts.
GeneRIF
Tokyo, Japan. In Endocrinology, 2011
ligation of TLR-3 by poly(I:C) induces IDO expression in human first-trimester trophoblasts via an IFN-beta-dependent pathway
Host indoleamine 2,3-dioxygenase: contribution to systemic acquired tumor tolerance.
Review
Augusta, United States. In Immunol Invest, 2011
Indoleamine 2,3-dioxygenase (IDO) is a natural mechanism of creating acquired tolerance in a variety of physiological settings.
Indoleamine 2,3-dioxygenase and dendritic cell tolerogenicity.
Review
Buffalo, United States. In Immunol Invest, 2011
This article summarizes the molecular and cellular mechanisms that regulate the activity of indoleamine 2,3-dioxygenase (IDO), a potent immune-suppressive enzyme, in dendritic cells (DCs).
Highlights of 10 years of immunology in Nature Reviews Immunology.
Impact
New Haven, United States. In Nat Rev Immunol, 2011
Highlights include our improved understanding of Toll-like receptor signalling, and of immune regulation mediated by regulatory T cells, indoleamine 2,3-dioxygenase, myeloid-derived suppressor cells and interleukin-10.
Indoleamine 2,3-dioxygenase is a signaling protein in long-term tolerance by dendritic cells.
Impact
GeneRIF
Perugia, Italy. In Nat Immunol, 2011
Indoleamine 2,3-dioxygenase is a signaling protein in long-term tolerance by dendritic cells.
Imatinib potentiates antitumor T cell responses in gastrointestinal stromal tumor through the inhibition of Ido.
Impact
New York City, United States. In Nat Med, 2011
Imatinib therapy activated CD8(+) T cells and induced regulatory T cell (T(reg) cell) apoptosis within the tumor by reducing tumor-cell expression of the immunosuppressive enzyme indoleamine 2,3-dioxygenase (Ido).
Reprogrammed foxp3(+) regulatory T cells provide essential help to support cross-presentation and CD8(+) T cell priming in naive mice.
Impact
Augusta, United States. In Immunity, 2011
In hosts with established tumors, Treg cell reprogramming was suppressed by tumor-induced indoleamine 2,3-dioxygenase (IDO) and vaccination failed because of lack of help.
Identification of a variable number of tandem repeats polymorphism and characterization of LEF-1 response elements in the promoter of the IDO1 gene.
GeneRIF
Lille, France. In Plos One, 2010
identification of a variable number of tandem repeats polymorphism in IDO1 promoter and characterization of LEF-1 response elements
Involvement of indoleamine 2,3-dioxygenase in impairing tumor-infiltrating CD8 T-cell functions in esophageal squamous cell carcinoma.
GeneRIF
Guangzhou, China. In Clin Dev Immunol, 2010
high expression in esophageal squamous cell carcinoma correlates with impaired overall survival time
Reversal of autoimmunity by boosting memory-like autoregulatory T cells.
Impact
Calgary, Canada. In Immunity, 2010
pMHC-NP-expanded autoregulatory T cells suppressed local presentation of autoantigens in an interferon-gamma-, indoleamine 2,3-dioxygenase-, and perforin-dependent manner.
