Results 171 to 180 of about 18,349 (196)

Indoleamine 2,3-dioxygenase, immunosuppression and pregnancy

Journal of Reproductive Immunology, 2002
Pharmacologic inhibition of indoleamine 2,3-dioxygenase (IDO) activity during murine pregnancy results in maternal T-cell-mediated rejection of allogeneic but not syngeneic conceptuses. Increased risk of allogeneic pregnancy failure induced by exposure to IDO inhibitor is strongly correlated with maternal C3 deposition at the maternal-fetal interface ...
Andrew L, Mellor, Phillip, Chandler, Geon Kook, Lee, Theodore, Johnson, Derin B, Keskin, Jeffrey, Lee, David H, Munn   +6 more
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Posttranslational modification of indoleamine 2,3-dioxygenase

Analytical and Bioanalytical Chemistry, 2012
Protein posttranslational modifications (PTMs) perform essential roles in the biological regulation of a cell. PTMs are extremely important because they can change a protein's physical or chemical properties, conformation, activity, cellular location, or stability.
Hidetsugu, Fujigaki, Mitsuru, Seishima, Kuniaki, Saito   +2 more
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Placental expression of indoleamine 2,3-dioxygenase

Wiener Medizinische Wochenschrift, 2012
This review focuses on the placental expression of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase-1 (IDO1) and its potential roles, which may not only encompass immunosuppression and antimicrobial activity, but also vasodilation based on the endothelial expression on both sides of the feto-maternal interface.
Peter, Sedlmayr, Astrid, Blaschitz
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Evolution of Vertebrate Indoleamine 2,3-Dioxygenases

Journal of Molecular Evolution, 2007
Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that catalyze the same reaction, the first step in tryptophan catabolism via the kynurenine pathway. TDO is widely distributed among life-forms, being found not only in eukaryotes but also in bacteria.
Hajime Julie, Yuasa, Miwa, Takubo, Ayumi, Takahashi, Tetsuo, Hasegawa, Hiroshi, Noma, Tomohiko, Suzuki   +5 more
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Indoleamine 2,3-Dioxygenase in Lung Allograft Tolerance

The Journal of Heart and Lung Transplantation, 2009
Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in the degradation of tryptophan (Try) to kynurenine (Kyn), is thought to suppress T-cell activity. Although a few experimental studies have suggested a role for IDO in graft acceptance, human data are scarce and inconclusive.
MELONI, FEDERICA, GIULIANO, SERENA, SOLARI, NADIA, DRAGHI, PAOLA, MISERERE, SIMONA MARGHERITA, BARDONI, ANNA MARIA, SALVINI, ROBERTA, BINI, FRANCESCO, FIETTA, ANNA MARIA   +8 more
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Indoleamine 2,3-dioxygenase

Indoleamine 2,3-dioxygenases, or IDOs, are the main enzymes responsible for the metabolism of l-Tryptophan (Trp), and the open gate of the kynurenine pathway, where the majority of the intake of the essential amino acid is conveyed. The kynurenine pathway produces a great variety of molecules, involved in a great spectrum of physio-pathological ...
Coluccia, Michele, Secci, Daniela, Guglielmi, Paolo   +2 more
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Copper Content of Indoleamine 2,3-Dioxygenase

1976
Indoleamine 2,3-dioxygenase is a hemoprotein which catalyzes the oxygenative ring cleavage of substituted and unsubstituted indoleamines such as tryptophan, 5-hydroxytryptophan, tryptamine and serotonin (1). This enzyme utilizes superoxide anion (O2 -) as an oxidizing agent (2).
F. Hirata, T. Shimizu, R. Yoshida, T. Ohnishi, M. Fujiwara, O. Hayaishi   +5 more
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Indoleamine 2,3-dioxygenase, Tregs and Cancer

Current Medicinal Chemistry, 2011
The IDO pathway is implicated in a number of settings which lead to acquired peripheral tolerance. One such setting may be the functional tolerance displayed by tumor-bearing hosts toward tumor-associated antigens. Foxp3(+) Tregs are now recognized as a major contributor to tumor-induced immune suppression and functional tolerance.
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Recombinant human indoleamine 2,3-dioxygenase

2022
Indoleamine 2,3-dioxygenase (IDO) is a heme-containing dioxygenase that catalyses the first and rate-limiting step in the kynurenine (Kyn) pathway of L-tryptophan (L-Trp)catabolism. Attention has been focused on IDO because the Kyn metabolic pathway is involved in a variety of physiological functions and diseases.
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A myoglobin evolved from indoleamine 2,3-dioxygenase

Journal of Molecular Biology, 1992
Hemoglobins and myoglobins are some of the best studied proteins. They are distributed in animals, plants and bacteria, and the characteristic two intron-three exon structure is widely conserved in animal globin genes (Jhiang et al., 1988). To date, all of the hemoglobins and myoglobins are believed to have a common origin, and so they are considered ...
T, Suzuki, T, Takagi
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