Posttranslational modification of indoleamine 2,3-dioxygenase. - Wikidata - awgldk - TriplyDB

Posttranslational modification of indoleamine 2,3-dioxygenase.

Posttranslational modification of indoleamine 2,3-dioxygenase.

http://www.wikidata.org/entity/Q37998306

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Kynurenines in CNS disease: regulation by inflammatory cytokines Structural Study of a Flexible Active Site Loop in Human Indoleamine 2,3-Dioxygenase and Its Functional Implications.IDO1 and IDO2 non-synonymous gene variants: correlation with crohn's disease risk and clinical phenotype.Amino acid catabolism: a pivotal regulator of innate and adaptive immunity.Aryl hydrocarbon receptor and kynurenine: recent advances in autoimmune disease research Abnormal kynurenine pathway of tryptophan catabolism in cardiovascular diseases.Redox control of indoleamine 2,3-dioxygenase expression and activity in human monocyte-derived dendritic cells is independent of changes in oxygen tension.Tryptophan Metabolism Along the Kynurenine Pathway Downstream of Toll-like Receptor Stimulation in Peripheral Monocytes.Endothelial indoleamine 2,3-dioxygenase-1 regulates the placental vascular tone and is deficient in intrauterine growth restriction and pre-eclampsia.

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P2860

Posttranslational modification of indoleamine 2,3-dioxygenase.

http://www.wikidata.org/entity/Q37998306

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artikel ilmiah

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name

Posttranslational modification of indoleamine 2,3-dioxygenase.

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Posttranslational modification of indoleamine 2,3-dioxygenase.

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type

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Posttranslational modification of indoleamine 2,3-dioxygenase.

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Posttranslational modification of indoleamine 2,3-dioxygenase.

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prefLabel

Posttranslational modification of indoleamine 2,3-dioxygenase.

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Posttranslational modification of indoleamine 2,3-dioxygenase.

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S00216-012-5946-2

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Analytical and Bioanalytical Chemistry

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Posttranslational modification of indoleamine 2,3-dioxygenase.

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Hidetsugu Fujigaki

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Kuniaki Saito

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Mitsuru Seishima

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P2860

Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice

Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan

Prevention of allogeneic fetal rejection by tryptophan catabolism

N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins.

Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase

Inhibition of T cell proliferation by macrophage tryptophan catabolism

The heme environment of recombinant human indoleamine 2,3-dioxygenase. Structural properties and substrate-ligand interactions

Interferon-induced indoleamine 2,3-dioxygenase activity inhibits Chlamydia psittaci replication in human macrophages

Dynamic range of mass accuracy in LTQ Orbitrap hybrid mass spectrometer

Inhibition of indoleamine 2,3-dioxygenase in dendritic cells by stereoisomers of 1-methyl-tryptophan correlates with antitumor responses

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s00216-012-5946-2

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1777-1782

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scholarly article

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10.1007/S00216-012-5946-2

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7

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403

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2012-03-31T00:00:00Z

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22460077

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