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1. Full Text Solid-State Metalized Reduction of Magnesium-Rich Low-Nickel Oxide Ores Using Coal as the Reductant Based on Thermodynamic Analysis
by Ma, Baozhong and Xing, Peng and Yang, Weijiao and Wang, Chengyan and Chen, Yongqiang and Wang, Hua
Metallurgical and Materials Transactions B: Process Metallurgy and Materials Processing Science, ISSN 1073-5615, 08/2017, Volume 48, Issue 4, pp. 2037 - 2046
The solid-state metalized reduction of magnesium-rich low-nickel oxide ore using coal as a reductant was studied based on thermodynamic analysis. The major... 
FERRONICKEL | FURNACE | CONCENTRATE | PLANT | MATERIALS SCIENCE, MULTIDISCIPLINARY | METALLURGY & METALLURGICAL ENGINEERING | PRODUCE | LIMONITIC LATERITE | Polymerization | Thermodynamics | Ferronickel | Nickel | Magnesium | Analysis | Concentrates (ores) | Migration | Alloys | Iron | Economic conditions | Minerals | Silicates | Beneficiation | Dosage | Reduction (metal working) | Bearing | Reduction | Magnetic separation | Coal | Surface tension | Calcium fluoride
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2. Full Text Challenges in the Discovery of Indoleamine 2,3-Dioxygenase 1 (IDO1) Inhibitors
by Röhrig, Ute F and Majjigapu, Somi Reddy and Vogel, Pierre and Zoete, Vincent and Michielin, Olivier
Journal of Medicinal Chemistry, ISSN 0022-2623, 12/2015, Volume 58, Issue 24, pp. 9421 - 9437
Since the discovery of indoleamine 2,3-dioxygenase 1 (IDO1) as an attractive target for anticancer therapy in 2003, the search for inhibitors has been... 
SCREENING LIBRARIES | CHEMISTRY, MEDICINAL | MAJOR REDUCTANT | COMPETITIVE INHIBITORS | SUBSTRATE-INHIBITION | ASSAY INTERFERENCE | TUMORAL IMMUNE RESISTANCE | TRYPTOPHAN DEGRADATION | CYTOCHROME B | (IDO). SYNTHESIS | RATIONAL DESIGN | Cell Survival - drug effects | Humans | Enzyme Inhibitors - pharmacology | Tryptophan - chemistry | Enzyme Assays | Structure-Activity Relationship | Drug Discovery | Tryptophan - metabolism | Animals | Tryptophan - analogs & derivatives | Enzyme Inhibitors - chemistry | Tryptophan - pharmacology | Kinetics | Indoleamine-Pyrrole 2,3,-Dioxygenase - antagonists & inhibitors
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3. Full Text Human Indoleamine 2,3-Dioxygenase 1 Is an Efficient Mammalian Nitrite Reductase
by Lim, Yean J and Foo, Timothy C and Yeung, Amanda W. S and Tu, Xiaofan and Ma, Yuanqing and Hawkins, Clare L and Witting, Paul K and Jameson, Guy N. L and Terentis, Andrew C and Thomas, Shane R
Biochemistry, ISSN 0006-2960, 02/2019, Volume 58, Issue 7, pp. 974 - 986
The heme enzyme indoleamine 2,3-dioxygenase-1 (IDO1) catalyzes the first reaction of L-tryptophan oxidation along the kynurenine pathway. IDOL is a central... 
OXIDE GENERATION | SITE | SUPEROXIDE ANION | MAGNITUDE | MAJOR REDUCTANT | NEUROGLOBIN | INFLAMMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MECHANISMS | ASCORBIC-ACID | EXPRESSION
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4. Full Text Potent Activation of Indoleamine 2,3-Dioxygenase by Polysulfides
by Nelp, MT and Zheng, V and Davis, KM and Stiefel, KJE and Groves, JT
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, ISSN 0002-7863, 09/2019, Volume 141, Issue 38, pp. 15288 - 15300
Indoleamine 2,3-dioxygenase (IDO1) is a heme enzyme that catalyzes the oxygenation of the indole ring of tryptophan to afford N-formylkynurenine. This activity... 
SUPEROXIDE ANION | MAJOR REDUCTANT | ACID | MECHANISM | IDO | H2S | POSTTRANSLATIONAL REGULATION | CYTOCHROME B | HYDROGEN-SULFIDE OXIDATION | CHEMISTRY, MULTIDISCIPLINARY | CYSTEINE PERSULFIDES
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5. Full Text Rational Design of Indoleamine 2,3-Dioxygenase Inhibitors
by Röhrig, Ute F and Awad, Loay and Grosdidier, Aurélien and Larrieu, Pierre and Stroobant, Vincent and Colau, Didier and Cerundolo, Vincenzo and Simpson, Andrew J. G and Vogel, Pierre and Van den Eynde, Benoît J and Zoete, Vincent and Michielin, Olivier
Journal of Medicinal Chemistry, ISSN 0022-2623, 02/2010, Volume 53, Issue 3, pp. 1172 - 1189
Indoleamine 2,3-dioxygenase (IDO) is an important therapeutic target for the treatment of diseases such as cancer that involve pathological immune escape. We... 
CHEMISTRY, MEDICINAL | HUMAN DENDRITIC CELLS | MAJOR REDUCTANT | LEAD DISCOVERY | EXIGUAMINE-A | IMMUNE ESCAPE | DRUG DISCOVERY | COMPETITIVE INHIBITORS | COUPLING REAGENTS | TRYPTOPHAN 2,3-DIOXYGENASE | SPACE GAUSSIAN PSEUDOPOTENTIALS | Humans | Cells, Cultured | Enzyme Inhibitors - pharmacology | Models, Molecular | Structure-Activity Relationship | Enzyme Inhibitors - chemical synthesis | Tryptophan - metabolism | Animals | Small Molecule Libraries | Enzyme Inhibitors - chemistry | Drug Design | Cell Proliferation - drug effects | Mice | Kynurenine - metabolism | Indoleamine-Pyrrole 2,3,-Dioxygenase - antagonists & inhibitors
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6. Full Text Indoleamine 2,3-dioxygenase 2 (IDO2) and the kynurenine pathway: characteristics and potential roles in health and disease
by Fatokun, Amos A and Hunt, Nicholas H and Ball, Helen J
Amino Acids, ISSN 0939-4451, 12/2013, Volume 45, Issue 6, pp. 1319 - 1329
The kynurenine pathway is the major route for the oxidative degradation of the amino acid tryptophan. Activity of the pathway is involved in several disease... 
Life Sciences | Biochemistry, general | 1-Methyltryptophan | Analytical Chemistry | Life Sciences, general | Biochemical Engineering | Proteomics | Neurobiology | Tryptophan | Indoleamine 2,3-dioxygenase | Tryptophan 2,3-dioxygenase | Kynurenine pathway | DENDRITIC CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | GAMMA-INTERFERON | COMPETITIVE INHIBITORS | DEXTRO-1-METHYL TRYPTOPHAN | TRYPTOPHAN CATABOLISM | QUINOLINIC ACID | MAJOR REDUCTANT | ANTITUMOR IMMUNITY | TUMORAL IMMUNE RESISTANCE | EXPRESSION | Indoleamine-Pyrrole 2,3,-Dioxygenase - metabolism | Animals | Kynurenine - metabolism | Disease | Health | Humans | Enzymes | Nervous system diseases | Chemotherapy | Physiological aspects | Mental illness | Cancer
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7. Full Text Structure and Reaction Mechanism in the Heme Dioxygenases
by Efimov, Igor and Basran, Jaswir and Thackray, Sarah J and Handa, Sandeep and Mowat, Christopher G and Raven, Emma Lloyd
Biochemistry, ISSN 0006-2960, 04/2011, Volume 50, Issue 14, pp. 2717 - 2724
As members of the family of heme-dependent enzymes, the heme dioxygenases are differentiated by virtue of their ability to catalyze the oxidation of... 
RAT-LIVER | MISSING PIECE | MAJOR REDUCTANT | ENZYME | CONTAINING OXYGENASES | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | HUMAN INDOLEAMINE 2,3-DIOXYGENASE | BINDING | HUMAN TRYPTOPHAN 2,3-DIOXYGENASE | Indoleamine-Pyrrole 2,3,-Dioxygenase - metabolism | Protein Structure, Tertiary | Indoleamine-Pyrrole 2,3,-Dioxygenase - chemistry | Biocatalysis | Humans | Models, Molecular | Tryptophan - chemistry | Kynurenine - chemistry | Kynurenine - analogs & derivatives | Tryptophan - metabolism | Tryptophan Oxygenase - metabolism | Animals | Tryptophan Oxygenase - chemistry | Molecular Structure | Kynurenine - metabolism | Oxidases | Analysis | Hemoproteins | Tryptophan | Cytochromes | Oxidation-reduction reaction | Chemical properties | Structure | Current Topic
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8. Full Text Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
by Kolawole, Ayodele O and Hixon, Brian P and Dameron, Laura S and Chrisman, Ian M and Smirnov, Valeriy V
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 03/2015, Volume 570, pp. 47 - 57
A cytokine-inducible extrahepatic human indoleamine 2,3-dioxygenase ( IDO1) catalyzes the first step of the kynurenine pathway. Immunosuppressive activity of... 
Oxygen electrode | Inhibition | Enzyme kinetics | Substrate analog | Global fit | Indoleamine dioxygenase | METHYLENE-BLUE | BIOCHEMISTRY & MOLECULAR BIOLOGY | EFFECTOR INTERACTIONS | SUPEROXIDE ANION | IN-VITRO | MAJOR REDUCTANT | ENZYME | BIOPHYSICS | SUBSTRATE-INHIBITION | BINDING-SITE | TRYPTOPHAN 2,3-DIOXYGENASE | CYTOCHROME B | Indoleamine-Pyrrole 2,3,-Dioxygenase - metabolism | Carbolines | Escherichia coli - enzymology | Harmine - analogs & derivatives | Humans | Substrate Specificity | Tryptophan - chemistry | Kynurenine - chemistry | Harmine - chemistry | Tryptophan - analogs & derivatives | Oxygen - chemistry | Protein Binding | Catalysis | Binding Sites | Immunosuppressive Agents - chemistry | indoleamine dioxygenase | substrate analog | inhibition | global fit | enzyme kinetics | oxygen electrode
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9. Full Text Highlights at the gate of tryptophan catabolism: A review on the mechanisms of activation and regulation of indoleamine 2,3-dioxygenase (IDO), a novel target in cancer disease
by MacChiarulo, Antonio and Camaioni, Emidio and Nuti, Roberto and Pellicciari, Roberto
Amino Acids, ISSN 0939-4451, 07/2009, Volume 37, Issue 2, pp. 219 - 229
Indoleamine 2,3-dioxygenase (IDO) catalyzes the first and rate-limiting step of Kynurenine pathway along the major route of Tryptophan catabolism. The... 
Indoleamine 2,3-dioxygenase | Tryptophan metabolism | Immune tolerance | Cancer | Kynurenine pathway | DIHYDROFLAVIN MONONUCLEOTIDE | DENDRITIC CELLS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | INDOLEAMINE-2,3-DIOXYGENASE IDO | COMPETITIVE INHIBITORS | EFFECTOR INTERACTIONS | SUPEROXIDE ANION | MAJOR REDUCTANT | SMALL-MOLECULE INHIBITORS | Indoleamine-Pyrrole 2,3,-Dioxygenase - genetics | Indoleamine-Pyrrole 2,3,-Dioxygenase - metabolism | Neoplasms - metabolism | Indoleamine-Pyrrole 2,3,-Dioxygenase - chemistry | Enzyme Inhibitors - metabolism | Isoenzymes - genetics | Humans | Models, Molecular | Substrate Specificity | Crystallography, X-Ray | Kynurenine - chemistry | Isoenzymes - chemistry | Tryptophan - metabolism | Neoplasms - drug therapy | Animals | Isoenzymes - metabolism | Enzyme Inhibitors - chemistry | Protein Conformation | Molecular Structure | Enzyme Activation | Kynurenine - metabolism | Physiological aspects | Tryptophan | Enzymes | Chemotherapy | Disease | Inhibitors | Amino acids | Activation | Catabolism | Tolerances
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10. Full Text Heme-containing dioxygenases involved in tryptophan oxidation
by Millett, Elizabeth S and Efimov, Igor and Basran, Jaswir and Handa, Sandeep and Mowat, Christopher G and Raven, Emma Lloyd
Current Opinion in Chemical Biology, ISSN 1367-5931, 04/2012, Volume 16, Issue 1-2, pp. 60 - 66
► This review looks at the heme-containing enzymes involved in tryptophan oxidation. ► Indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase are the main... 
MISSING PIECE | PEROXIDASE | SUBSTRATE-BINDING | MAJOR REDUCTANT | ENZYME | BIOPHYSICS | ACTIVE-SITE | REACTION-MECHANISM | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HUMAN INDOLEAMINE 2,3-DIOXYGENASE | CYTOCHROME B | Dioxygenases - metabolism | Biocatalysis | Dioxygenases - chemistry | Dioxygenases - classification | Heme - metabolism | Heme - chemistry | Oxidation-Reduction | Humans | Substrate Specificity | Tryptophan - chemistry | Tryptophan - metabolism | Tryptophan | Enzymes | Oxidation-reduction reaction | Amino acids | Analysis | Heme
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11. Full Text Indol-2-yl ethanones as novel indoleamine 2,3-dioxygenase (IDO) inhibitors
by Dolušić, Eduard and Larrieu, Pierre and Blanc, Sébastien and Sapunaric, Frédéric and Norberg, Bernadette and Moineaux, Laurence and Colette, Delphine and Stroobant, Vincent and Pilotte, Luc and Colau, Didier and Ferain, Thierry and Fraser, Graeme and Galeni, Moreno and Frère, Jean-Marie and Masereel, Bernard and Van den Eynde, Benoît and Wouters, Johan and Frédérick, Raphaël
Bioorganic & Medicinal Chemistry, ISSN 0968-0896, 02/2011, Volume 19, Issue 4, pp. 1550 - 1561
Indoleamine 2,3-dioxygenase (IDO) is a heme dioxygenase which has been shown to be involved in the pathological immune escape of diseases such as cancer. The... 
Indoleamine 2,3-dioxygenase | Anticancer | IDO | Immunotherapy | CHEMISTRY, MEDICINAL | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | IMMUNE ESCAPE | CHEMISTRY, ORGANIC | CANCER | MAJOR REDUCTANT | ACYL CHLORIDES | SMALL-MOLECULE INHIBITORS | EXIGUAMINE-A | IN-VIVO | TRYPTOPHAN 2,3-DIOXYGENASE | DERIVATIVES | Cell Line | Catalytic Domain | Indoleamine-Pyrrole 2,3,-Dioxygenase - chemistry | Humans | Ethane - chemistry | Models, Molecular | Indoles - pharmacology | Protein Interaction Domains and Motifs | Structure-Activity Relationship | Indoles - chemistry | Indoleamine-Pyrrole 2,3,-Dioxygenase - antagonists & inhibitors | Oncology, Experimental | Research | Cancer
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12. Full Text Biochemical characteristics and inhibitor selectivity of mouse indoleamine 2,3-dioxygenase-2
by Austin, Christopher Jonathan Daraius and Mailu, B M and Maghzal, G J and Sanchez-Perez, A and Rahlfs, S and Zocher, K and Yuasa, H J and Arthur, J W and Becker, K and Stocker, R and Hunt, N H and Ball, H J
Amino Acids, ISSN 0939-4451, 7/2010, Volume 39, Issue 2, pp. 565 - 578
The first step in the kynurenine pathway of tryptophan catabolism is the cleavage of the 2,3-double bond of the indole ring of tryptophan. In mammals, this... 
Life Sciences | Biochemistry, general | Oxidation/reduction | Analytical Chemistry | Life Sciences, general | Electron donation | Neurobiology | Proteomics | Biochemical Engineering | IDO2 | Cytochrome b 5 | Cytochrome b | TRYPTOPHAN OXYGENASE GENE | DENDRITIC CELLS | KYNURENINE PATHWAY | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | QUINOLINIC ACID | SUPEROXIDE ANION | MAJOR REDUCTANT | INTERFERON-GAMMA | EXPRESSION | Indoleamine-Pyrrole 2,3,-Dioxygenase - metabolism | Amino Acid Sequence | Nitric Oxide - pharmacology | Humans | Enzyme Stability | Models, Molecular | Molecular Sequence Data | Recombinant Proteins - isolation & purification | Sequence Alignment | Animals | Tryptophan - analogs & derivatives | Mice | Tryptophan - pharmacology | Kinetics | Indoleamine-Pyrrole 2,3,-Dioxygenase - antagonists & inhibitors | Hydrogen-Ion Concentration | Physiological aspects | Tryptophan | Medical colleges | Enzymes | Medical research
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13. Full Text In Vitro Modulation of Cytochrome P450 Reductase Supported Indoleamine 2,3-Dioxygenase Activity by Allosteric Effectors Cytochrome b(5) and Methylene Blue
by Pearson, JT and Siu, S and Meininger, DP and Wienkers, LC and Rock, DA
BIOCHEMISTRY, ISSN 0006-2960, 03/2010, Volume 49, Issue 12, pp. 2647 - 2656
Indoleamine 2,3-dioxygenase (IDO) is a heme-containing dioxygenase involved in the degradation of several indoleamine derivatives and has been Indicated as ail... 
ELECTRON-TRANSFER | MAJOR REDUCTANT | SUBSTRATE-BINDING SITE | DENDRITIC CELLS | 3A4 | BIOCHEMISTRY & MOLECULAR BIOLOGY | P450 REDUCTASE | NITRIC-OXIDE | T-CELL | EXPRESSION | TRYPTOPHAN CATABOLISM | Allosteric Regulation - drug effects | Indoleamine-Pyrrole 2,3,-Dioxygenase - metabolism | Cricetinae | NADPH-Ferrihemoprotein Reductase - metabolism | Cricetulus | Oxidation-Reduction | Cytochromes b - pharmacology | Methylene Blue - pharmacology | Animals | Saccharomyces cerevisiae Proteins - metabolism | Indoles - pharmacology | Tryptophan - pharmacology | Enzyme Activation | Binding Sites | CHO Cells
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14. Full Text Cytochrome b(5) from Giardia lamblia
by Alam, S and Yee, J and Couture, M and Takayama, SJ and Tseng, WH and Mauk, AG and Rafferty, S
METALLOMICS, ISSN 1756-5901, 2012, Volume 4, Issue 12, pp. 1255 - 1261
The protozoan intestinal parasite Giardia lamblia lacks mitochondria and the ability to make haem yet encodes several putative haem-binding proteins, including... 
EUKARYOTE | MAJOR REDUCTANT | PROTEIN | HEME | NITRIC-OXIDE SYNTHASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | INDOLEAMINE 2,3-DIOXYGENASE | PURIFICATION | ENVIRONMENT | RESONANCE RAMAN
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15. Heme-containing Dioxygenases
by Efimov, Igor and Basran, Jaswir and Thackray, Sarah J and Handa, Sandeep and Mowat, Christopher G and Raven, Emma Lloyd
Advances in Inorganic Chemistry, ISSN 0898-8838, 2012, Volume 64, pp. 33 - 51
The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway-the O -dependent oxidation of... 
Iron | Heme | Dioxygenases | RAT-LIVER | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | CHEMISTRY, INORGANIC & NUCLEAR | MISSING PIECE | QUINOLINIC ACID | MAJOR REDUCTANT | REACTION-MECHANISM | HUMAN INDOLEAMINE 2,3-DIOXYGENASE | STRUCTURAL-PROPERTIES | HUMAN TRYPTOPHAN 2,3-DIOXYGENASE
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16. Full Text Formation of the thiol conjugates and active metabolite of clopidogrel by human liver microsomes
by Zhang, Haoming and Lau, Wei C and Hollenberg, Paul F
Molecular Pharmacology, ISSN 0026-895X, 08/2012, Volume 82, Issue 2, pp. 302 - 309
We reported previously the formation of a glutathionyl conjugate of the active metabolite (AM) of clopidogrel and the covalent modification of a cysteinyl... 
INACTIVATION | ACID | POLYMORPHISMS | METAANALYSIS | HEALTHY-SUBJECTS | GLUTATHIONE | MAJOR DETERMINANT | RISK | BIOACTIVATION | PHARMACOLOGY & PHARMACY | HUMAN P2Y RECEPTOR | Dose-Response Relationship, Drug | Glutathione - pharmacology | Sulfhydryl Compounds - metabolism | Oxidation-Reduction | Microsomes, Liver - drug effects | Humans | Microsomes, Liver - metabolism | Ticlopidine - metabolism | Sulfhydryl Compounds - chemical synthesis | Ticlopidine - chemical synthesis | Ticlopidine - analogs & derivatives
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17. Full Text Betablockers in perioperative period: Drop the bombshell
by Piriou, V and Marret, E and Albaladejo, P and Samain, E
ANNALES FRANCAISES D ANESTHESIE ET DE REANIMATION, ISSN 0750-7658, 03/2008, Volume 27, Issue 3, pp. 197 - 199
MORTALITY | TRIAL | CARDIOVASCULAR EVALUATION | HIGH-RISK PATIENTS | BISOPROLOL | REDUCTION | MORBIDITY | ANESTHESIOLOGY | BLOCKADE | VASCULAR-SURGERY | MAJOR NONCARDIAC SURGERY | Cardiotonic Agents - therapeutic use | Intraoperative Period | Adrenergic beta-Antagonists - adverse effects | Treatment Outcome | Humans | Adrenergic beta-Antagonists - therapeutic use
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18. Full Text Impact of natural re-oxygenation on the sediment dynamics of manganese, iron and phosphorus in a euxinic Baltic Sea basin
by Hermans, Martijn and Lenstra, Wytze K and van Helmond, Niels A.G.M and Behrends, Thilo and Egger, Matthias and Séguret, Marie J.M and Gustafsson, Erik and Gustafsson, Bo G and Slomp, Caroline P and Naturvetenskapliga fakulteten and Stockholms universitets Östersjöcentrum and Stockholms universitet and Baltic Nest Institute
Geochimica et Cosmochimica Acta, ISSN 0016-7037, 02/2019, Volume 246, pp. 174 - 196
The Baltic Sea is characterized by the largest area of hypoxic (oxygen (O ) < 2 mg L ) bottom waters in the world’s ocean induced by human activities. Natural... 
Phosphorus | Iron | Major Baltic Inflow | Re-oxygenation | Baltic Sea | Manganese | TRACE-METALS | ORGANIC-MATTER | CABLE BACTERIA | HYPOXIA | GOTLAND BASIN | GEOCHEMISTRY & GEOPHYSICS | COLORIMETRIC DETERMINATION | BIOGEOCHEMICAL CYCLES | PHOSPHATE RELEASE | DEAD ZONES | DEEP-WATER | Naturvetenskap | Natural Sciences | Earth and Related Environmental Sciences | Geovetenskap och miljövetenskap
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