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1. Full Text Heme Enzyme Structure and Function
by Poulos, Thomas L
Chemical reviews, ISSN 0009-2665, 04/2014, Volume 114, Issue 7, pp. 3919 - 3962
Physical Sciences | Chemistry | Chemistry, Multidisciplinary | Science & Technology | Enzymes - chemistry | Indoleamine-Pyrrole 2,3,-Dioxygenase - metabolism | Chloride Peroxidase - chemistry | Catalytic Domain | Indoleamine-Pyrrole 2,3,-Dioxygenase - chemistry | Nitric Oxide Synthase - chemistry | Biocatalysis | Cytochrome P-450 Enzyme System - metabolism | Heme Oxygenase (Decyclizing) - chemistry | Tryptophan Oxygenase - metabolism | Cytochrome P-450 Enzyme System - chemistry | Heme - chemistry | Peroxidases - chemistry | Tryptophan Oxygenase - chemistry | Chloride Peroxidase - metabolism | Peroxidases - metabolism | Nitric Oxide Synthase - metabolism | Protoporphyrins - chemistry | Heme Oxygenase (Decyclizing) - metabolism | Enzymes - metabolism | Proteins | Chemical properties | Research | Structure | Hemoproteins | Enzymes | Oxygen | Hydrogen peroxide | Enzyme kinetics | Index Medicus
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2. Full Text Publisher Correction: The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases
by Markolovic, Suzana and Zhuang, Qinqin and Wilkins, Sarah E and Eaton, Charlotte D and Abboud, Martine I and Katz, Maximiliano J and McNeil, Helen E and Leśniak, Robert K and Hall, Charlotte and Struwe, Weston B and Konietzny, Rebecca and Davis, Simon and Yang, Ming and Ge, Wei and Benesch, Justin L. P and Kessler, Benedikt M and Ratcliffe, Peter J and Cockman, Matthew E and Fischer, Roman and Wappner, Pablo and Chowdhury, Rasheduzzaman and Coleman, Mathew L and Schofield, Christopher J
Nature chemical biology, ISSN 1552-4450, 06/2018, Volume 14, Issue 10, pp. 1 - 988
Oxygenase | Hydroxylation
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3. Molecular mechanisms of oxygen activation
by Hayaishi, Osamu, 1920-2015
1974, Molecular biology; an international series of monographs and textbooks, 678
Oxygenases
Book
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4. Oxygenases
by Hayaishi, O
1962, xii, 588
oxygenases
Book
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5. Oxygenases
by Hayaishi, Osamu, 1920-2015
1962, 588
Oxygenases
Book
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6. Full Text Transcriptional and translational modulation of myo-inositol oxygenase (Miox) by fatty acids: Implications in renal tubular injury induced in obesity and diabetes
by Tominaga, Tatsuya and Dutta, Rajesh K and Joladarashi, Darukeshwara and Doi, Toshio and Reddy, Janardan K and Kanwar, Yashpal S
The Journal of biological chemistry, ISSN 0021-9258, 01/2016, Volume 291, Issue 3, pp. 1348 - 1367
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Up-Regulation | Phosphorylation | Oxidative Stress | Diabetic Nephropathies - etiology | Humans | Diet, High-Fat - adverse effects | Male | Oxygenases - antagonists & inhibitors | RNA Interference | Inositol Oxygenase - metabolism | Oxygenases - metabolism | Obesity - etiology | Kidney Tubules - pathology | Kidney Tubules - metabolism | Sterol Regulatory Element Binding Protein 1 - metabolism | Cell Line | Promoter Regions, Genetic | Diabetic Nephropathies - pathology | Diabetic Nephropathies - metabolism | Rats | Obesity - metabolism | Obesity - pathology | Proteins - genetics | Animals | Proteins - metabolism | Inositol Oxygenase - antagonists & inhibitors | Sterol Regulatory Element Binding Protein 1 - genetics | Kidney Tubules - enzymology | Sterol Regulatory Element Binding Protein 1 - antagonists & inhibitors | Inositol Oxygenase - genetics | Mice | Protein Processing, Post-Translational | Oxygenases - genetics | Proteins - antagonists & inhibitors | Sus scrofa | Apoptosis | Index Medicus | kidney | renal tubular injury | kidney metabolism | fatty acid | myo-inositol oxygenase | Metabolism | diabetic nephropathy | obesity
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7. Full Text The Heme Oxygenase System in Hematological Malignancies
by Li Volti, Giovanni and Tibullo, Daniele and Vanella, Luca and Giallongo, Cesarina and Di Raimondo, Francesco and Forte, Stefano and Di Rosa, Michelino and Signorelli, Salvatore Santo and Barbagallo, Ignazio
Antioxidants & redox signaling, ISSN 1523-0864, 08/2017, Volume 27, Issue 6, pp. 363 - 377
Review Article | leukemia | hematology | multiple myeloma | cancer | Heme oxygenase | Biochemistry & Molecular Biology | Endocrinology & Metabolism | Life Sciences & Biomedicine | Science & Technology | Heme Oxygenase-1 - chemistry | Heme Oxygenase-1 - metabolism | Heme - metabolism | Oxidation-Reduction | Epigenesis, Genetic | Humans | Biliverdine - metabolism | Models, Molecular | Antineoplastic Agents - therapeutic use | Carbon Monoxide - metabolism | Heme Oxygenase (Decyclizing) - chemistry | Iron - metabolism | Xenograft Model Antitumor Assays | Heme Oxygenase-1 - genetics | Animals | Signal Transduction - drug effects | Hematologic Neoplasms - drug therapy | Antineoplastic Agents - pharmacology | Heme Oxygenase (Decyclizing) - metabolism | Heme Oxygenase (Decyclizing) - genetics | Hematologic Neoplasms - metabolism | Oxidases | Usage | Hematology | Heme | Multiple myeloma | Research | Health aspects | Risk factors | Animal models | Leukemia | Chemoresistance | Bone marrow transplantation | Homeostasis | Iron | Genomic instability | Degradation | Pathways | Bone marrow | Carbon monoxide | Inhibition | Stability | Biliverdin | Myeloid leukemia | Heme oxygenase (decyclizing) | Transplants | siRNA | Chronic myeloid leukemia | Oxygenase | Chemotherapy | Inhibitors | Index Medicus
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8. Full Text Amazing Diversity in Biochemical Roles of Fe(II)/2-Oxoglutarate Oxygenases
by Herr, Caitlyn Q and Hausinger, Robert P
Trends in biochemical sciences (Amsterdam. Regular ed.), ISSN 0968-0004, 07/2018, Volume 43, Issue 7, pp. 517 - 532
translation | biodegradation | Nonheme iron oxygenase | chromatin modification | transcription | biosynthesis | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Protein Biosynthesis | Species Specificity | Humans | Ribosomes - metabolism | Substrate Specificity | Mixed Function Oxygenases - metabolism | Isoenzymes - chemistry | Mixed Function Oxygenases - chemistry | RNA, Messenger - metabolism | Ketoglutaric Acids - chemistry | DNA-Binding Proteins - metabolism | Ribosomes - enzymology | Isoenzymes - metabolism | Ketoglutaric Acids - metabolism | RNA, Transfer - chemistry | Binding Sites | Hydroxylation | RNA Processing, Post-Transcriptional | Isoenzymes - genetics | RNA, Transfer - metabolism | Iron - chemistry | Ribosomes - chemistry | Models, Molecular | Terminology as Topic | DNA-Binding Proteins - chemistry | Iron - metabolism | Animals | Halogenation | RNA, Messenger - chemistry | Protein Processing, Post-Translational | Mixed Function Oxygenases - genetics | Oxidases | Physiological aspects | Genetic translation | Index Medicus | non-heme iron oxygenase
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9. Full Text The IsdG‐family of haem oxygenases degrades haem to a novel chromophore
by Reniere, Michelle L and Ukpabi, Georgia N and Harry, S. Reese and Stec, Donald F and Krull, Robert and Wright, David W and Bachmann, Brian O and Murphy, Michael E and Skaar, Eric P
Molecular microbiology, ISSN 0950-382X, 03/2010, Volume 75, Issue 6, pp. 1529 - 1538
Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Microbiology | Science & Technology | Fundamental and applied biological sciences. Psychology | Biological and medical sciences | Protein Structure, Tertiary | Staphylococcus aureus - enzymology | Heme - metabolism | Oxidation-Reduction | Bacterial Proteins - chemistry | Models, Molecular | Crystallography, X-Ray | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Oxygenases - chemistry | Heme Oxygenase (Decyclizing) - chemistry | Oxygenases - metabolism | Bacterial Proteins - metabolism | Molecular Structure | Heme Oxygenase (Decyclizing) - metabolism | Oxidases | Carbon monoxide | Structure | Crystals | Heme | Enzymes | Staphylococcus infections | Iron | Metabolism | Index Medicus
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