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1. Full Text Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin
by Veenstra, Timothy D and Klamt, Fábio and Shacter, Emily and Yu, Li-Rong and Zhang, Yaqin and Levine, Rodney L and Pariser, Ashley and Zhang, Baolin and Zdanov, Stéphanie
Nature Cell Biology, ISSN 1465-7392, 10/2009, Volume 11, Issue 10, pp. 1241 - 1246
Physiological oxidants that are generated by activated phagocytes comprise the main source of oxidative stress during inflammation. Oxidants such as taurine... 
CHLORAMINES | LYMPHOMA-CELLS | HYPOCHLOROUS ACID | CYSTEINE | HYDROGEN-PEROXIDE | MITOCHONDRIAL PERMEABILITY | STRESS | CANCER | CELL-DEATH | PERMEABILITY TRANSITION | CELL BIOLOGY | Mitochondria, Liver - metabolism | Humans | Oxidants - metabolism | Cercopithecus aethiops | bcl-2 Homologous Antagonist-Killer Protein - metabolism | Recombinant Proteins - isolation & purification | Transfection | Time Factors | Plasmids - genetics | Cysteine - metabolism | Cofilin 1 - chemistry | Fibroblasts - metabolism | Recombinant Proteins - metabolism | Taurine - analogs & derivatives | Enzyme Inhibitors - metabolism | Oxidation-Reduction | bcl-2-Associated X Protein - metabolism | Rats | Alanine - metabolism | Etoposide - metabolism | Subcellular Fractions - metabolism | Cofilin 1 - genetics | Cytochrome c Group - metabolism | Hydrogen Peroxide - metabolism | Animals | Cofilin 1 - metabolism | Fibroblasts - cytology | Enzyme Activation | COS Cells | Taurine - metabolism | Amino Acid Substitution | Apoptosis | RNA, Small Interfering - metabolism | Oxidative stress | Usage | Control | Actin | Physiological aspects | Causes of | Oxidation-reduction reaction | Research | Health aspects | Index Medicus
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2. Full Text Nutritional regulation of bile acid metabolism is associated with improved pathological characteristics of the metabolic syndrome
by Liaset, Bjørn and Hao, Qin and Jørgensen, Henry and Hallenborg, Philip and Du, Zhen-Yu and Ma, Tao and Marschall, Hanns-Ulrich and Kruhøffer, Mogens and Li, Ruiqiang and Li, Qibin and Yde, Christian Clement and Criales, Gabriel and Bertram, Hanne C and Mellgren, Gunnar and Øfjord, Erik Snorre and Lock, Erik-Jan and Espe, Marit and Frøyland, Livar and Madsen, Lise and Kristiansen, Karsten and Sahlgrenska akademin and Institute of Medicine and Göteborgs universitet and Gothenburg University and Sahlgrenska Academy and Institutionen för medicin
Journal of Biological Chemistry, ISSN 0021-9258, 08/2011, Volume 286, Issue 32, pp. 28382 - 28395
Bile acids (BAs) are powerful regulators of metabolism, and mice treated orally with cholic acid are protected from diet-induced obesity, hepatic lipid... 
SKELETAL-MUSCLE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BROWN ADIPOCYTES | GENE-EXPRESSION | ENZYMATIC-HYDROLYSIS | FARNESOID-X-RECEPTOR | LOW-DENSITY LIPOPROTEIN | WHITE FAT DEPOTS | DIETARY TAURINE | NUCLEAR RECEPTOR | ADIPOSE-TISSUE | Ion Channels | Rats, Wistar | Humans | Male | Metabolic Syndrome - metabolism | Muscle, Skeletal - metabolism | Mitochondrial Proteins | Metabolic Syndrome - blood | Angiopoietin-like 4 Protein | Dietary Proteins - pharmacology | Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha | Iodide Peroxidase - metabolism | Metabolic Syndrome - diet therapy | Female | Membrane Proteins - metabolism | Angiopoietins - metabolism | PPAR-beta - metabolism | Salmon | Heat-Shock Proteins - metabolism | Liver - metabolism | Rats | Bile Acids and Salts - metabolism | Triglycerides - metabolism | Transcription Factors - metabolism | Animals | Glucose - metabolism | Trans-Activators - metabolism | Adipose Tissue, Brown - metabolism | Mice | Uncoupling Protein 1 | Perilipin-2 | RNA-Binding Proteins - metabolism | Receptors, Cytoplasmic and Nuclear - metabolism | Index Medicus | Adipose Tissue Metabolism | Bile Acid | Obesity | Taurine | Amino Acid | Metabolic Syndrome | Diabetes | Metabolism | Peroxisome Proliferator-activated Receptor (PPAR) | Diet-induced Obesity | Medicinska grundvetenskaper | Basic Medicine
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3. Full Text Sulfur amino acid metabolism in Zucker diabetic fatty rats
by Kwak, Hui Chan and Kim, Young-Mi and Kim, Sang Kyum and Oh, Soo Jin
Biochemical Pharmacology, ISSN 0006-2952, 08/2015, Volume 96, Issue 3, pp. 256 - 266
The present study was aimed to investigate the metabolomics of sulfur amino acids in Zucker diabetic fatty (ZDF) rats, an obese type 2 diabetic animal model.... 
Type 2 diabetes | ZDF rat | Sulfur amino acids | METHIONINE LOADING TEST | PLASMA HOMOCYSTEINE ELEVATION | BETAINE | PERFORMANCE LIQUID-CHROMATOGRAPHY | ADENOSYL-L-METHIONINE | CYSTEINE DIOXYGENASE | METHYL-GROUP | LIVER | PHARMACOLOGY & PHARMACY | HEPATIC-METABOLISM | EXPRESSION | S-Adenosylhomocysteine - metabolism | Area Under Curve | Glutathione - metabolism | Betaine - metabolism | Spermidine - metabolism | Male | Homocysteine - metabolism | Methylenetetrahydrofolate Reductase (NADPH2) - metabolism | Liver - drug effects | Methylenetetrahydrofolate Reductase (NADPH2) - genetics | Adenosylhomocysteinase - genetics | Cysteine - metabolism | Glutamate-Cysteine Ligase - metabolism | Dipeptides - metabolism | Betaine-Homocysteine S-Methyltransferase - metabolism | Taurine - analogs & derivatives | Methionine - metabolism | Liver - metabolism | Gene Expression Regulation | Rats | Adenosylhomocysteinase - metabolism | Methionine - administration & dosage | Rats, Zucker | Animals | 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase - metabolism | Spermine - metabolism | 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase - genetics | Glutamate-Cysteine Ligase - genetics | Taurine - metabolism | S-Adenosylmethionine - metabolism | Betaine-Homocysteine S-Methyltransferase - genetics | Index Medicus
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4. Full Text Statistical total correlation spectroscopy: An exploratory approach for latent biomarker identification from metabolic 1H NMR data sets
by Cloarec, Olivier and Dumas, Marc-Emmanuel and Craig, Andrew and Barton, Richard H and Trygg, Johan and Hudson, Jane and Blancher, Christine and Gauguier, Dominique and Lindon, John C and Holmes, Elaine and Nicholson, Jeremy
Analytical Chemistry, ISSN 0003-2700, 03/2005, Volume 77, Issue 5, pp. 1282 - 1289
We describe here the implementation of the statistical total correlation spectroscopy (STOCSY) analysis method for aiding the identification of potential... 
Protons | Propionates - metabolism | Biomarkers - urine | Creatine - analysis | Male | Sarcosine - metabolism | Dietary Carbohydrates - metabolism | Creatinine - metabolism | Pentanoic Acids - analysis | Amines - analysis | Hippurates - metabolism | Creatine - metabolism | Pentanoic Acids - metabolism | Sarcosine - analogs & derivatives | Ketoglutaric Acids - metabolism | Principal Component Analysis | Citric Acid - analysis | Glyceric Acids - analysis | Biomarkers - metabolism | Ketoglutaric Acids - analysis | Magnetic Resonance Spectroscopy - methods | Sarcosine - analysis | Mice, Inbred C57BL | Biomarkers - analysis | Insulin Resistance | Hippurates - analysis | Taurine - analysis | Mice, Inbred Strains | Amines - metabolism | Succinic Acid - analysis | Propionates - analysis | Discriminant Analysis | Glyceric Acids - metabolism | Animals | Succinic Acid - metabolism | Magnetic Resonance Spectroscopy - statistics & numerical data | Creatinine - analysis | Phenols | Citric Acid - metabolism | Mice | Mice, Inbred BALB C | Dietary Carbohydrates - analysis | Taurine - metabolism | NMR | Data analysis | Nuclear magnetic resonance | Correlation analysis | Statistics | Spectrum analysis | Index Medicus
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5. Full Text The Cysteine Dioxgenase Knockout Mouse: Altered Cysteine Metabolism in Nonhepatic Tissues Leads to Excess H2S/HS− Production and Evidence of Pancreatic and Lung Toxicity
by Roman, Heather B and Hirschberger, Lawrence L and Krijt, Jakub and Valli, Alessandro and Kožich, Viktor and Stipanuk, Martha H
Antioxidants & Redox Signaling, ISSN 1523-0864, 10/2013, Volume 19, Issue 12, pp. 1321 - 1336
Aims: To define the consequences of loss of cysteine dioxygenase (CDO) on cysteine metabolism at the tissue level, we determined levels of relevant metabolites... 
Original Research Communications | SYSTEM | DIOXYGENASE GENE | AMINO-ACIDS | ENZYMES | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENDOCRINOLOGY & METABOLISM | CYSTATHIONINE BETA-SYNTHASE | HYDROGEN-SULFIDE METABOLISM | SULFUR | ETHYLMALONIC ENCEPHALOPATHY | TAURINE SYNTHESIS | STRUCTURAL ORGANIZATION | Hydrogen Sulfide - metabolism | Cysteine Dioxygenase - deficiency | Glutathione - metabolism | Male | Electron Transport Complex IV - metabolism | Alanine - analogs & derivatives | Kidney - metabolism | Female | Cysteine - metabolism | Lung - metabolism | Sulfides - metabolism | Cystathionine - metabolism | Cysteine Dioxygenase - genetics | Taurine - analogs & derivatives | Lung - pathology | Liver - metabolism | Enzyme Stability | Pancreas - pathology | Alanine - metabolism | Pancreas - metabolism | Organ Specificity | Mice, Knockout | Animals | Diet | Mice | Taurine - metabolism | Physiological aspects | Cysteine proteinases | Research | Enzyme activation | Analysis | Index Medicus
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6. Full Text Methionine deficiency does not increase polyamine turnover through depletion of hepatic S-adenosylmethionine in juvenile Atlantic salmon
by Espe, Marit and Andersen, Synne Marte and Holen, Elisabeth and Rønnestad, Ivar and Veiseth-Kent, Eva and Zerrahn, Jens-Erik and Aksnes, Anders
British Journal of Nutrition, ISSN 0007-1145, 10/2014, Volume 112, Issue 8, pp. 1274 - 1285
During the last few decades, plant protein ingredients such as soya proteins have replaced fishmeal in the diets of aquacultured species. This may affect the... 
Taurine | Methionine | Atlantic salmon | Trans-sulphuration | Spermine/spermidine acetyltransferase | Polyamine turnover | S-Adenosylmethionine decarboxylase | HOMOCYSTEINE | LIPID-METABOLISM | CHOLINE | SALAR L | TAURINE SUPPLEMENTATION | ENZYMATIC-HYDROLYSIS | AMINO-ACID | NUTRITION & DIETETICS | Spermine | spermidine acetyltransferase | LIVER | MICE | EXPRESSION | Acetyltransferases - metabolism | Liver - pathology | Ornithine Decarboxylase - metabolism | Diet - adverse effects | Adenosylmethionine Decarboxylase - metabolism | Salmo salar - metabolism | Muscle, Skeletal - metabolism | Adenosylmethionine Decarboxylase - genetics | Salmo salar - growth & development | Acetyltransferases - genetics | Liver - growth & development | Methionine - therapeutic use | Fish Proteins - genetics | Gene Expression Regulation, Developmental | Weight Gain | Diet - veterinary | Methionine - deficiency | Ornithine Decarboxylase - genetics | Methionine - metabolism | Liver - metabolism | Deficiency Diseases - metabolism | Fish Proteins - metabolism | Lipid Metabolism | Deficiency Diseases - prevention & control | Energy Intake | Plant Proteins - adverse effects | Polyamines - metabolism | Animals | Norway | Spermine - metabolism | Deficiency Diseases - veterinary | Muscle, Skeletal - pathology | S-Adenosylmethionine - metabolism | Aquaculture | Putrescine - metabolism | Amino acids | Biochemistry | Diet | Nutrition | Feeds | Salmon | Index Medicus | Spermine/ spermidine acetyltransferase
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7. Full Text Effects of salinity on gonadal development, osmoregulation and metabolism of adult male Chinese mitten crab, Eriocheir sinensis
by Long, Xiaowen and Wu, Xugan and Zhao, Lei and Ye, Haihui and Cheng, Yongxu and Zeng, Chaoshu
PLoS ONE, ISSN 1932-6203, 06/2017, Volume 12, Issue 6, pp. e0179036 - e0179036
As a catadromous species, salinity is a key parameter that affects gonadal development of Chinese mitten crab Eriocheir sinensis during reproductive migration.... 
ANIMAL-TISSUES | NA+/K+-ATPASE ACTIVITY | IONIC REGULATION | K+-ATPASE | MULTIDISCIPLINARY SCIENCES | SEAWATER ACCLIMATION | LITOPENAEUS-VANNAMEI | FREE AMINO-ACIDS | GILLS | CARCINUS-MAENAS | FRESH-WATER | Malondialdehyde - metabolism | Sodium-Potassium-Exchanging ATPase - genetics | Uric Acid - metabolism | Gonads - drug effects | Lipoproteins, HDL - metabolism | Brachyura - growth & development | Hemolymph - metabolism | Gills - metabolism | Male | gamma-Glutamyltransferase - metabolism | Osmoregulation - drug effects | RNA, Messenger - metabolism | Fatty Acids, Omega-6 - metabolism | Amino Acids - metabolism | Sodium-Potassium-Exchanging ATPase - metabolism | Brachyura - metabolism | Gills - drug effects | Gonads - metabolism | Salts - pharmacology | Animals | Gonads - growth & development | Glucose - metabolism | Hemolymph - chemistry | Fatty Acids - metabolism | Physiological aspects | Research | Crabs | Salinity | Taurine | Science education | Physiological effects | Polyunsaturated fatty acids | Migration | Zoology | Estuaries | Amino acids | Glucose | Physiological responses | Crustaceans | Arginine | Salinity effects | Physiology | Magnesium | Catadromous species | Malonaldehyde | Enzymes | Alanine | Nutrition | Phenylalanine | Threonine | Gills | Tryptophan | Hemolymph | Osmoregulation | Marine biology | Gender differences | Ecology | Uric acid | Permeability | Brackish water | Metabolism | Gene expression | Na+/K+-exchanging ATPase | Fatty acids | Cholesterol | Studies | Ammonia | Lysine | Ornithine | Females | Aquaculture | Index Medicus
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8. Full Text Intrinsic carnosine metabolism in the human kidney
by Peters, Verena and Klessens, Celine Q. F and Baelde, Hans J and Singler, Benjamin and Veraar, Kimberley A. M and Zutinic, Ana and Drozak, Jakub and Zschocke, Johannes and Schmitt, Claus P and de Heer, Emile
Amino Acids, ISSN 0939-4451, 12/2015, Volume 47, Issue 12, pp. 2541 - 2550
Histidine-containing dipeptides like carnosine and anserine have protective functions in both health and disease. Animal studies suggest that carnosine can be... 
Life Sciences | Biochemistry, general | Analytical Chemistry | Life Sciences, general | Carnosinase (CNDP1) | Anserine | Biochemical Engineering | Proteomics | Neurobiology | Diabetic nephropathy | Carnosine | Metabolism | Carnosinase (CNDP1) | ANTIOXIDANT ACTIVITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | DIABETIC-NEPHROPATHY | BRAIN-DAMAGE | BETA-ALANINE | HOMOCARNOSINE | PROXIMAL TUBULE | PODOCYTE LOSS | END-PRODUCTS | EXPRESSION | Immunohistochemistry | Epithelial Cells - metabolism | Podocytes - metabolism | Dipeptidases - metabolism | Membrane Glycoproteins - metabolism | Endothelial Cells - metabolism | Humans | Gene Expression Regulation | Gene Expression Profiling | Chromatography, High Pressure Liquid | RNA, Messenger - metabolism | Peptide Synthases - metabolism | Hydrolysis | Anserine - metabolism | Kidney - metabolism | Carnosine - metabolism | Membrane Transport Proteins - metabolism | Diabetic Neuropathies - metabolism | Kidney Tubules - metabolism | Nephrons - metabolism | Physiological aspects | Enzymes | Taurine | RNA | Diabetic nephropathies | Index Medicus | Human | Kidneys | Amino acids | Position (location) | Patients | Endothelial cells | Original
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9. Full Text Regnase-1 controls colon epithelial regeneration via regulation of mTOR and purine metabolism
by Nagahama, Y and Shimoda, M and Mao, GL and Singh, SK and Kozakai, Y and Sun, X and Motooka, D and Nakamura, S and Tanaka, H and Satoh, T and Maeda, K and Akira, S
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, ISSN 0027-8424, 10/2018, Volume 115, Issue 43, pp. 11036 - 11041
Damage to intestinal epithelial cell (IEC) layers during intestinal inflammation is associated with inflammatory bowel disease. Here we show that the... 
RNA stability | ACTIVATION | purine metabolism | BLOOD-COAGULATION | T-CELL METABOLISM | MULTIDISCIPLINARY SCIENCES | inflammatory bowel disease | CHILDREN | DISEASE TOLERANCE | INFLAMMATION | mTOR | INFECTION | MICE | epithelial regeneration | ANOREXIA | CEREBRAL MALARIA | Intestinal Mucosa - metabolism | Epithelial Cells - metabolism | TOR Serine-Threonine Kinases - metabolism | Purines - metabolism | Cell Proliferation - physiology | Regeneration - physiology | Inflammatory Bowel Diseases - metabolism | Colon - metabolism | Ribonucleases - metabolism | Inflammation - metabolism | Animals | Colitis - metabolism | Signal Transduction - physiology | Mice | Apoptosis - physiology | Disease Models, Animal | Physiological aspects | Taurine | Rapamycin | Epithelial cells | TOR protein | Cell proliferation | Energy metabolism | Inflammatory bowel diseases | Body weight | Body weight loss | Inflammatory diseases | Proteins | Microbiota | Intestine | Dextran sulfate | Colon | Immune system | Weight loss | Inflammation | Metabolism | Epithelium | Disease control | Inflammatory bowel disease | Dextran | Regeneration | Sodium | Protein kinase | Colitis | Apoptosis | Index Medicus | Biological Sciences
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10. Full Text Hydrogen sulfide modulates cadmium-induced physiological and biochemical responses to alleviate cadmium toxicity in rice
by Mostofa, Mohammad Golam and Rahman, Anisur and Ansary, Md. Mesbah Uddin and Watanabe, Ayaka and Fujita, Masayuki and Tran, Lam-Son Phan
Scientific Reports, ISSN 2045-2322, 09/2015, Volume 5, Issue 1, pp. 14078 - 14078
We investigated the physiological and biochemical mechanisms by which H2S mitigates the cadmium stress in rice. Results revealed that cadmium exposure resulted... 
GLUTATHIONE | SEEDLINGS | ABIOTIC STRESS TOLERANCE | INDUCED OXIDATIVE STRESS | MULTIDISCIPLINARY SCIENCES | ALUMINUM TOXICITY | PLANTS | ANTIOXIDATIVE RESPONSE | GLYOXALASE I | METHYLGLYOXAL | PEROXIDE | Malondialdehyde - metabolism | Plant Leaves - chemistry | Taurine - analogs & derivatives | Hydrogen Sulfide - pharmacology | Plant Roots - metabolism | Reactive Oxygen Species - metabolism | Cadmium - toxicity | Oxidoreductases - metabolism | Glutathione - metabolism | Oryza - metabolism | Oryza - chemistry | Antioxidants - pharmacology | Biomass | Chlorophyll - metabolism | Oryza - drug effects | Ascorbic Acid - metabolism | Hydrogen Peroxide - metabolism | Lipoxygenase - metabolism | Phenotype | Plant Leaves - metabolism | Plant Roots - chemistry | Carotenoids - metabolism | Oxidative Stress - drug effects | Taurine - pharmacology | Sulfide | Oxidative stress | Cadmium | Enzymes | Reactive oxygen species | Hydrogen peroxide | Toxicity | Superoxide | Minerals | Photosynthetic pigments | Malondialdehyde | Heavy metals | Hydrogen sulfide | Antioxidants | Pigments | Physiology | Pyruvaldehyde | Rice | Index Medicus
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11. Full Text Taurine is a liver X receptor-α ligand and activates transcription of key genes in the reverse cholesterol transport without inducing hepatic lipogenesis
by Hoang, Minh-Hien and Jia, Yaoyao and Jun, Hee-jin and Lee, Ji Hae and Hwang, Kwang-Yeon and Choi, Dal-Woong and Um, Soo-Jong and Lee, Boo-Yong and You, Sang-Guan and Lee, Sung-Joon
Molecular Nutrition and Food Research, ISSN 1613-4125, 06/2012, Volume 56, Issue 6, pp. 900 - 911
Scope: Taurine, which is abundant in seafood, has antiatherogenic activities in both animals and humans; however, its molecular target has been elusive. We... 
Taurine | LXR-α | SREBP-1c | Cholesterol | Insig-2a | LIPID-METABOLISM | FOOD SCIENCE & TECHNOLOGY | PHARMACOLOGICAL ACTIVATION | MECHANISMS | NUCLEAR RECEPTOR | MICE | HDL-CHOLESTEROL | LXR-alpha | EXPRESSION | DIETARY TAURINE | BILE-ACIDS | Cricetulus | Enterocytes - metabolism | Humans | Intracellular Signaling Peptides and Proteins - metabolism | Orphan Nuclear Receptors - metabolism | RNA, Messenger - metabolism | Protein Isoforms - metabolism | ATP-Binding Cassette Transporters - genetics | Anticholesteremic Agents - metabolism | Biological Transport | Liver X Receptors | ATP-Binding Cassette Transporters - metabolism | Membrane Proteins - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Sterol Regulatory Element Binding Protein 1 - metabolism | Recombinant Proteins - metabolism | Cell Line | Cricetinae | Membrane Proteins - genetics | Liver - metabolism | Gene Expression Regulation | Cholesterol - metabolism | Orphan Nuclear Receptors - genetics | Lipolysis | Macrophages - metabolism | Animals | Ligands | Taurine - metabolism | Protein Isoforms - genetics | Index Medicus
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