Redox Potential

Vascular Endothelial Dysfunction In Diabetic Cardiomyopathy: Pathogenesis and Potential Treatment Targets

Pharmacology / Clinical Trial / Extracellular Matrix / Heart Failure / Protein Structure and Function / CAD / NO / Humans / Age / Hyperglycemia / Basement Membrane / VEGF / Animals / Vascular endothelium / PKC / Structural Change / Lipoprotein(a) / Glucose Transport / Nitric Oxide Synthase / Endothelial cell / Fatty Acid / PPAR / Toll-Like Receptors Therapeutics Pharmacology / MAPK / Cardiomyopathies / NAD / Vascular Endothelial Function / Intracellular Signaling / PARP / Redox Potential / CAD / NO / Humans / Age / Hyperglycemia / Basement Membrane / VEGF / Animals / Vascular endothelium / PKC / Structural Change / Lipoprotein(a) / Glucose Transport / Nitric Oxide Synthase / Endothelial cell / Fatty Acid / PPAR / Toll-Like Receptors Therapeutics Pharmacology / MAPK / Cardiomyopathies / NAD / Vascular Endothelial Function / Intracellular Signaling / PARP / Redox Potential

Hydrogen peroxide-induced oxidative stress responses in Desulfovibrio vulgaris Hildenborough

Genetics / Microbiology / Environmental microbiology / Network Analysis / Oxidative Stress / DNA repair / Gene expression / Molecular Mechanics / Protein synthesis / Signal Transduction / Stress response / Detoxification / Sulfate reducing Bacteria / Hydrogen Peroxide / Cellular Automaton Model / Thioredoxin / Sulfate reduction / Proteome / Environmental / Sulphate Reducing Bacteria / Oxidants / Redox Potential / DNA repair / Gene expression / Molecular Mechanics / Protein synthesis / Signal Transduction / Stress response / Detoxification / Sulfate reducing Bacteria / Hydrogen Peroxide / Cellular Automaton Model / Thioredoxin / Sulfate reduction / Proteome / Environmental / Sulphate Reducing Bacteria / Oxidants / Redox Potential

Hydrogen-peroxide-induced oxidative stress responses in Desulfovibrio vulgaris Hildenborough

Genetics / Microbiology / Environmental microbiology / Network Analysis / Oxidative Stress / DNA repair / Gene expression / Molecular Mechanics / Protein synthesis / Signal Transduction / Stress response / Detoxification / Sulfate reducing Bacteria / Hydrogen Peroxide / Cellular Automaton Model / Thioredoxin / Sulfate reduction / Proteome / Environmental / Sulphate Reducing Bacteria / Oxidants / Redox Potential / DNA repair / Gene expression / Molecular Mechanics / Protein synthesis / Signal Transduction / Stress response / Detoxification / Sulfate reducing Bacteria / Hydrogen Peroxide / Cellular Automaton Model / Thioredoxin / Sulfate reduction / Proteome / Environmental / Sulphate Reducing Bacteria / Oxidants / Redox Potential

Propiedades antioxidantes del maguey morado ( Rhoeo discolor ) Purple maguey ( Rhoeo discolor ) antioxidant properties

Food Sciences / Aqueous Extract / Antioxidant Capacity / Total Phenolic Content / Redox Potential

Propiedades antioxidantes del maguey morado (Rhoeo discolor)

Food Sciences / Aqueous Extract / Antioxidant Capacity / Total Phenolic Content / Redox Potential

Manganese peroxidase production by Bjerkandera sp. BOS55

Chemical Engineering / Biomedical Engineering / Agricultural Biotechnology / Bioprocess Engineering / Experimental Research / Peroxidase / Nitrogen / Scaling up / Enzyme / Production System / Large Scale / Submerged Culture / Redox Potential / Peroxidase / Nitrogen / Scaling up / Enzyme / Production System / Large Scale / Submerged Culture / Redox Potential

Synthesis, characterisation and catalase-like activity of dimanganese(III) complexes of 1,5-bis(5-X-salicylidenamino)pentan-3-ol (X=nitro and chloro)

Thermodynamics / Inorganic Chemistry / Electrochemistry / Kinetics / Inorganic / Manganese / Crystal structure / Catalase / Proton Transfer / Spectrophotometry / Schiff Base / Molecular Conformation / Inorganic Biochemistry / Catalytic Activity / Redox Potential / Manganese / Crystal structure / Catalase / Proton Transfer / Spectrophotometry / Schiff Base / Molecular Conformation / Inorganic Biochemistry / Catalytic Activity / Redox Potential

Copyright © 2017 DATOSPDF Inc.