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AMILORIDE --- CALCIUM CHANNELS --- SODIUM CHANNELS --- BIOLOGICAL TRANSPORT, ACTIVE --- MOLECULAR STRUCTURE-BIOLOGICAL ACTIVITY RELATIONSHIP --- CELLS, CULTURED --- ANALOGS AND DERIVATIVES --- DRUG EFFECTS
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Salt (NaCl) is a key component of the human diet because it provides the sodium ion (Na+), an essential mineral for our body. Na+ regulates extracellular fluid volume and plays a key role in many physiological processes, such as the generation of nerve impulses. Na+ is lost continuously through the kidneys, intestine, and sweating. Thus, to maintain proper bodily balance, losses have to be balanced with foods containing this cation. The need for salt explains our ability to detect Na+ in foodstuffs: Na+ elicits a specific taste sensation called “salty”, and gustatory sensitivity to this cation is crucial for regulating its intake. Indeed, the widespread use of salt in food products for flavoring and to improve their palatability exploits our sense of taste for Na+. When consumed in excess, however, salt might be detrimental to health because it may determine an increase in blood pressure—a major risk factor for many cardiovascular diseases. Understanding how salt taste works and how it affects food preference and consumption is therefore of paramount importance for improving human nutrition. This book comprises cutting-edge research dealing with salt taste mechanisms relevant for nutrition and health.
taste sensitivity --- taste thresholds --- food records --- food intake --- oral microbiota --- eating habits --- taste --- sodium taste --- renin --- angiotensin II --- angiotensinogen --- angiotensin-converting enzyme --- high-salt diet --- blood pressure --- doenjang --- soybean paste --- epithelial sodium channel --- sodium homeostasis --- amiloride --- salt deprivation --- short-term preference test --- salt --- TRPV1 gene --- rs806500 --- dietary --- biomarker --- elderly --- nutrigenetics --- salt taste perception --- taste threshold --- sodium chloride --- metabolic syndrome --- Mediterranean diet --- sodium receptor --- salt taste --- taste transduction --- Korean soy sauce --- kokumi --- umami --- salty --- chorda tympani --- amiloride-insensitive salt taste pathway --- n/a
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Salt (NaCl) is a key component of the human diet because it provides the sodium ion (Na+), an essential mineral for our body. Na+ regulates extracellular fluid volume and plays a key role in many physiological processes, such as the generation of nerve impulses. Na+ is lost continuously through the kidneys, intestine, and sweating. Thus, to maintain proper bodily balance, losses have to be balanced with foods containing this cation. The need for salt explains our ability to detect Na+ in foodstuffs: Na+ elicits a specific taste sensation called “salty”, and gustatory sensitivity to this cation is crucial for regulating its intake. Indeed, the widespread use of salt in food products for flavoring and to improve their palatability exploits our sense of taste for Na+. When consumed in excess, however, salt might be detrimental to health because it may determine an increase in blood pressure—a major risk factor for many cardiovascular diseases. Understanding how salt taste works and how it affects food preference and consumption is therefore of paramount importance for improving human nutrition. This book comprises cutting-edge research dealing with salt taste mechanisms relevant for nutrition and health.
Research & information: general --- Biology, life sciences --- Food & society --- taste sensitivity --- taste thresholds --- food records --- food intake --- oral microbiota --- eating habits --- taste --- sodium taste --- renin --- angiotensin II --- angiotensinogen --- angiotensin-converting enzyme --- high-salt diet --- blood pressure --- doenjang --- soybean paste --- epithelial sodium channel --- sodium homeostasis --- amiloride --- salt deprivation --- short-term preference test --- salt --- TRPV1 gene --- rs806500 --- dietary --- biomarker --- elderly --- nutrigenetics --- salt taste perception --- taste threshold --- sodium chloride --- metabolic syndrome --- Mediterranean diet --- sodium receptor --- salt taste --- taste transduction --- Korean soy sauce --- kokumi --- umami --- salty --- chorda tympani --- amiloride-insensitive salt taste pathway
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Iron–sulfur (FeS) centers are essential protein cofactors in all forms of life. They are involved in many key biological processes. In particular, Fe-S centers not only serve as enzyme cofactors in catalysis and electron transfer, they are also indispensable for the biosynthesis of complex metal-containing cofactors. Among these cofactors are the molybdenum (Moco) and tungsten (Wco) cofactors. Both Moco/Wco biosynthesis and Fe-S cluster assembly are highly conserved among all kingdoms of life. After formation, Fe-S clusters are transferred to carrier proteins, which insert them into recipient apo-proteins. Moco/Wco cofactors are composed of a tricyclic pterin compound, with the metal coordinated to its unique dithiolene group. Moco/Wco biosynthesis starts with an Fe-S cluster-dependent step involving radical/S-adenosylmethionine (SAM) chemistry. The current lack of knowledge of the connection of the assembly/biosynthesis of complex metal-containing cofactors is due to the sheer complexity of their synthesis with regard to both the (genetic) regulation and (chemical) metal center assembly. Studies on these metal-cofactors/cofactor-containing enzymes are important for understanding fundamental cellular processes. They will also provide a comprehensive view of the complex biosynthesis and the catalytic mechanism of metalloenzymes that underlie metal-related human diseases.
Research & information: general --- Biology, life sciences --- CO dehydrogenase --- dihydrogen --- hydrogenase --- quantum/classical modeling --- density functional theory --- metal–dithiolene --- pyranopterin molybdenum enzymes --- fold-angle --- tungsten enzymes --- electronic structure --- pseudo-Jahn–Teller effect --- thione --- molybdenum cofactor --- Moco --- mixed-valence complex --- dithiolene ligand --- tetra-nuclear nickel complex --- X-ray structure --- magnetic moment --- formate hydrogenlyase --- hydrogen metabolism --- energy conservation --- MRP (multiple resistance and pH)-type Na+/H+ antiporter --- CCCP—carbonyl cyanide m-chlorophenyl-hydrazone --- EIPA—5-(N-ethyl-N-isopropyl)-amiloride --- nicotinamide adenine dinucleotide (NADH) --- electron transfer --- enzyme kinetics --- enzyme structure --- formate dehydrogenase --- carbon assimilation --- Moco biosynthesis --- Fe-S cluster assembly --- l-cysteine desulfurase --- ISC --- SUF --- NIF --- iron --- molybdenum --- sulfur --- tungsten cofactor --- aldehyde:ferredoxin oxidoreductase --- benzoyl-CoA reductase --- acetylene hydratase --- [Fe]-hydrogenase --- FeGP cofactor --- guanylylpyridinol --- conformational changes --- X-ray crystallography --- iron-sulfur cluster --- persulfide --- metallocofactor --- frataxin --- Friedreich’s ataxia --- n/a --- metal-dithiolene --- pseudo-Jahn-Teller effect --- CCCP-carbonyl cyanide m-chlorophenyl-hydrazone --- EIPA-5-(N-ethyl-N-isopropyl)-amiloride --- Friedreich's ataxia
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Iron–sulfur (FeS) centers are essential protein cofactors in all forms of life. They are involved in many key biological processes. In particular, Fe-S centers not only serve as enzyme cofactors in catalysis and electron transfer, they are also indispensable for the biosynthesis of complex metal-containing cofactors. Among these cofactors are the molybdenum (Moco) and tungsten (Wco) cofactors. Both Moco/Wco biosynthesis and Fe-S cluster assembly are highly conserved among all kingdoms of life. After formation, Fe-S clusters are transferred to carrier proteins, which insert them into recipient apo-proteins. Moco/Wco cofactors are composed of a tricyclic pterin compound, with the metal coordinated to its unique dithiolene group. Moco/Wco biosynthesis starts with an Fe-S cluster-dependent step involving radical/S-adenosylmethionine (SAM) chemistry. The current lack of knowledge of the connection of the assembly/biosynthesis of complex metal-containing cofactors is due to the sheer complexity of their synthesis with regard to both the (genetic) regulation and (chemical) metal center assembly. Studies on these metal-cofactors/cofactor-containing enzymes are important for understanding fundamental cellular processes. They will also provide a comprehensive view of the complex biosynthesis and the catalytic mechanism of metalloenzymes that underlie metal-related human diseases.
CO dehydrogenase --- dihydrogen --- hydrogenase --- quantum/classical modeling --- density functional theory --- metal–dithiolene --- pyranopterin molybdenum enzymes --- fold-angle --- tungsten enzymes --- electronic structure --- pseudo-Jahn–Teller effect --- thione --- molybdenum cofactor --- Moco --- mixed-valence complex --- dithiolene ligand --- tetra-nuclear nickel complex --- X-ray structure --- magnetic moment --- formate hydrogenlyase --- hydrogen metabolism --- energy conservation --- MRP (multiple resistance and pH)-type Na+/H+ antiporter --- CCCP—carbonyl cyanide m-chlorophenyl-hydrazone --- EIPA—5-(N-ethyl-N-isopropyl)-amiloride --- nicotinamide adenine dinucleotide (NADH) --- electron transfer --- enzyme kinetics --- enzyme structure --- formate dehydrogenase --- carbon assimilation --- Moco biosynthesis --- Fe-S cluster assembly --- l-cysteine desulfurase --- ISC --- SUF --- NIF --- iron --- molybdenum --- sulfur --- tungsten cofactor --- aldehyde:ferredoxin oxidoreductase --- benzoyl-CoA reductase --- acetylene hydratase --- [Fe]-hydrogenase --- FeGP cofactor --- guanylylpyridinol --- conformational changes --- X-ray crystallography --- iron-sulfur cluster --- persulfide --- metallocofactor --- frataxin --- Friedreich’s ataxia --- n/a --- metal-dithiolene --- pseudo-Jahn-Teller effect --- CCCP-carbonyl cyanide m-chlorophenyl-hydrazone --- EIPA-5-(N-ethyl-N-isopropyl)-amiloride --- Friedreich's ataxia
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Iron–sulfur (FeS) centers are essential protein cofactors in all forms of life. They are involved in many key biological processes. In particular, Fe-S centers not only serve as enzyme cofactors in catalysis and electron transfer, they are also indispensable for the biosynthesis of complex metal-containing cofactors. Among these cofactors are the molybdenum (Moco) and tungsten (Wco) cofactors. Both Moco/Wco biosynthesis and Fe-S cluster assembly are highly conserved among all kingdoms of life. After formation, Fe-S clusters are transferred to carrier proteins, which insert them into recipient apo-proteins. Moco/Wco cofactors are composed of a tricyclic pterin compound, with the metal coordinated to its unique dithiolene group. Moco/Wco biosynthesis starts with an Fe-S cluster-dependent step involving radical/S-adenosylmethionine (SAM) chemistry. The current lack of knowledge of the connection of the assembly/biosynthesis of complex metal-containing cofactors is due to the sheer complexity of their synthesis with regard to both the (genetic) regulation and (chemical) metal center assembly. Studies on these metal-cofactors/cofactor-containing enzymes are important for understanding fundamental cellular processes. They will also provide a comprehensive view of the complex biosynthesis and the catalytic mechanism of metalloenzymes that underlie metal-related human diseases.
Research & information: general --- Biology, life sciences --- CO dehydrogenase --- dihydrogen --- hydrogenase --- quantum/classical modeling --- density functional theory --- metal-dithiolene --- pyranopterin molybdenum enzymes --- fold-angle --- tungsten enzymes --- electronic structure --- pseudo-Jahn-Teller effect --- thione --- molybdenum cofactor --- Moco --- mixed-valence complex --- dithiolene ligand --- tetra-nuclear nickel complex --- X-ray structure --- magnetic moment --- formate hydrogenlyase --- hydrogen metabolism --- energy conservation --- MRP (multiple resistance and pH)-type Na+/H+ antiporter --- CCCP-carbonyl cyanide m-chlorophenyl-hydrazone --- EIPA-5-(N-ethyl-N-isopropyl)-amiloride --- nicotinamide adenine dinucleotide (NADH) --- electron transfer --- enzyme kinetics --- enzyme structure --- formate dehydrogenase --- carbon assimilation --- Moco biosynthesis --- Fe-S cluster assembly --- l-cysteine desulfurase --- ISC --- SUF --- NIF --- iron --- molybdenum --- sulfur --- tungsten cofactor --- aldehyde:ferredoxin oxidoreductase --- benzoyl-CoA reductase --- acetylene hydratase --- [Fe]-hydrogenase --- FeGP cofactor --- guanylylpyridinol --- conformational changes --- X-ray crystallography --- iron-sulfur cluster --- persulfide --- metallocofactor --- frataxin --- Friedreich's ataxia
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Pharmaceutical Preparations --- analysis --- Drugs --- Pharmaceutical chemistry --- Médicaments --- Chimie pharmaceutique --- Analysis --- Yearbooks. --- Analyse --- Pharmaceutical Preparations - analysis --- Atenolol --- Camphre --- Chloroquine --- Cholecalciferol --- Cimetidine --- Disopyramide (phosphate) --- Indomethacine --- Ketofifene --- Melphalan --- Moxalactam (disodium) --- Oxyphenbutazone --- Pentazocine --- Phenytoine --- Pyridoxine --- Reserpine --- Saccharine --- Salicylamide --- Sulfadadiazine argent --- Sulindac --- Tetracycline (chlorhydrate --- Tolbutamide --- Vitamine d3 --- CHLORTHALIDONE --- IMIPRAMINE HCl --- CISPLATIN --- ANALYTICAL PROFILE --- TRIPELENNAMINE HCl --- XYLOMETAZOLINE HCl --- MEFLOQUINE HCl --- ACIDE IOPOANOIQUE --- LIDOCAINE --- LIDOCAINE HCl --- BENPERIDOL --- HYDRATE DE TERPINE --- ATROPINE --- ISOPROTERENOL --- WARFARIN --- NALOXONE HCl --- DIFLUNISAL --- BACLOFEN --- ACETAMINOPHEN --- HALOTHANE --- Bacitracine --- Bretylium --- Carbamazepine --- Ccyproheptadine --- Cefaclor --- Cefamandole --- Dibenzepine --- Digoxine --- Doxorubicine --- Fluphenazine --- Gentamicine (sulfate) --- Griseofulvine --- Haloperidol --- Khellin --- Lorazepam --- Methadone --- Methoxsalen --- Monographies medicaments --- Nadolol --- Nitrazepam --- Nitroglycerin --- Trifluoroperazine --- Acide ascorbique --- Acide flufenamique --- Aminophylline --- Captopril --- Cefotaxime --- Cefoxitine sodium --- Clofibrate --- Clotrimazole --- Dopamine chlorhydrate --- Ergonovine maleate --- Hexestrol --- Mestranol --- Noscapine --- Penicilline-g benzathine --- Phenylbutazone --- Sulfadiazine --- Amantadine --- Amikacine sulfate --- Benzocaine --- Dibucaine --- Dibucaine chlorhydrate --- Dioctylsulfosuccinate de sodium --- Estrone --- Etomidate --- Heparine sodium --- Hydrocortisone --- Isopropamide --- Metoprolol tartrate --- Phenylpropanolamine chlorhydrate --- Pilocarpine --- Pyrazinamide --- Pyrimethamine --- Quinine chlorhydrate --- Quinine sulfate --- Rutine --- Trimipramine maleate --- AMILORIDE CHLORHYDRATE --- AMINOGLUTETHIMIDE --- CAFEINE --- COCAINE CHLORHYDRATE --- EPHEDRINE CHLORHYDRATE --- OESTRADIOL --- GUANABENZ ACETATE --- IODAMIDE --- LITHIUM CARBONATE --- MAPROTILINE CHLORHYDRATE --- PENICILLIN G --- POTASSIUM --- PIROXICAM --- RANITIDINE --- STRYCHNINE --- VIDARABINE --- ZOMEPIRAC --- SODIUM --- CHLORAMPHENICOL --- LIDOCAINE CHLORHYDRATE --- SODIUM NITROPRUSSIATE --- Acide aminosalicylique --- Azathioprine --- Benzoate de benzyle --- Chlorhydrate d'emetine --- Chlorhydrate de clindamycine --- Chlorhydrate de methylphenidate --- Colchicine --- Cyanocobalamine --- Glibenclamide --- Heroine --- Hydrochlorothiazide --- Ketoprofen --- Nabinole --- Natamycine --- Oxytocine --- Penicillamine --- Phosphate de codeine
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