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Adenosine --- Nervous system --- Receptors. --- Degeneration --- Molecular aspects.

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Adenosine triphosphatase --- Biological transport, Active --- Ion channels --- Congresses. --- Enzymology --- Biomembranes --- Adenosinetrifosfatase --- Congresses --- Biological transport [Active ] --- Adenosine triphosphatase - Congresses. --- Ion channels - Congresses. --- Biological transport, Active - Congresses. --- ADENOSINE TRIPHOSPHATASE --- BIOLOGICAL TRANSPORT, ACTIVE --- CHEMISTRY --- PHYSIOLOGY

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Since their discovery approximately 25 years ago, adenosine receptors have now emerged as important novel molecular targets in disease and drug discovery. These proteins play important roles in the entire spectrum of disease from inflammation to immune suppression. Because of their expression on a number of different cell types and in a number of different organ systems they play important roles in specific diseases, including asthma, rheumatoid arthritis, Parkinson's disease, multiple sclerosis, Alzheimer's disease, heart disease, stroke, cancer, sepsis, and obesity. As a result of intense investigations into understanding the molecular structures and pharmacology of these proteins, new molecules have been synthesized that have high specificity for these proteins and are now entering clinical trials. These molecules will define the next new classes of drugs for a number of diseases with unmet medical needs.

Adenosine --- Adenosinrezeptor --- Pharmacokinetics. --- Purinergic P1 Receptor Antagonists. --- Receptors, Purinergic P1 --- Receptors. --- Pathophysiologie --- Physiologie --- therapeutic use.

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This book is dedicated to studying the thermodynamic bases of the structure-function relationship of proteins. It moves from the elementary principles of physical chemistry to the most current topics of biochemistry, including those that may be subject to some controversy. It considers thermodynamic properties related to the stability and function of proteins from the point of view of physics in a language that, without sacrificing conceptual rigor, is easy to read. Detailing the thermodynamics of protein-ligand interactions, protein naturation, allostery, oxidative phosphorylation and protein phosphorylation, the book will be of interest to students and teachers of chemistry, physics, biochemistry and biotechnology.

Biothermodynamics. --- Bioenergetics. --- Energy Metabolism. --- Thermodynamics. --- Allosteric regulation. --- Adenosine triphosphate. --- Biochimie physique. --- Thermodynamique. --- Métabolisme énergétique. --- Bioénergétique. --- Allostérie. --- ATP. --- Ligands (biochimie) --- Fixation. --- Métabolisme énergétique. --- Bioénergétique. --- Allostérie.

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This book discusses biochemical adaptation to environments from freezing polar oceans to boiling hot springs, and under hydrostatic pressures up to 1,000 times that at sea level.Originally published in 1984.The Princeton Legacy Library uses the latest print-on-demand technology to again make available previously out-of-print books from the distinguished backlist of Princeton University Press. These editions preserve the original texts of these important books while presenting them in durable paperback and hardcover editions. The goal of the Princeton Legacy Library is to vastly increase access to the rich scholarly heritage found in the thousands of books published by Princeton University Press since its founding in 1905.

Adaptation (Physiology) --- Biochemistry. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Compensation (Physiology) --- Plasticity (Physiology) --- Composition --- Biology --- Chemistry --- Medical sciences --- Ecophysiology --- Biochemistry --- 57.017.32 --- 575.826 --- 575.826 Adaptation --- Adaptation --- Biologische wetenschappen in het algemeen. Biologie--?.017.32 --- 6-bisphosphatase. --- ATPase. --- Acid–base homeostasis. --- Adenosine monophosphate. --- Alanine. --- Alcohol dehydrogenase. --- Amino acid. --- Aminooxyacetic acid. --- Anabolism. --- Anaerobic glycolysis. --- Antifreeze. --- Arginine. --- Basal rate. --- Beta oxidation. --- Bohr effect. --- Carbohydrate. --- Carnitine. --- Catabolism. --- Catalase. --- Catalysis. --- Cellular respiration. --- Cofactor (biochemistry). --- Competitive inhibition. --- Cooperativity. --- Deep sea. --- Dehydrogenase. --- Detergent. --- Dissociation constant. --- Enzyme Repression. --- Enzyme inhibitor. --- Enzyme. --- Facultative anaerobic organism. --- Fatty acid. --- Fermentation. --- Flavin adenine dinucleotide. --- Fructose 1. --- Futile cycle. --- Glucagon. --- Gluconeogenesis. --- Glucose-6-phosphate dehydrogenase. --- Glucose. --- Glyceraldehyde 3-phosphate dehydrogenase. --- Glycerol. --- Glycogen phosphorylase. --- Glycogen. --- Glycogenolysis. --- Glycolysis. --- Hemoglobin. --- Hibernation. --- High-energy phosphate. --- Hill equation (biochemistry). --- Histidine. --- Hofmeister series. --- Hormone-sensitive lipase. --- Insulin. --- Isozyme. --- Ketosis. --- Lactic acid. --- Lipid. --- Lipolysis. --- Lysine. --- Mammalian diving reflex. --- Metabolic intermediate. --- Metabolism. --- Michaelis–Menten kinetics. --- Mitochondrial matrix. --- Mitochondrion. --- Molecular mimicry. --- Muscle. --- Nicotinamide adenine dinucleotide. --- Obligate anaerobe. --- Obligate. --- Organism. --- Ornithine. --- Osmolyte. --- Oxidative deamination. --- Peroxidase. --- Phosphagen. --- Phosphofructokinase. --- Phospholipid. --- Phosphorylase kinase. --- Proline. --- Proofreading (biology). --- Protein turnover. --- Protein. --- Proteolysis. --- Pyruvate carboxylase. --- Pyruvic acid. --- Redox. --- Regulatory enzyme. --- Root effect. --- Substrate-level phosphorylation. --- Thermoregulation. --- Thermus aquaticus. --- Thermus thermophilus. --- Triglyceride. --- Tryptophan. --- Turnover number. --- Urea cycle. --- Urea.