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Aspartic proteinases --- Congresses --- ASPARTIC PROTEINASES --- PHYSIOLOGY
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Aspartic proteinases --- Aspartic Proteinases --- Congresses. --- genetics --- congresses. --- physiology --- Congresses --- Aspartic proteinases - Congresses. --- Genetics --- Physiology
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The book details the synthesis of molecules designed to inhibit the hepatitis C virus (HCV) NS3 serine protease and the human aspartic protease BACE-1. It explores the relationships between potential inhibitors and the targeted enzymes while discussing the class of enzymes known as proteases. The book also discusses why such enzymes can be regarded as suitable targets for developing drugs to combat diseases. It presents the results of the design and synthesis of linear and macrocyclic NS3 protease inhibitors containing a novel trisubstituted cyclopentane moiety as an N-acyl-(4 bioisostere. The book is intended for researchers and students in the field of medicinal chemistry and drug design.
Aspartic Proteinases. --- Hepatitis C Virus. --- Enzyme Inhibitors.
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Enzymology --- Enzymes protéolytiques --- Peptide hydrolases --- Peptidohydrolases --- Proteases --- Proteolytic enzymes --- Proteolytiques [Enzymes ] --- Proteolytische enzymen --- Peptidases. --- Endopeptidases aspartiques. --- Metalloproteinases. --- Endopeptidases aspartiques --- Metalloproteinases --- Peptidases --- Peptidase --- Aspartic proteinases --- Enzymes --- Hydrolases --- Metallocarboxypeptidases --- Peptide Hydrolases. --- Enzymes and Coenzymes. --- Metalloendopeptidases. --- Aspartic Acid Endopeptidases.
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How exciting it is to see a field so well established as the ren- angiotensin system continue to grow and mature. Originally, following the original identification of renin by Tigerstedt and Bergman over 100 years ago, workers in this area spent years attempting to establish its role in experimental and renal hypertension. The early work by Goldblatt, in 1934, demonstrated that the placement of a clip around a renal artery was clearly related to the subsequent development of hypertension. However, it wasn't until the simultaneous finding by two different geographically separated teams, Page, et al, in the United States and Braun-Menendez, et al, in Argentina that the peptide angiotensin was identified. Thus, the rate-limiting enzyme renin was released from the kidney and catalyzed a biochemical cascade which was eventually shown to produce the elevated arterial pressure. Subsequently, many workers contributed to the elucidation of the concept and sequence of angiotensin I1 generation. Thus, the enzyme renin acted upon its protein substrate, produced in the liver, to liberate the decapeptide angiotensin I which, upon circulating through the pulmonary circulation, finally produced the potent octapeptide angiotensin. Several important subsequent findings demonstrated that angiotensin I1 promoted the release of the adrenal corticosteroid from that gland, thereby resulting in a larger system, the renin-angiotensin-aldosterone system. Further, this system demonstrated a classical biofeedback and the circulating octapeptide was shown to have additional biological activities in organs other than heart, vessels, kidney, adrenals, and even brain.
Renin-angiotensin system. --- Heart --- Renal hypertension. --- Renin. --- Physiology. --- Aspartic proteinases --- Juxtaglomerular apparatus --- Renal parenchymatous hypertension --- Hypertension --- Kidneys --- RA system --- RAA system --- RAAS (Physiology) --- RAS (Physiology) --- Renin-angiotensin-aldosterone axis --- Renin-angiotensin-aldosterone system --- Aldosterone --- Angiotensins --- Renin --- Water-electrolyte balance (Physiology) --- Blood pressure --- Diseases --- Regulation --- Cardiology. --- Internal medicine
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Enzymology --- Aspartic Acid Proteases. --- Metalloproteases. --- Peptide Hydrolases. --- Esteroproteases --- Peptidases --- Proteases --- Proteinases --- Proteolytic Enzymes --- Gene Products, pol --- Metallopeptidases --- Metalloproteinases --- Aspartyl Proteases --- Aspartic Acid Proteinases --- Aspartic Proteinases --- Aspartyl Proteinases --- Acid Proteases, Aspartic --- Proteases, Aspartic Acid --- Proteases, Aspartyl --- Proteinases, Aspartic --- Proteinases, Aspartic Acid --- Proteinases, Aspartyl --- Peptidase --- Peptide Hydrolase --- Protease --- Proteinase --- Proteolytic Enzyme --- Enzyme, Proteolytic --- Hydrolase, Peptide --- Metallopeptidase --- Metalloprotease --- Metalloproteinase --- Aspartic Acid Protease --- Aspartic Acid Proteinase --- Aspartic Proteinase --- Aspartyl Protease --- Aspartyl Proteinase --- Acid Protease, Aspartic --- Acid Proteinase, Aspartic --- Protease, Aspartic Acid --- Protease, Aspartyl --- Proteinase, Aspartic --- Proteinase, Aspartic Acid --- Proteinase, Aspartyl --- Aspartic Acid Proteases --- Metalloproteases --- Peptide Hydrolases
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The human pancreas has vital roles in the regulation of glucose homeostasis and digestion and its dysfunction leads to pancreatic disease as diabetes and pancreatitis. Recent researches have highlighted the novel roles of a local renin-angiotensin system (RAS) in the pancreas and its clinical relevances; its inapprporiate activation leads to pancreatic endocrine and exocrine disease, notably type 2 diabetes. As such, manipulation of the overactive RAS may improve pancreatic islet cell function, cell mass and insulin sensitivity, as well as enhancing the growth and differentiation of pancreatic stem cells. Blockade of the RAS may be protective against pancreatitis and pancreatic cancer. The research outcome of current progress on the RAS in the pancreas should provide an alternative approach to preventing and treating, as well as curing pancreatic disease. This book discusses the progress of research on the renin-angiotensin system in the pancreas from the science to the bedside, providing a timely review of this expanding area. It consists of ten interrelated chapters covering subjects as: – Structure, physiology and disease of the pancreas – Biochemistry and physiology of the pancreatic renin-angiotensin system – RAS in diabetes, stem cells and pancreatitis This book is of special value to basic and clinical scientists, clinicians, graduate students, as well as novices in this field. .
Pancreas. --- Renin-angiotensin system. --- Renin-angiotensin system --- Pancreas --- Research --- Digestive System --- Digestive System Diseases --- Hemodynamics --- Metabolism --- Diseases --- Science --- Anatomy --- Cardiovascular Physiological Processes --- Metabolic Phenomena --- Biomedical Research --- Renin-Angiotensin System --- Pancreatic Diseases --- Natural Science Disciplines --- Cardiovascular Physiological Phenomena --- Phenomena and Processes --- Disciplines and Occupations --- Circulatory and Respiratory Physiological Phenomena --- Human Anatomy & Physiology --- Health & Biological Sciences --- Animal Biochemistry --- Angiotensins --- Renin --- Kidneys --- Physiology. --- Pathophysiology. --- Angiotensin --- Medicine. --- Human physiology. --- Diabetes. --- Gastroenterology. --- Biomedicine. --- Biomedicine general. --- Human Physiology. --- Internal medicine --- Digestive organs --- Brittle diabetes --- Diabetes mellitus --- IDDM (Disease) --- Insulin-dependent diabetes --- Ketosis prone diabetes --- Type 1 diabetes --- Carbohydrate intolerance --- Endocrine glands --- Diabetic acidosis --- Glycosylated hemoglobin --- Human biology --- Medical sciences --- Physiology --- Human body --- Clinical sciences --- Medical profession --- Life sciences --- Pathology --- Physicians --- Aspartic proteinases --- Juxtaglomerular apparatus --- Neuropeptides --- Oligopeptides --- Peptide hormones --- Health Workforce --- Gastroenterology . --- Biomedicine, general.
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Angiotensins --- Enzyme activation --- Kallikrein --- Kinins --- Renin --- Enzyme Activation --- Kallikreins --- Peptides --- Angiotensin --- Neuropeptides --- Oligopeptides --- Peptide hormones --- Aspartic proteinases --- Juxtaglomerular apparatus --- Hypotensive agents --- Inflammation --- Polypeptides --- Vasodilators --- Padutin --- Vascormone --- Pancreas --- Serine proteinases --- Activation, Enzyme --- Enzymes --- Big Renin --- Cryorenin --- Inactive Renin --- Pre-Prorenin --- Preprorenin --- Prorenin --- Angiotensin-Forming Enzyme --- Angiotensinogenase --- Angiotensin Forming Enzyme --- Pre Prorenin --- Renin, Big --- Renin, Inactive --- Juxtaglomerular Apparatus --- Peptide --- Polypeptide --- Kinin --- Callicrein --- Dilminal --- Kallidinogenase --- Kalliginogenase --- Kallikrein A --- Kallikrein B' --- Kallikrein Light Chain --- Kinin-Forming Enzyme --- alpha-Kallikrein --- beta-Kallikrein --- beta-Kallikrein B --- Kininogenase --- Enzyme, Kinin-Forming --- Kinin Forming Enzyme --- Light Chain, Kallikrein --- alpha Kallikrein --- beta Kallikrein --- beta Kallikrein B --- Activations, Enzyme --- Enzyme Activations --- Enzyme Activators --- Mediators --- Secretions --- Regulation --- Enzymology --- Human biochemistry --- Pharmacology. Therapy --- Pathology of the circulatory system --- Pathological endocrinology
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