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Insulin

Insulin (from Latin insula, island) is a peptide hormone produced by beta cells of the pancreatic islets; it is considered to be the main anabolic hormone of the body. It regulates the metabolism of carbohydrates, fats and protein by promoting the absorption of carbohydrates, especially glucose from the blood into liver, fat and skeletal muscle cells. In these tissues the absorbed glucose is converted into either glycogen via glycogenesis or fats (triglycerides) via lipogenesis, or, in the case of the liver, into both. Glucose production and secretion by the liver is strongly inhibited by high concentrations of insulin in the blood. Circulating insulin also affects the synthesis of proteins in a wide variety of tissues. It is therefore an anabolic hormone, promoting the conversion of small molecules in the blood into large molecules inside the cells. Low insulin levels in the blood have the opposite effect by promoting widespread catabolism, especially of reserve body fat.1A7F, 1AI0, 1AIY, 1B9E, 1BEN, 1EFE, 1EV3, 1EV6, 1EVR, 1FU2, 1FUB, 1G7A, 1G7B, 1GUJ, 1HIQ, 1HIS, 1HIT, 1HLS, 1HTV, 1HUI, 1IOG, 1IOH, 1J73, 1JCA, 1JCO, 1K3M, 1KMF, 1LKQ, 1LPH, 1MHI, 1MHJ, 1MSO, 1OS3, 1OS4, 1Q4V, 1QIY, 1QIZ, 1QJ0, 1RWE, 1SF1, 1SJT, 1SJU, 1T0C, 1T1K, 1T1P, 1T1Q, 1TRZ, 1TYL, 1TYM, 1UZ9, 1VKT, 1W8P, 1XDA, 1XGL, 1XW7, 1ZEG, 1ZEH, 1ZNJ, 2AIY, 2C8Q, 2C8R, 2CEU, 2G54, 2G56, 2H67, 2HH4, 2HHO, 2HIU, 2JMN, 2JUM, 2JUU, 2JUV, 2JV1, 2JZQ, 2K91, 2K9R, 2KJJ, 2KJU, 2KQP, 2KQQ, 2KXK, 2L1Y, 2L1Z, 2LGB, 2M1D, 2M1E, 2M2M, 2M2N, 2M2O, 2M2P, 2OLY, 2OLZ, 2OM0, 2OM1, 2OMG, 2OMH, 2OMI, 2QIU, 2R34, 2R35, 2R36, 2RN5, 2VJZ, 2VK0, 2W44, 2WBY, 2WC0, 2WRU, 2WRV, 2WRW, 2WRX, 2WS0, 2WS1, 2WS4, 2WS6, 2WS7, 3AIY, 3BXQ, 3E7Y, 3E7Z, 3EXX, 3FQ9, 3HYD, 3I3Z, 3I40, 3ILG, 3INC, 3IR0, 3Q6E, 3ROV, 3TT8, 3U4N, 3UTQ, 3UTS, 3UTT, 3V19, 3V1G, 3W11, 3W12, 3W13, 3W7Y, 3W7Z, 3W80, 3ZI3, 3ZQR, 3ZS2, 3ZU1, 4AIY, 4AJX, 4AJZ, 4AK0, 4AKJ, 4EFX, 4EWW, 4EWX, 4EWZ, 4EX0, 4EX1, 4EXX, 4EY1, 4EY9, 4EYD, 4EYN, 4EYP, 4F0N, 4F0O, 4F1A, 4F1B, 4F1C, 4F1D, 4F1F, 4F1G, 4F4T, 4F4V, 4F51, 4F8F, 4FG3, 4FKA, 4GBC, 4GBI, 4GBK, 4GBL, 4GBN, 4IUZ, 5AIY, 2LWZ, 3JSD, 3KQ6, 3P2X, 3P33, 1JK8, 2MLI, 2MPG, 2MPI, 2MVC, 2MVD, 2OMQ, 4CXL, 4CXN, 4CY7, 4IYD, 4IYF, 4NIB, 4OGA, 4P65, 4Q5Z, 4RXW, 4UNE, 4UNG, 4UNH, 4XC4, 4WDI, 4Z76, 4Z77, 4Z78, 2N2W, 5CO6, 5ENA, 4Y19, 5BQQ, 5BOQ, 2N2V, 5CNY, 5CO9, 5EN9, 4Y1A, 2N2X, 5BPO, 5CO2, 5BTS, 5HYJ, 5C0D,%%s1A7F, 1AI0, 1AIY, 1B9E, 1BEN, 1EFE, 1EV3, 1EV6, 1EVR, 1FU2, 1FUB, 1G7A, 1G7B, 1GUJ, 1HIQ, 1HIS, 1HIT, 1HLS, 1HTV, 1HUI, 1IOG, 1IOH, 1J73, 1JCA, 1JCO, 1K3M, 1KMF, 1LKQ, 1LPH, 1MHI, 1MHJ, 1MSO, 1OS3, 1OS4, 1Q4V, 1QIY, 1QIZ, 1QJ0, 1RWE, 1SF1, 1SJT, 1SJU, 1T0C, 1T1K, 1T1P, 1T1Q, 1TRZ, 1TYL, 1TYM, 1UZ9, 1VKT, 1W8P, 1XDA, 1XGL, 1XW7, 1ZEG, 1ZEH, 1ZNJ, 2AIY, 2C8Q, 2C8R, 2CEU, 2G54, 2G56, 2H67, 2HH4, 2HHO, 2HIU, 2JMN, 2JUM, 2JUU, 2JUV, 2JV1, 2JZQ, 2K91, 2K9R, 2KJJ, 2KJU, 2KQP, 2KQQ, 2KXK, 2L1Y, 2L1Z, 2LGB, 2M1D, 2M1E, 2M2M, 2M2N, 2M2O, 2M2P, 2OLY, 2OLZ, 2OM0, 2OM1, 2OMG, 2OMH, 2OMI, 2QIU, 2R34, 2R35, 2R36, 2RN5, 2VJZ, 2VK0, 2W44, 2WBY, 2WC0, 2WRU, 2WRV, 2WRW, 2WRX, 2WS0, 2WS1, 2WS4, 2WS6, 2WS7, 3AIY, 3BXQ, 3E7Y, 3E7Z, 3EXX, 3FQ9, 3HYD, 3I3Z, 3I40, 3ILG, 3INC, 3IR0, 3Q6E, 3ROV, 3TT8, 3U4N, 3UTQ, 3UTS, 3UTT, 3V19, 3V1G, 3W11, 3W12, 3W13, 3W7Y, 3W7Z, 3W80, 3ZI3, 3ZQR, 3ZS2, 3ZU1, 4AIY, 4AJX, 4AJZ, 4AK0, 4AKJ, 4EFX, 4EWW, 4EWX, 4EWZ, 4EX0, 4EX1, 4EXX, 4EY1, 4EY9, 4EYD, 4EYN, 4EYP, 4F0N, 4F0O, 4F1A, 4F1B, 4F1C, 4F1D, 4F1F, 4F1G, 4F4T, 4F4V, 4F51, 4F8F, 4FG3, 4FKA, 4GBC, 4GBI, 4GBK, 4GBL, 4GBN, 4IUZ, 5AIY, 2LWZ, 3JSD, 3KQ6, 3P2X, 3P33, 1JK8, 2MLI, 2MPG, 2MPI, 2MVC, 2MVD, 2OMQ, 4CXL, 4CXN, 4CY7, 4IYD, 4IYF, 4NIB, 4OGA, 4P65, 4Q5Z, 4RXW, 4UNE, 4UNG, 4UNH, 4XC4, 4WDI, 4Z76, 4Z77, 4Z78, 2N2W, 5CO6, 5ENA, 4Y19, 5BQQ, 5BOQ, 2N2V, 5CNY, 5CO9, 5EN9, 4Y1A, 2N2X, 5BPO, 5CO2, 5BTS, 5HYJ, 5C0D363016334ENSG00000254647ENSMUSG00000000215P01308P01326NM_000207NM_001185097NM_001185098NM_001291897NM_001185083NM_001185084NM_008387NP_001172026.1NP_001172027.1NP_001278826.1NP_000198NP_001172026NP_001172027NP_001278826NP_001172012NP_001172013NP_032413Insufficient recognition has been given to Paulescu, the distinguished Romanian scientist, who at the time when the Toronto team were commencing their research had already succeeded in extracting the antidiabetic hormone of the pancreas and proving its efficacy in reducing the hyperglycaemia in diabetic dogs.1ai0: R6 HUMAN INSULIN HEXAMER (NON-SYMMETRIC), NMR, 10 STRUCTURES1aiy: R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, 10 STRUCTURES1aph: CONFORMATIONAL CHANGES IN CUBIC INSULIN CRYSTALS IN THE PH RANGE 7-111b17: PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 5.00 COORDINATES)1b18: PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 5.53 COORDINATES)1b19: PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 5.80 COORDINATES)1b2a: PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.00 COORDINATES)1b2b: PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.16 COORDINATES)1b2c: PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.26 COORDINATES)1b2d: PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.35 COORDINATES)1b2e: PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.50 COORDINATES)1b2f: PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.98 COORDINATES)1b2g: PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 9.00 COORDINATES)1b9e: HUMAN INSULIN MUTANT SERB9GLU1ben: INSULIN COMPLEXED WITH 4-HYDROXYBENZAMIDE1bph: CONFORMATIONAL CHANGES IN CUBIC INSULIN CRYSTALS IN THE PH RANGE 7-111cph: CONFORMATIONAL CHANGES IN CUBIC INSULIN CRYSTALS IN THE PH RANGE 7-111dph: CONFORMATIONAL CHANGES IN CUBIC INSULIN CRYSTALS IN THE PH RANGE 7-111ev3: Structure of the rhombohedral form of the M-cresol/insulin R6 hexamer1ev6: Structure of the monoclinic form of the M-cresol/insulin R6 hexamer1evr: The structure of the resorcinol/insulin R6 hexamer1fu2: FIRST PROTEIN STRUCTURE DETERMINED FROM X-RAY POWDER DIFFRACTION DATA1fub: FIRST PROTEIN STRUCTURE DETERMINED FROM X-RAY POWDER DIFFRACTION DATA1g7a: 1.2 A structure of T3R3 human insulin at 100 K1g7b: 1.3 A STRUCTURE OF T3R3 HUMAN INSULIN AT 100 K1guj: INSULIN AT PH 2: STRUCTURAL ANALYSIS OF THE CONDITIONS PROMOTING INSULIN FIBRE FORMATION.1hiq: PARADOXICAL STRUCTURE AND FUNCTION IN A MUTANT HUMAN INSULIN ASSOCIATED WITH DIABETES MELLITUS1hit: RECEPTOR BINDING REDEFINED BY A STRUCTURAL SWITCH IN A MUTANT HUMAN INSULIN1hls: NMR STRUCTURE OF THE HUMAN INSULIN-HIS(B16)1htv: CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN1iza: ROLE OF B13 GLU IN INSULIN ASSEMBLY: THE HEXAMER STRUCTURE OF RECOMBINANT MUTANT (B13 GLU-> GLN) INSULIN1izb: ROLE OF B13 GLU IN INSULIN ASSEMBLY: THE HEXAMER STRUCTURE OF RECOMBINANT MUTANT (B13 GLU-> GLN) INSULIN1j73: Crystal structure of an unstable insulin analog with native activity.1jca: Non-standard Design of Unstable Insulin Analogues with Enhanced Activity1jco: Solution structure of the monomeric insulin mutant (PT insulin)1lph: LYS(B28)PRO(B29)-HUMAN INSULIN1m5a: Crystal Structure of 2-Co(2+)-Insulin at 1.2A Resolution1mhi: THREE-DIMENSIONAL SOLUTION STRUCTURE OF AN INSULIN DIMER. A STUDY OF THE B9(ASP) MUTANT OF HUMAN INSULIN USING NUCLEAR MAGNETIC RESONANCE DISTANCE GEOMETRY AND RESTRAINED MOLECULAR DYNAMICS1mhj: SOLUTION STRUCTURE OF THE SUPERACTIVE MONOMERIC DES- HUMAN INSULIN MUTANT. ELUCIDATION OF THE STRUCTURAL BASIS FOR THE MONOMERIZATION OF THE DES- INSULIN AND THE DIMERIZATION OF NATIVE INSULIN1mpj: X-RAY CRYSTALLOGRAPHIC STUDIES ON HEXAMERIC INSULINS IN THE PRESENCE OF HELIX-STABILIZING AGENTS, THIOCYANATE, METHYLPARABEN AND PHENOL1mso: T6 Human Insulin at 1.0 A Resolution1os3: Dehydrated T6 human insulin at 100 K1os4: Dehydrated T6 human insulin at 295 K1q4v: CRYSTAL STRUCTURE OF ALLO-ILEA2-INSULIN, AN INACTIVE CHIRAL ANALOGUE: IMPLICATIONS FOR THE MECHANISM OF RECEPTOR1qiy: HUMAN INSULIN HEXAMERS WITH CHAIN B HIS MUTATED TO TYR COMPLEXED WITH PHENOL1qiz: HUMAN INSULIN HEXAMERS WITH CHAIN B HIS MUTATED TO TYR COMPLEXED WITH RESORCINOL1qj0: HUMAN INSULIN HEXAMERS WITH CHAIN B HIS MUTATED TO TYR1rwe: Enhancing the activity of insulin at receptor edge: crystal structure and photo-cross-linking of A8 analogues1sf1: NMR STRUCTURE OF HUMAN INSULIN under Amyloidogenic Condition, 15 STRUCTURES1t0c: Solution Structure of Human Proinsulin C-Peptide1trz: CRYSTALLOGRAPHIC EVIDENCE FOR DUAL COORDINATION AROUND ZINC IN THE T3R3 HUMAN INSULIN HEXAMER1tyl: THE STRUCTURE OF A COMPLEX OF HEXAMERIC INSULIN AND 4'-HYDROXYACETANILIDE1tym: THE STRUCTURE OF A COMPLEX OF HEXAMERIC INSULIN AND 4'-HYDROXYACETANILIDE1uz9: CRYSTALLOGRAPHIC AND SOLUTION STUDIES OF N-LITHOCHOLYL INSULIN: A NEW GENERATION OF PROLONGED-ACTING INSULINS.1w8p: STRUCTURAL PROPERTIES OF THE B25TYR-NME-B26PHE INSULIN MUTANT.1wav: CRYSTAL STRUCTURE OF FORM B MONOCLINIC CRYSTAL OF INSULIN1xda: STRUCTURE OF INSULIN1xgl: HUMAN INSULIN DISULFIDE ISOMER, NMR, 10 STRUCTURES1xw7: Diabetes-Associated Mutations in Human Insulin: Crystal Structure and Photo-Cross-Linking Studies of A-Chain Variant Insulin Wakayama1zeg: STRUCTURE OF B28 ASP INSULIN IN COMPLEX WITH PHENOL1zeh: STRUCTURE OF INSULIN1zni: INSULIN1znj: INSULIN, MONOCLINIC CRYSTAL FORM2a3g: The structure of T6 bovine insulin2aiy: R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, 20 STRUCTURES2bn1: INSULIN AFTER A HIGH DOSE X-RAY BURN2bn3: INSULIN BEFORE A HIGH DOSE X-RAY BURN2c8q: INSULINE(1SEC) AND UV LASER EXCITED FLUORESCENCE2c8r: INSULINE(60SEC) AND UV LASER EXCITED FLUORESCENCE2g4m: Insulin collected at 2.0 A wavelength2g54: Crystal structure of Zn-bound human insulin-degrading enzyme in complex with insulin B chain2g56: crystal structure of human insulin-degrading enzyme in complex with insulin B chain2hiu: NMR STRUCTURE OF HUMAN INSULIN IN 20% ACETIC ACID, ZINC-FREE, 10 STRUCTURES2ins: THE STRUCTURE OF DES-PHE B1 BOVINE INSULIN2omg: Structure of human insulin cocrystallized with protamine and urea2omh: Structure of human insulin cocrystallized with ARG-12 peptide in presence of urea2omi: Structure of human insulin cocrystallized with protamine2tci: X-RAY CRYSTALLOGRAPHIC STUDIES ON HEXAMERIC INSULINS IN THE PRESENCE OF HELIX-STABILIZING AGENTS, THIOCYANATE, METHYLPARABEN AND PHENOL3aiy: R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, REFINED AVERAGE STRUCTURE3ins: STRUCTURE OF INSULIN. RESULTS OF JOINT NEUTRON AND X-RAY REFINEMENT3mth: X-RAY CRYSTALLOGRAPHIC STUDIES ON HEXAMERIC INSULINS IN THE PRESENCE OF HELIX-STABILIZING AGENTS, THIOCYANATE, METHYLPARABEN AND PHENOL4aiy: R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, 'GREEN' SUBSTATE, AVERAGE STRUCTURE4ins: THE STRUCTURE OF 2ZN PIG INSULIN CRYSTALS AT 1.5 ANGSTROMS RESOLUTION5aiy: R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, 'RED' SUBSTATE, AVERAGE STRUCTURE6ins: X-RAY ANALYSIS OF THE SINGLE CHAIN /B29-A1$ PEPTIDE-LINKED INSULIN MOLECULE. A COMPLETELY INACTIVE ANALOGUE7ins: STRUCTURE OF PORCINE INSULIN COCRYSTALLIZED WITH CLUPEINE Z9ins: MONOVALENT CATION BINDING IN CUBIC INSULIN CRYSTALS Insulin (from Latin insula, island) is a peptide hormone produced by beta cells of the pancreatic islets; it is considered to be the main anabolic hormone of the body. It regulates the metabolism of carbohydrates, fats and protein by promoting the absorption of carbohydrates, especially glucose from the blood into liver, fat and skeletal muscle cells. In these tissues the absorbed glucose is converted into either glycogen via glycogenesis or fats (triglycerides) via lipogenesis, or, in the case of the liver, into both. Glucose production and secretion by the liver is strongly inhibited by high concentrations of insulin in the blood. Circulating insulin also affects the synthesis of proteins in a wide variety of tissues. It is therefore an anabolic hormone, promoting the conversion of small molecules in the blood into large molecules inside the cells. Low insulin levels in the blood have the opposite effect by promoting widespread catabolism, especially of reserve body fat. Beta cells are sensitive to glucose concentrations, also known as blood sugar levels. When the glucose level is high, the beta cells secrete insulin into the blood; when glucose levels are low, secretion of insulin is inhibited. Their neighboring alpha cells, by taking their cues from the beta cells, secrete glucagon into the blood in the opposite manner: increased secretion when blood glucose is low, and decreased secretion when glucose concentrations are high. Glucagon, through stimulating the liver to release glucose by glycogenolysis and gluconeogenesis, has the opposite effect of insulin. The secretion of insulin and glucagon into the blood in response to the blood glucose concentration is the primary mechanism of glucose homeostasis. If beta cells are destroyed by an autoimmune reaction, insulin can no longer be synthesized or be secreted into the blood. This results in type 1 diabetes mellitus, which is characterized by abnormally high blood glucose concentrations, and generalized body wasting. In type 2 diabetes mellitus the destruction of beta cells is less pronounced than in type 1 diabetes, and is not due to an autoimmune process. Instead there is an accumulation of amyloid in the pancreatic islets, which likely disrupts their anatomy and physiology. The pathogenesis of type 2 diabetes is not well understood but patients exhibit a reduced population of islet beta-cells, reduced secretory function of islet beta-cells that survive, and peripheral tissue insulin resistance. Type 2 diabetes is characterized by high rates of glucagon secretion into the blood which are unaffected by, and unresponsive to the concentration of glucose in the blood. Insulin is still secreted into the blood in response to the blood glucose. As a result, the insulin levels, even when the blood sugar level is normal, are much higher than they are in healthy persons. The human insulin protein is composed of 51 amino acids, and has a molecular mass of 5808 Da. It is a dimer of an A-chain and a B-chain, which are linked together by disulfide bonds. Insulin's structure varies slightly between species of animals. Insulin from animal sources differs somewhat in effectiveness (in carbohydrate metabolism effects) from human insulin because of these variations. Porcine insulin is especially close to the human version, and was widely used to treat type 1 diabetics before human insulin could be produced in large quantities by recombinant DNA technologies. The crystal structure of insulin in the solid state was determined by Dorothy Hodgkin. It is on the WHO Model List of Essential Medicines, the most important medications needed in a basic health system. Insulin may have originated more than a billion years ago. The molecular origins of insulin go at least as far back as the simplest unicellular eukaryotes. Apart from animals, insulin-like proteins are also known to exist in the Fungi and Protista kingdoms. Insulin is produced by beta cells of the pancreatic islets in most vertebrates and by the Brockmann body in some teleost fish. Cone snails Conus geographus and Conus tulipa, venomous sea snails that hunt small fish, use modified forms of insulin in their venom cocktails. The insulin toxin, closer in structure to fishes' than to snails' native insulin, slows down the prey fishes by lowering their blood glucose levels. The preproinsulin precursor of insulin is encoded by the INS gene. A variety of mutant alleles with changes in the coding region have been identified. A read-through gene, INS-IGF2, overlaps with this gene at the 5' region and with the IGF2 gene at the 3' region.

[ "Diabetes mellitus", "Internal medicine", "Endocrinology", "Biotechnology", "diabetic animal", "Hyperglycemic agent", "Intensive insulinotherapy", "Oreocnide integrifolia", "Home blood glucose monitoring" ]
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