Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications

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9780306448300: Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications

The 5th International Conference on Aspartic Proteinases was held on September 19 through 24, 1993, at Naito Museum of Pharmaceutical Science and Industry, Kawashima- cho, Gifu Prefecture, Japan, about 15 miles northwest of Nagoya City. About 100 scientists attended the conference, including 52 from 14 countries outside Japan, and 32 papers were presented by invited speakers, and 58 papers as posters. The purpose of this conference was to present and discuss new information on the structure, function, and biology, and related topics, including biomedical implications, of aspartic proteinases, and this book is a collec- tion of nearly all the papers presented at the meeting. Aspartic proteinases belong to one of the four major classes of proteinases, the others being serine, cysteine, and metalloproteinases, and are so called since they have two catalytic aspartic acid residues in common in their active sites. Most of them are optimally active at acidic pH, hence the long-used name "acid proteinases," which, indeed, was the major title of the first conference of this series. However, some of them are active at around neutral pH, indicating their physiological roles in a wider range of pH than hitherto considered.

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Contenuti:

Gastric Aspartic Proteinases: Plenary Lectures.- 1. Comparison of the Active Site Specificity of the Aspartic Proteinases Based on a Systematic Series of Peptide Substrates.- 2. The Molecular Structure of Human Progastricsin and Its Comparison with that of Porcine Pepsinogen.- 3. A New Way of Looking at Aspartic Proteinase Structures: A Comparison of Pepsin Structure to Other Aspartic Proteinases in the Near Active Site Region.- 4. Rearranging Pepsinogen and Pepsin by Protein Engineering.- 5. Comparative Investigations on Pig Gastric Proteases and Their Zymogens.- 6. Non-Mammalian Vertebrate Pepsinogens and Pepsins: Isolation and Characterization.- 7. Transcription Regulation of Human and Porcine Pepsinogen A.- Gastric Aspartic Proteinases: Poster Reports.- 8. A Comparative Study on Amino Acid Sequences of Three Major Isoforms of Human Pepsin A.- 9. Molecular Mass Determination by Electrospray Mass Spectrometry of Human Pepsins, Gastricsin, and Porcine Pepsin A Variants.- 10. Evidence for Electrostatic Interactions in the S2 Subsite of Porcine Pepsin.- 11. Protein Engineering of Surface Loops: Preliminary X-Ray Analysis of the CHY155-165RHI Mutant.- 12. Seminal Progastricsin.- 13. Effects of Hydrocortisone on the Pepsinogen-Producing Cells in Rat Stomach Mucosa.- 14. Effects of Omeprazole, a Proton Pump Inhibitor on Pepsinogen-Producing Cells, with Special Reference to Neonatal Development.- 15. Transcription of Embryonic Chick Pepsinogen Gene Is Affected by Mesenchymal Signals through Its 5?-Flanking Region.- 16. Serum Pepsinogen Values as Possible Markers for Evaluating the Possibility of Peptic Ulcer Recurrence under H2-Blocker Half-Dose Maintenance Therapy.- 17. The Clinical Application of the Serum Pepsinogen I and II Levels as a Mass Screening Method for Gastric Cancer.- 18. A Minute Gastric Cancer Detected by a New Screening Method Using Serum Pepsinogen I and II.- 19. Two Cases of Early Colorectal Cancer Associated with Gastric Adenoma Detected by Serum Pepsinogen Screening Method.- Non-Gastric Aspartic Proteinases: Plenary Lectures.- 20. Comparisons of the Three-Dimensional Structures, Specificities and Glycosylation of Renins, Yeast Proteinase A and Cathepsin D.- 21. Discovery of Inhibitors of Human Renin with High Oral Bioavailability.- 22. Structure of Human Cathepsin D: Comparison of Inhibitor Binding and Subdomain Displacement with Other Aspartic Proteases.- 23. Cathepsin D Crystal Structures and Lysosomal Sorting.- 24. Isolation and Characterization of Human Gastric Procathepsin E and Cathepsin E.- 25. Isolation, Characterization, and Structure of Procathepsin E and Cathepsin E from the Gastric Mucosa of Guinea Pig.- 26. Cathepsin E and Cathepsin D: Biosynthesis, Processing, and Subcellular Location.- 27. Glycoproteins of the Aspartyl Proteinase Gene Family Secreted by the Developing Placenta.- 28. Structure and Possible Function of Aspartic Proteinases in Barley and Other Plants.- 29. Aspartic Proteinases (Cyprosins) from Cynara cardunculus spp. flavescens cv. Cardoon Purification, Characterisation, and Tissue-Specific Expression.- Non-Gastric Aspartic Proteinases: Poster Reports.- 30. Acid-Activation of Rat Prorenin following Non-Proteolytic Alteration.- 31. Human Procathepsin D: Three-Dimensional Model and Isolation.- 32. Identification of Five Molecular Forms of Cathepsin D in Bovine Milk.- 33. Site-Directed Mutagenesis of a Disulfide Bridge in Cathepsin D: Expression, Activation, Purification, and Characterization.- 34. Expression of Rat Cathepsin D cDNA in Saccharomyces cerevisiae: Intracellular Sorting of Cathepsin D to Yeast Vacuole.- 35. Molecular Cloning and Immunocytochemical Localization of Jasmonic Acid Inducible Cathepsin D Inhibitors from Potato.- 36. Purification and Characterization of an Acid Proteinase from Dirofilaria immitis Worms.- 37. Inhibition and Entrapment of Aspartic Proteinases by ?2-Macroglobulin.- 38. Recombinant Human Cathepsin E.- 39. Expression of Human Cathepsin E in Methylotrophic Yeast, Pichia pastoris.- 40. Purification and Characterization of Recombinant Human Cathepsin E.- 41. Comparison of Biochemical Properties of Natural and Recombinant Cathepsin E.- 42. Increased Expression and Specific Localization of Cathepsins E and D in Vulnerable Brain Regions of Aged and Postischemic Rats.- 43. Characterization of Cathepsins E and D Accumulated at Early Stages of Neuronal Damage in Hippocampal Neurons of Rats.- 44. Functional Aspects of Cathepsin E: Is It an Embryonic or Fetal Type of Aspartic Proteinase?.- 45. Tissue- and Cell-Specific Control of Guinea Pig Cathepsin E Gene Expression.- 46. Cathepsin E Is Expressed in Fetal Rat Glandular Stomach Epithelial Cells in Primary Culture in the Absence of Mesenchymes.- 47. Cathepsin E Expressed in Pancreatic Cancer.- 48. Plant Aspartic Proteinases from Cynara cardunculus spp. flavescens cv. Cardoon; Nucleotide Sequence of a cDNA Encoding Cyprosin and Its Organ-Specific Expression.- 49. Cardosin A and B, Aspartic Proteases from the Flowers of Cardoon.- Retroviral Aspartic Proteinases: Plenary Lectures.- 50. Mechanism of Autoprocessing of a Mini-Precursor of the Aspartic Protease of Human Immunodeficiency Virus Type 1.- 51. Mutants of HIV-1 Protease with Enhanced Stability to Autodegradation.- 52. Identification of Amino Acid Residues of the Retroviral Aspartic Proteinases Important for Substrate Specificity and Catalytic Efficiency.- 53. Inhibitor-Resistant Mutants of the HIV-1 Aspartic Protease.- 54. Design and Synthesis of HIV Protease Inhibitors Containing Allophenylnorstatine as a Transition-State Mimic.- 55. Breaking the Shackles of the Genetic Code: Engineering Retroviral Proteases through Total Chemical Synthesis.- Retroviral Aspartic Proteinases: Poster Reports.- 56. X-Ray Structure of a Tethered Dimer for HIV-1 Protease.- 57. Structure of HIV-1 Protease with KNI-272: A Transition State Mimetic Inhibitor Containing Allophenylnorstatine.- 58. Molecular Dynamics of HIV-1 Protease in Complex with a Difluoroketone-Containing Inhibitor: Implications for the Catalytic Mechanism.- 59. Activated Dynamics of Flap Opening in HIV-1 Protease.- 60. Computer Simulation and Analysis of the Reaction Pathway for the Decomposition of the Hydrated Peptide Bond in Aspartic Proteases.- 61. Activities of Precursor and Tethered Dimer Forms of HIV Proteinase.- 62. Site-Directed Mutagenesis of HIV-1 Protease: Generation of Mutant Proteases with Increased Stability to Autodigestion.- 63. Molecular Modeling of the Structure of FIV Protease.- 64. Processing, Purification, and Kinetic Characterization of the Gag-Pol Encoded Retroviral Proteinase of Myeloblastosis Associated Virus Expressed in E. coli.- Microbial Aspartic Proteinases: Plenary Lectures.- 65. Extracellular Aspartic Proteinases from Candida Yeasts.- 66. Tyrosine 75 on the Flap Contributes to Enhance Catalytic Efficiency of a Fungal Aspartic Proteinase, Mucor pusillus Pepsin.- 67. Aspartic Proteinases from the Human Malaria Parasite Plasmodium falciparum.- 68. Yeast and Mammalian Basic Residue-Specific Aspartic Proteases in Prohormone Conversion.- 69. Pepstatin-Insensitive Carboxyl Proteinases.- Microbial Aspartic Proteinases: Poster Reports.- 70. The Three-Dimensional X-Ray Crystal Structure of the Aspartic Proteinase Native to Trichoderma reesei Complexed with a Renin Inhibitor CP-80794.- 71. A Quantum Mechanical Model of the Hydration and Acidity of the Active Site in Aspartic Proteases.- 72. Site-Directed Mutagenesis of Rhizopuspepsin: An Analysis of Unique Specificity.- 73. Site-Directed Mutagenesis Revealed Role of Subsite Residues of Mucor pusillus Pepsin in Catalytic Function.- 74. A Novel Intracellular Acid Proteinase from the Plasmodia of a True Slime Mold, Physarum polycephalum.- 75. Characteristics of YAP3, a New Prohormone Processing Aspartic Protease from S. cerevisiae.- 76. Candida albicans Aspartic Proteinase: cDNA Cloning and Comparison among Strains.- 77. Molecular Cloning and Sequence Analysis of a Gene Encoding an Aspartic Proteinase from Aspergillus oryzae.- 78. Aspergillus niger var. macrosporus Proteinase B. cDNA Cloning, Expression, and Activation of the Proenzyme.- 79. Expression and Secretion of Recombinant Aspartic Proteinases by Bacillus brevis.- 80. Expression in E.coliAspergillus niger var. macrosporus Proteinase A, a Non-Pepsin Type Acid Proteinase.- 81. X-Ray Crystallographic Study of a Non-Pepsin-Type Acid Proteinase, Aspergillus niger Proteinase A.- 82. Conformation Analysis of Non-Pepsin-Type Acid Proteinase A from the Fungus Aspergillus niger by NMR.- Author Index.

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Descrizione libro Springer Aug 1995, 1995. Buch. Condizione libro: Neu. 254x178x45 mm. This item is printed on demand - Print on Demand Neuware - The 5th International Conference on Aspartic Proteinases was held on September 19 through 24, 1993, at Naito Museum of Pharmaceutical Science and Industry, Kawashima cho, Gifu Prefecture, Japan, about 15 miles northwest of Nagoya City. About 100 scientists attended the conference, including 52 from 14 countries outside Japan, and 32 papers were presented by invited speakers, and 58 papers as posters. The purpose of this conference was to present and discuss new information on the structure, function, and biology, and related topics, including biomedical implications, of aspartic proteinases, and this book is a collec tion of nearly all the papers presented at the meeting. Aspartic proteinases belong to one of the four major classes of proteinases, the others being serine, cysteine, and metalloproteinases, and are so called since they have two catalytic aspartic acid residues in common in their active sites. Most of them are optimally active at acidic pH, hence the long-used name 'acid proteinases,' which, indeed, was the major title of the first conference of this series. However, some of them are active at around neutral pH, indicating their physiological roles in a wider range of pH than hitherto considered. 656 pp. Englisch. Codice libro della libreria 9780306448300

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Descrizione libro Springer Science+Business Media, United States, 1995. Hardback. Condizione libro: New. 1995 ed.. 251 x 165 mm. Language: English . Brand New Book ***** Print on Demand *****. The 5th International Conference on Aspartic Proteinases was held on September 19 through 24, 1993, at Naito Museum of Pharmaceutical Science and Industry, Kawashima- cho, Gifu Prefecture, Japan, about 15 miles northwest of Nagoya City. About 100 scientists attended the conference, including 52 from 14 countries outside Japan, and 32 papers were presented by invited speakers, and 58 papers as posters. The purpose of this conference was to present and discuss new information on the structure, function, and biology, and related topics, including biomedical implications, of aspartic proteinases, and this book is a collec- tion of nearly all the papers presented at the meeting. Aspartic proteinases belong to one of the four major classes of proteinases, the others being serine, cysteine, and metalloproteinases, and are so called since they have two catalytic aspartic acid residues in common in their active sites. Most of them are optimally active at acidic pH, hence the long-used name acid proteinases, which, indeed, was the major title of the first conference of this series. However, some of them are active at around neutral pH, indicating their physiological roles in a wider range of pH than hitherto considered. Codice libro della libreria APC9780306448300

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Descrizione libro Springer Science+Business Media, United States, 1995. Hardback. Condizione libro: New. 1995 ed.. 251 x 165 mm. Language: English . Brand New Book ***** Print on Demand *****.The 5th International Conference on Aspartic Proteinases was held on September 19 through 24, 1993, at Naito Museum of Pharmaceutical Science and Industry, Kawashima- cho, Gifu Prefecture, Japan, about 15 miles northwest of Nagoya City. About 100 scientists attended the conference, including 52 from 14 countries outside Japan, and 32 papers were presented by invited speakers, and 58 papers as posters. The purpose of this conference was to present and discuss new information on the structure, function, and biology, and related topics, including biomedical implications, of aspartic proteinases, and this book is a collec- tion of nearly all the papers presented at the meeting. Aspartic proteinases belong to one of the four major classes of proteinases, the others being serine, cysteine, and metalloproteinases, and are so called since they have two catalytic aspartic acid residues in common in their active sites. Most of them are optimally active at acidic pH, hence the long-used name acid proteinases, which, indeed, was the major title of the first conference of this series. However, some of them are active at around neutral pH, indicating their physiological roles in a wider range of pH than hitherto considered. Codice libro della libreria APC9780306448300

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