Structure and Function of the Aspartic Proteinases

Table of Contents

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   Book Overview
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   Chapter 1 Studies on Pepsin Mutagenesis and Recombinant Rhizopuspepsinogen
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   Chapter 2 Inhibitor Binding Induces Structural Changes in Porcine Pepsin
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   Chapter 3 Functional implications of the three-dimensional structure of bovine chymosin.
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   Chapter 4 Why Does Pepsin Have a Negative Charge at Very Low pH? An Analysis of Conserved Charged Residues in Aspartic Proteinases
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   Chapter 5 X-Ray Structural Studies of Mammalian Aspartic Proteinases
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   Chapter 6 Aspartic Protease Inhibitors from the Parasitic Nematode Ascaris
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   Chapter 7 Nonspecific Electrostatic Binding of Substrates and Inhibitors to Porcine Pepsin
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   Chapter 8 Analysis of the Promoter of a Human Pepsinogen a Gene
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    Chapter 9 Separation and Characterization of Human Pepsinogens and Pepsins by High-Resolution Discontinuous Electrophoresis
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    Chapter 10 A Highly Informative Polymorphism of the Pepsinogen C Gene Detected by Polymerase Chain Reaction
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    Chapter 11 Consequences of Intramolecular Ionic Interactions for the Activation Rate of Human Pepsinogens A and C as Revealed by Molecular Modelling
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    Chapter 12 Characteristics and Composition of Pepsins from Atlantic Cod
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    Chapter 13 Reduction of Non-Steroidal Anti-Inflammatory Drug Induced Gastric Damage in the Rat by Soluble Pepstatin Derivatives
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    Chapter 14 Production of Prochymosin in Lactococci
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    Chapter 15 Structure and Chromosomal Localization of the Human Prochymosin Pseudogene
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    Chapter 16 Amino Acid Sequence of Lamb Preprochymosin and its Comparison to Other Chymosins
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    Chapter 17 Quantum-Chemical Study of the Catalytic Mechanism of Aspartic Proteinases
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    Chapter 18 Effects of Viscosity and Solvent Deuterium Identify Multiple Partially Rate-Limiting Steps in the Kinetics of Porcine Pepsin
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    Chapter 19 Structure-Function Database for Active Site Binding to the Aspartic Proteinases
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    Chapter 20 Introduction to Fungal Proteinases and Expression in Fungal Systems
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    Chapter 21 Characterization of the Bar proteinase, an extracellular enzyme from the yeast Saccharomyces cerevisiae.
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    Chapter 22 Candida Albicans Acid Proteinase: Characterization and Role in Candidiasis
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    Chapter 23 Pepstatin-Insensitive Carboxyl Proteinases
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    Chapter 24 Structure and Function of a Pepstatin-Insensitive Acid Proteinase from Aspergillus Niger var. Macrosporus
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    Chapter 25 Infection and Pathogenesis of Cash Crops by Botrytis Cinerea : Primary Role of an Aspartic Proteinase
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    Chapter 26 Crystal Structures of Rhizopuspepsin/Inhibitor Complexes
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    Chapter 27 A Yeast Expression System and Site-Directed Mutagenesis of a Fungal Aspartic Proteinase, Mucor Rennin
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    Chapter 28 Studies on the Mechanism of Action of Penicillopepsin
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    Chapter 29 Thermopsin, A Thermostable Acid Protease from Sulfolobus Acidocaldarius
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    Chapter 30 Purification of an Aspartic Proteinase from Aspergillus Aculeatus
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    Chapter 31 Effect of Growth Conditions on the Extracellular Production of the Aspartic Proteinase by Candida Albicans
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    Chapter 32 X-ray analysis of a difluorostatone renin inhibitor bound as the tetrahedral hydrate to the aspartic protease endothiapepsin.
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    Chapter 33 Substrate Specificity Study of Recombinant Rhizopus Chinensis Aspartic Proteinase
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    Chapter 34 Localization of Cathepsin D in Endosomes: Characterization and Biological Importance
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    Chapter 35 Proteolytic Activation of Human Procathepsin D
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    Chapter 36 Biological significance and activity control of cathepsin E compared with cathepsin D.
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    Chapter 37 Exploiting the Molecular Template of Angiotensinogen in the Discovery and Design of Peptidyl, Pseudopeptidyl and Peptidemimetic Inhibitors of Human Renin: A Structure-Activity Perspective
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    Chapter 38 Design of Renin Inhibitors Containing Conformationally Restricted Mimetics of the P 1 -P 1 ′ and P 1 through P 2 ′ Sites
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    Chapter 39 Efficient Mutagenesis, Expression and Purification of Procathepsin D
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    Chapter 40 Mapping of Lysosomal Targeting Determinants of Cathepsin D
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    Chapter 41 Comparison of Kinetic Properties of Native and Recombinant Human Cathepsin D
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    Chapter 42 Cathepsin D Inhibitor from Potato Tubers ( Solanum tuberosum L.)
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    Chapter 43 Aspartic Proteinase from Barley Seeds is Related to Animal Cathepsin D
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    Chapter 44 Immunohistochemical and Immunocytochemical Localization of Cathepsin E Compared with Cathepsin D
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    Chapter 45 Origins of the Multiple Cathepsin E Transcripts Observed in Human Gastric Mucosa and Gastric Adenocarcinoma
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    Chapter 46 Human Stomach Cathepsin E Action on Human Immunoglobulins
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    Chapter 47 The Engineering of Recombinant Active Human Prerenin and its Expression in Mammalian and Insect Cells
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    Chapter 48 Simple Procedure for Recovery of Crystallizable Human Recombinant Renin from Mammalian Cell-Conditioned Medium
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    Chapter 49 Substrate Specificity of Human Renin: The Effect of Substitutions at the Amino Terminus and P 3 Position of the Substrate
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    Chapter 50 Substrate Analogue Renin Inhibitors Containing Replacements of Histidine in P 2 or Isosteres of the Amide Bond Between P 3 and P 2 Sites
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    Chapter 51 Molecular modeling of renin inhibitor P2 substituents.
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    Chapter 52 Human Immunodeficiency Virus Proteinase: Now, Then, What’s Next?
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    Chapter 53 Substrate Specificity of the Human (Type 1) and Simian Immunodeficiency Virus Proteases
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    Chapter 54 Expression and Characterization of Genetically Linked Homo- and Hetero-Dimers of Hiv Proteinase
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    Chapter 55 Expression of the HIV Aspartic Protease Fused to a Bacterial Phenotypic Marker
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    Chapter 56 Comparison of Three Inhibitor Complexes of Human Immunodeficiency Virus Protease
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    Chapter 57 Comparisons of the sequences, 3-D structures and mechanisms of pepsin-like and retroviral aspartic proteinases.
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    Chapter 58 The Three-Dimensional X-Ray Crystal Structure of HIV-1 Protease Complexed with a Hydroxyethylene Inhibitor
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    Chapter 59 Substrate Cleavage by HIV-1 Proteinase
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    Chapter 60 The Evaluation of Non-Viral Substrates of the HIV Protease as Leads in the Design of Inhibitors for Aids Therapy
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    Chapter 61 Interaction of Mutant Forms of the HIV-1 Protease with Substrate and Inhibitors
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    Chapter 62 Structure-Based Inhibition of HIV-1 Protease Activity and Viral Infectivity
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    Chapter 63 Analysis of Temperature-Sensitive Mutants of the HIV-1 Protease
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    Chapter 64 Studies of the Autoprocessing of the HIV-1 Protease Using Cleavage Site Mutants
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    Chapter 65 Mutational analysis of a native substrate of the HIV-1 proteinase.
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    Chapter 66 Monoclonal and Polyclonal Antibodies: Reagents for Studying HIV-1 Proteinase Variants
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    Chapter 67 Cloning, Expression and Kinetic Characterization of the Feline Immunodeficiency Virus Proteinase
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    Chapter 68 Protein-Engineered Proteinase of Myeloblastosis Associated Virus, An Enzyme of High Activity and HIV-1 Proteinase-Like Specificity
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    Chapter 69 p15 gag Proteinase of Myeloblastosis Associated Virus: Specificity Studies with Substrate Based Inhibitors
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    Chapter 70 Scintillation Proximity Enzyme Assay a Rapid and Novel Assay Technique Applied to HIV Proteinase
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    Chapter 71 Improved Chromatographic Method for the Assay of Retroviral Proteases
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    Chapter 72 Cleavage of the Intermediate Filament Subunit Protein Vimentin by HIV-1 Protease: Utilization of a Novel Cleavage Site and Identification of Higher Order Polymers of Pepstatin A
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    Chapter 73 A New Type of Aspartic Proteinase Inhibitors with a Symmetric Structure
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    Chapter 74 Time Dependent Heterodimer Formation Leads to Inhibition of HIV Protease Activity
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    Chapter 75 Molecular Modeling of the HIV-2 Protease
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    Chapter 76 Theoretical Models of Aspartic Proteases: Active Site Properties, Dimer Stability and Interactions with Model Inhibitors
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    Chapter 77 A Consensus Template for the Aspartic Proteinase Fold