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Aspartic Proteinases

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Cover of 'Aspartic Proteinases'

Table of Contents

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    Book Overview
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    Chapter 1 Comparison of the Active Site Specificity of the Aspartic Proteinases Based on a Systematic Series of Peptide Substrates
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    Chapter 2 The Molecular Structure of Human Progastricsin and its Comparison with that of Porcine Pepsinogen
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    Chapter 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
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    Chapter 4 Rearranging Pepsinogen and Pepsin by Protein Engineering
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    Chapter 5 Comparative Investigations on Pig Gastric Proteases and Their Zymogens
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    Chapter 6 Non-Mammalian Vertebrate Pepsinogens and Pepsins: Isolation and Characterization
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    Chapter 7 Transcription Regulation of Human and Porcine Pepsinogen A
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    Chapter 8 A Comparative Study on Amino Acid Sequences of Three Major Isoforms of Human Pepsin A
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    Chapter 9 Molecular Mass Determination by Electrospray Mass Spectrometry of Human Pepsins, Gastricsin, and Porcine Pepsin A Variants
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    Chapter 10 Evidence for Electrostatic Interactions in the S 2 Subsite of Porcine Pepsin
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    Chapter 11 Protein engineering of surface loops: preliminary X-ray analysis of the CHY155-165RHI mutant.
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    Chapter 12 Seminal Progastricsin
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    Chapter 13 Effects of Hydrocortisone on the Pepsinogen-Producing Cells in Rat Stomach Mucosa
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    Chapter 14 Effects of Omeprazole, a Proton Pump Inhibitor, on Pepsinogen-Producing Cells, with Special Reference to Neonatal Development
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    Chapter 15 Transcription of Embryonic Chick Pepsinogen Gene is Affected by Mesenchymal Signals through its 5′-Flanking Region
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    Chapter 16 Serum Pepsinogen Values as Possible Markers for Evaluating the Possibility of Peptic Ulcer Recurrence under H 2 -Blocker Half-Dose Maintenance Therapy
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    Chapter 17 The Clinical Application of the Serum Pepsinogen I And II Levels as a Mass Screening Method for Gastric Cancer
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    Chapter 18 A Minute Gastric Cancer Detected by a New Screening Method Using Serum Pepsinogen I and II
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    Chapter 19 Two Cases of Early Colorectal Cancer Associated with Gastric Adenoma Detected by Serum Pepsinogen Screening Method
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    Chapter 20 Comparisons of the three-dimensional structures, specificities and glycosylation of renins, yeast proteinase A and cathepsin D.
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    Chapter 21 Discovery of Inhibitors of Human Renin with High Oral Bioavailability
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    Chapter 22 Structure of Human Cathepsin D: Comparison of Inhibitor Binding and Subdomain Displacement with other Aspartic Proteases
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    Chapter 23 Cathepsin D Crystal Structures and Lysosomal Sorting
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    Chapter 24 Isolation and Characterization of Human Gastric Procathepsin E and Cathepsin E
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    Chapter 25 Isolation, Characterization, and Structure of Procathepsin E and Cathepsin E from the Gastric Mucosa of Guinea Pig
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    Chapter 26 Cathepsin E and Cathepsin D: Biosynthesis, Processing and Subcellular Location
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    Chapter 27 Glycoproteins of the Aspartyl Proteinase Gene Family Secreted by the Developing Placenta
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    Chapter 28 Structure and possible function of aspartic proteinases in barley and other plants.
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    Chapter 29 Aspartic Proteinases (Cyprosins) from Cynara Cardunculus Spp. Flavescens Cv. Cardoon; Purification, Characterisation, and Tissue-Specific Expression
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    Chapter 30 Acid-Activation of Rat Prorenin following Non-Proteolytic Alteration
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    Chapter 31 Human procathepsin D: three-dimensional model and isolation.
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    Chapter 32 Identification of Five Molecular forms of Cathepsin D in Bovine Milk
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    Chapter 33 Site-Directed Mutagenesis of a Disulfide Bridge in Cathepsin D: Expression, Activation, Purification, and Characterization
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    Chapter 34 Expression of Rat Cathepsin D cDNA in Saccharomyces Cerevisiae : Intracellular Sorting of Cathepsin D to Yeast Vacuole
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    Chapter 35 Molecular Cloning and Immunocytochemical Localization of Jasmonic Acid Inducible Cathepsin D Inhibitors from Potato
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    Chapter 36 Purification and Characterization of an Acid Proteinase from Dirofilaria Immitis Worms
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    Chapter 37 Inhibition and Entrapment of Aspartic Proteinases by α 2 -Macroglobulin
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    Chapter 38 Recombinant Human Cathepsin E
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    Chapter 39 Expression of Human Cathepsin E in Methylotrophic Yeast, Pichia Pastoris
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    Chapter 40 Purification and Characterization of Recombinant Human Cathepsin E
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    Chapter 41 Comparison of Biochemical Properties of Natural and Recombinant Cathepsin E
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    Chapter 42 Increased Expression and Specific Localization of Cathepsins E and D in Vulnerable Brain Regions of Aged and Postischemic Rats
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    Chapter 43 Characterization of Cathepsins E and D Accumulated at Early Stages of Neuronal Damage in Hippocampal Neurons of Rats
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    Chapter 44 Functional Aspects of Cathepsin E: Is it an Embryonic or Fetal Type of Aspartic Proteinase?
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    Chapter 45 Tissue- and Cell-Specific Control of Guinea Pig Cathepsin E Gene Expression
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    Chapter 46 Cathepsin E is Expressed in Fetal Rat Glandular Stomach Epithelial Cells in Primary Culture in the Absence of Mesenchymes
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    Chapter 47 Cathepsin E expressed in pancreatic cancer.
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    Chapter 48 Plant Aspartic Proteinases from Cynara Cardunculus Spp. Flavescens Cv. Cardoon; Nucleotide Sequence of a cDNA Encoding Cyprosin and its Organ-Specific Expression
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    Chapter 49 Cardosin A and B, Aspartic Proteases from the Flowers of Cardoon
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    Chapter 50 Mechanism of Autoprocessing of a Mini-Precursor of the Aspartic Protease of Human Immunodeficiency Virus Type 1
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    Chapter 51 Mutants of HIV-1 Protease with Enhanced Stability to Autodegradation
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    Chapter 52 Identification of Amino Acid Residues of the Retroviral Aspartic Proteinases Important for Substrate Specificity and Catalytic Efficiency
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    Chapter 53 Inhibitor-Resistant Mutants of the HIV-1 Aspartic Protease
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    Chapter 54 Design and Synthesis of HIV Protease Inhibitors Containing Allophenylnorstatine as a Transition-State Mimic
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    Chapter 55 Breaking the Shackles of the Genetic Code: Engineering Retroviral Proteases Through Total Chemical Synthesis
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    Chapter 56 X-Ray Structure of a Tethered Dimer for HIV-1 Protease
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    Chapter 57 Structure of HIV-1 Protease with KNI-272: A Transition State mimetic Inhibitor Containing Allophenylnorstatine
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    Chapter 58 Molecular Dynamics of HIV-1 Protease in Complex with a Difluoroketone-Containing Inhibitor: Implications for the Catalytic Mechanism
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    Chapter 59 Activated Dynamics of Flap Opening in Hiv-1 Protease
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    Chapter 60 Computer Simulation and Analysis of the Reaction Pathway for the Decomposition of the Hydrated Peptide Bond in Aspartic Proteases
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    Chapter 61 Activities of Precursor and Tethered Dimer Forms of HIV Proteinase
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    Chapter 62 Site-Directed Mutagenesis of HIV-1 Protease: Generation of Mutant Proteases with Increased Stability to Autodigestion
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    Chapter 63 Molecular Modeling of the Structure of FIV Protease
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    Chapter 64 Processing, Purification, and Kinetic Characterization of the Gag-Pol Encoded Retroviral Proteinase of Myeloblastosis Associated Virus Expressed in E. Coli
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    Chapter 65 Extracellular Aspartic Proteinases from Candida Yeasts
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    Chapter 66 Tyrosine 75 on the Flap Contributes to Enhance Catalytic Efficiency of a Fungal Aspartic Proteinase, Mucor Pusillus Pepsin
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    Chapter 67 Aspartic Proteinases from the Human Malaria Parasite Plasmodium Falciparum
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    Chapter 68 Yeast and Mammalian Basic Residue-Specific Aspartic Proteases in Prohormone Conversion
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    Chapter 69 Pepstatin-Insensitive Carboxyl Proteinases
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    Chapter 70 The Three-Dimensional X-Ray Crystal Structure of the Aspartic Proteinase Native to Trichoderma Reesei Complexed with a Renin Inhibitor CP-80794
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    Chapter 71 A Quantum Mechanical Model of the Hydration and Acidity of the Active Site in Aspartic Proteases
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    Chapter 72 Site-Directed Mutagenesis of Rhizopuspepsin: An Analysis of Unique Specificity
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    Chapter 73 Site-Directed Mutagenesis Revealed Role of Subsite Residues of Mucor Pusillus Pepsin in Catalytic Function
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    Chapter 74 A Novel Intracellular Acid Proteinase from the Plasmodia of a True Slime Mold, Physarum Polycephalum
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    Chapter 75 Characteristics of YAP3, a New Prohormone Processing Aspartic Protease from S. Cerevisiae
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    Chapter 76 Candida Albicans Aspartic Proteinase: cDNA Cloning and Comparison among Strains
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    Chapter 77 Molecular Cloning and Sequence Analysis of a Gene Encoding an Aspartic Proteinase from Aspergillus Oryzae
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    Chapter 78 Aspergillus Niger Var. Macrosporus Proteinase B. cDNA Cloning, Expression, and Activation of the Proenzyme
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    Chapter 79 Expression and Secretion of Recombinant Aspartic Proteinases by Bacillus Brevis
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    Chapter 80 Expression in E.Coli of Aspergillus Niger Var. Macrosporus Proteinase A, a Non-Pepsin Type Acid Proteinase
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    Chapter 81 X-Ray Crystallographic Study of a Non-Pepsin-Type Acid Proteinase, Aspergillus Niger Proteinase A
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    Chapter 82 Conformation Analysis of Non-Pepsin-Type Acid Proteinase a from the Fungus Aspergillus Niger by NMR
Overall attention for this book and its chapters
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Title
Aspartic Proteinases
Published by
Springer US, December 2012
DOI 10.1007/978-1-4615-1871-6
ISBNs
978-1-4613-5761-2, 978-1-4615-1871-6
Editors

Takahashi, Kenji

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Mendeley readers

The data shown below were compiled from readership statistics for 2 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 2 100%

Demographic breakdown

Readers by professional status Count As %
Professor 1 50%
Student > Bachelor 1 50%
Readers by discipline Count As %
Agricultural and Biological Sciences 1 50%
Chemistry 1 50%

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