Aspartic Proteinases: Retroviral and Cellular EnzymesMichael N.G. James Springer Science & Business Media, 31 mrt 1998 - 499 pagina's The VIIth International Conference on Aspartic Proteinases was held in Banff, Alberta, Canada, from October 22 to 27, 1996. The venue was the Banff Centre in the Canadian Rockies, a setting well known worldwide for the scenic beauty and mountain grandeur. It was perhaps presumptuous of the organizers to call this the seventh Aspartic Proteinase Conference but it was felt that the meeting in 1982, organized by Tom Blundell and John Kay, was of an international stature and covered topics sufficiently broad to constitute a conference. Thus, there is a discontinuity in that the Gifu Conference organized by Prof. Kenji Takahashi was the fifth International Conference on Aspartic Proteinases. Officially, there has not been a sixth Conference and if there is confusion, it is the result of my desire to recognize the importance of the London meeting. Banffhosted 106 scientists from 14 different countries. There were 26 invited speak ers among the 44 oral presentations of the 7 main sessions. In addition, there were 53 con tributed poster presentations that spanned the whole range of interest in aspartic proteinases. |
Inhoudsopgave
An Historical Overview | 1 |
A Cellular AntiApoptosis Protein Is Cleaved by the HIV1 Protease | 27 |
The Aspartic Proteinase from Equine Infectious Anaemia Virus | 41 |
The Effect of Substrates on the Kinetics and the in Vivo Threshold Activity | 47 |
A Comparison of gagpol Precursor Cleavage in Naturally Arising HIV Variants | 53 |
Abstracts | 71 |
Sensitivity to Inhibition and Catalytic Efficiency of HIV Proteinase Mutants | 85 |
Computer Assisted Evaluation of Inhibitor Sensitivity to HIV1 PR Mutants | 91 |
Crystal Structure of Human Pepsinogen A | 259 |
Crystallographic Studies of an Activation Intermediate of Human Gastricsin | 265 |
Abstracts | 271 |
Crystal Structure of the Rhizomucor miehei Aspartic Proteinase | 283 |
Rhizomucor miehei Aspartic Proteinases Having Improved Properties | 293 |
Structure Biosynthesis and Specificity | 315 |
Bacterial Aspartic Proteinases as Novel Antibiotic Targets | 321 |
Structural Thermodynamic Study of the Binding of Renin Inhibitors | 325 |
Investigation of an Allosteric Site of HIV1 Proteinase Involved in Inhibition | 99 |
Mechanism of Action of Aspartic Proteases | 115 |
Theory and Method of a Priori Computation of Catalytic Acts of Aspartic | 123 |
Comparison of the Specificity of the Aspartic Proteinases Towards Internally | 133 |
Expression of Chimeric Human Aspartic Proteinases | 139 |
The Best Laid Plans of Mice and Men | 147 |
Biosynthesis and Intracellular Targeting of the Lysosomal Aspartic Proteinase | 153 |
An Aspartic Proteinase Expressed in the Equine Placenta | 163 |
SiteDirected Mutagenesis | 169 |
The Role | 179 |
Epitope Mapping of Recombinant Human Procathepsin D | 185 |
Construction of Chimeric Enzymes to Probe Subsite Contributions to Catalytic | 191 |
Mass Spectrometry as a Tool for Studying the Action of Human Aspartic | 201 |
Partial Characterization and Identification | 207 |
Cathepsin E in the Central Nervous System | 213 |
Detailed Analysis of Human Cathepsin E Prime Region Specificity | 219 |
Proteolytic and NonProteolytic Activation of Prorenin | 229 |
The Roles of the Basic Residues in the Prosegment of Aspergillopepsinogen I | 239 |
Activation Mechanism of Pepsinogen as Compared to the Processing of | 245 |
The Precursor Form of the Major Aspartic Proteinase from | 253 |
Primary Substrate Specificities of Secreted Aspartic Proteases of Candida | 335 |
Substrate Specificity of NonPepsinType Acid Proteinase Aspergillus niger | 345 |
Overcoming the Unfavourable Entropic Contribution of Ligand Binding with | 355 |
Abstracts | 361 |
Screening Aspartyl Proteases with Combinatorial Libraries | 375 |
Thermodynamics and Proton Uptake for Pepstatin Binding to Retroviral | 381 |
Expression Purification and Characterization of the Recombinant Pepsin | 387 |
Studies on Plasmepsins I and II from the Malarial Parasite Plasmodium | 397 |
Plasmepsins I and II from the Malarial Parasite Plasmodium falciparum | 407 |
Abstracts | 413 |
Structural and Functional Aspects of Cardosins | 423 |
Molecular Cloning of Aspartic Proteinases from Flowers of Cynara cardunculus | 435 |
Aspartic Proteinases and Inhibitors in Plant Pathogenesis | 441 |
Acid Proteinase from Nepenthes distillatoria Badura | 453 |
A Comparative Study on the Aspartic Proteinases from Different Species | 459 |
Purification | 465 |
481 | |
Author Index | 489 |
Overige edities - Alles bekijken
Aspartic Proteinases: Retroviral and Cellular Enzymes Michael N.G. James Gedeeltelijke weergave - 2012 |
Aspartic Proteinases: Retroviral and Cellular Enzymes Michael N.G. James Geen voorbeeld beschikbaar - 2011 |
Aspartic Proteinases: Retroviral and Cellular Enzymes Michael N.G. James Geen voorbeeld beschikbaar - 2012 |
Veelvoorkomende woorden en zinsdelen
acid residues active site albicans amino acid amino acid sequence aspartic proteinases assay binding Biochem Biochemistry Biol Blundell buffer Candida cardosin catalytic cathepsin D cDNA cells Chem chymosin cleavage cleaved cloned coli complex conformation crystal structure cyprosin dimer domain Dunn edited by James encoding enzyme expression Figure flap function gag-pol gene glycosylation hemoglobin hGSI HIV PR HIV-1 protease human cathepsin hydrogen bonds hydrolysis hydrophobic infectivity inhibition interactions kinetic loop lysosomal mature membrane molecular molecule mutant N-terminal Natl pepsin pepsinogen pepstatin peptide plant aspartic proteinases plasmepsin Plenum Press polyprotein porcine position precursor Proc procathepsin processing propeptide prorenin prosegment protease inhibitors protein proteolytic proteolytic activity purified recombinant region renin retroviral rhizopuspepsin role SAP2 SAP2X SAPS shown side chain specificity studies subsite substrate Table targeting tion viral virion virus vitro wild type wild-type zymogen
Populaire passages
Pagina 433 - Molscript, a program to produce both detailed and schematic plots of protein structures.