Retroviral ProteasesEdited by
- Lawrence Kuo, Merck Sharp & Dohme Research Laboratories, Merck & Co., West Point, Pennsylvania, U.S.A.
- Jules Shafer, Merck Sharp & Dohme Research Laboratories, Merck & Co., Inc., West Point, Pennsylvania, U.S.A.
- John Abelson, California Institute of Technology, Division of Biology, Pasadena, U.S.A.
- Melvin Simon, California Institute of Technology, Division of Biology, Pasadena, USA
Methods included in this volume apply to the expression and characterization of retroviral proteases and their inhibitor/substrate design.
Biochemists, virologists, medicinal chemists, molecular biologists, immunologists, graduate students in these disciplines, and drug company researchers.
Methods in Enzymology
Published: September 1994
Imprint: Academic Press
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- Bacterial Expression and Enzymatic Assays:J. Stebbins and C. Debouck, Expression Systems for Retroviral Proteases.C.J. Rizzo and B.D. Korant, Genetic Approaches Designed to Minimize Cytotoxicity of Retroviral Protease.E. Chen, Host Strain Selection for Bacterial Expression of Toxic Proteins.C.U.T. Hellen, Assay Methods for Retroviral Proteases.A.H. Kaplan, M. Manchester, L. Everitt, and R. Swanstrom, Analysis of Human Immunodeficiency Virus 1 Protease Activity in Eukaryotic and Bacterial Cells.G. A. Krafft and G.T. Wang, Synthetic Approaches to Continuous Assays of Retroviral Proteases.Purification and Characterization:K. von der Helm, S. Seelmeier, A. Kisselev, and H.Nitschko, Identification, Purification, and Cell Culture Assays of Retroviral Proteases.P.L. Darke, Stability of Dimeric Retroviral Proteases.T.D. Meek, E.J. Rodriguez, and T.S. Angeles, Use of Steady State Kinetic Methods to Elucidate the Kinetic and Chemical Mechanisms of Retroviral Proteases.D. Ringe, X-Ray Structures of Retroviral Proteases and Their Inhibitor-Bound Complexes.W.E. Harte, Jr., and D.L. Beveridge, Probing Structure--Function Relationships in Human Immunodeficiency Virus 1 Protease via Molecular Dynamics Simulation.X.-L. Lin, Y.-Z. Lin, and J. Tang, Relationships of Human Immunodeficiency Virus Protease with Eukaryotic Aspartic Proteases.Substrate Specificity and Inhibitor Design:C. Carterand G. Zybarth, Processing of Retroviral Gag Polyproteins: An in Vitro Approach.B.M. Dunn, A. Gustchina, A. Wlodawer, and J. Kay, Subsite Preferences of Retroviral Proteinases.A.G. Tomasselli and R.L. Heinrikson, Specificity of Retroviral Proteases: An Analysis of Viral and Nonviral Protein Substrates.F.R. Masiarz and B.A. Malcolm, Rapid Determination of Endoprotease Specificity Using Peptide Mixtures and Edman Degradation Analysis.J.P. Vacca, Design of Tight-Binding Human Immunodeficiency Virus Type 1 Protease Inhibitors.D.J. Kempf, Design of Symmetry-Based, Peptidomimetic Inhibitors of Human Immunodeficiency Virus Protease.M.D. Miller, R.P. Sheridan, S.K. Kearsley, and D.J. Underwood, Advances in Automated Docking Applied to Human Immunodeficiency Virus Type 1 Protease.M.A. McCarrick and P. Kollman, Use of Molecular Dynamics and Free Energy Pertubation Calculations in Anti- Human Immunodeficiency Virus Drug Design.J.C. Culberson, B.L. Bush, and V.V. Sardana, Qualitative Study of Drug Resistance in Retroviral Protease Using Structural Modeling and Site-Directed Mutagenesis.Author Index.Subject Index.