SEARCH

SEARCH BY CITATION

References

  • Andreeva, N.S., Zdanov, A.S., Gustchina, A.E., & Fedorov, A.A. (1984). Structure of ethanol-inhibited porcine pepsin at 2-Å resolution and binding of the methyl ester of phenylalanyl-diiodotyrosine to the enzyme. J. Biol. Chem. 259, 1135311365.
  • Babé, L.M., Pichuantes, S., Barr, P.J., Bathurst, I.C., Masiarz, F.R., & Craik, C.S. (1990). HIV1 protease: Bacterial expression, purification and characterization. In Proteins and Pharmaceutical Engineering (Craik, C.S., Fletterick, R., Matthews, C.R., & Wells, J., Eds.), pp. 7188. Wiley-Liss, New York.
  • Babé, L.M., Pichuantes, S., & Craik, C.S. (1991). Inhibition of HIV protease by heterodimer formation. Biochemistry 30, 106111.
  • Cheng, Y.-S.E., Yin, F.H., Foundling, S., Blomstrom, D., & Kettner, C.A. (1990). Stability and activity of human immunodeficiency virus protease: Comparison of the natural dimer with a homologous, single-chain tethered dimer. Proc. Natl. Acad. Sci. USA 87, 96609664.
  • Coombs, K. & Brown, D.T. (1987). Organization of the Sindbis virus nucleocapsid as revealed by bifunctional cross-linking agents. J. Mol. Biol. 195, 359371.
  • DesJarlais, R.L., Seibel, G.L., Kuntz, I.D., Ortiz de Montellano, P.R., Furth, P.S., Alvarez, J.C., DeCamp, D.L., Babé, L.M., & Craik, C.S. (1990). Structure-based design of non-peptide inhibitors specific for the human immunodeficiency virus 1 protease. Proc. Natl. Acad. Sci. USA 87, 66446648.
  • Dilanni, C.L., Davis, L.J., Hollowat, M.K., Herber, W.K., Darke, P.L., Kohl, N.E., & Dixon, R.A.F. (1990). Characterization of an active single polypeptide form of the human immunodeficiency virus type 1 protease. J. Biol. Chem. 265, 1734817354.
  • Dutia, B.M., Frame, M.C., Subak-Sharpe, J.H., Clark, W.N., & Marsden, H.S. (1986). Specific inhibition of herpesvirus ribonuclease reductase by synthetic peptides. Nature 321, 439443.
  • Gustchina, A. & Weber, I.T. (1991). Comparative analysis of the sequences and structures of HIV1 and HIV2 proteases. Proteins Struct. Funct. Genet. 10, 325339.
  • Haigh, A., Greaves, R., & O'Hare, P. (1990). Interference with the assembly of virus-host transcription complex by peptide competition. Nature 344, 257259.
  • Heimbach, J.C., Garsky, V.M., Michelson, S.R., Dixon, R.A.F., Sigal, I.S., & Darke, P.L. (1989). Affinity purification of the HIV-1 protease. Biochem. Biophys. Res. Commun. 163, 955960.
  • Jordan, S.P., Zugay, J., Darke, P.L., & Kuo, L.C. (1992). Activity and dimerization of human immunodeficiency virus protease as a function of solvent composition and enzyme concentration. J. Biol. Chem., in press.
  • Kohl, N.E., Emini, E.A., Schleif, W.A., Davis, L.J., Heimbach, J.C., Dixon, R.A.F., Scolnick, E.M., & Sigal, I.S. (1988). Active human immunodeficiency virus protease is required for viral infectivity. Proc. Natl. Acad. Sci. USA 85, 46864690.
  • Kräusslich, H.-G. (1991). Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly, and viral infectivity. Proc. Natl. Acad. Sci. USA 88, 32133217.
  • Kräusslich, H.-G. & Wimmer, E. (1988). Viral proteinases. Annu. Rev. Biochem. 57, 701754.
  • McClements, W., Yamanaka, G., Garsky, V., Perry, H., Bacchetti, S., Colonno, R., & Stein, R.B. (1988). Oligopeptides inhibit the ribonucleotide reductase of herpes simplex virus by causing subunit separation. Virology 162, 270273.
  • Miller, M., Jaskolski, M., Rao, J.K.M., Leis, J., & Wlodawer, A. (1989). Crystal structure of a retroviral protease proves relationship to aspartic protease family. Nature 337, 576579.
  • Muchmore, D.C., McIntosh, L.P., Russell, C.B., Anderson, D.E., & Dahlquist, F.W. (1989). Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Methods Enzymol. 177, 4469.
  • Navia, M.A., Fitzgerald, P.M.D., McKeever, B.M., Leu, C.-T., Heimbach, J.C., Herber, W.K., Sigal, I.S., Darke, P.L., & Springer, J.P. (1989). Three-dimensional structure of the aspartyl protease from human immunodeficiency virus HIV-1. Nature 337, 615620.
  • Patterson, C.E., Seetharam, R., Kettner, C.A., & Cheng, Y.-S.E. (1992). Human immunodeficiency virus type 1 and type 2 protease monomers are functionally interchangeable in the dimeric enzymes. J. Virol. 66, 12281231.
  • Pichuantes, S., Babé, L.M., Barr, P.J., DeCamp, D.L., & Craik, C.S. (1989). Recombinant HIV2 protease processes HIV1 Pr53gag and analogous junction peptides in vitro. J. Biol. Chem. 265, 1389013898.
  • Segel, I.H. (1975). Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems. John Wiley & Sons, New York.
  • Tomasselli, A.G., Olsen, M.K., Hui, J.O., Staples, D.J., Sawyer, T.K., Heinrikson, R.L., & Tomich, C.-S. (1990). Substrate analogue inhibition and active site titration of purified recombinant HIV-1 protease. Biochemistry 29, 264269.
  • Weber, I.T. (1990). Comparison of the crystal structures and intersubunit interactions of human immunodeficiency and Rous sarcoma virus proteases. J. Biol. Chem. 265, 1049210496.
  • Wlodawer, A., Miller, M., Kaskolski, M., Sathyanarayana, B.K., Baldwin, E., Weber, I.T., Selk, L.M., Clawson, L., Schneider, J., & Kent, S.B.H. (1989). Conserved folding in retroviral proteases: Crystal structure of a synthetic HIV-1 protease. Science 245, 616621.
  • Zhang, Z.-Y., Poorman, R.A., Maggiora, L.L., Heinrikson, R.L., & Kézdy, F.J. (1991). Dissociative inhibition of dimeric enzymes. Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetrapeptide. J. Biol. Chem. 266, 1559115594.