References
Abdel-Meguid S., Zhao B., Murthy K., Winborne E., Choi J.-K., Des Jarlais R., Minnich M., Culp J., Debouck C., Tomaszek T., Meek T.,Dreyer G. (1993) Inhibition of human immunodeficiency virus-1 protease by a C2-symmetric phosphinate. Synthesis and crystallographic analysis. Biochemistry 32 7972-7980.Appelt, K. (1993) Crystal structures of HIV-1 protease-inhibitor complexes. Persp. Drug Discov. Design. 1. 23-48.
Babe, L. Rose, J. Craik C. (1995) Trans-dominant inhibitory human immunodeficiency virus type 1 protease monomers prevent protease activation and virion maturation Proc. Natl. Acad. Sci. 92 10069-10073.
Baldwin, E. Bhat, T. Gulnik, S. Liu, B. Topol, I. Kiso, Y. Mimoto, T. Mitsuya, H. Erickson, J. (1995) Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophyenylnorstatine Structure 3 581-590.
Bernstein, F. Koetzle, T. Williams, G. Meyer, E. Brice, M. Rodgers, J. Kennerd, O. Shimanouchi, T. Tasumi, M. (1977) The protein data bank: a computer based archival file for macromolecular structures. J. Mol. Biol. 112. 535-542.
Billich, A. Charpiot, B. Fricker, G. Gstach, H. Lehr, P. Peichl, P. Scholz, D. Rosenwirth, B. (1994) HIV proteinase inhibitors containing 2-aminobenzylstatine as a novel scissile bond replacement: biochemical and pharmacological characterization.Antiviral Res. 25. 215-233.
Bhat, T. Baldwin, E. Liu, B. Cheng, Y. Erickson, J. (1994) Crystal structureof a tethered dimer of HIV-1 proteinase complexed with an inhibitor Nature Struct. Biol. 1. 552-556.
Chou, K.-C. Tomasselli, A. Reardon, I. Heinrikson, R. (1996) Predicting human immunodeficiency virus protease cleavage sites in proteins by a discriminant function method. Proteins: Struct. Funct. Genet. 24. 51-72.
Debouck, C. (1992) The HIV-1 protease as a therapeutic target for AIDS. Res. Hum. Retroviruses. 8. 153-164.
De Clercq, E. (1995) Toward improved anti-HIV chemotherapy: therapeutic strategies for intervention with HIV infections. J. Med. Chem. 38. 2491-2517.
Dreyer, G. Lambert, D. Meek, T. Carr, T. Tomaszek, J. Fernandez, A. Bartus, H. Cacciavillani, E. Hassel, A. Minnich, M. Petteway, S. Metcalf, B. (1992) Hydroxyethylene isostere inhibitors of human immunodeficency virus-1 protease: structure-activity analysis using enzyme kinetics, X-raycrystallography and infected T-cell assays.Biochemistry31, 6646-6659.
Erickson, J. Burt, S. (1996) Structural mechanisms of HIV drug resistance. Annu. Rev. Pharmacol. Toxicol. 36, 545-571.
Fitzgerald, P. McKeever, B. Van Middlesworth, J. Springer, J. Heimbach, J. Leu, C. Herber, W. Dixon, R. Darke, P. (1990) Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0 A resolution J. Biol. Chem. 265 14209-14219.
Fitzgerald, P. Springer, J. (1991) Structure and function of retroviral proteases. Annu. Rev. Biophys. Biomol. Struct. 20. 299-320.
Gustchina, A. Weber, I. (1990) Comparison of inhibitor binding in HIV-1 protease and in non-viral aspartic proteases: the role of the flap.FEBS Letters. 269. 269-272.
Gustchina, A. Sansom, C. Prevost, M. Richelle, J. Wodak, S. Wlodawer, A. Weber, I. (1994) Energy calculations and analysis of HIV-1 protease-inhibitor crystal structures. Protein Eng. 7, 309-317.
Hong, L. Treharne, A. Hartsuck, J. Foundling, S. Tang, J. (1996) Crystal structures of complexes of a peptidic inhibitor with wild-type and two mutant HIV-1 proteases. Biochemistry 35. 10627-10633.
Hosur, M. Bhat, T. Kempf, D. Baldwin, E. Liu, B. Gulnik, S. Wideburg, N. Norbeck, D. Apelt, K. Erickson, J. (1994) Influence of stereochemistry on activity and binding modes of C2 symmetry-based diol inhibitors of HIV-1 protease. J. Am. Chem. Soc. 116 847-855.
Jaskolski, M. Tomasselli, A. Sawyer, T. Staples, D. Heinrikson, R. Schneider,J. Kent, S. Wlodawer, A. (1991) Structure of 2.5 A resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene-based inhibitor. Biochemistry30 1600-1609.
Kohl, N. Emini, E. Schleif, W. Davis, L. Heimbach, J. Dixon, R. Scolnick, E. Sigal, I. (1988) Active human immunodeficiency virus protease is required for viral infectivity. Proc. Natl. Acad. Sci. 85 4686-4690.
Krohn, A. Redshaw, S. Ritchie, J. Graves, B. Hatada, M. (1991) Novel binding mode of highly potent HIV-proteinase inhibitors incorporating the (R)-hydroxyethylamine isostere. J. Med. Chem. 34 3340-3342.
Laco, G. Schalk-Hihi, C. Lubkowski, J. Morris, G. Zdanov, A. Olson, A. Elder, J. Wlodawer, A. Gustchina, A. (1997) Crystal structures of the inactive D30N mutant of feline immunodeficiency virus protease complexed with a substrate and an inhibitor. Biochemistry 36 10696-10708.
Lawrence, M.G. Colman, P. M. (1993) Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234, 946-950.
Loeb, D. Swanstrom, R. Everitt, L. Manchester, M. Stamper, S. Hutchison, C. (1989) Complete mutagenesis of the HIV-1 protease. Nature 340 397-400.
Martin, J. Begun, J. Schindeler, A. Wickramasinghe, W. Alewood, D. Alewood, P. Bergman, D. Brinkworth, R. Abbenante, G. March, D. Reid, R. Fairlie, D. (1999) Molecular recognition of macrocyclic peptidomimetic inhibitors by HIV-1 protease. Biochemistry 38. 7978-7988.
Miller, M. Schneider, J. Sathyanarayana, B. Toth, M. Marshall, G. Clawson, L. Selk, L. Kent, S. Wlodawer, A. (1989) Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution. Science 246 .1149-1152.
Nicholson, L. Yamazaki, T. Torchia, D. Grzesiek, S. Bax, A. Stahl, S. Kaufman, J. Wingfield, P. Lam, P. Jadhav, P. Hodge, C. Domaille, P. Chang, C.-H. (1995) Flexibility and function in HIV-1 protease. Nature Struct. Biol. 2. 274-280.
Priestle, J. Fassler, A. Rosel, J. Tintelnot-Blomley, M. Strop, P. Grutter, M. (1995) Comparative analysis of the X-ray structures of HIV-1 and HIV-2 proteases in complex with CGP53820, a novel pseudosymmetric inhibitor. Structure 3 381-389.
Rasnick, D. (1997) Kinetics analysis of consecutive HIV proteolytic cleavages of the Gag-Pol polyprotein. J. Biol. Chem. 272 6348-6353.
Rose, J. Babe, L. Craik, C. (1995) Defining the level of human immunodeficiency virus type 1 (HIV-1) protease activity required for HIV-1 particle maturation and infectivity J. Virol. 69 2751-2758.
Rose, R. Craik, C. Douglas, N. Stroud, R. (1996) Three dimensional structures of HIV-1 and SIV protease product complexes. Biochemistry 35 12933-12944.
Silva, A. Cachau, R. Sham, H. Erickson, J. (1996) Inhibition and catalytic mechanism of HIV-1 aspartic protease. J. Mol. Biol. 255 321-346.
Swain, A. L. Miller, M. M. Green, J. Rich, D. H. Schneider, J. Kent, S. B. H. Wlodawer, A.(1990) X-ray crystallographic structure of a complex between a synthetic protease of human immunodeficiency virus 1 and a substrate-based hydroxyethylamine inhibitor. Proc. Natl. Acad. Sci. 87 8805-8809.
Umezawa, H. Aoyagi, T. Morishima, H. Matsuzaki, M. Hamada, M. Takeuchi, T. (1970) Pepstatin, a new pepsin inhibitor produced by Actinomycetes. J. Antibiot. 23. 259-262.
Vondrasek, J. van Buskirk, C. Wlodawer, A. (1997) Database of three-dimensional structures of HIV proteinases. Nature Struct. Biol. 4 .8.
Weber, I. Wu, J. Adomat, J. Harrison, R. Kimmel, A. Wondrak, E. Louis, J. (1997) Crystallographic analysis of human immunodeficiency virus 1 protease with, an analog of the conserved CA-p2 substrate-interactions with frequently occurring glutamic acid residue at P2' position of substrates. Eur.J. Biochem. 249. 523-530.
Wlodawer, A. Erickson, J. (1993) Structure-based inhibitors of HIV-1 protease. Annu. Rev. Biochem. 62 543-585.
Wlodawer, A. Miller, M. Jaskolski, M. Sathyanarayana, B. Baldwin, E.Weber, I. Selk, L. Clawson, L. Schneider, J. Kent, S. (1989) Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease. Science 245 616-621.
JournalsScience The American Associationforthe Advancement of Science (AAAS) journal--the premier weekly US sciencejournal.
JAMA TheJournalof the American Medical Association operates this HIV/AIDS Information Center with abstracts and full text from select JAMA articles, abstractsfrom scientific journals, news, and practice guideline.
AIDS This publication of theInternationalAIDS Society operates a free web site, which lists tables of contents andhas abstracts of articles.
Journal of AIDS/HIV Electronic versions of one fo the leading peer-reviewed journals on AIDS. Select articles are free as HTML or PDF files.
Nature The prestigious international(British)journal on science.
New England Journal of Medicine Thisvenerablepublication (perhaps the most important medical journal in theUS) putssome full text and some abstracts on-line.
Web Sites
AIDSonline: http://www.aidsonline.com/
Antiviral Agents Bulletin: http://www.bioinfo.com/antiviral.html
American Society for Microbiology Journals: http://www.journals.asm.org/
British Medical Journal: http://www.tecc.co.uk/bmj/
Cell Press Online: http://www.cell.com/
Clinical Infectious Diseases: http://www.journals.uchicago.edu/CID/journal/
HIV Clinical Trials: http://www.thomasland.com/_nonsearch/hctissues.htm
Infectious Disease News Online Articles: http://www.slackinc.com/general/idn/idncurr.htm
Journal of AIDS/HIV: http://www.ccspublishing.com/j_aids.htm
Journal of Clinical Investigation: http://www.jci.org/current.shtml
Journal of Infectious Diseases: http://www.journals.uchicago.edu/JID/
Lancet: http://www.thelancet.com/
Nature: http://www.nature.com/
Nature Medicine: http://medicine.nature.com/
New England Journal of Medicine On-line: http://www.nejm.org/content/index.asp
Proceedings of the National Academy of Sciences: http://www.pnas.org/
Science On-Line: http://www.sciencemag.org/
Stanford University HighWire Press: http://highwire.stanford.edu/
Index of the Enzyme Report: