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  1. 1.   The Early Years of Retroviral Protease Crystal Structures
  2. Miller, M.
  3. Biopolymers. 2010 94(4): 521-529.
  1. 2.   Cockroach allergen Bla g 2: An unusual aspartic proteinase
  2. Wunschmann, S.; Gustchina, A.; Chapman, M. D.; Pomes, A.
  3. Journal of Allergy and Clinical Immunology. 2005, JUL; 116(1): 140-145.
  1. 3.   Kinetics of the dimerization of retroviral proteases: The "fireman's grip" and dimerization
  2. Ingr, M.; Uhlikova, T.; Strisovsky, K.; Majerova, E.; Konvalinka, J.
  3. Protein Science. 2003 12(10): 2173-2182.
  1. 4.   An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae
  2. Gustchina, A.; Li, M.; Phylip, L. H.; Lees, W. E.; Kay, J.; Wlodawer, A.
  3. Biochemical and Biophysical Research Communications. 2002 295(4): 1020-1026.
  1. 5.   Structural study of the complex between human pepsin and a phosphorus-containing peptidic transition-state analog
  2. Fujinaga, M.; Cherney, M. M.; Tarasova, N. I.; Bartlett, P. A.; Hanson, J. E.; James, M. N. G.
  3. Acta Crystallographica Section D-Biological Crystallography. 2000 56(Part 3): 272-279.
  1. 6.   Structural and biochemical studies of retroviral proteases
  2. Wlodawer, A.; Gustchina, A.
  3. Biochimica et Biophysica Acta - Protein Structure & Molecular Enzymology. 2000 1477(1-2): 16-34.
  1. 7.   Stabilization from autoproteolysis and kinetic characterization of the human T-cell leukemia virus type 1 proteinase
  2. Louis, J. M.; Oroszlan, S.; Tozser, J.
  3. Journal of Biological Chemistry. 1999 274(10): 6660-6666.
  1. 8.   Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting
  2. Kervinen, J.; Tobin, G. J.; Costa, J.; Waugh, D. S.; Wlodawer, A.; Zdanov, A.
  3. Embo Journal. 1999 18(14): 3947-3955.
  1. 9.   Mass spectrometry as a tool for studying the action of human aspartic proteases on peptides and proteins
  2. Tarasova, N. I.; Czerwinski, G.; Roberts, N. B.; Lubkowski, J.; Sumpter, T. L.; Green, B. N.; Michejda, C. J.; James, M. N. G.
  3. Aspartic Proteinases: Retroviral and Cellular Enzymes. 1998; 436 : 201-206.
  1. 10.   Probing the Structural Basis of the Catalytic Activity of Hiv-1 Pr Through Total Chemical Protein Synthesis
  2. Miller, M.; Baca, M.; Rao, J. K. M.; Kent, S. B. H.
  3. Theochem-Journal of Molecular Structure. 1998 423(1-2): 137-152.
  1. 11.   Structural analysis of plasmepsin II. A comparison with human aspartic proteases
  2. Silva, A. M.; Lee, A. Y.; Erickson, J. W.; Goldberg, D. E.
  3. Advances in Experimental Medicine and Biology. 1998 436: 363-373.
  1. 12.   Thermodynamics and proton uptake for pepstatin binding to retroviral and eukaryotic aspartic proteases
  2. Xie, D.; Gulnik, S.; Collins, L.; Gustchina, E.; Bhat, T. N.; Erickson, J. W.
  3. Advances in Experimental Medicine and Biology. 1998 436: 381-386.
  1. 13.   Inhibitors of Hiv-1 Protease - a Major Success of Structure-Assisted Drug Design
  2. Wlodawer, A.; Vondrasek, J.
  3. Annual Review of Biophysics and Biomolecular Structure. 1998 27: 249-284.
  1. 14.   The Glycosylation of the Aspartic Proteinases From Barley (Hordeum Vulgare L) and Cardoon (Cynara Cardunculus L)
  2. Costa, J.; Ashford, D. A.; Nimtz, M.; Bento, I.; Frazao, C.; Esteves, C. L.; Faro, C. J.; Kervinen, J.; Pires, E.; Verissimo, P.; Wlodawer, A.; Carrondo, M. A.
  3. European Journal of Biochemistry. 1997 243(3): 695-700.
  1. 16.   Crystal Structures of the Inactive D30n Mutant of Feline Immunodeficiency Virus Protease Complexed With a Substrate and an Inhibitor
  2. Laco, G. S.; Schalkhihi, C.; Lubkowski, J.; Morris, G.; Zdanov, A.; Olson, A.; Elder, J. H.; Wlodawer, A.; Gustchina, A.
  3. Biochemistry. 1997 36(35): 10696-10708.
  1. 18.   Plasmodium Falciparum, P-Vivax, and P-Malariae - a Comparison of the Active Site Properties of Plasmepsins Cloned and Expressed From Three Different Species of the Malaria Parasite
  2. Westling, J.; Yowell, C. A.; Majer, P.; Erickson, J. W.; Dame, J. B.; Dunn, B. M.
  3. Experimental Parasitology. 1997 87(3): 185-193.
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