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• The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction.

  Stubbs MT, Laber B, Bode W, Huber R, Jerala R, Lenarcic B, Turk V. Stubbs MT, et al. EMBO J. 1990 Jun;9(6):1939-47. doi: 10.1002/j.1460-2075.1990.tb08321.x. EMBO J. 1990. PMID: 2347312 Free PMC article.
• Chemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sites.

  Willenbrock F, Brocklehurst K. Willenbrock F, et al. Biochem J. 1986 Aug 15;238(1):103-7. doi: 10.1042/bj2380103. Biochem J. 1986. PMID: 3800926 Free PMC article.
• Kinetic specificity in papain-catalysed hydrolyses.

  Lowe G, Yuthavong Y. Lowe G, et al. Biochem J. 1971 Aug;124(1):107-15. doi: 10.1042/bj1240107. Biochem J. 1971. PMID: 5126466 Free PMC article.
• Consequences of molecular recognition in the S1-S2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P1-P2 amide bond into a two-protonic-state reactivity probe.

  Brocklehurst K, Kowlessur D, Patel G, Templeton W, Quigley K, Thomas EW, Wharton CW, Willenbrock F, Szawelski RJ. Brocklehurst K, et al. Biochem J. 1988 Mar 15;250(3):761-72. doi: 10.1042/bj2500761. Biochem J. 1988. PMID: 2839145 Free PMC article.
• Effects of conformational selectivity and of overlapping kinetically influential ionizations on the characteristics of pH-dependent enzyme kinetics. Implications of free-enzyme pKa variability in reactions of papain for its catalytic mechanism.

  Brocklehurst K, Willenbrock SJ, Salih E. Brocklehurst K, et al. Biochem J. 1983 Jun 1;211(3):701-8. doi: 10.1042/bj2110701. Biochem J. 1983. PMID: 6309137 Free PMC article.