Proteases example

Enzymes and their Inhibitors: Drug Development

Volumn , Issue , 2004, Pages 88-117

  Niestroj, André J ^a   Demuth, Hans Ulrich ^a  

^a PROBIODRUG AG   (Germany)

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EID: 30344466709     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter

References (113)

1. Ciardelli, T. and Smith, K.A. (1989). Interleukin 2: prototype for a new generation of immunoactive pharmaceuticals. Trends in Pharmacological Science, 10, 239-243.
2. Hopfinger, A.J. (1985). Computer-assisted drug design. Journal of Medicinal Chemistry, 28, 1133-1139.
3. Keseru, G.M. (2001). A virtual high throughput screen for high affinity cytochrome P450 cam substrates. Implications for in silico prediction of drug metabolism. Journal of Computer-Aided Molecular Design, 15, 649-657.
4. Shia, K.S., Li, W.T., Chang, C.M., Hsu, M.C., Chern, J.H., Leong, M.K., Tseng, S.N., Lee, C.C., Lee, Y.C., Chen, S.J., Peng, K.C., Tseng, H.Y., Chang, Y.L., Tai, C.L., and Shih, S.R. (2002). Design, synthesis, and structure-activity relationship of pyridyl imidazolidinones: a novel class of potent and selective human enterovirus 71 inhibitors. Journal of Medicinal Chemistry, 45, 1644-1655.
5. Pickett, S.D., McLay, I.M., and Clark, D.E. (2000). Enhancing the hit-to-lead properties of lead optimization libraries. Journal of Chemical Information and Computer Science, 40, 263-272.
6. Colmenarejo, G. (2003). In silico prediction of drug-binding strengths to human serum albumin. Medicinal Research Reviews, 23, 275-301.
7. Demuth, H.U. (1990). Recent developments in inhibiting cysteine and serine proteases. Journal of Enzyme Inhibition, 3, 249-278.
8. Rando, R.R. (1974). Chemistry and enzymology of kcat inhibitors. Science, 185, 320-324.
9. Carter, P. and Wells, J.A. (1988). Dissecting the catalytic triad of a serine protease. Nature, 332, 564-568.
10. Carter, P. and Wells, J.A. (1987). Engineering enzyme specificity by substrate-assisted catalysis. Science, 237, 394-399.
11. Dunn, B.M. (2002). Structure and mechanism of the pepsin-like family of aspartic peptidases. Chemical Reviews, 102, 4431-4458.
12. Hartley, B.S. (1960). Proteolytic enzymes. Annual Reviews in Biochemistry, 29, 45-72.
13. Gerhartz, B., Niestroj, A.J., and Demuth, H.U. (2002). Enzyme classes and mechanisms. In Proteinase and Peptidase Inhibition, Smith, H.J. and Simons, C., Eds. Taylor & Francis, London, pp. 1-20.
14. Schechter, I. and Berger, A. (1967). On the size of the active site in proteases. I. Papain. Biochemical and Biophysical Research Communications, 27, 157-162.
15. Kamphuis, I.G., Kalk, K.H., Swarte, M.B., and Drenth, J. (1984). Structure of papain refined at 1.65 Å resolution. Journal of Molecular Biology, 179, 233-256.
16. Perona, J.J., Tsu, C.A., McGrath, M.E., Craik, C.S., and Fletterick, R.J. (1993). Relocating a negative charge in the binding pocket of trypsin. Journal of Molecular Biology, 230, 934-949.
17. Polgar, L. and Halasz, P. (1982). Current problems in mechanistic studies of serine and cysteine proteinases. Biochemical Journal, 207, 1-10.
18. Akahane, K. and Umeyama, H. (1986). Binding specificity of papain and cathepsin B. Enzyme, 36, 141-149.
19. Asboth, B., Majer, Z., and Polgar, L. (1988). Cysteine proteases: the S2P2 hydrogen bond is more important for catalysis than is the analogous S1P1 bond. FEBS Letters, 233, 339-341.
20. Liebman, J.F. and Greenberg, A. (1989). Molecular Structure and Energetics, Vol. 9, Mechanistic Principles of Enzyme Activity. John Wiley & Sons, London.
21. Fastrez, J. (1983). On the stability of tetrahedral intermediates within the active sites of serine and cysteine proteases. European Journal of Biochemistry, 135, 339-341.
22. Asboth, B., Stokum, E., Khan, I.U., and Polgar, L. (1985). Mechanism of action of cysteine proteinases: oxyanion binding site is not essential in the hydrolysis of specific substrates. Biochemistry, 24, 606-609.
23. Polgar, L. and Csoma, C. (1987). Dissociation of ionizing groups in the binding cleft inversely controls the endo- and exopeptidase activities of cathepsin B. Journal of Biological Chemistry, 262, 14448-14453.
24. Brocklehurst, K., Brocklehurst, S.M., Kowlessur, D., O’Driscoll, M., Patel, G., Salih, E., Templeton, W., Thomas, E., Topham, C.M., and Willenbrock, F. (1988). Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics. Biochemical Journal, 256, 543-558.
25. Pickersgill, R.W., Goodenough, P.W., Sumner, I.G., and Collins, M.E. (1988). The electrostatic fields in the active-site clefts of actinidin and papain. Biochemical Journal, 254, 235-238.
26. Brocklehurst, K., O’Driscoll, M., Kowlessur, D., Phillips, I.R., Templeton, W., Thomas, E.W., Topham, C.M., and Wharton, C.W. (1989). The interplay of electrostatic and binding interactions determining active centre chemistry and catalytic activity in actinidin and papain. Biochemical Journal, 257, 309-310.
27. Varughese, K.I., Ahmed, F.R., Carey, P.R., Hasnain, S., Huber, C.P., and Storer, A.C. (1989). Crystal structure of a papain-E-64 complex. Biochemistry, 28, 1330-1332.
28. Storer, A.C., Angus, R.H., and Carey, P.R. (1988). Comparison of the kinetics of the papain-catalyzed hydrolysis of glycine- and alanine-based esters and thiono esters. Biochemistry, 27, 264-268.
29. Baker, B.R. (2003). Design of Active-Site-Directed Irreversible Enzyme Inhibitors, John Wiley & Sons, New York.
30. Harada, N. and Nakanishi, K. (1983). Circular Dichroic Spectroscopy: Exciton Coupling in Organic Stereochemistry, University Science Books, Mill Valley, CA.
31. Muller, D.J., Janovjak, H., Lehto, T., Kuerschner, L., and Anderson, K. (2002). Observing structure, function and assembly of single proteins by AFM. Progress in Biophysics and Molecular Biology, 79, 1-43.
32. Blow, D.M. and Steitz, T.A. (1970). X-ray diffraction studies of enzymes. Annual Reviews in Biochemistry, 39, 63-100.
33. Lipscomb, W.N. (1983). Structure and catalysis of enzymes. Annual Reviews in Biochemistry, 52, 17-34.
34. Johnson, L.N. and Blundell, T.L. (1976). Protein Crystallography. Academic Press, New York.
35. Drenth, J. (1994). Principles of Protein X-ray Crystallography, Springer, New York.
36. Ernst, R.R. (1975). Two-dimensional spectroscopy. Chimica, 29, 179-183.
37. Williamson, M.P., Havel, T.F., and Wuthrich, K. (1985). Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry. Journal of Molecular Biology, 182, 295-315.
38. Otting, G., Qian, Y.Q., Billeter, M., Muller, M., Affolter, M., Gehring, W.J., and Wuthrich, K. (1990). Protein-DNA contacts in the structure of a homeodomain-DNA complex determined by nuclear magnetic resonance spectroscopy in solution. EMBO Journal, 9, 3085-3092.
39. Wüthrich, K. (1986). NMR of Proteins and Nucleic Acids, John Wiley & Sons, New York.
40. Fischer, E. (1894). Einfluss der configuration auf die wirkung der enzyme. Chemische Berichte, 27, 2985-2993.
41. Koshland, D.E., Jr. (1958). Application of a theory of enzyme specificity to proteinase synthesis. Proceedings of the National Academy of Sciences U.S.A., 44, 98-104.
42. Lipscomb, W.N. (1972). Structures and mechanisms of enzymes. Proceedings of the Robert A. Welch Foundation Conferences on Chemical Research, 15, 130-182.
43. Quiocho, F.A. and Lipscomb, W.N. (1971). Carboxypeptidase A: a protein and an enzyme. Advances in Protein Chemistry, 25, 1-78.
44. Christianson, D. W. and Lipscomb, W. N. (1986). X-ray crystallographic investigation of substrate binding to carboxypeptidase A at subzero temperature. Proceedings of the National Academy of Science U.S.A., 83, 7568-7572.
45. Kilshtain-Vardi, A., Glick, M., Greenblatt, H.M., Goldblum, A., and Shoham, G. (2003). Refined structure of bovine carboxypeptidase A at 1.25 Å resolution. Acta Crystallographica Section D - Biological Crystallography, 59, 323-333.
46. Walsh, K.A. (1975). Unifying concepts among proteases. In Proteases and Biological Control, Reich, E., Rifkin, D.B., and Shaw, E., Eds., Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, pp. 1-11.
47. Neurath, H. (1984). Evolution of proteolytic enzymes. Science, 224, 350-357.
48. Rose, T. and Di Cera, E. (2002). Substrate recognition drives the evolution of serine proteases. Journal of Biological Chemistry, 277, 19243-19246.
49. Krem, M.M., Prasad, S., and Di Cera, E. (2002). Ser(214) is crucial for substrate binding to serine proteases. Journal of Biological Chemistry, 277, 40260-40264.
50. Barrett, A.J. and Rawlings, N.D. (1995). Families and clans of serine peptidases. Archives of Biochemistry and Biophysics, 318, 247-250.
51. Barrett, A.J. and Rawlings, N.D. (2001). Evolutionary lines of cysteine peptidases. Biological Chemistry, 382, 727-733.
52. Webb, E.C. (1992). Enzyme Nomenclature 1992, Academic Press, San Diego, CA.
53. Tipton, K.F. (1994). Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Enzyme nomenclature. Recommendations 1992. Supplement 1: corrections and additions. European Journal of Biochemistry, 223, 1-5.
54. Barrett, A.J. (1995). Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Enzyme nomenclature. Recommendations 1992. Supplement 2: corrections and additions. European Journal of Biochemistry, 232, 1-6.
55. Barrett, A.J. (1996). Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Enzyme nomenclature. Recommendations 1992. Supplement 3: corrections and additions. European Journal of Biochemistry, 237, 1-5.
56. Barrett, A.J. (1997). Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Enzyme Nomenclature. Recommendations 1992. Supplement 4: corrections and additions. European Journal of Biochemistry, 250, 1-6.
57. Tipton, K. and Boyce, S. (1999). Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Enzyme Supplement 5. European Journal of Biochemistry, 264, 610-650.
58. Lecaile, F., Kaleta, J., and Brömme, D. (2003). Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chemical Reviews, 102, 4459-4488.
59. Yamamoto, D., Matsumoto, K., Ohishi, H., Ishida, T., Inoue, M., Kitamura, K., and Mizuno, H. (1991). Refined x-ray structure of papain E-64-c complex at 2.1-Å resolution. Journal of Biological Chemistry, 266, 14771-14777.
60. Joshua-Tor, L., Xu, H.E., Johnston, S.A., and Rees, D.C. (1995). Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6. Science, 269, 945-950.
61. Sivaraman, J., Nagler, D.K., Zhang, R., Menard, R., and Cygler, M. (2000). Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine. Journal of Molecular Biology, 295, 939-951.
62. Drenth, J., Kalk, K.H., and Swen, H.M. (1976). Binding of chloromethyl ketone substrate analogues to crystalline papain. Biochemistry, 15, 3731-3738.
63. Ton-That, H., Liu, G., Mazmanian, S.K., Faull, K.F., and Schneewind, O. (1999). Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif. Proceedings of the National Academy of Sciences U.S.A., 96, 12424-12429.
64. Meldal, M., Svendsen, I., and Scharfenstein, J. (1998). Inhibition of cruzipain visualized in a fluorescence-quenched solid-phase inhibitor library assay. D-amino acid inhibitors for cruzipain, cathepsin B, and cathepsin L. Journal of Peptide Science, 4, 83-91.
65. Mazmanian, S.K., Liu, G., Jensen, E.R., Lenoy, E., and Schneewind, O. (2000). Staphylococcus aureus sortase mutants defective in the display of surface proteins and in the pathogenesis of animal infections. Proceedings of the National Academy of Sciences U.S.A., 97, 5510-5515.
66. Mazmanian, S.K., Liu, G., Ton-That, H., and Schneewind, O. (1999). Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science, 285, 760-763.
67. Ilangovan, U., Ton-That, H., Iwahara, J., Schneewind, O., and Clubb, R. T. (2001). Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus. Proceedings of the National Academy of Sciences U.S.A., 98, 6056-6061.
68. Ding, J., McGrath, W.J., Sweet, R.M., and Mangel, W.F. (1996). Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactors. EMBO Journal, 15, 1778-1783.
69. Walker, N.P., Talanian, R.V., Brady, K.D., Dang, L.C., Bump, N.J., Ferenz, C.R., Franklin, S., Ghayur, T., Hackett, M.C., and Hammill, L.D. (1994). Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: a (p20/p10)2 homodimer. Cell, 78, 343-352.
70. Rotonda, J., Nicholson, D.W., Fazil, K.M., Gallant, M., Gareau, Y., Labelle, M., Peterson, E.P., Rasper, D.M., Ruel, R., Vaillancourt, J.P., Thornberry, N.A., and Becker, J.W. (1996). The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis. Nature Structural Biology, 3, 619-625.
71. Denault, J.B. and Salvesen, G.S. (2002). Caspases: keys in the ignition of cell death. Chemical Reviews, 102, 4489-4500.
72. Yoneda, M., Hirofuji, T., Anan, H., Matsumoto, A., Hamachi, T., Nakayama, K., and Maeda, K. (2001). Mixed infection of Porphyromonas gingivalis and Bacteroides forsythus in a murine abscess model: involvement of gingipains in a synergistic effect. Journal of Periodontal Research, 36, 237-243.
73. Imamura, T., Potempa, J., and Travis, J. (2000). Comparison of pathogenic properties between two types of arginine-specific cysteine proteinases (gingipains-R) from porphyromonas gingivalis [In Process Citation]. Microbial Pathogenesis, 29, 155-163.
74. Manoury, B., Hewitt, E.W., Morrice, N., Dando, P.M., Barrett, A.J., and Watts, C. (1998). An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation [see comments]. Nature, 396, 695-699.
75. Urade, R., Oda, T., Ito, H., Moriyama, T., Utsumi, S., and Kito, M. (1997). Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease. Journal of Biochemistry (Tokyo), 122, 834-842.
76. Okudo, H., Urade, R., Moriyama, T., and Kito, M. (2000). Catalytic cysteine residues of ER-60 protease. FEBS Letters, 465, 145-147.
77. Hall, T.M., Porter, J.A., Young, K.E., Koonin, E.V., Beachy, P.A., and Leahy, D.J. (1997). Crystal structure of a hedgehog autoprocessing domain: homology between hedgehog and self-splicing proteins. Cell, 91, 85-97.
78. Perler, F.B. (1998). Protein splicing of inteins and hedgehog autoproteolysis: structure, function, and evolution. Cell, 92, 1-4.
79. Liebeschuetz, J.W., Jones, S.D., Morgan, P.J., Murray, C.W., Rimmer, A.D., Roscoe, J.M., Waszkowycz, B., Welsh, P.M., Wylie, W.A., Young, S.C., Martin, H., Mahler, J., Brady, L., and Wilkinson, K. (2002). PRO_SELECT: combining structure-based drug design and array-based chemistry for rapid lead discovery. 2. The development of a series of highly potent and selective factor Xa inhibitors. Journal of Medicinal Chemistry, 45, 1221-1232.
80. Steinmetz, A.C., Demuth, H.U., and Ringe, D. (1994). Inactivation of subtilisin Carlsberg by N-((tert-butoxycarbonyl)alanylprolylphenylalanyl)-O-benzoylhydroxylamine:formation of a covalent enzyme-inhibitor linkage in the form of a carbamate derivative. Biochemistry, 33, 10535-10544.
81. Toide, K., Shinoda, M., and Miyazaki, A. (1998). A novel prolyl endopeptidase inhibitor, JTP-4819 - its behavioral and neurochemical properties for the treatment of Alzheimer’s disease. Reviews in Neuroscience, 9, 17-29.
82. Fulop, V., Bocskei, Z., and Polgar, L. (1998). Prolyl oligopeptidase: an unusual betapropeller domain regulates proteolysis. Cell, 94, 161-170.
83. Tong, L., Qian, C., Massariol, M.J., Bonneau, P.R., Cordingley, M.G., and Lagace, L. (1996). A new serine-protease fold revealed by the crystal structure of human cytomegalovirus protease. Nature, 383, 272-275.
84. Hoog, S.S., Smith, W.W., Qiu, X., Janson, C.A., Hellmig, B., McQueney, M.S., O’Donnell, K., O’Shannessy, D., DiLella, A.G., Debouck, C., and Abdel-Meguid, S.S. (1997). Active site cavity of herpesvirus proteases revealed by the crystal structure of herpes simplex virus protease/inhibitor complex. Biochemistry, 36, 14023-14029.
85. Paetzel, M., Dalbey, R.E., and Strynadka, N.C. (2002). Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism. Journal of Biological Chemistry, 277, 9512-9519.
86. Paetzel, M., Dalbey, R.E., and Strynadka, N.C. (1998). Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature, 396, 186-190.
87. Brannigan, J.A., Dodson, G., Duggleby, H.J., Moody, P.C., Smith, J.L., Tomchick, D.R., and Murzin, A.G. (1995). A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature, 378, 416-419.
88. Smith, J.L., Zaluzec, E.J., Wery, J.P., Niu, L., Switzer, R.L., Zalkin, H., and Satow, Y. (1994). Structure of the allosteric regulatory enzyme of purine biosynthesis. Science, 264, 1427-1433.
89. Duggleby, H.J., Tolley, S.P., Hill, C.P., Dodson, E.J., Dodson, G., and Moody, P.C. (1995). Penicillin acylase has a single-amino-acid catalytic centre. Nature, 373, 264-268.
90. Lowe, J., Stock, D., Jap, B., Zwickl, P., Baumeister, W., and Huber, R. (1995). Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science, 268, 533-539.
91. Groll, M., Brandstetter, H., Bartunik, H., Bourenkow, G., and Huber, R. (2003). Investigations on the maturation and regulation of archaebacterial proteasomes. Journal of Molecular Biology, 327, 75-83.
92. Almond, J.B. and Cohen, G.M. (2002). The proteasome: a novel target for cancer chemotherapy. Leukemia, 16, 433-443.
93. Puehler, G., Pitzer, F., Zwickl, P., and Baumeister, W. (1994). Proteasome: multisubunit proteinases common to thermoplasma and eukaryotes. Systematic and Applied Microbiology, 16, 734-741.
94. Groll, M., Ditzel, L., Lowe, J., Stock, D., Bochtler, M., Bartunik, H.D., and Huber, R. (1997). Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature, 386, 463-471.
95. Silva, A.M., Cachau, R.E., Sham, H.L., and Erickson, J.W. (1996). Inhibition and catalytic mechanism of HIV-1 aspartic protease. Journal of Molecular Biology, 255, 321-346.
96. Kim, E.E., Baker, C.T., Dwyer, M.D., Murcko, M.A., Rao, B.G., Tung, R.D., and Navia, M. A. (1995). Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme. Journal of the American Chemical Society, 117, 1181-1182.
97. Christianson, D.W. and Lipscomb, W.N. (1989). Carboxypeptidase A. Accounts of Chemical Research, 22, 62-69.
98. Matthews, B.W. (1989). Structural basis of the action of thermolysin and related zinc peptidases. Accounts of Chemical Research, 21, 333-340.
99. Mangani, S., Carloni, P., and Orioli, P. (1992). Crystal structure of the complex between carboxypeptidase A and the biproduct analog inhibitor L-benzylsuccinate at 2.0 Å resolution. Journal of Molecular Biology, 223, 573-578.
100. Strater, N. and Lipscomb, W.N. (1995). Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by x-ray crystallography. Biochemistry, 34, 14792-14800.
101. Tahirov, T.H., Oki, H., Tsukihara, T., Ogasahara, K., Yutani, K., Ogata, K., Izu, Y., Tsunasawa, S., and Kato, I. (1998). Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus. Journal of Molecular Biology, 284, 101-124.
102. Kim, H. and Lipscomb, W.N. (1993). X-ray crystallographic determination of the structure of bovine lens leucine aminopeptidase complexed with amastatin: formulation of a catalytic mechanism featuring a gem-diolate transition state. Biochemistry, 32, 8465-8478.
103. Zollner, H. (1989). Handbook of Enzyme Inhibitors, VCH, Weinheim, Germany.
104. Bode, W. and Huber, R. (2000). Structural basis of the endoproteinase-protein inhibitor interaction. Biochimica et Biophysica Acta, 1477, 241-252.
105. Vendrell, J., Querol, E., and Aviles, F.X. (2000). Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties. Biochimica et Biophysica Acta, 1477, 284-298.
106. Ala, P.J. and Chang, C.-H. (2002). HIV aspartate proteinase: resistance to inhibitors. In Proteinase and Peptidase Inhibition, Smith, H.J. and Simons, C., Eds., Taylor & Francis, London, pp. 367-382.
107. Hooper, N.M. (2002). Zinc metallopeptidases. In Proteinase and Peptidase Inhibition, Smith, H.J. and Simons, C., Eds., Taylor & Francis, London, pp. 352-366.
108. Renkiewicz, R., Qiu, L., Lesch, C., Sun, X., Devalaraja, R., Cody, T., Kaldjian, E., Welgus, H., and Baragi, V. (2003). Broad-spectrum matrix metalloproteinase inhibitor marimastat-induced musculoskeletal side effects in rats. Arthritis and Rheumatism, 48, 1742-1749.
109. Edwards, P.D. (2002). Human neutrophil elastase inhibitors. In Proteinase and Peptidase Inhibition, Smith, H.J. and Simons, C., Eds., Taylor & Francis, London, pp. 154-177.
110. Hoffmann, T., Glund, K., McIntosh, C.H., Pederson, R.A., Hanefeld, M., Rosenkranz, B., and Demuth, H.-U. (2001). DPPIV-inhibition as treatment of type II diabetes. In Cell-Surface Aminopeptidases: Basic and Clinical Aspects, Mizutani, S., Ed., Elsevier Science, Amsterdam, pp. 381-387.
111. Villhauer, E.B., Brinkman, J.A., Naderi, G.B., Burkey, B.F., Dunning, B.E., Prasad, K., Mangold, B.L., Russell, M.E., and Hughes, T.E. (2003). 1-[[(3-hydroxy-1-adamantyl) amino]acetyl]-2-cyano-(S)-pyrrolidine: a potent, selective, and orally bioavailable dipeptidyl peptidase IV inhibitor with antihyperglycemic properties. Journal of Medicinal Chemistry, 46, 2774-2789.
112. Rukamp, B. and Powers, J.C. (2002). Cathepsins. In Proteinase and Peptidase Inhibition, Smith, H.J. and Simons, C., Eds., Taylor & Francis, London, pp. 84-126.
113. Bartenschlager, R. and Koch, J.-O. (2002). The hepatitis C virus NS3 serine-type proteinase. In Proteinase and Peptidase Inhibition, Smith, H.J. and Simons, C., Eds., Taylor & Francis, London, 333-351.