Cathepsin B inhibitors as potential anti-metastatic agents

Bibliography

• GOLDFARB RH, BRUNSON KW: Overview of current un-derstanding of tumor spread. In: Cancer Growth and Progression. Goldfarb RH (Ed.), Kluwer Academic, Dor-drecht (1989).
   Google Scholar
• FIDLER IJ: Critical factors in the biology of human can-cer metastasis: twenty-eighth GHA Clowes memorial award Llecture. Cancer Res. (1990) 50:6130–6138.
   PubMed Web of Science ®Google Scholar
• •Comprehensive review of the metastatic process.
   Google Scholar
• POSTE G, FIDLER IJ: The pathogenesis of cancer metas-tasis. Nature (1979) 238:139–146.
   Google Scholar
• DUFFY MJ: The role of proteolytic enzymes in cancer invasion and metastasis. Clin. Exp. Metastasis (1992) 10:145–155.
   PubMed Web of Science ®Google Scholar
• •Review of the proteolytic enzyme involved in invasion and metastasis.
   Google Scholar
• LIOTTA LA, RAO CN, WEWER UM: Biochemical interac-tions of tumor cells with the basement membrane. Ann. Rev. Biochem. (1986) 55:1037–1057.
   PubMed Web of Science ®Google Scholar
• MIGNATTI P, RIFKIN DB: Biology and biochemistry ofproteinases in tumor invasion. Physiol. Rev. (1993) 73:161–195.
   PubMed Web of Science ®Google Scholar
• KANE SE, GOTTESMAN MM: The role of cathepsin L inmalignant transformation. Semin. Cancer Biol. (1990) 1(2):127–136.
   PubMedGoogle Scholar
• BERQUIN IM, SLOANE BF: Cysteine proteases and tu-mor progression. Perspect. Drug Discov. Design (1994) 2:371-388. Review of the cysteine proteases and their role in tumour progression.
   Google Scholar
• TEDONE T, CORREALE M, BARBAROSSA G et al Release of the aspartyl protease cathepsin D is associated with and facilitates human breast cancer cell invasion. FASEB J (1997) 11(10):785–792.
   PubMed Web of Science ®Google Scholar
• KAWADA A, HARA K, KOMINAMI E et al.: Expression ofcathepin D and B in invasion and metastasis of squa-mous cell carcinoma. Br. J. Dermatol. (1997) 137:361–366.
   Google Scholar
• ELLIOTT E, SLOANE BF: The cysteine protease cathep-sin B in cancer. Perspect. Drug Discov. Design (1996) 6:12–32.
   Google Scholar
• ••Review of cathepsin B and its role in cancer metastasis andinvasion.
   Google Scholar
• BUCK MR, KARUSTIS DG, DAY NA et al.: Degradation ofextracellular-matrix proteins by human cathepsin B from normal and tumour tissues. Biochem. J. (1992) 282:273–278.
   PubMedGoogle Scholar
• LAH TT, BUCK MR, HONN KV et al: Degradation oflaminin by human tumor cathepsin B. Clin. Exp. Metas-tasis (1989) 7(4):461–468.
   Google Scholar
• KEPPLER D, SAMENI M, MOIN K et al.: Tumor progres-sion and angiogenesis: cathepsin B and Co. Biochem. Cell Biol. (1996) 74(6):799–810.
   Google Scholar
• ••First report implicating cathepsin B in angiogenesis.
   Google Scholar
• BERQUIN IM, SLOANE BF: Cathepsin B expression in human tumors. In: Intracellular Protein Catabolism. Suzuki K, Bond J (Eds.), Plenum Press, New York (1996).
   Google Scholar
• ••Review on the altered expression of cathepsin B in cancermetastasis.
   Google Scholar
• KOBAYASHI H, SCHMITT M, GORETZKI L et al.: Cathep-sin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinase-type plaminogen activator (pro-uPA). J. Biol. Chem. (1991) 266(8):5147–5152.
   PubMed Web of Science ®Google Scholar
• KOBAYASHI H, OHI H, SUGIMURA M et al.: Inhibition of in vitro ovarian cancer cell invasion by modulation of urokinase-type plasminogen activator and cathepsin B. Cancer Res. (1992) 52(13):3610–3614.
   Google Scholar
• KEPPLER D, SLOANE1 BF: Cathepsin B - multiple enzyme forms from a single gene and their relation to cancer. Enzyme Protein (1996) 49 (1-3) :94–105.
   Google Scholar
• SINHA AA, GLEASON DF, DELEON OF et al.: Localization of a biotinylated cathepsin B oligonucleotide probe in human prostate including invasive cells and invasive edges by in situ hybridization. Anat. Record (1993) 235 (2) :233–240.
   Google Scholar
• SINHA AA, WILSON MJ, GLEASON DF et al: Immunohis-tochemical localization of cathepsin B in neoplastic human prostate. Prostate (1995) 26(4):171–178.
   Google Scholar
• VISSCHER DW, SLOANE BF, SAMENI M et al: Clinicopa-thologic significance of cathepsin B immunostaining in transitional neoplasia. Modern Pathol (1994) 7(1)76–
   Google Scholar
• CAMPO E, MUNOZ J, MIQUEL R et al: Cathepsin B ex-pression in colorectal carcinomas correlates with tu-mor progression and shortened patient survival. Am. J. Pathol (1994) 145(2):301–309.
   PubMed Web of Science ®Google Scholar
• WERLE B, EBERT W, KLEIN W et al.: Cathepsin B in tu-mors, normal tissue and isolated cells from the normal lung. Anticancer Res. (1994) 14 (3A):1169–1176.
   Google Scholar
• SATOH Y, HIGASHI T, NOUSO K etal.: Cathepsin B in the growth of colorectal cancer: increased activity of cathepsin B in human colorectal cancer. Acta Med. Okayama (1996) 50(6):305–311.
   Google Scholar
• BENITEZ-BRIBIESCA L, MARTINEZ G, RUIZ MT et al.: Pro-teinase activity in invasive cancer of the breast. Corre-lation with tumor progression. Arch. Med. Res. (1995) 26(Suppl.):S163–S168.
   Google Scholar
• WERLE B, JULKE B, LAH T et al.: Cathepsin B fraction ac-tive at physiological pH of 7.5 is of prognostic signifi-cance in squamous cell carcinoma of human lung. Br. J. Cancer. (1997) 75(8):1137–1143.
   Google Scholar
• CALKINS CC, SLOANE BF: Mammalian cysteine protease inhibitors: biochemical properties and possible roles in tumor progression. Biol. Chem. Hoppe-Seyler (1995) 376(2)71–80.
   Google Scholar
• •Review of endogenous cysteine protease inhibitors and their correlation with cancer metastasis.
   Google Scholar
• SYLVEN B, SNELLMAN 0, STRAULI P: Immunofluores-cent studies of the ocurence of cathepsin B1 at tumor cell surfaces. Virchows Arch. LBI (1974) 17:97–112.
   PubMedGoogle Scholar
• ROZHIN J, SAMENI M, ZIEGLER G et al.: Pericellular pH affects distribution and secretion of cathepsin B in ma-lignant cells. Cancer Res. (1994) 54:6517–6525.
   PubMed Web of Science ®Google Scholar
• VAN NOORDEN CJF, JONGES TGN, VAN MARLE J et al.: Heterogeneous suppression of experimentally in-duced colon cancer metastasis in rat liver lobes by in-hibition of extracellular cathepsin B. Clin. Exp. Metastasis (1998) 16:159–167.
   Google Scholar
• ••First report on the localisation of active cathepsin B only andsuppresion of metastasis by inhibition of extracellular enzymes.
   Google Scholar
• REDWOOD SM, LIU BC-S, WEISS RE et al.: Abrogation of the invasion of human bladder tumor cells by using protease inhibitor(s). Cancer (1992) 69:1212–1219.
   Google Scholar
• WEISS RE, CORDON-CARDO C, FAIR WR: Characteriza-tion of cathepsin B-mediated protease cascade in pros-tate cancer cell lines. Proc. Ann. Am. Assoc. Cancer. Res. (1993) 34:A480.
   Google Scholar
• LETO G, PIZZOLANTI G, TUMMINELLO FM et al: Effects of E-64 (cysteine-proteinase inhibitor) and pepstatin (aspartyl-proteinase inhibitor) on metastasis forma-tion in mice with mammary and ovarian tumors. In vivo (1994) 8:231–236.
   PubMedGoogle Scholar
• NAVAB R, MORT JS, BRODT P: Inhibition of carcinoma cell invasion and liver metastases formation by the cysteine proteinase inhibitor E-64. Clin. Exp. Metastasis (1997) 15(2):121–129.
   Google Scholar
• INSOGHA KL, STEWART AF, VIGNERY AM et al.: Bio-chemical and histomorphometric characterization of a rat model for humoral hypercalcaemia of malig-nancy. Endocrinology (1984) 114 (3) :888–896.
   Google Scholar
• MORT JS, BUTTLE DJ: Molecules in focus: cathepsin B. Int. j Biochem. Cell. Biol. (1997) 29(5):715–720.
   PubMed Web of Science ®Google Scholar
• ESSER RE, ANGELO RA, MURPHEY MD et al.: Cysteine proteinase inhibitors decrease articular cartilage and bone destruction in chronic inflammatory arthritis. Arthrit. Rheum. (1994) 37(2):236–247.
   Google Scholar
• KATUNUMA N, KOMINAMI E: Abnormal expression of lysosomal cysteine proteinases in muscle wasting dis-eases. Rev. Physiol. Biochem. Pharmacol. (1987) 108:1–20.
   PubMedGoogle Scholar
• SAITO K, ELCE JS, HAMOS JE et al.: Widespread activa-tion of calcium-activaed neutral proteinase (calpain) in the brain in Alzheimer's disease: a potential molecu-lar basis for neuronal degeneration. Proc. Natl. Acad. Sci. USA (1993) 90(7):2628–2632.
   Google Scholar
• LEMERE CA, MUNGER JS, SHI G-P et al.: The lysosomal cysteine protease, cathepsin S is increased in Alz-heimer's disease and Down's syndrome brain. An immunocytochemical study. Am. J. Pathol. (1995) 146 (4) 848–860.
   Google Scholar
• DRAKE FH, DODDS RA, JAMES IE et al: Cathepsin K butnot cathepsins B, L, or S, is abundantly expressed in human osteoclasts. j Biol. Chem. (1996) 271:12511–12516.
   PubMed Web of Science ®Google Scholar
• MCGRATH ME, EAKIN AE, ENGEL JC et al.: The crystalstructure of cruzain: a therapeutic target for Chagas' disease. J. Mol. Biol. (1995) 247(2) :251–259.
   Google Scholar
• FRANCIS SE, GLUZMAN IY, OKSMAN A et al.: Characteri-zation of native falcipain, an enzyme involved in Plas-modium falciparum hemoglobin degradation. Mol Biochem. Parasitol. (1996) 83(2):189–200.
   Google Scholar
• SAKANARI JA, NADLER SA, CHAN VJ et al.: Leishmania major comparison of the cathepsin L- and B-like cys-teine protease genes with those of other trypanoso-matids. Exp. Parasitol. (1997) 85(0:63–76.
   Google Scholar
• STANLEY SLJ, ZHANG T, RUBIN D et al.: Role of the Enta-moeba histolytica cysteine proteinase in amebic liver abscess formation in severe combined immunodefi-cient mice. Infect. Immun. (1995) 63 (4) :1587–1590.
   Google Scholar
• LUMKOWSKI S, SREEVATSAN S, AMBERG C et al.: Inacti-vation of Streptococcus pyogenes extracellular cys-teine protease significantly decreases mouse lethality of serotype M3 and M49 strains. J. Clin. Invest. (1997) 99(102574–2580.
   Google Scholar
• POTEMPA J, PIKE R, TRAVIS J: Titration and mapping of the active-site of cysteine proteinases from Porphyro-monas gingivalis (gingipains) using peptidyl chloro-methanes. Biol. Chem. (1997) 378(3–4)223–230.
   Google Scholar
• BOSSARD MJ, TOMASZED TA, THOMPSON SC et al.: Pro-teolytic activity of human osteoclast cathepsin K. J. Biol. Chem (1996) 271:12516–12524.
   Google Scholar
• THOMPSON SK, HALBERT SM, BOSSARD MJ et al: Design of potent and selective human cathepsin K inhibitors that span the active-site. Proc. Nat. Acad. Sci. USA (1997) 94(26):14249–14254.
   Google Scholar
• DINARELLO CA, RC T: Blocking 11-1: Interleukin recep-tor agonist in vivo and in vitro. Immunol. Today (1991) 12:404–410.
   PubMedGoogle Scholar
• THORNBERRY NA, MOLINEAUX S: Interleukin-18 con-verting enzyme: A novel cysteine protease is required for 11-18. Protein Sci. (1995) 4:3–12.
   PubMed Web of Science ®Google Scholar
• NAKAGAWA N, ROTH W, WONG P et al.: Cathepsin L: critical role in EL degradation and CD4 T cell selection in the thymus. Science (1998) 280:450–453.
   PubMed Web of Science ®Google Scholar
• SCHIELKE GP, YANG GY, SHIVERS BD et al.: Reduced is-chaemic brain injury in interleukin-1 Bconverting enzyme-defcient mice. J. Cerebral Blood Flow Met. (1998) 18(2):180–185.
   PubMed Web of Science ®Google Scholar
• JOHNSON MR, POLYMEROPOULOS MH, VOS HL et al: A nonsense mutation in the cathepsin K gene in a family with pycnodysostosis. Genome Res. (1996) 6(1 0:1050–1055.
   Google Scholar
• KIRSCHKE H, WOOD L, ROISIN FJ et al. An investigation of intracellular proteinases during differentiation of cultured muscle cells. In: Proteinase Inhibitors. Katanuma N, Holzu H, Umezawa H (Eds.), Japan Scientific Societies Press, Tokyo (1983).
   Google Scholar
• HONN KV, CAVANAUGH P, EVENS C et al.: Tumour cell- platelet aggregation: induced by cathepsin B-like pro-teinase and inhibited by prostacyclin. Science (1982) 217:540–542.
   PubMed Web of Science ®Google Scholar
• MIZUNO K, MIYATO A, KONGAWAND K et al.: A unique pseukephalin-converting enzyme purified from bo-vine adrenal chromatin granules. Biochem. Biophys. Res. Commun. (1982) 108:1235–1242.
   Google Scholar
• KIRSCHKE H, BARRETT AJ: Chemistry of lysosomal pro-teases. In: Lysosomes: Their Role in Protein Breakdown. Glaumann H, Ballard FJ (Eds.), Academic Press, London (1987).
   Google Scholar
• BARRETT AJ: The cystatins: a new class of peptidases in-hibitors. Trends Biol. Sci. (1987) 12:193–196.
   Web of Science ®Google Scholar
• TURK V, BODE W: Lysosomal cysteine proteinases and their inhibitors cystatins. In: Innovations in Proteases and Their Inhibitors. Aviles FX (Ed.), Walter de Gruyter & Co., Berlin (1993).
   Google Scholar
• BROCKLEHURST K, WILLENBROCK F, SALIH E: Cysteine proteases. In: Hydrolytic Enzymes. Brocklehurst K, Neu-berger A (Eds.), Elsevier Press, Amsterdam (1987).
   Google Scholar
• VARUGHESE KI, AHMED FR, CAREY PR et al.: Crystal structure of a papain-E-64 comlex. Biochemistry (1989) 28 (3): 1330–1332.
   Google Scholar
• •First report of papain complexed to an epoxysuccinyl inhibitor.
   Google Scholar
• MUSIL D, ZUCIC D, TURK D et al.: The refined 2.15 Ax- ray crystal structure of human liver cathepsin B: the structural basis for its specificity. EMBO J. (1991) 10:2321–2330.
   Google Scholar
• GOUR-SALIN BJ, LACHANCE P, PLOUFFE C et al.: Epoxy- succinyl dipeptides as selective inhibitors of cathepsin B. J. Med. Chem. (1993) 36(6):720–725.
   Google Scholar
• ••First report on the design of selective inhibitors of cathepsinB proposed to bind in the St site.
   Google Scholar
• TURK D, PODOBNIK M, POPOVIC T et al.: Crystal struc- ture of cathepsin B inhibited with CA030 at 2.0-A reso-lution: A basis for the design of specific epoxysuccinyl inhibitors. Biochemistry (1995) 34(14) :4791–4797.
   Google Scholar
• ••First report on basus of specificity of inhibitors binding tothe St site
   Google Scholar
• YAMAMOTO A, HARA T, TOMOO K et al.: Binding mode of CA074, a specific irreversible inhibitor, to bovine cathepsin B as determined by X-ray crystal analysis of the complex. J. Biochem. (1997) 121 (5):974–977.
   Google Scholar
• ILLY C, QURAISHI 0, WANG J et al.: Role of the occluding loop in cathepsin B activity. J. Biol. Chem. (1997) 272(2):1197–1202.
   Google Scholar
• •Present experimental evidence for the role of Hisim and Hisil 1 in the cathepsin B's exopeptidase activity.
   Google Scholar
• BERGER A, SCHECHTER I: On the active-site in prote- ases. I. Papain. Biochem. Biophys. Res. Commun. (1967) 27:157–162.
   Google Scholar
• BAKER EN, DRENTH J: The thiol proteases: structure and mechanism. In: Biological Macromolecules and As-semblies. Jurnack FA, MacPherson A (Eds.), John Wiley & Sons, New York (1987).
   Google Scholar
• BERGER A, SCHECHTER I: Mapping the active-site of pa-pain with the aid of peptide substrates and inhibitors. Philos. Trans. Royal Soc. London, SerB (1970) 257:249–264.
   PubMed Web of Science ®Google Scholar
• BARRETT AJ, KIRSHKE H: Cathepsin B, cathepsin H and cathepsin L. Methods Enzymol. (1981) 80:535–561.
   PubMed Web of Science ®Google Scholar
• JIA Z, HASNAIN S, HIRAMA T et al.: Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design. J. Biol. Chem. (1995) 270 (10):5527–5533.
   Google Scholar
• KHOURI HE, VERNET T, MENARD R et al.: Engineering of papain: selective alteration of substrate specificity by site-directed mutagenesis. Biochemistry (1991) 30:8929–8936.
   Google Scholar
• SHAW E, WIKSTROM P, RUSCICA J: An exploration of the primary specificity site of cathepsin B. Arch. Biochem. Biophys. (1983) 222(2):424–429.
   Google Scholar
• KIRSCHKE H, WIKSTROM P, SHAW E: Active centre dif-ferences between cahtepsins L and B: the Si binding region. FEBS Lett. (1988) 228(1): 128–130.
   Google Scholar
• STORER AC, MENARD R: Recent insights into cysteine protease specificity: lessons for drug design. Perspect. Drug Discov. Design (1996) 6:33–46.
   Google Scholar
• ••Review of the recent literature on cysteine proteasespecificity.
   Google Scholar
• TARALP A, KAPLAN H, SYTWU II et al.: Characterization of the S3 specificity of cathepsin B. J. Biol. Chem. (1995) 270 (30) :18036–18043.
   Google Scholar
• MENARD R, CARMONA E, PLOUFFE C et al.: The specific-ity of the Si' subsite of cysteine proteases. FEBS Lett. (1993) 328(12):107–110.
   Google Scholar
• FENG MH, CHAN SL, XIANG YF et al.: The binding mode of an E-64 analog to the active-site of cathepsin B. Pro-tein Engineer. (1996) 9(1 1) 977–986.
   Google Scholar
• •Molecular modelling studies on the preferential enrgy of binding of a specific inhibitor of cathepsin B to the St sub-sites versus the S subsites.
   Google Scholar
• DRENTH J, KALK KH, SWEN HM: Binding of chloro-methyl ketone substrate analogues to crystalline pa-pain. Biochemistry (1976) 15:3731–3738.
   PubMed Web of Science ®Google Scholar
• GOUR-SALIN BJ, LACHANCE P, MAGNY MC et al.: E64 [trans-epoxysuccinyl-L-leucylamido-(4-guanidino)bu-tane] analogues as inhibitors of cysteine proteinases: investigation of S2 subsite interactions. Biochem. (1994) 299 (Pt 2):389–392.
   Google Scholar
• CYGLER M, SIVARAMAN J, GROCHULSKI P et al.: Struc-ture of rat procathepsin B - model for inhibition of cys-teine protease activity by the proregion. Structure (1996) 4(4):405–416.
   PubMed Web of Science ®Google Scholar
• ••First reported x-ray crystal structure of a cysteine proteaseproenzyme.
   Google Scholar
• TURK D, PODOBNIK M, KUHELJ R et al. Crystal struc- tures of human procathepsin B at 3.2 and 3.3 angstrom resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide. FEBS Lett. (1996) 384(3):211–214.
   Google Scholar
• CHEN Y, PLOUFFE C, MENARD R et al.: Delineating fun-tionally important regions and residues in the cathep-sin B propeptde for inhibitory activity. FEBS Lett. (1996) 393(1)24–26.
   Google Scholar
• SILVERMAN RB: Enzyme inhibition and inactivation. In: The Organic Chemistry of Drug Design and Drug Action. (Eds.), Academic Press, London (1992).
   Google Scholar
• KRANTZ A: Some thoughts of enzyme inhibition and the quiescent affinity label concept. Adv. Med. Chem. (1992) 1:235–261.
   Google Scholar
• •Excellent review on the development of quiescent affinity labels.
   Google Scholar
• DEMUTH H-U: Recent developments in inhibiting cys-teine and serine proteases. j Enzyme Inhibit. (1990) 3 :249–278.
   Google Scholar
• SHAW E: Cysteinyl proteinases and their selective inac-tivation. Adv. Enzymol Relat. Areas Mol. Biol. (1990) 63:271–347.
   PubMedGoogle Scholar
• RASNICK D: Small synthetic inhibitors of cysteine pro-teases. Perspect. Drug Discov. Design (1996) 6:47–63.
   Google Scholar
• ••Review on recent developments of cysteine proteaseinhibitors.
   Google Scholar
• OTTO H-H, SCHIRMEISTER T: Cysteine proteases and their inhibitors. Chem. Rev. (1997) 97:133–171.
   PubMed Web of Science ®Google Scholar
• ••Most recent comprehensive review of cysteine proteaseinhibitors.
   Google Scholar
• HANADA K, TAMAI M, OHMURA S et al: Studies on thiolprotease inhibitors. Part I. Isolation and characteriza-tion of E-64, a new cysteine protease inhibitor. Agric. Biol. Chem. (1978) 42:523–527.
   Google Scholar
• BARRETT AJ, KEMBHAVI AA, BROWN MA et al: L-trans-e poxysuccinyl-leucylamido (4 -guanidino)butane (E-64) and its analogues as inhibitors of cysteine prote-inases including cathepsin B, H, and L. Biochem. J. (1982) 201 (1) :189–198.
   Google Scholar
• SCHASCHKE N, ASSFALG-MACHLEIDT I, MACHLEID W etE-64 analogues as inhibitors of cathepsin B - on the role of the absolute configuration of the epoxysucci-nyl group. Bioorg. Med. Chem. (1997) 5(9):1789–1797.
   Google Scholar
• •Report of influence of epoxysuccinyl stereochemistry on in-hibitory activity and selectivity.
   Google Scholar
• SCHASCHKE N, ASSFALG-MACHLEIDT I, MACHLEID W et Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selctive cathepsin B in-hibitors. FEBS Lett. (1998) 421:80–82.
   Google Scholar
• •Report of the most potent epoxysuccinyl inhibitor to date.
   Google Scholar
• NODA T, ISOGAI K, KATANUMA N et al: Effects of cathepsin B, H, and Din pectoral muscle of dystrophic chickens (line 413) of in vivo administration of E-64c (N4N-(L-3-transcarboxyoxirane-2-carbony1)-L-leucy1]-3-methyl-butylamine). J. Biochem. (1981) 90 (3):893–896.
   Google Scholar
• TAMAI M, MATSUMOTO K, OMURA S et al. In vitro and in vivo inhibition of cysteine proteinases by EST, a new analog of E-64. J. PharmacobioL-Dynamics (1986) 9(8):672–677.
   Google Scholar
• FUKUSHIMA K, MASAYUKI A, KOHNO Y eta].: An epoxy- succinic acid derivative (Loxistatin)-induced hepatic injury in rats and hamsters. Tox. Appl. Pharm. (1990) 105:1–12.
   Google Scholar
• Scrip. World Pharmaceutical News (1992) 1765:11.
   Google Scholar
• YU CM, CURTIS JM, WALTER JA et al: Potent inhibitors of cysteine proteases from the marine fungus Microas-cus longirostris. J. Antibiotics (1996) 49(4)395–397.
   Google Scholar
• KNIGHT CG: The characterization of enzyme inhibi-tion. In: Proteinase Inhibitors. Barrett A SG (Ed.), Elsevier, Amsterdam (1986).
   Google Scholar
• MARTICHONOK V, PLOUFFE C, STORER AC et al.: Aziridine analogs of Rtrans-(Epoxysucciny1)-L-leucyllamino]-4- guanidinobutane (E-64) as inhibitors of cysteine proteases. j Med. Chem. (1995) 38(16):3078–3085.
   Google Scholar
• HANZLIK RP, SAT: Vinylogous amino acid esters: a new class of inactivators for thiol proteases. J. Med. Chem. (1984) 27:711–712.
   Google Scholar
• THOMPSON SA, ANDREWS PR, HANZLIK RP: Carboxyl-modified amino acids and peptides as protease inhibi-tors. Med. Chem (1986) 29:104–111.
   Google Scholar
• LIU S, HANZLIK RP: Structure-activity relationships for inhibition of papain by peptide Michael inhibitors. J. Med. Chem. (1992) 35 (6) :1067–1075.
   Google Scholar
• PALMER JT, RASNICK D, KLAUS JL et al.: Vinyl sulfones as mechanism-based cysteine protease inhibitors. J. Med. Chem (1995) 38(17):3193–3196.
   PubMed Web of Science ®Google Scholar
• •Inhibition constants for various cysteine proteases with vi-nyl sulfones are reported.
   Google Scholar
• BROMME D, KLAUS JL, OKAMOTO K eta].: Peptidyl vinyl sulfones: a new class of potent and selective protease inhibitors. S2P2 specificity of human cathepsin 02 in comparison with cathepsins S and L. Biochem. J. (1996) 315:85–89.
   Google Scholar
• ROSENTHAL PJ, OLSON JE, LEE GK et al.: Antimalarial ef-fects of vinyl sulfone cysteine proteinase inhibitors. Antimicrob. Agents Chemo. (1996) 40(7):1600–1603.
   Google Scholar
• ERMER A, BAUMANN H SG, PETERS K et al.: Peptide dia-zomethyl ketones are inhibitors of subtilisin-type ser-ine proteases. j Enzyme Inhib. (1990) 4(0:35–42.
   Google Scholar
• AMBROSO JL, HARRIS C: In vitro embryotoxicity of the cysteine proteinase inhibitors benzyloxycarbonyl-phenylalanine-alanine-diazomethane (Z-Phe-Ala-CHN2) and benzyloxycarbonyl-phenylalanine-phenylalanine- diazomethane (Z-Phe-Phe-CHN2)• Teratology (1994) 50(3):214–228.
   Google Scholar
• IMPERIALI B, ABELES RH: Inhibition of serine proteases by peptidyl fluoromethyl ketones. Biochemistry (1986) 25:3760–3767.
   PubMed Web of Science ®Google Scholar
• ROBINSON VJ, PAULS HW, COLES PJ et al.: Carbon-13 NMR characterization of the papain adduct formed by the peptidyl acyloxy-, aryloxy- and chloromethyl ke-tone inhibitors. Bioorg. Chem. (1992) 20:42–54.
   Google Scholar
• KRANTZ A, COPP LI COLES PJ et al.: Peptidyl (acy-loxy) methyl ketones and the quiescent affinity label concept: the departing group as a variable structural element in the design of inactivators of cysteine prote-ases. Biochemistry (1991) 30:4678–4687.
   Google Scholar
• WAGNER BM, SMITH RA, COLES PJ et al: In vivo inhibi-tion of cathepsin B by peptidyl (acyloxy)methyl ke-tones. J. Med. Chem. (1994) 37(12):1833–1840.
   Google Scholar
• •First report of the evaluation of vinyl sulfone inhibitors in vivo.
   Google Scholar
• HANZLIK RP, ZYGMUT J, MOON JB: Reversible covalent binding of peptide nitriles to papain. Biochim. Biophys. Acta (1990) 1035(1):62–70.
   Google Scholar
• GAMCSIK MP, MALTHOUSE J, PAUL G et al.: Structure and stereochemistry of tetrahedral inhibitor complexes of papain by direct NMR observation. J. Am. Chem. Soc. (1983) 105:6324–6325.
   Google Scholar
• INOUE S, SHARMA RC, SCHIMKE RT et al: Cellular detoxi-fication of tripeptidyl aldehydes by an aldo-keto re-ductase. J. Biol. Chem. (1993) 268(8):5894–5898.
   Google Scholar
• MCCONNELL RM, YORK J, FRIZZELL D et al.: Inhibition studies of some serine and thiol proteinases by new leupeptin analogues. J. Med. Chem. (1993) 36:1084–1089.
   PubMedGoogle Scholar
• WOO J-A, SIGEIZUMI S, YAMAGUCHI K et al.: Peptidyl al-dehyde derivatives as potent and selective inhibitors of cathepsin L. Bioorg. Med. Chem. Lett. (1995) 5(14):1501–1504.
   Google Scholar
• SMITH RA, COPP LJ, DONNELLY SL et al.: Inhibition of cathepsin B by peptidyl aldehydes and ketones: slow binding behavior of a trifluoromethyl ketone. Bio-chemistry (1988) 27(17)6568–6573.
   Google Scholar
• BROMME D, BARTELS B, KIRSCHKE H et al.: Peptide methyl ketones as reversible inhibitors of cysteine proteinases. j Enzyme Inhib. (1989) 3 (1):13–21.
   Google Scholar
• PETERS K, FITTKAU S: Affinity chromatography of pro-teases using peptide methyl ketones as ligands. Bio-med. Biochim. Acta (1990) 49(4):173–178.
   Google Scholar
• ANGELASTRO MR, MEHDI S, BURKHART JP et al.: Alpha-diketone and alp ha-keto ester derivatives of N-protected amino acids and peptides as novel inhibi-tors of cysteine and serine proteinases. J. Med. Chem. (1990) 33(1):11–13.
   Google Scholar
• LIZ, PATIL GS, GOLUBSKI ZE et al: Peptide a-keto ester, a-keto amide, and a-keto acid inhibitors of calpains and other cysteine proteases. J. Med. Chem. (1993) 36(22)3472–3480.
   Google Scholar
• HABERSON SL, ABELLEIRA SM, AKIYAMA A et al.: Stereo-specific synthesis of peptidyl a-keto amides as inhibi-tors of calpain. J. Med. Chem. (1994) 37(18):2918–2929.
   Google Scholar
• LI Z, ORTEGA-VILAIN AC, PATIL GS et al.: Novel peptidyl a-keto amide inhibitors of calpains and other cysteine proteases. J. Med. Chem. (1996) 39(204089–4098.
   Google Scholar
• LINDERMAN RJ, TENNYSON SD, SCHULTZ DA: Compara-tive stability of fluoroketones hemi-thio acetals, ketals and hydrates. Tetrahedron Lett. (1994) 35(35):6437–6440.
   Google Scholar
• ANDO R, MORINAKA Y: A new class of proteinases in-hibitor. Cyclopropenone-containing inhibitor of pa-pain. J. Am. Chem. Soc. (1993) 115:1174–1175.
   Web of Science ®Google Scholar
• YAMASHITA DS, SMITH WW, ZHAO B et al.: Structure and design of potent and selective cathepsin K inhibitors. J. Am. Chem. Soc. (1997) 119:11351–11352.
   Web of Science ®Google Scholar
• SELZER PM, CHEN X, CHAN VJ et al.: Leishmania major: molecular modeling of cysteine proteases and predic-tion of new nonpeptide inhibitors. Exp. Parasitol (1997) 87:212–221.
   PubMed Web of Science ®Google Scholar
• •Combinatorial chemistry approach based on leads obtained from molecular modelling using the DOCK approach.
   Google Scholar
• KUNTZ ID, MENG EC, STOICHET BK: Structure based in-hibitor design. Acc. Chem. Res. (1994) 27:117–123.
   Web of Science ®Google Scholar
• RING CS, SUN E, MCKERROW JH et al.: Structure-based inhibitor design using protein models for the develop-ment of anti-parasitic agents. Proc. Natl. Acad. Sci. USA (1993) 90(8):3583–3587.
   Google Scholar
• RASMUSSEN HS, MCCANN PP: Matrixmetalloprotease inhibition as a novel ancticancer strategy: a review with special focus on batimastat and marimastat. Phar-macol. Ther. (1997) 75(0:69–75.
   PubMed Web of Science ®Google Scholar