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  • Aibe, K., Yazawa, H., Abe, K., Teramura, K., Kumegawa, M., Kawashima, H., and Honda, K. 1996. Substrate specificity of recombinant osteoclast-specific cathepsin K from rabbits. Biol. Pharm. Bull. 19: 10261031.
  • Barrett, A.J., Kembhavi, A.A., Brown, M.A., Kirschke, H., Knight, C.G., Tamai, M., and Hanada, K. 1982. L-Trans-epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem. J. 201: 189198.
  • Brömme, D. and Kaleta, J. 2002. Thiol-dependent cathepsins: Pathophysiological implications and recent advances in inhibitor design. Curr. Pharm. Des. 8: 16391658.
  • Brömme, D., Klaus, J.L., Okamoto, K., Rasnick, D., and Palmer, J.T. 1996. Peptidyl vinyl sulphones: A new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L. Biochem. J. 315: 8589.
  • Bühling, F., Rocken, C., Brasch, F., Hartig, R., Yasuda, Y., Saftig, P., Brömme, D., and Welte, T. 2004. Pivotal role of cathepsin K in lung fibrosis. Am. J. Pathol. 164: 22032216.
  • Chapman, H.A. Jr and Shi, G.P. 2000. Protease injury in the development of COPD: Thomas A. Neff Lecture. Chest 117: 295S299S.
  • Chapman, H.A., Riese, R.J., and Shi, G.P. 1997. Emerging roles for cysteine proteases in human biology. Annu. Rev. Physiol. 59: 6388.
  • Choe, Y., Leonetti, F., Greenbaum, D.C., Lecaille, F., Bogyo, M., Brömme, D., Ellman, J.A., and Craik, C.S. 2006. Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities. J. Biol. Chem. 281: 1282412832.
  • Chowdhury, S.F., Sivaraman, J., Wang, J., Devanathan, G., Lachance, P., Qi, H., Menard, R., Lefebvre, J., Konishi, Y., Cygler, M., et al. 2002. Design of noncovalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides. J. Med. Chem. 45: 53215329.
  • Cornell, W.D., Cieplak, P., Bayly, C.I., Gould, I.R., Merz, K.M. Jr, Ferguson, D.M., Spellmeyer, D.C., Fox, T., Caldwell, J.W., and Kollman, P.A. 1995. A second generation force field for the simulation of proteins, nucleic acids and organic molecules. J. Am. Chem. Soc. 117: 51795197.
  • Garnero, P., Borel, O., Byrjalsen, I., Ferreras, M., Drake, F.H., McQueney, M.S., Foged, N.T., Delmas, P.D., and Delaisse, J.M. 1998. The collagenolytic activity of cathepsin K is unique among mammalian proteinases. J. Biol. Chem. 273: 3234732352.
  • Godat, E., Lecaille, F., Desmazes, C., Duchene, S., Weidauer, E., Saftig, P., Brömme, D., Vandier, C., and Lalmanach, G. 2004. Cathepsin K: A cysteine protease with unique kinin-degrading properties. Biochem. J. 383: 501506.
  • Joyce, J.A. and Hanahan, D. 2004. Multiple roles for cysteine cathepsins in cancer. Cell Cycle 3: 15161519.
  • Kafienah, W., Brömme, D., Buttle, D.J., Croucher, L.J., and Hollander, A.P. 1998. Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix. Biochem. J. 331: 727732.
  • Lecaille, F., Kaleta, J., and Brömme, D. 2002a. Human and parasitic papain-like cysteine proteases: Their role in physiology and pathology and recent developments in inhibitor design. Chem. Rev. 102: 44594488.
  • Lecaille, F., Choe, Y., Brandt, W., Li, Z., Craik, C.S., and Brömme, D. 2002b. Selective inhibition of the collagenolytic activity of human cathepsin K by altering its S2 subsite specificity. Biochemistry 41: 84478454.
  • Lecaille, F., Vandier, C., Godat, E., Hervé-Grépinet, V., Brömme, D., and Lalmanach, G. 2007. Modulation of hypotensive effects of kinins by cathepsin K. Arch. Biochem. Biophys 459: 129136.
  • Li, Z. and Scheraga, H.A. 1987. Monte Carlo-minimization approach to the multiple-minima problem in protein folding. Proc. Natl. Acad. Sci. 84: 66116615.
  • Li, Z., Hou, W.S., and Brömme, D. 2000. Collagenolytic activity of cathepsin K is specifically modulated by cartilage-resident chondroitin sulfates. Biochemistry 39: 529536.
  • Li, Z., Hou, W.S., Escalante-Torres, C.R., Gelb, B.D., and Brömme, D. 2002. Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate. J. Biol. Chem. 277: 2866928676.
  • Li, Z., Yasuda, Y., Li, W., Bogyo, M., Katz, N., Gordon, R.E., Fields, G.B., and Brömme, D. 2004. Regulation of collagenase activities of human cathepsins by glycosaminoglycans. J. Biol. Chem. 279: 54705479.
  • Nägler, D.K. and Menard, R. 2003. Family C1 cysteine proteases: Biological diversity or redundancy? Biol. Chem. 384: 837843.
  • Naim, M., Bhat, S., Rankin, K.N., Dennis, S., Chowdhury, S.F., Siddiqi, I., Drabik, P., Sulea, T., Bayly, C.I., Jakalian, A., et al. 2007. Solvated interation Energy (SIE) for scoring protein-ligand binding affinities. I. Exploring the parameter space. J. Chem. Inf. Model. 47: 122133.
  • Nicklin, M.J. and Barrett, A.J. 1984. Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg-white cystatin. Biochem. J. 223: 245253.
  • Ortega, M.M., Nascimento, H., Costa, F.F., Teori, M.T., and Lima, C.S. 2003. A polymorphism in the angiogenesis inhibitor, endostatin, in multiple myeloma. Leuk. Res. 27: 9394.
  • Prockop, D.J. and Kivirikko, K.I. 1995. Collagens: Molecular biology, diseases, and potentials for therapy. Annu. Rev. Biochem. 64: 403434.
  • Purisima, E.O. 1998. Fast summation boundary element methods for calculating solvation free energies of macromolecules. J. Comput. Chem. 19: 14941505.
  • Purisima, E.O. and Nilar, S.H. 1995. A simple yet accurate boundary element method for continuum dielectric calculations. J. Comput. Chem. 16: 681689.
  • Puzer, L., Vercesi, J., Alves, M.F., Barros, N.M., Araujo, M.S., Aparecida Juliano, M., Reis, M.L., Juliano, L., and Carmona, A.K. 2005. A possible alternative mechanism of kinin generation in vivo by cathepsin L. Biol. Chem. 386: 699704.
  • Rawlings, N.D., Morton, F.R., and Barrett, A.J. 2006. MEROPS: The peptidase database. Nucleic Acids Res. 34: D270D272.
  • Riese, R.J. and Chapman, H.A. 2000. Cathepsins and compartmentalization in antigen presentation. Curr. Opin. Immunol. 12: 107113.
  • Roth, W., Deussing, J., Botchkarev, V.A., Pauly-Evers, M., Saftig, P., Hafner, A., Schmidt, P., Schmahl, W., Scherer, J., Anton-Lamprecht, I., et al. 2000. Cathepsin L deficiency as molecular defect of furless: Hyperproliferation of keratinocytes and perturbation of hair follicle cycling. FASEB J. 14: 20752086.
  • Smooker, P.M., Whisstock, J.C., Irving, J.A., Siyaguna, S., Spithill, T.W., and Pike, R.N. 2000. A single amino acid substitution affects substrate specificity in cysteine proteinases from Fasciola hepatica. Protein Sci. 9: 25672572.
  • Taleb, S., Lacasa, D., Bastard, J.P., Poitou, C., Cancello, R., Pelloux, V., Viguerie, N., Benis, A., Zucker, J.D., Bouillot, J.L., et al. 2005. Cathepsin S, a novel biomarker of adiposity: Relevance to atherogenesis. FASEB J. 19: 15401542.
  • Tepel, C., Brömme, D., Herzog, V., and Brix, K. 2000. Cathepsin K in thyroid epithelial cells: Sequence, localization and possible function in extracellular proteolysis of thyroglobulin. J. Cell Sci. 113: 44874498.
  • Thompson, S.K., Halbert, S.M., Bossard, M.J., Tomaszek, T.A., Levy, M.A., Zhao, B., Smith, W.W., Abdel-Meguid, S.S., Janson, C.A., D'Alessio, K.J., et al. 1997. Design of potent and selective human cathepsin K inhibitors that span the active site. Proc. Natl. Acad. Sci. 94: 1424914254.
  • Turk, V., Turk, B., and Turk, D. 2001. Lysosomal cysteine proteases: Facts and opportunities. EMBO J. 20: 46294633.
  • Wang, D., Pechar, M., Li, W., Kopeckova, P., Brömme, D., and Kopecek, J. 2002. Inhibition of cathepsin K with lysosomotropic macromolecular inhibitors. Biochemistry 41: 88498859.
  • Williams, J.W. and Morrison, J.F. 1979. The kinetics of reversible tight-binding inhibition. Methods Enzymol. 63: 437467.
  • Word, J.M., Lovell, S.C., Richardson, J.S., and Richardson, D.C. 1999. Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation. J. Mol. Biol. 285: 17351747.
  • Xia, L., Kilb, J., Wex, H., Lipyansky, A., Breuil, V., Stein, L., Palmer, J.T., Dempster, D.W., and Brömme, D. 1999. Localization of rat cathepsin K in osteoclasts and resorption pits: Inhibition of bone resorption cathepsin K-activity by peptidyl vinyl sulfones. Biol. Chem. 380: 679687.
  • Yasothornsrikul, S., Greenbaum, D., Medzihradszky, K.F., Toneff, T., Bundey, R., Miller, R., Schilling, B., Petermann, I., Dehnert, J., Logvinova, A., et al. 2003. Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter. Proc. Natl. Acad. Sci. 100: 95909595.
  • Yasuda, Y., Li, Z., Greenbaum, D., Bogyo, M., Weber, E., and Brömme, D. 2004. Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. J. Biol. Chem. 279: 3676136770.