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Volumn 28, Issue , 1999, Pages 181-204

The lysosomal cysteine proteases

Author keywords

Cathepsins; Crystallography; Papain; Structure based drug design; Thiol

Indexed keywords

CATHEPSIN B; CATHEPSIN H; CATHEPSIN K; CATHEPSIN L; CATHEPSIN S; CYSTEINE PROTEINASE; ENZYME PRECURSOR; PAPAIN;

EID: 0032986028     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.28.1.181     Document Type: Article
Times cited : (298)

References (112)
  • 1
    • 0001452325 scopus 로고
    • Crystallographic refinement of the structure of actinidin at 1.7 Å resolution by fast Fourier least-squares methods
    • 1. Baker EN, Dodson EJ. 1980. Crystallographic refinement of the structure of actinidin at 1.7 Å resolution by fast Fourier least-squares methods. Acta Crystallogr. A36:559-72
    • (1980) Acta Crystallogr. , vol.A36 , pp. 559-572
    • Baker, E.N.1    Dodson, E.J.2
  • 2
    • 0029740267 scopus 로고    scopus 로고
    • Structural requirements for cathepsin B and cathepsin H inhibition by kininogens
    • 2. Bano B, Kunapuli SP, Bradford HN, Colman RW. 1996. Structural requirements for cathepsin B and cathepsin H inhibition by kininogens. J. Protein Chem. 15:519-25
    • (1996) J. Protein Chem. , vol.15 , pp. 519-525
    • Bano, B.1    Kunapuli, S.P.2    Bradford, H.N.3    Colman, R.W.4
  • 3
  • 7
    • 0025944975 scopus 로고
    • S-S bridges of cathepsin B and H from bovine spleen: A basis for cathepsin B model building and possible functional implications for discrimination between exo-and endopeptidase activities among cathepsins B, H, and L
    • 7. Baudys M, Meloun B, Gan-Erdene T, Fusek M, Mares M, et al. 1991. S-S bridges of cathepsin B and H from bovine spleen: a basis for cathepsin B model building and possible functional implications for discrimination between exo-and endopeptidase activities among cathepsins B, H, and L. Biomed. Biochim. Acta 50:569-637
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 569-637
    • Baudys, M.1    Meloun, B.2    Gan-Erdene, T.3    Fusek, M.4    Mares, M.5
  • 9
  • 10
    • 0028923541 scopus 로고
    • Alignment/ phylogeny of the papain superfamily of cysteine proteases
    • 10. Berti PJ, Storer AC. 1995. Alignment/ phylogeny of the papain superfamily of cysteine proteases. J. Mol. Biol. 246:273-83
    • (1995) J. Mol. Biol. , vol.246 , pp. 273-283
    • Berti, P.J.1    Storer, A.C.2
  • 11
    • 0028171897 scopus 로고
    • Engineering the S2 subsite specificity of human cathepsin S to a cathepsin L-and cathepsin B-like specificity
    • 11. Brömme D, Bonneau PR, Lachance P, Storer AC. 1994. Engineering the S2 subsite specificity of human cathepsin S to a cathepsin L-and cathepsin B-like specificity. J. Biol. Chem. 269:30238-42
    • (1994) J. Biol. Chem. , vol.269 , pp. 30238-30242
    • Brömme, D.1    Bonneau, P.R.2    Lachance, P.3    Storer, A.C.4
  • 13
    • 0029911570 scopus 로고    scopus 로고
    • 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
    • 13. Brömme D, Klaus JL, Okamoto K, Rasnick D, Palmer JT. 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. 315:85-89
    • (1996) Biochem. J. , vol.315 , pp. 85-89
    • Brömme, D.1    Klaus, J.L.2    Okamoto, K.3    Rasnick, D.4    Palmer, J.T.5
  • 14
    • 0029996205 scopus 로고    scopus 로고
    • High level expression and crystallization of recombinant human cathepsin S
    • 14. Brömme D, McGrath ME. 1996. High level expression and crystallization of recombinant human cathepsin S. Protein Sci. 5:789-91
    • (1996) Protein Sci. , vol.5 , pp. 789-791
    • Brömme, D.1    McGrath, M.E.2
  • 15
    • 0029310512 scopus 로고
    • Human cathepsin O2: A novel cysteine protease highly expressed in osteoclastoma and ovary
    • 15. Brömme D, Okamoto K. 1995. Human cathepsin O2: a novel cysteine protease highly expressed in osteoclastoma and ovary. Biol. Chem. Hoppe-Seyler 376: 379-84
    • (1995) Biol. Chem. Hoppe-seyler , vol.376 , pp. 379-384
    • Brömme, D.1    Okamoto, K.2
  • 16
    • 0030026637 scopus 로고    scopus 로고
    • Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts
    • 16. Brömme D, Okamoto K, Wang BB, Biroc S. 1996. Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. J. Biol. Chem. 271:2126-32
    • (1996) J. Biol. Chem. , vol.271 , pp. 2126-2132
    • Brömme, D.1    Okamoto, K.2    Wang, B.B.3    Biroc, S.4
  • 18
    • 0030864522 scopus 로고    scopus 로고
    • Crystallographic Refinement by Simulated Annealing: Methods and Applications
    • 18. Brünger AT, Rice LM. 1997. Crystallographic Refinement by Simulated Annealing: Methods and Applications. Methods Enzymol. 277:243-69
    • (1997) Methods Enzymol. , vol.277 , pp. 243-269
    • Brünger, A.T.1    Rice, L.M.2
  • 19
    • 0031440450 scopus 로고    scopus 로고
    • Affinity isolation and characterization of the cathepsin B-like proteinase Sj31 from Schistosoma japonicum
    • 19. Caffrey CR, Ruppel A. 1997. Affinity isolation and characterization of the cathepsin B-like proteinase Sj31 from Schistosoma japonicum. J. Parasitol. 83:1112-18
    • (1997) J. Parasitol. , vol.83 , pp. 1112-1118
    • Caffrey, C.R.1    Ruppel, A.2
  • 20
    • 0030038759 scopus 로고    scopus 로고
    • Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases
    • 20. Carmona E, Dufour E, Plouffe C, Takebe S, Mason P, et al. 1996. Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases. Biochemistry 35:8149-57
    • (1996) Biochemistry , vol.35 , pp. 8149-8157
    • Carmona, E.1    Dufour, E.2    Plouffe, C.3    Takebe, S.4    Mason, P.5
  • 21
    • 0030577020 scopus 로고    scopus 로고
    • Delineating functionally important regions and residues in the cathepsin B propeptide for inhibitory activity
    • 21. Chen Y, Plouffe C, Menard R, Storer AC. 1996. Delineating functionally important regions and residues in the cathepsin B propeptide for inhibitory activity. FEBS Lett. 393:24-26
    • (1996) FEBS Lett. , vol.393 , pp. 24-26
    • Chen, Y.1    Plouffe, C.2    Menard, R.3    Storer, A.C.4
  • 22
    • 0029902382 scopus 로고    scopus 로고
    • Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
    • 22. Coulombe R, Grochulski P, Sivaraman J, Menard R, Mort J, et al. 1996. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J. 15:5492-503
    • (1996) EMBO J. , vol.15 , pp. 5492-5503
    • Coulombe, R.1    Grochulski, P.2    Sivaraman, J.3    Menard, R.4    Mort, J.5
  • 23
    • 0030584678 scopus 로고    scopus 로고
    • Structure of rat procathepsin B: Model for inhibition of cysteine protease activity by the proregion
    • 23. Cygler M, Sivaraman J, Grochulski P, Coulomb R, Storer AC, et al. 1996. Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion. Structure 4:405-16
    • (1996) Structure , vol.4 , pp. 405-416
    • Cygler, M.1    Sivaraman, J.2    Grochulski, P.3    Coulomb, R.4    Storer, A.C.5
  • 24
    • 0030891637 scopus 로고    scopus 로고
    • Characterization of the substrate specificity of the major cysteine protease (cruzipain) from Trypanosoma cruzi using a portion-mixing combinatorial library and fluorogenic peptides
    • 24. Del Nery E, Juliano MA, Meldal M, Svendsen I, Scharfstein J, et al. 1997. Characterization of the substrate specificity of the major cysteine protease (cruzipain) from Trypanosoma cruzi using a portion-mixing combinatorial library and fluorogenic peptides. Biochem. J. 323:427-33
    • (1997) Biochem. J. , vol.323 , pp. 427-433
    • Del Nery, E.1    Juliano, M.A.2    Meldal, M.3    Svendsen, I.4    Scharfstein, J.5
  • 25
    • 0029163155 scopus 로고
    • Oligomeric structure and substrate induced inhibition of human cathepsin C
    • 25. Dolenc I, Turk B, Pungercic G, Ritonja A, Turk V. 1995. Oligomeric structure and substrate induced inhibition of human cathepsin C. J. Biol. Chem. 270:21626-31
    • (1995) J. Biol. Chem. , vol.270 , pp. 21626-21631
    • Dolenc, I.1    Turk, B.2    Pungercic, G.3    Ritonja, A.4    Turk, V.5
  • 26
    • 15844422855 scopus 로고    scopus 로고
    • Cathepsin K, but not cathpsins B, L, or S, is abundantly expressed in human osteoclasts
    • 26. Drake FH, Dodds RA, James IE, Connor JR, Debouck C, et al. 1996. Cathepsin K, but not cathpsins B, L, or S, is abundantly expressed in human osteoclasts. J. Biol. Chem. 271:12511-16
    • (1996) J. Biol. Chem. , vol.271 , pp. 12511-12516
    • Drake, F.H.1    Dodds, R.A.2    James, I.E.3    Connor, J.R.4    Debouck, C.5
  • 28
    • 0017138215 scopus 로고
    • Binding of chloromethyl ketone substrate analogues to crystalline papain
    • 28. Drenth J, Kalk KH, Swen HM. 1976. Binding of chloromethyl ketone substrate analogues to crystalline papain. Biochemistry 15:3731-18
    • (1976) Biochemistry , vol.15 , pp. 3731-3818
    • Drenth, J.1    Kalk, K.H.2    Swen, H.M.3
  • 29
    • 0028055132 scopus 로고
    • Cysteine proteinase inhibitors decrease articular cartilage and bone destruction in chronic inflammatory arthritis
    • 29. Esser RE, Angelo RA, Murphey MD, Watts LM, Thornburg LP, et al. 1994. Cysteine proteinase inhibitors decrease articular cartilage and bone destruction in chronic inflammatory arthritis. Arthritis Rheum. 37:236-47
    • (1994) Arthritis Rheum. , vol.37 , pp. 236-247
    • Esser, R.E.1    Angelo, R.A.2    Murphey, M.D.3    Watts, L.M.4    Thornburg, L.P.5
  • 30
    • 0029800840 scopus 로고    scopus 로고
    • The binding mode of an E-64 analog to the active site of cathepsin B
    • 30. Feng M-H, Chan SL, Xiang YF, Huber CP, Lim C. 1996. The binding mode of an E-64 analog to the active site of cathepsin B. Protein Eng. 9:977-86
    • (1996) Protein Eng. , vol.9 , pp. 977-986
    • Feng, M.-H.1    Chan, S.L.2    Xiang, Y.F.3    Huber, C.P.4    Lim, C.5
  • 31
    • 0031582237 scopus 로고    scopus 로고
    • The crystal structure of human cathepsin L complexed with E-64
    • 31. Fujishima A, Imai Y, Nomura T, Fujisawa Y, Yamamoto Y, et al. 1997. The crystal structure of human cathepsin L complexed with E-64. FEBS Lett. 407:47-50
    • (1997) FEBS Lett. , vol.407 , pp. 47-50
    • Fujishima, A.1    Imai, Y.2    Nomura, T.3    Fujisawa, Y.4    Yamamoto, Y.5
  • 32
    • 0029314871 scopus 로고
    • Linkage of pycnodysostosis to chromosome Iq21 by homozygosity mapping
    • 32. Gelb BD, Edelson JG, Desnick RJ. 1995. Linkage of pycnodysostosis to chromosome Iq21 by homozygosity mapping. Nat. Genet. 10:235-57
    • (1995) Nat. Genet. , vol.10 , pp. 235-257
    • Gelb, B.D.1    Edelson, J.G.2    Desnick, R.J.3
  • 33
    • 0029809357 scopus 로고    scopus 로고
    • Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency
    • 33. Gelb BD, Shi G-P, Chapman HA, Desnick RJ. 1996. Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency. Science 273:1236-68
    • (1996) Science , vol.273 , pp. 1236-1268
    • Gelb, B.D.1    Shi, G.-P.2    Chapman, H.A.3    Desnick, R.J.4
  • 34
    • 0030841381 scopus 로고    scopus 로고
    • Structural determinants of specificity in the cysteine protease cruzain
    • 34. Gillmor SA, Craik C, Fletterick RJ. 1997. Structural determinants of specificity in the cysteine protease cruzain. Protein Sci. 6:1603-11
    • (1997) Protein Sci. , vol.6 , pp. 1603-1611
    • Gillmor, S.A.1    Craik, C.2    Fletterick, R.J.3
  • 35
    • 0021346826 scopus 로고
    • Cystatin-like cysteine proteinase inhibitors from human liver
    • 35. Green GD, Kembhavi AA, Davies ME, Karrett AJ. 1984. Cystatin-like cysteine proteinase inhibitors from human liver. Biochem. J. 218:939-46
    • (1984) Biochem. J. , vol.218 , pp. 939-946
    • Green, G.D.1    Kembhavi, A.A.2    Davies, M.E.3    Karrett, A.J.4
  • 36
    • 0030587773 scopus 로고    scopus 로고
    • The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft
    • 36. Groves MR, Taylor MA, Scott M, Cummings NJ, Pickersgill RW, et al. 1996. The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft. Structure 4:1193-203
    • (1996) Structure , vol.4 , pp. 1193-1203
    • Groves, M.R.1    Taylor, M.A.2    Scott, M.3    Cummings, N.J.4    Pickersgill, R.W.5
  • 37
    • 0032518496 scopus 로고    scopus 로고
    • Crystal structure of porcine cathepsin H determined at 2.1 Å resolution: Location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopcptidasc function
    • 37. Guncar G, Podobnik M, Pungercar J, Strukelj B, Turk V, et al. 1998. Crystal structure of porcine cathepsin H determined at 2.1 Å resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopcptidasc function. Structure 6:51-61
    • (1998) Structure , vol.6 , pp. 51-61
    • Guncar, G.1    Podobnik, M.2    Pungercar, J.3    Strukelj, B.4    Turk, V.5
  • 38
    • 0027398184 scopus 로고
    • Peptide-fluoromethyl ketones arrest intracellular replication and intercellular transmission of T. Cruzi
    • 38. Hart G, Andrews N, Mills AA, Engel J, Smith R, et al. 1993. Peptide-fluoromethyl ketones arrest intracellular replication and intercellular transmission of T. cruzi. Mol. Biochem. Parasitol. 58:17-24
    • (1993) Mol. Biochem. Parasitol. , vol.58 , pp. 17-24
    • Hart, G.1    Andrews, N.2    Mills, A.A.3    Engel, J.4    Smith, R.5
  • 39
    • 0020484334 scopus 로고
    • Crystal and molecular structure of the sulfhydryl protease calotropin at 3.2 Å resolution
    • 39. Heinemann U, Pal GP, Hilgenfeld R, Saenger W. 1982. Crystal and molecular structure of the sulfhydryl protease calotropin at 3.2 Å resolution. J. Mol. Biol. 161:591-606
    • (1982) J. Mol. Biol. , vol.161 , pp. 591-606
    • Heinemann, U.1    Pal, G.P.2    Hilgenfeld, R.3    Saenger, W.4
  • 40
    • 0017221441 scopus 로고
    • Crystalline leucine aminopeptidase from lens (alpha-aminoacyl-peptide hydrolase; EC 3.4.11.1)
    • 40. Henson H, Frohne M. 1976. Crystalline leucine aminopeptidase from lens (alpha-aminoacyl-peptide hydrolase; EC 3.4.11.1). Methods Enzymol. 45:504-20
    • (1976) Methods Enzymol. , vol.45 , pp. 504-520
    • Henson, H.1    Frohne, M.2
  • 42
    • 0028968184 scopus 로고
    • Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex
    • 42. Jia Z, Hasnain S, Hirama T, Lee X, Mort JS, et al. 1995. Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. J. Biol. Chem. 270:5527-33
    • (1995) J. Biol. Chem. , vol.270 , pp. 5527-5533
    • Jia, Z.1    Hasnain, S.2    Hirama, T.3    Lee, X.4    Mort, J.S.5
  • 43
    • 0027509798 scopus 로고
    • Participation of cathepsin L in bone resorption
    • 43. Kakegawa H. 1993. Participation of cathepsin L in bone resorption. FEBS Lett. 321:247-50
    • (1993) FEBS Lett. , vol.321 , pp. 247-250
    • Kakegawa, H.1
  • 47
    • 0000420069 scopus 로고
    • Catalysis of amide hydrolysis and formation under neutral conditions by a zwitterionic imidazolium thiolate
    • 47. Keillor JW, Niverov AA, Brown RS. 1994. Catalysis of amide hydrolysis and formation under neutral conditions by a zwitterionic imidazolium thiolate. J. Am. Chem. Soc. 116:4669-73
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4669-4673
    • Keillor, J.W.1    Niverov, A.A.2    Brown, R.S.3
  • 48
    • 0031438087 scopus 로고    scopus 로고
    • Ultrastructural localization of cathepsin B in gingival tissue from chronic periodontitis patients
    • 48. Kennett CN, Cox SW, Eley BM. 1997. Ultrastructural localization of cathepsin B in gingival tissue from chronic periodontitis patients. Histochem. J. 29:727-34
    • (1997) Histochem. J. , vol.29 , pp. 727-734
    • Kennett, C.N.1    Cox, S.W.2    Eley, B.M.3
  • 49
    • 0022970858 scopus 로고
    • Cathepsin S: The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin L
    • 49. Kirschke H, Schmidt I, Wiederanders B. 1986. Cathepsin S: The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin L. Biochem. J. 240:455-59
    • (1986) Biochem. J. , vol.240 , pp. 455-459
    • Kirschke, H.1    Schmidt, I.2    Wiederanders, B.3
  • 50
    • 0024814219 scopus 로고
    • Cathepsin S from bovine spleen: Purification, distribution, intracellular localization, and action on proteins
    • 50. Kirschke H, Wiederanders B, Brömme D, Rinne A. 1989. Cathepsin S from bovine spleen: purification, distribution, intracellular localization, and action on proteins. Biochem. J. 246:467-73
    • (1989) Biochem. J. , vol.246 , pp. 467-473
    • Kirschke, H.1    Wiederanders, B.2    Brömme, D.3    Rinne, A.4
  • 51
    • 0028886558 scopus 로고
    • Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family
    • 51. Kortemme T, Creighton TE. 1995. Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family. J. Mol. Biol. 253:799-812
    • (1995) J. Mol. Biol. , vol.253 , pp. 799-812
    • Kortemme, T.1    Creighton, T.E.2
  • 52
    • 0031450624 scopus 로고    scopus 로고
    • Cathepsin, a major protease of the marine sponge Geodia cydonium: Purification of the enzyme and molecular cloning of cDNA
    • 52. Krasko A, Gamulin V, Seack J, Steffen R, Schroder HC, et al. 1997. Cathepsin, a major protease of the marine sponge Geodia cydonium: purification of the enzyme and molecular cloning of cDNA. Mol. Mar. Biol. Biotechnol. 6:296-307
    • (1997) Mol. Mar. Biol. Biotechnol. , vol.6 , pp. 296-307
    • Krasko, A.1    Gamulin, V.2    Seack, J.3    Steffen, R.4    Schroder, H.C.5
  • 53
    • 0026244229 scopus 로고
    • Molscript-A program to produce both detailed and specific plots of protein structures
    • 53. Kraulis P. 1991. Molscript-A program to produce both detailed and specific plots of protein structures. J. Appl. Crystallog. 24:946-50
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 54
    • 0021715928 scopus 로고
    • Cathepsins J and K: High molecular weight cysteine proteinases from human tissues
    • 54. Liao JC, Lenney JF. 1984. Cathepsins J and K: high molecular weight cysteine proteinases from human tissues. Biochem. Biophys. Res. Commun. 124:909-16
    • (1984) Biochem. Biophys. Res. Commun. , vol.124 , pp. 909-916
    • Liao, J.C.1    Lenney, J.F.2
  • 55
    • 15144356711 scopus 로고    scopus 로고
    • The osteoclast-associated protease cathepsin K is expressed in human breast carcinoma
    • 55. Littlewood-Evans AJ, Bilbe G, Bowler WB, Farley D, Wlodarski B, et al. 1997. The osteoclast-associated protease cathepsin K is expressed in human breast carcinoma. Cancer Res. 57:5386-90
    • (1997) Cancer Res. , vol.57 , pp. 5386-5390
    • Littlewood-Evans, A.J.1    Bilbe, G.2    Bowler, W.B.3    Farley, D.4    Wlodarski, B.5
  • 58
    • 0028988335 scopus 로고
    • The crystal structure of cruzain: A therapeutic target for Chagas' disease
    • 58. McGrath ME, Eakin AE, Engel J, McKerrow JH, Craik CS, et al. 1995. The crystal structure of cruzain: a therapeutic target for Chagas' disease. J. Mol. Biol. 247:251-59
    • (1995) J. Mol. Biol. , vol.247 , pp. 251-259
    • McGrath, M.E.1    Eakin, A.E.2    Engel, J.3    McKerrow, J.H.4    Craik, C.S.5
  • 59
    • 0031030808 scopus 로고    scopus 로고
    • Crystal structure of human cathepsin K completed with a potent inhibitor
    • 59. McGrath ME, Klaus JL, Barnes MG, Bromme D. 1997. Crystal structure of human cathepsin K completed with a potent inhibitor. Nat. Struct. Biol. 4:105-9
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 105-109
    • McGrath, M.E.1    Klaus, J.L.2    Barnes, M.G.3    Bromme, D.4
  • 61
    • 0026606269 scopus 로고
    • Inhibitors of the major cysteinyl proteinase (GP57/51) impair host cell invasion and arrest the intracellular development of Trypanosoma cruzi in vitro
    • 61. Meirelles MNL, Juliano L, Carmona E, Silva SG, Costa EM, et al. 1992. Inhibitors of the major cysteinyl proteinase (GP57/51) impair host cell invasion and arrest the intracellular development of Trypanosoma cruzi in vitro. Mol. Biochem. Parasitol. 52:175-84
    • (1992) Mol. Biochem. Parasitol. , vol.52 , pp. 175-184
    • Meirelles, M.N.L.1    Juliano, L.2    Carmona, E.3    Silva, S.G.4    Costa, E.M.5
  • 62
    • 0027499868 scopus 로고
    • The ionization characteristics of the Cys-25-His-159 interactive system and of the modulatory group of papain. Resolution of ambiguity by electronic perturbation of the quasi 2-mercaptopyridine leaving group in a new pyrimidyl disulphide reactivity probe
    • 62. Mellor GW, Thomas HW, Topham CM, Brocklehurst K. 1993. The ionization characteristics of the Cys-25-His-159 interactive system and of the modulatory group of papain. Resolution of ambiguity by electronic perturbation of the quasi 2-mercaptopyridine leaving group in a new pyrimidyl disulphide reactivity probe. Biochem. J. 290:289-96
    • (1993) Biochem. J. , vol.290 , pp. 289-296
    • Mellor, G.W.1    Thomas, H.W.2    Topham, C.M.3    Brocklehurst, K.4
  • 63
    • 0026003243 scopus 로고
    • Contribution of the glutamine 19 side chain to transition-state stabilization in the oxyanion hole of papain
    • 63. Menard R, Carriere J, LaFlamme P, Plouffe C, Khouri H, et al. 1991. Contribution of the glutamine 19 side chain to transition-state stabilization in the oxyanion hole of papain. Biochemistry 30:8924-28
    • (1991) Biochemistry , vol.30 , pp. 8924-8928
    • Menard, R.1    Carriere, J.2    LaFlamme, P.3    Plouffe, C.4    Khouri, H.5
  • 64
    • 0025813346 scopus 로고
    • Importance of hydrogen-bonding interactions involving the side chain of Asp 158 in the catalytic mechanism of papain
    • 64. Menard R, Khouri H, Plouffe C, Laflamme P, Dupras R, et al. 1991. Importance of hydrogen-bonding interactions involving the side chain of Asp 158 in the catalytic mechanism of papain. Biochemistry 30:5531-18
    • (1991) Biochemistry , vol.30 , pp. 5531-5618
    • Menard, R.1    Khouri, H.2    Plouffe, C.3    Laflamme, P.4    Dupras, R.5
  • 65
    • 0025376135 scopus 로고
    • A protein engineering study of the role of aspartate 158 in the catalytic mechanism of papain
    • 65. Ménard R, Khouri HE, Plouffe C, Dupras R, Ripoll D, et al. 1990. A protein engineering study of the role of aspartate 158 in the catalytic mechanism of papain. Biochemistry 29:6706-13
    • (1990) Biochemistry , vol.29 , pp. 6706-6713
    • Ménard, R.1    Khouri, H.E.2    Plouffe, C.3    Dupras, R.4    Ripoll, D.5
  • 66
    • 12044253640 scopus 로고
    • The refined 2.15 Å X-ray crystal structure of human liver cathepsin B: The structural basis for its specificity
    • 66. Musil D, Zucic D, Turk D, Engh RA, Mayr I, et al. 1991. The refined 2.15 Å X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. EMBO J. 10:2321-30
    • (1991) EMBO J. , vol.10 , pp. 2321-2330
    • Musil, D.1    Zucic, D.2    Turk, D.3    Engh, R.A.4    Mayr, I.5
  • 67
    • 0040084898 scopus 로고    scopus 로고
    • Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts
    • 67. Nagler DK, Storer AC, Portara FCV, Carmona E, Juliano L, et al. 1997. Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts. Biochemistry 36:12608-15
    • (1997) Biochemistry , vol.36 , pp. 12608-12615
    • Nagler, D.K.1    Storer, A.C.2    Portara, F.C.V.3    Carmona, E.4    Juliano, L.5
  • 68
    • 0032540474 scopus 로고    scopus 로고
    • Cathepsin L: Critical role in Ii degradation and CD4 T cell selection in the thymus
    • 68. Nakagawa T, Roth W, Wong P, Nelson A, Farr A, et al. 1998. Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus. Science 280:450-53
    • (1998) Science , vol.280 , pp. 450-453
    • Nakagawa, T.1    Roth, W.2    Wong, P.3    Nelson, A.4    Farr, A.5
  • 69
    • 0028360184 scopus 로고
    • Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo
    • 69. Nelson JW, Creighton TE. 1994. Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry 33:5974-83
    • (1994) Biochemistry , vol.33 , pp. 5974-5983
    • Nelson, J.W.1    Creighton, T.E.2
  • 70
    • 0028799348 scopus 로고
    • Crystal structure of glycyl endopeptidase from carica papaya: A cysteine endopeptidase of unusual substrate specificity
    • 70. O'Hara BP, Hemmings AM, Buttle DJ, Pearl LH. 1995. Crystal structure of glycyl endopeptidase from carica papaya: a cysteine endopeptidase of unusual substrate specificity. Biochemistry 34:13190-95
    • (1995) Biochemistry , vol.34 , pp. 13190-13195
    • O'Hara, B.P.1    Hemmings, A.M.2    Buttle, D.J.3    Pearl, L.H.4
  • 71
    • 0343433408 scopus 로고    scopus 로고
    • Cysteine protease and their inhibitors
    • 71. Otto H-H, Schirmeister T. 1997. Cysteine protease and their inhibitors. Chem. Rev. 97:133-71
    • (1997) Chem. Rev. , vol.97 , pp. 133-171
    • Otto, H.-H.1    Schirmeister, T.2
  • 72
    • 0029099619 scopus 로고
    • Vinyl sulfones as mechanism-based cysteine protease inhibitors
    • 72. Palmer JT, Rasnick D, Klaus JL. 1995. Vinyl sulfones as mechanism-based cysteine protease inhibitors. J. Med. Chem. 38:3193-96
    • (1995) J. Med. Chem. , vol.38 , pp. 3193-3196
    • Palmer, J.T.1    Rasnick, D.2    Klaus, J.L.3
  • 73
    • 0028206592 scopus 로고
    • Differential distribution of messenger RNAs for cathepsins B, L, and S in adult rat brain: An in situ hybridization study
    • 73. Petanceska S, Burke S, Watson SJ, Devi L. 1994. Differential distribution of messenger RNAs for cathepsins B, L, and S in adult rat brain: an in situ hybridization study. Neuroscience 59:729-38
    • (1994) Neuroscience , vol.59 , pp. 729-738
    • Petanceska, S.1    Burke, S.2    Watson, S.J.3    Devi, L.4
  • 76
    • 18544398901 scopus 로고    scopus 로고
    • A classical enzyme active center motif lacks catalytic competence until modulated electrostatically
    • 76. Pinitglang S, Watts AB, Patel M, Reid JD, Noble MA, et al. 1997. A classical enzyme active center motif lacks catalytic competence until modulated electrostatically. Biochemistry 36:9968-82
    • (1997) Biochemistry , vol.36 , pp. 9968-9982
    • Pinitglang, S.1    Watts, A.B.2    Patel, M.3    Reid, J.D.4    Noble, M.A.5
  • 77
    • 0029929393 scopus 로고    scopus 로고
    • -/(His)-Im+H ion pair in one type of serine proteinase architecture by kinetic and computational studies on chemically mutated subtilisin variants
    • -/(His)-Im+H ion pair in one type of serine proteinase architecture by kinetic and computational studies on chemically mutated subtilisin variants. J. Mol. Biol. 257:1088-111
    • (1996) J. Mol. Biol. , vol.257 , pp. 1088-1111
    • Plou, F.J.1    Kowlessur, D.2    Malthouse, J.P.G.3    Mellor, G.W.4    Hartshorn, M.J.5
  • 78
    • 0031554904 scopus 로고    scopus 로고
    • Crystal structure of the wild-type human procathepsin B at 2.5 Å resolution reveals the native active site of a papain-like cysteine protease zymogen
    • 78. Podobnik M, Kuhelj R, Turk V, Turk D. 1997. Crystal structure of the wild-type human procathepsin B at 2.5 Å resolution reveals the native active site of a papain-like cysteine protease zymogen. J. Mol. Biol. 271:774-88
    • (1997) J. Mol. Biol. , vol.271 , pp. 774-788
    • Podobnik, M.1    Kuhelj, R.2    Turk, V.3    Turk, D.4
  • 79
    • 0016115206 scopus 로고
    • Mercaptide-imidazolium ion-pair: The reactive nucleophile in papain catalysis
    • 79. Polgar L. 1974. Mercaptide-imidazolium ion-pair: the reactive nucleophile in papain catalysis. FEBS Lett. 47:15-18
    • (1974) FEBS Lett. , vol.47 , pp. 15-18
    • Polgar, L.1
  • 81
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class H-associated invariant chain processing and peptide loading
    • 81. Riese RJ, Wolf PR, Bromme D, Natkin LR, Villadangos JA, et al. 1996. Essential role for cathepsin S in MHC class H-associated invariant chain processing and peptide loading. Immunity 4:357-66
    • (1996) Immunity , vol.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.R.2    Bromme, D.3    Natkin, L.R.4    Villadangos, J.A.5
  • 82
    • 0028948564 scopus 로고
    • Plasmodium falciparum: Effects of proteinase inhibitors on globin hydrolysis by cultured malaria parasites
    • 82. Rosenthal PJ. 1995. Plasmodium falciparum: effects of proteinase inhibitors on globin hydrolysis by cultured malaria parasites. Exp. Parasitol. 80:272-81
    • (1995) Exp. Parasitol. , vol.80 , pp. 272-281
    • Rosenthal, P.J.1
  • 83
    • 0024961758 scopus 로고
    • The active site of papain: Allatom study of interactions with protein matrix and solvent
    • 83. Rullmann JAC, Bellido MN, van Duijnen PT. 1989. The active site of papain: allatom study of interactions with protein matrix and solvent. J. Mol. Biol. 206:101-18
    • (1989) J. Mol. Biol. , vol.206 , pp. 101-118
    • Rullmann, J.A.C.1    Bellido, M.N.2    Van Duijnen, P.T.3
  • 84
    • 0032522413 scopus 로고    scopus 로고
    • Cathepsin L2, a novel cysteine proteinase produced by breast and colorectal carcinomas
    • 84. Santamaria I, Velasco G, Cazorla M, Fueyo A, Campo E, et al. 1998. Cathepsin L2, a novel cysteine proteinase produced by breast and colorectal carcinomas. Cancer Res. 58:1624-30
    • (1998) Cancer Res. , vol.58 , pp. 1624-1630
    • Santamaria, I.1    Velasco, G.2    Cazorla, M.3    Fueyo, A.4    Campo, E.5
  • 85
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • 85. Schechter I, Berger A. 1967. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27:157-62
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 86
    • 0032515939 scopus 로고    scopus 로고
    • Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: A kinetic analysis
    • 86. Schick C, Bemberton PA, Shi GP, Kamachi Y, Cataltepe S, et al. 1998. Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: a kinetic analysis. Biochemistry 37:5258-66
    • (1998) Biochemistry , vol.37 , pp. 5258-5266
    • Schick, C.1    Bemberton, P.A.2    Shi, G.P.3    Kamachi, Y.4    Cataltepe, S.5
  • 88
    • 0024544349 scopus 로고
    • Intracellular hydrolases of Aspergillus parasiticus and Aspergillus flavus
    • 88. Sharma A, Padwal-Desai S, Ninjoor V. 1989. Intracellular hydrolases of Aspergillus parasiticus and Aspergillus flavus. Biochem. Biophys. Res. Commun. 159:464-71
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 464-471
    • Sharma, A.1    Padwal-Desai, S.2    Ninjoor, V.3
  • 89
    • 0032472272 scopus 로고    scopus 로고
    • Substrate/ propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors
    • 89. Shaschke N, Assfalg-Machleidt I, Machleidt W, Moroder L. 1998. Substrate/ propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS Lett. 421:80-82
    • (1998) FEBS Lett. , vol.421 , pp. 80-82
    • Shaschke, N.1    Assfalg-Machleidt, I.2    Machleidt, W.3    Moroder, L.4
  • 91
    • 0025301658 scopus 로고
    • The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction
    • 91. Stubbs MT, Laber B, Bode W, Huber R, Jerala R, et al. 1990. The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. EMBO J. 9:1939-47
    • (1990) EMBO J. , vol.9 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5
  • 92
    • 0019757154 scopus 로고
    • Cathepsin D from porcine and bovine spleen
    • 92. Takahashi T, Tang J. 1981. Cathepsin D from porcine and bovine spleen. Methods Enzymol. 80:565-81
    • (1981) Methods Enzymol. , vol.80 , pp. 565-581
    • Takahashi, T.1    Tang, J.2
  • 93
    • 0028123480 scopus 로고
    • Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts
    • 93. Tezuka K, Tezuka Y, Maejima A, Sato T, Nemoto K, et al. 1994. Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts. J. Biol. Chem. 269:1106-9
    • (1994) J. Biol. Chem. , vol.269 , pp. 1106-1109
    • Tezuka, K.1    Tezuka, Y.2    Maejima, A.3    Sato, T.4    Nemoto, K.5
  • 95
    • 0025867012 scopus 로고
    • Characterization of a cathepsin H-like enzyme from a human melanoma cell line
    • 95. Tsushima H, Ueki A, Matsuoka Y, Mihara H, Hopsu-Havu VK. 1991. Characterization of a cathepsin H-like enzyme from a human melanoma cell line. Int. J. Cancer 48:726-32
    • (1991) Int. J. Cancer , vol.48 , pp. 726-732
    • Tsushima, H.1    Ueki, A.2    Matsuoka, Y.3    Mihara, H.4    Hopsu-Havu, V.K.5
  • 96
    • 0029115002 scopus 로고
    • High-affinity binding to two molecules of cysteine proteinases to low-molecular-weight kininogen
    • 96. Turk B, Stoka V, Bjork I, Boudier C, Johansson G, et al. 1995. High-affinity binding to two molecules of cysteine proteinases to low-molecular-weight kininogen. Protein Sci. 4:1874-80
    • (1995) Protein Sci. , vol.4 , pp. 1874-1880
    • Turk, B.1    Stoka, V.2    Bjork, I.3    Boudier, C.4    Johansson, G.5
  • 97
    • 0345310073 scopus 로고    scopus 로고
    • Revised definition of substrate binding sites of papain-like cysteine proteases
    • 97. Turk D, Guncar G, Podobnik. M, Turk B. 1998. Revised definition of substrate binding sites of papain-like cysteine proteases. Biol. Chem. 379:137-47
    • (1998) Biol. Chem. , vol.379 , pp. 137-147
    • Turk, D.1    Guncar, G.2    Podobnik, M.3    Turk, B.4
  • 98
    • 0029976244 scopus 로고    scopus 로고
    • Crystal structures of human procathepsin B at 3.2 and 3.3 Å resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide
    • 98. Turk D, Podobnik M, Kuhelj R, Dolinar M, Turk V. 1996. Crystal structures of human procathepsin B at 3.2 and 3.3 Å resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide. FEBS Lett. 384:211-14
    • (1996) FEBS Lett. , vol.384 , pp. 211-214
    • Turk, D.1    Podobnik, M.2    Kuhelj, R.3    Dolinar, M.4    Turk, V.5
  • 99
    • 0028908350 scopus 로고
    • Crystal structure of cathepsin B inhibited with CA030 at 2.1 Å resolution: A basis for the design of specific epoxysuccinyl inhibitors
    • 99. Turk D, Podobnik M, Popovic T, Katunuma N, Bode W, et al. 1995. Crystal structure of cathepsin B inhibited with CA030 at 2.1 Å resolution: a basis for the design of specific epoxysuccinyl inhibitors. Biochemistry 34:4791-97
    • (1995) Biochemistry , vol.34 , pp. 4791-4797
    • Turk, D.1    Podobnik, M.2    Popovic, T.3    Katunuma, N.4    Bode, W.5
  • 100
    • 0016776255 scopus 로고
    • Acid sulfhydryl protease from calf lymph nodes
    • 100. Turnsek T, Kregar I, Lebez D. 1975. Acid sulfhydryl protease from calf lymph nodes. Biochim. Biophys. Acta 403:514-20
    • (1975) Biochim. Biophys. Acta , vol.403 , pp. 514-520
    • Turnsek, T.1    Kregar, I.2    Lebez, D.3
  • 102
    • 0030790341 scopus 로고    scopus 로고
    • Degradation of mouse invariant chain: Roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism
    • 102. Villadangos JA, Riese RJ, Peters C, Chapman HA, Ploegh HL, 1997. Degradation of mouse invariant chain: roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism. J. Exp. Med. 186:549-60
    • (1997) J. Exp. Med. , vol.186 , pp. 549-560
    • Villadangos, J.A.1    Riese, R.J.2    Peters, C.3    Chapman, H.A.4    Ploegh, H.L.5
  • 103
    • 0021764208 scopus 로고
    • Natural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-Dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state reactivity probe (2,2′-dipyridyl disulphide) and with a specific synthetic substrate
    • (N-benzyloxy-carbonyl-L-arginyl-L-arginine-2-naphthylamide)
    • 103. Willenbrock F, Brocklehurst K. 1984. Natural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-Dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state reactivity probe (2,2′-dipyridyl disulphide) and with a specific synthetic substrate (N-benzyloxy-carbonyl-L-arginyl-L-arginine-2-naphthylamide). Biochem. J. 222:805-14
    • (1984) Biochem. J. , vol.222 , pp. 805-814
    • Willenbrock, F.1    Brocklehurst, K.2
  • 105
    • 0024348296 scopus 로고
    • Suppression by cathepsin L inhibitors of the invasion of amnion membranes by murine cancer cells
    • 105. Yagel S, Warner AH, Nellans HN, Lala PK, Waghorne C, et al. 1989. Suppression by cathepsin L inhibitors of the invasion of amnion membranes by murine cancer cells. Cancer Res. 49:3553-57
    • (1989) Cancer Res. , vol.49 , pp. 3553-3557
    • Yagel, S.1    Warner, A.H.2    Nellans, H.N.3    Lala, P.K.4    Waghorne, C.5
  • 106
    • 0030961306 scopus 로고    scopus 로고
    • Binding mode of CA074, a specific irreversible inhibitor, to bovine cathepsin B as determined by X-ray crystal analysis of the complex
    • 106. Yamamoto A, Hara T, Tomoo K, Ishida T, Fujii T, et al. 1997. Binding mode of CA074, a specific irreversible inhibitor, to bovine cathepsin B as determined by X-ray crystal analysis of the complex. J. Biochem. 121:974-47
    • (1997) J. Biochem. , vol.121 , pp. 974-947
    • Yamamoto, A.1    Hara, T.2    Tomoo, K.3    Ishida, T.4    Fujii, T.5
  • 107
    • 0026454259 scopus 로고
    • Crystal structure of papain-succinyl-Gln-Val-Val-Ala-Ala-p-Nitroanilide complex at 1.7 Å: Noncovalent binding mode of a common sequence of endogenous thiol protease inhibitors
    • 107. Yamamoto A, Tomoo K, Doi M, Ohishi H, Inoue M, et al. 1992. Crystal structure of papain-succinyl-Gln-Val-Val-Ala-Ala-p-Nitroanilide complex at 1.7 Å: noncovalent binding mode of a common sequence of endogenous thiol protease inhibitors. Biochemistry 31:11305-9
    • (1992) Biochemistry , vol.31 , pp. 11305-11309
    • Yamamoto, A.1    Tomoo, K.2    Doi, M.3    Ohishi, H.4    Inoue, M.5
  • 108
    • 0026353352 scopus 로고
    • Refined X-ray structure of papain:E64c complex at 2.1 Å resolution
    • 108. Yamamoto D, Matsumoto K, Ohishi H, Tshida T, Inoue M, et al. 1991. Refined X-ray structure of papain:E64c complex at 2.1 Å resolution. J. Biol. Chem. 266:14771-57
    • (1991) J. Biol. Chem. , vol.266 , pp. 14771-14857
    • Yamamoto, D.1    Matsumoto, K.2    Ohishi, H.3    Tshida, T.4    Inoue, M.5
  • 110
    • 0031884265 scopus 로고    scopus 로고
    • Cathepsin B and human tumor progression
    • 110. Yan S, Sameni M, Sloane BF. 1998. Cathepsin B and human tumor progression. Biol. Chem. 379:113-23
    • (1998) Biol. Chem. , vol.379 , pp. 113-123
    • Yan, S.1    Sameni, M.2    Sloane, B.F.3
  • 111
    • 0025788552 scopus 로고
    • Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis
    • 111. Yang Y, Wells WW. 1991. Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis. J. Biol. Chem. 166:12759-65
    • (1991) J. Biol. Chem. , vol.166 , pp. 12759-12765
    • Yang, Y.1    Wells, W.W.2


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