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Volumn 10, Issue 3, 2010, Pages 294-322

Development of nitrile-based peptidic inhibitors of cysteine cathepsins

Author keywords

Cathepsin; Covalent modifier; Cysteine protease; Lysosomotropic property; Osteoporosis; Peptide nitrile; Peptidomimetic; Protease inhibitor; Thioimidate

Indexed keywords

BALICATIB; BORTEZOMIB; CATHEPSIN B; CATHEPSIN B INHIBITOR; CATHEPSIN K; CATHEPSIN K INHIBITOR; CATHEPSIN L; CATHEPSIN S; CLAVULANIC ACID; CLOPIDOGREL; CYANAMIDE; CYCLOSERINE; CYSTEINE PROTEINASE INHIBITOR; DIPEPTIDYL PEPTIDASE I; DIPEPTIDYL PEPTIDASE IV INHIBITOR; NILVADIPINE; NITRILE; ODANACATIB; OMEPRAZOLE; PEPTIDOMIMETIC AGENT; RIVASTIGMINE; TELAPREVIR; TETRAHYDROLIPSTATIN;

EID: 77949483288     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/156802610790725452     Document Type: Review
Times cited : (98)

References (200)
  • 1
    • 0036302814 scopus 로고    scopus 로고
    • Protease degradomics: A new challenge for proteomics
    • López-Otín, C.; Overall, C. M. Protease degradomics: a new challenge for proteomics. Nat. Rev. Mol. Cell Biol., 2002, 3, 509-519.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 509-519
    • López-Otín, C.1    Overall, C.M.2
  • 3
    • 33748297890 scopus 로고    scopus 로고
    • Catalytic mechanisms of cysteine peptidase
    • Barrett, A. J, Rawlings, N. D, Woessner, J. F. Eds, Elsevier, London
    • Polgar, L. Catalytic mechanisms of cysteine peptidase. In: Barrett, A. J.; Rawlings, N. D.; Woessner, J. F. Eds., Handbook of Proteolytic Enzymes, Elsevier, London, 2004, 1072-1079.
    • (2004) Handbook of Proteolytic Enzymes , pp. 1072-1079
    • Polgar, L.1
  • 4
    • 38649111363 scopus 로고    scopus 로고
    • Cysteine cathepsins: Cellular roadmap to different functions
    • Brix, K.; Dunkhorst, A.; Mayer, K.; Jordans, S. Cysteine cathepsins: cellular roadmap to different functions. Biochimie., 2008, 90, 194-207.
    • (2008) Biochimie , vol.90 , pp. 194-207
    • Brix, K.1    Dunkhorst, A.2    Mayer, K.3    Jordans, S.4
  • 5
    • 0030810557 scopus 로고    scopus 로고
    • Mort, J. S.; Buttle, D. J. Cathepsin B. Int. J. Biochem. Cell Biol., 1997, 29, 715-720.
    • Mort, J. S.; Buttle, D. J. Cathepsin B. Int. J. Biochem. Cell Biol., 1997, 29, 715-720.
  • 6
    • 0036929283 scopus 로고    scopus 로고
    • Processing and activation of lysosomal proteinases
    • Ishidoh, K.; Kominami, E. Processing and activation of lysosomal proteinases. Biol. Chem., 2002, 383, 1827-1831.
    • (2002) Biol. Chem , vol.383 , pp. 1827-1831
    • Ishidoh, K.1    Kominami, E.2
  • 7
    • 0023905240 scopus 로고
    • Identification of latent procathepsins B and L in microsomal lumen: Characterization of enzymatic activation and proteolytic processing in vitro
    • Nishimura, Y.; Kawabata, T.; Kato, K. Identification of latent procathepsins B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro. Arch. Biochem. Biophys., 1988, 261, 64-71.
    • (1988) Arch. Biochem. Biophys , vol.261 , pp. 64-71
    • Nishimura, Y.1    Kawabata, T.2    Kato, K.3
  • 8
    • 0024284209 scopus 로고
    • Biosyntheses and processing of lysosomal cysteine proteinases in rat macrophages
    • Kominami, E.; Tsukahara, T.; Hara, K.; Katunuma, N. Biosyntheses and processing of lysosomal cysteine proteinases in rat macrophages. FEBS Lett., 1988, 231, 225-228.
    • (1988) FEBS Lett , vol.231 , pp. 225-228
    • Kominami, E.1    Tsukahara, T.2    Hara, K.3    Katunuma, N.4
  • 9
    • 0242452190 scopus 로고    scopus 로고
    • Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro
    • Ménard, R.; Carmona, E.; Takebe, S.; Dufour, E.; Plouffe, C.; Mason, P.; Mort, J. S. Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro. J. Biol. Chem., 1998, 273, 4478-4484.
    • (1998) J. Biol. Chem , vol.273 , pp. 4478-4484
    • Ménard, R.1    Carmona, E.2    Takebe, S.3    Dufour, E.4    Plouffe, C.5    Mason, P.6    Mort, J.S.7
  • 10
    • 0028237920 scopus 로고
    • Maturation of human procathepsin B. Proenzyme activation and proteolytic processing of the precursor to the mature proteinase, in vitro, are primarily unimolecular processes
    • Mach, L.; Mort, J. S.; Glössl, J. Maturation of human procathepsin B. Proenzyme activation and proteolytic processing of the precursor to the mature proteinase, in vitro, are primarily unimolecular processes. J. Biol. Chem., 1994, 269, 13030-13035.
    • (1994) J. Biol. Chem , vol.269 , pp. 13030-13035
    • Mach, L.1    Mort, J.S.2    Glössl, J.3
  • 11
    • 0027483205 scopus 로고
    • Purification and processing of rat liver procathepsin B
    • Kawabata, T.; Nishimura, Y.; Higaki, M.; Kato, K. Purification and processing of rat liver procathepsin B. J. Biochem., 1993, 113, 389-394.
    • (1993) J. Biochem , vol.113 , pp. 389-394
    • Kawabata, T.1    Nishimura, Y.2    Higaki, M.3    Kato, K.4
  • 12
    • 0035852855 scopus 로고    scopus 로고
    • Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing
    • Dahl, S. W.; Halkier, T.; Lauritzen, C.; Dolenc, I.; Pedersen, J.; Turk, V.; Turk B. Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing. Biochemistry, 2001, 40, 1671-1678.
    • (2001) Biochemistry , vol.40 , pp. 1671-1678
    • Dahl, S.W.1    Halkier, T.2    Lauritzen, C.3    Dolenc, I.4    Pedersen, J.5    Turk, V.6    Turk, B.7
  • 13
    • 85177156133 scopus 로고    scopus 로고
    • Dolenc, I.; Turk, B.; Pungercic, G.; Ritonja, A.; Turk, V. Oligomeric structure and substrate induced inhibition of human cathepsin C. J. Biol. Chem., 1995, 270, 21626-21631.
    • Dolenc, I.; Turk, B.; Pungercic, G.; Ritonja, A.; Turk, V. Oligomeric structure and substrate induced inhibition of human cathepsin C. J. Biol. Chem., 1995, 270, 21626-21631.
  • 17
    • 0035850917 scopus 로고    scopus 로고
    • Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain
    • Olsen, J. G.; Kadziola, A.; Lauritzen, C.; Pedersen, J.; Larsen, S.; Dahl, S. W. Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain. FEBS Lett., 2001, 506, 201-206.
    • (2001) FEBS Lett , vol.506 , pp. 201-206
    • Olsen, J.G.1    Kadziola, A.2    Lauritzen, C.3    Pedersen, J.4    Larsen, S.5    Dahl, S.W.6
  • 18
    • 17944366493 scopus 로고    scopus 로고
    • Structure of human dipeptidyl peptidase I (cathepsin C): Exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases
    • Turk, D.; Janjić, V.; Stern, I.; Podobnik, M.; Lamba, D.; Dahl, S. W.; Lauritzen, C.; Pedersen, J.; Turk, V.; Turk, B. Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases. EMBO J., 2001, 20, 6570-6582.
    • (2001) EMBO J , vol.20 , pp. 6570-6582
    • Turk, D.1    Janjić, V.2    Stern, I.3    Podobnik, M.4    Lamba, D.5    Dahl, S.W.6    Lauritzen, C.7    Pedersen, J.8    Turk, V.9    Turk, B.10
  • 19
    • 0036382928 scopus 로고    scopus 로고
    • The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators
    • Somoza, J. R.; Palmer, J. T.; Ho, J. D. The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators. J. Mol. Biol., 2002, 322, 559-568.
    • (2002) J. Mol. Biol , vol.322 , pp. 559-568
    • Somoza, J.R.1    Palmer, J.T.2    Ho, J.D.3
  • 20
    • 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 aminopeptidase function
    • Gunčar, G.; Podobnik, M.; Pungerčar, J.; Štrukelj, B.; Turk, V.; Turk, D. Crystal structure of porcine cathepsin H determined at 2.1 Å resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function. Structure, 1998, 6, 51-61.
    • (1998) Structure , vol.6 , pp. 51-61
    • Gunčar, G.1    Podobnik, M.2    Pungerčar, J.3    Štrukelj, B.4    Turk, V.5    Turk, D.6
  • 22
    • 0039547996 scopus 로고    scopus 로고
    • Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S
    • Gunčar, G.; Pungerčar, G.; Klemenčič , I.; Turk, V.; Turk, D. Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. EMBO J., 1999, 18, 793-803.
    • (1999) EMBO J , vol.18 , pp. 793-803
    • Gunčar, G.1    Pungerčar, G.2    Klemenčič, I.3    Turk, V.4    Turk, D.5
  • 23
    • 0031030808 scopus 로고    scopus 로고
    • Crystal structure of human cathepsin K complexed with a potent inhibitor
    • McGrath, M. E.; Klaus, J. L.; Barnes, M. G.; Brömme, D. Crystal structure of human cathepsin K complexed with a potent inhibitor. Nat. Struct. Biol., 1997, 4, 105-109.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 105-109
    • McGrath, M.E.1    Klaus, J.L.2    Barnes, M.G.3    Brömme, D.4
  • 29
    • 0242599721 scopus 로고    scopus 로고
    • Crystal structure of cathepsin X: A flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease
    • Gunčar, G.; Klemenčič, I.; Turk, B.; Turk, V.; Karaoglanovic-Carmona, A.; Juliano, L.; Turk, D. Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease. Structure, 2000, 8, 305-313.
    • (2000) Structure , vol.8 , pp. 305-313
    • Gunčar, G.1    Klemenčič, I.2    Turk, B.3    Turk, V.4    Karaoglanovic-Carmona, A.5    Juliano, L.6    Turk, D.7
  • 30
    • 0037322932 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases (cathepsins): Promising drug targets
    • Turk, D.; Gunčar, G. Lysosomal cysteine proteases (cathepsins): promising drug targets. Acta Crystallogr. D Biol. Crystallogr., 2003, 59, 203-213.
    • (2003) Acta Crystallogr. D Biol. Crystallogr , vol.59 , pp. 203-213
    • Turk, D.1    Gunčar, G.2
  • 31
    • 0030584678 scopus 로고    scopus 로고
    • Structure of procathepsin B. Model for inhibition of cysteine protease activity by the proregion
    • Cygler, M.; Sivaraman, J.; Grochulski, P.; Coulombe, R.; Storer, A. C.; Mort, J. S. Structure of procathepsin B. Model for inhibition of cysteine protease activity by the proregion. Structure, 1996, 4, 405-416.
    • (1996) Structure , vol.4 , pp. 405-416
    • Cygler, M.1    Sivaraman, J.2    Grochulski, P.3    Coulombe, R.4    Storer, A.C.5    Mort, J.S.6
  • 32
    • 0029976244 scopus 로고    scopus 로고
    • Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its Propeptide
    • Turk, D.; Podobnik, M.; Kuhelj, R.; Dolinar, M.; Turk, V. Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its Propeptide. FEBS Lett., 1996, 384, 211-214.
    • (1996) FEBS Lett , vol.384 , pp. 211-214
    • Turk, D.1    Podobnik, M.2    Kuhelj, R.3    Dolinar, M.4    Turk, V.5
  • 33
    • 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
    • Podobnik, M.; Kuhelj, R.; Turk, V.; Turk, D. 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., 1997, 271, 774-788.
    • (1997) J. Mol. Biol , vol.271 , pp. 774-788
    • Podobnik, M.1    Kuhelj, R.2    Turk, V.3    Turk, D.4
  • 34
    • 0029902382 scopus 로고    scopus 로고
    • Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
    • Coulombe, R.; Grochulski, P.; Sivaraman, J.; Ménard, R.; Mort, J. S.; Cygler, M. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J., 1996, 15, 5492-5503.
    • (1996) EMBO J , vol.15 , pp. 5492-5503
    • Coulombe, R.1    Grochulski, P.2    Sivaraman, J.3    Ménard, R.4    Mort, J.S.5    Cygler, M.6
  • 35
  • 36
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • Turk, V.; Turk, B.; Turk, D. Lysosomal cysteine proteases: facts and opportunities. EMBO J., 2001, 20, 4629-4633.
    • (2001) EMBO J , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 38
    • 0034723144 scopus 로고    scopus 로고
    • Crystal structure of human procathepsin X: A cysteine protease with the proregion covalently linked to the active site cysteine
    • Sivaraman, J.; Nägler, D. K.; Zhang, R.; Ménard, R.; Cygler, M. Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine. J. Mol. Biol., 2000, 295, 939-951.
    • (2000) J. Mol. Biol , vol.295 , pp. 939-951
    • Sivaraman, J.1    Nägler, D.K.2    Zhang, R.3    Ménard, R.4    Cygler, M.5
  • 39
    • 0031468018 scopus 로고    scopus 로고
    • Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity
    • Cygler, M.; Mort, J. S. Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity. Biochimie, 1997, 79, 645-652.
    • (1997) Biochimie , vol.79 , pp. 645-652
    • Cygler, M.1    Mort, J.S.2
  • 40
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: More than scavengers
    • Turk, B.; Turk, D.; Turk, V. Lysosomal cysteine proteases: more than scavengers. Biochim. Biophys. Acta, 2000, 1477, 98-111.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 41
    • 0033776087 scopus 로고    scopus 로고
    • Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides
    • Guay, J.; Falgueyret, J. P.; Ducret, A.; Percival, M. D.; Mancini, J. A. Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides. Eur. J. Biochem., 2000, 267, 6311-6318.
    • (2000) Eur. J. Biochem , vol.267 , pp. 6311-6318
    • Guay, J.1    Falgueyret, J.P.2    Ducret, A.3    Percival, M.D.4    Mancini, J.A.5
  • 42
    • 0040366645 scopus 로고    scopus 로고
    • Human cathepsin X: A cysteine protease with unique carboxypeptidase activity
    • Nägler, D. K.; Zhang, R.; Tam, W.; Sulea, T.; Purisima, E. O.; Ménard, R: Human cathepsin X: a cysteine protease with unique carboxypeptidase activity. Biochemistry, 1999, 38, 12648-12654.
    • (1999) Biochemistry , vol.38 , pp. 12648-12654
    • Nägler, D.K.1    Zhang, R.2    Tam, W.3    Sulea, T.4    Purisima, E.O.5    Ménard, R.6
  • 43
    • 0033850811 scopus 로고    scopus 로고
    • Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase
    • Klemenčič, I.; Carmona, A. K.; Cezari, M. H.; Juliano, M. A.; Juliano, L.; Gunčar, G.; Turk, D.; Križaj, I.; Turk, V.; Turk, B. Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase. Eur. J. Biochem., 2000, 267, 5404-5412.
    • (2000) Eur. J. Biochem , vol.267 , pp. 5404-5412
    • Klemenčič, I.1    Carmona, A.K.2    Cezari, M.H.3    Juliano, M.A.4    Juliano, L.5    Gunčar, G.6    Turk, D.7    Križaj, I.8    Turk, V.9    Turk, B.10
  • 44
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • Chapman, H. A.; Riese, R. J.; Shi G. P. Emerging roles for cysteine proteases in human biology. Annu. Rev. Physiol., 1997, 59, 63-88.
    • (1997) Annu. Rev. Physiol , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.P.3
  • 45
    • 0025098737 scopus 로고
    • A cysteine-specific lysosomal transport system provides a major route for the delivery of thiol to human fibroblast lysosomes: Possible role in supporting lysosomal proteolysis
    • Pisoni, R. L.; Acker, T. L.; Lisowski, K. M.; Lemons, R. M.; Thoene, J. G. A cysteine-specific lysosomal transport system provides a major route for the delivery of thiol to human fibroblast lysosomes: possible role in supporting lysosomal proteolysis. J. Cell Biol., 1990, 110, 327-335.
    • (1990) J. Cell Biol , vol.110 , pp. 327-335
    • Pisoni, R.L.1    Acker, T.L.2    Lisowski, K.M.3    Lemons, R.M.4    Thoene, J.G.5
  • 46
    • 52049096824 scopus 로고    scopus 로고
    • Cystatins: Biochemical and structural properties, and medical relevance
    • Turk, V.; Stoka, V.; Turk, D. Cystatins: biochemical and structural properties, and medical relevance. Front. Biosci., 2008, 13, 5406-5420.
    • (2008) Front. Biosci , vol.13 , pp. 5406-5420
    • Turk, V.1    Stoka, V.2    Turk, D.3
  • 47
    • 0032516003 scopus 로고    scopus 로고
    • Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation
    • Deussing, J.; Roth, W.; Saftig, P.; Peters, C.; Ploegh, H. L.; Villadangos, J. A. Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation. Proc. Natl. Acad. Sci. USA, 1998, 95, 4516-4521.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4516-4521
    • Deussing, J.1    Roth, W.2    Saftig, P.3    Peters, C.4    Ploegh, H.L.5    Villadangos, J.A.6
  • 51
    • 0033587689 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo
    • Pham, C. T.; Ley, T. J. Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. Proc. Natl. Acad. Sci. USA, 1999, 96, 8627-8632.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8627-8632
    • Pham, C.T.1    Ley, T.J.2
  • 53
    • 0037810410 scopus 로고    scopus 로고
    • Family C1 cysteine proteases: Biological diversity or redundancy?
    • Nägler, D. K.; Ménard, R. Family C1 cysteine proteases: biological diversity or redundancy? Biol. Chem., 2003, 384, 837-843.
    • (2003) Biol. Chem , vol.384 , pp. 837-843
    • Nägler, D.K.1    Ménard, R.2
  • 54
    • 0024814219 scopus 로고
    • Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins
    • Kirschke, H.; Wiederanders, B.; Brömme, D.; Rinne, A. Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins. Biochem. J., 1989, 264, 467-473.
    • (1989) Biochem. J , vol.264 , pp. 467-473
    • Kirschke, H.1    Wiederanders, B.2    Brömme, D.3    Rinne, A.4
  • 55
    • 0038687865 scopus 로고    scopus 로고
    • Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization
    • Brömme, D.; Li, Z.; Barnes, M.; Mehler, E. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry, 1999, 38, 2377-2385.
    • (1999) Biochemistry , vol.38 , pp. 2377-2385
    • Brömme, D.1    Li, Z.2    Barnes, M.3    Mehler, E.4
  • 56
    • 0030026637 scopus 로고    scopus 로고
    • Human cathepsin O2, a matrix protein degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme
    • Brömme, D.; Okamoto, K.; Wang, B. B.; Biroc, S. Human cathepsin O2, a matrix protein degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme. J. Biol. Chem., 1996, 271, 2126-2132.
    • (1996) J. Biol. Chem , vol.271 , pp. 2126-2132
    • Brömme, D.1    Okamoto, K.2    Wang, B.B.3    Biroc, S.4
  • 57
    • 0029996240 scopus 로고    scopus 로고
    • Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells
    • Brix, K.; Lemansky, P.; Herzog, V. Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells. Endocrinology, 1996, 137, 1963-1974.
    • (1996) Endocrinology , vol.137 , pp. 1963-1974
    • Brix, K.1    Lemansky, P.2    Herzog, V.3
  • 58
    • 0034256042 scopus 로고    scopus 로고
    • Regulated secretion of conventional lysosomes
    • Andrews, N. W. Regulated secretion of conventional lysosomes. Trends Cell. Biol. 2000, 10, 316-321.
    • (2000) Trends Cell. Biol , vol.10 , pp. 316-321
    • Andrews, N.W.1
  • 59
    • 0034930528 scopus 로고    scopus 로고
    • Towards specific functions of lysosomal cysteine peptidases: Phenotypes of mice deficient for cathepsin B or cathepsin L
    • Reinheckel, T.; Deussing, J.; Roth, W.; Peters, C. Towards specific functions of lysosomal cysteine peptidases: phenotypes of mice deficient for cathepsin B or cathepsin L. Biol. Chem., 2001, 382, 735-741.
    • (2001) Biol. Chem , vol.382 , pp. 735-741
    • Reinheckel, T.1    Deussing, J.2    Roth, W.3    Peters, C.4
  • 61
    • 48549096292 scopus 로고    scopus 로고
    • Role of cysteine cathepsins in matrix degradation and cell signalling
    • Obermajer, N.; Jevnikar, Z.; Doljak, B.; Kos, J. Role of cysteine cathepsins in matrix degradation and cell signalling. Connect. Tissue Res., 2008, 49, 193-196.
    • (2008) Connect. Tissue Res , vol.49 , pp. 193-196
    • Obermajer, N.1    Jevnikar, Z.2    Doljak, B.3    Kos, J.4
  • 63
    • 0942265544 scopus 로고    scopus 로고
    • Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins
    • Cirman, T.; Oresić, K.; Mazovec, G. D.; Turk, V.; Reed, J. C.; Myers, R. M.; Salvesen, G. S.; Turk, B. Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins. J. Biol. Chem., 2004, 279, 3578-3587.
    • (2004) J. Biol. Chem , vol.279 , pp. 3578-3587
    • Cirman, T.1    Oresić, K.2    Mazovec, G.D.3    Turk, V.4    Reed, J.C.5    Myers, R.M.6    Salvesen, G.S.7    Turk, B.8
  • 64
    • 34250020188 scopus 로고    scopus 로고
    • Lysosomal cysteine cathepsins: Signaling pathways in apoptosis
    • Stoka, V.; Turk, V.; Turk, B. Lysosomal cysteine cathepsins: signaling pathways in apoptosis. Biol. Chem., 2007, 388, 555-360.
    • (2007) Biol. Chem , vol.388 , pp. 555-360
    • Stoka, V.1    Turk, V.2    Turk, B.3
  • 65
    • 55949117482 scopus 로고    scopus 로고
    • Cathepsins: Key modulators of cell death and inflammatory responses
    • Conus, S.; Simon, H. U. Cathepsins: key modulators of cell death and inflammatory responses. Biochem. Pharmacol., 2008, 76, 1374-1382.
    • (2008) Biochem. Pharmacol , vol.76 , pp. 1374-1382
    • Conus, S.1    Simon, H.U.2
  • 69
    • 0029310512 scopus 로고
    • Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary. Molecular cloning, sequencing and tissue distribution
    • Brömme, D.; Okamoto, K. Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary. Molecular cloning, sequencing and tissue distribution. Biol. Chem. Hoppe Seyler, 1995, 376, 379-384.
    • (1995) Biol. Chem. Hoppe Seyler , vol.376 , pp. 379-384
    • Brömme, D.1    Okamoto, K.2
  • 70
    • 0028831635 scopus 로고
    • Molecular cloning of human cDNA for cathepsin K: Novel cysteine proteinase predominantly expressed in bone
    • Inaoka, T.; Bilbe, B.; Ishibashi, O.; Tezuka, K.; Kumegawa, M.; Kokubo, T. Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone. Biochem. Biophys. Res. Comm., 1995, 206, 89-96.
    • (1995) Biochem. Biophys. Res. Comm , vol.206 , pp. 89-96
    • Inaoka, T.1    Bilbe, B.2    Ishibashi, O.3    Tezuka, K.4    Kumegawa, M.5    Kokubo, T.6
  • 72
    • 0034502852 scopus 로고    scopus 로고
    • Cathepsin K in thyroid epithelial cells: Sequence, localization and possible function in extracellular proteolysis of thyroglobulin
    • Tepel, C.; Brömme, D.; Herzog, V.; Brix, K. Cathepsin K in thyroid epithelial cells: sequence, localization and possible function in extracellular proteolysis of thyroglobulin. J. Cell Sci., 2000, 113, 4487-4498.
    • (2000) J. Cell Sci , vol.113 , pp. 4487-4498
    • Tepel, C.1    Brömme, D.2    Herzog, V.3    Brix, K.4
  • 75
    • 60849134818 scopus 로고    scopus 로고
    • Zhao, Q.; Jia, Y.; Xiao, Y. Cathepsin K: a therapeutic target for bone diseases. Biochem. Biophys. Res. Commun., 2009, 380, 721-723.
    • Zhao, Q.; Jia, Y.; Xiao, Y. Cathepsin K: a therapeutic target for bone diseases. Biochem. Biophys. Res. Commun., 2009, 380, 721-723.
  • 76
    • 59049085396 scopus 로고    scopus 로고
    • Cathepsin K activity-dependent regulation of osteoclast actin ring formation and bone resorption
    • Wilson, S. R.; Peters, C.; Saftig, P.; Brömme, D. Cathepsin K activity-dependent regulation of osteoclast actin ring formation and bone resorption. J. Biol. Chem., 2009, 284, 2584-1592.
    • (2009) J. Biol. Chem , vol.284 , pp. 2584-1592
    • Wilson, S.R.1    Peters, C.2    Saftig, P.3    Brömme, D.4
  • 77
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
    • Riese, R. J.; Wolf, P. R.; Brömme, D.; Natkin, L. R.; Villadangos, J. A.; Ploegh, H. L.; Chapman, H. A. Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity, 1996, 4, 357-366.
    • (1996) Immunity , vol.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.R.2    Brömme, D.3    Natkin, L.R.4    Villadangos, J.A.5    Ploegh, H.L.6    Chapman, H.A.7
  • 78
    • 0030790341 scopus 로고    scopus 로고
    • Degradation of mouse invariant chain: Roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism
    • Villadangos, J. A.; Riese, R. J.; Peters, C.; Chapman, H. A.; Ploegh, H. L. Degradation of mouse invariant chain: roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism. J. Exp. Med., 1997, 186, 549-560.
    • (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
  • 80
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • Honey, K.; Rudensky, A. Y. Lysosomal cysteine proteases regulate antigen presentation. Nat. Rev. Immunol., 2003, 3, 472-482.
    • (2003) Nat. Rev. Immunol , vol.3 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 81
    • 41049107484 scopus 로고    scopus 로고
    • Cysteine cathepsin S as an immunomodulatory target: Present and future trends
    • Gupta, S.; Singh, R. K.; Dastidar, S.; Ray, A. Cysteine cathepsin S as an immunomodulatory target: present and future trends. Expert Opin. Ther. Targets, 2008, 12, 291-299.
    • (2008) Expert Opin. Ther. Targets , vol.12 , pp. 291-299
    • Gupta, S.1    Singh, R.K.2    Dastidar, S.3    Ray, A.4
  • 82
    • 0029099619 scopus 로고
    • Vinyl sulfones as mechanism-based cysteine protease inhibitors
    • Palmer, J. T.; Rasnick, D.; Klaus, J. L.; Brömme, D. Vinyl sulfones as mechanism-based cysteine protease inhibitors. J. Med. Chem., 1995, 38, 3193-3196.
    • (1995) J. Med. Chem , vol.38 , pp. 3193-3196
    • Palmer, J.T.1    Rasnick, D.2    Klaus, J.L.3    Brömme, D.4
  • 83
    • 60549085844 scopus 로고    scopus 로고
    • Quantifying cathepsin S activity in antigen presenting cells using a novel specific substrate
    • Lützner, N.; Kalbacher, H. Quantifying cathepsin S activity in antigen presenting cells using a novel specific substrate. J. Biol. Chem., 2008, 283, 36185-36194.
    • (2008) J. Biol. Chem , vol.283 , pp. 36185-36194
    • Lützner, N.1    Kalbacher, H.2
  • 84
    • 0034599498 scopus 로고    scopus 로고
    • Role of cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages
    • Shi, G. P.; Bryant, R. A.; Riese, R.; Verhelst, S.; Driessen, C.; Li, Z.; Brömme, D.; Ploegh, H. L.; Chapman, H. A. Role of cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. J. Exp. Med., 2000, 191, 1177-1186.
    • (2000) J. Exp. Med , vol.191 , pp. 1177-1186
    • Shi, G.P.1    Bryant, R.A.2    Riese, R.3    Verhelst, S.4    Driessen, C.5    Li, Z.6    Brömme, D.7    Ploegh, H.L.8    Chapman, H.A.9
  • 85
    • 0000701072 scopus 로고
    • The genetics of a new hair deficiency, furless
    • Green, E. L. The genetics of a new hair deficiency, furless. J. Hered., 1954, 45, 115-118.
    • (1954) J. Hered , vol.45 , pp. 115-118
    • Green, E.L.1
  • 86
    • 34748883569 scopus 로고    scopus 로고
    • Protease pathways in peptide neurotransmission and neurodegenerative diseases
    • Hook, V. Y. Protease pathways in peptide neurotransmission and neurodegenerative diseases. Cell. Mol. Neurobiol., 2006, 26, 449-469.
    • (2006) Cell. Mol. Neurobiol , vol.26 , pp. 449-469
    • Hook, V.Y.1
  • 87
    • 49649094763 scopus 로고    scopus 로고
    • Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment
    • Abboud-Jarrous, G.; Atzmon, R.; Peretz, T.; Palermo, C.; Gadea, B. B.; Joyce, J. A.; Vlodavsky, I. Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment. J. Biol. Chem., 2008, 283, 18167-18176.
    • (2008) J. Biol. Chem , vol.283 , pp. 18167-18176
    • Abboud-Jarrous, G.1    Atzmon, R.2    Peretz, T.3    Palermo, C.4    Gadea, B.B.5    Joyce, J.A.6    Vlodavsky, I.7
  • 88
    • 35848948133 scopus 로고    scopus 로고
    • Cysteine proteases: Destruction ability versus immunomodulation capacity in immune cells
    • Zavašnik-Bergant, T.; Turk, B. Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells. Biol. Chem., 2007, 388, 1141-1149.
    • (2007) Biol. Chem , vol.388 , pp. 1141-1149
    • Zavašnik-Bergant, T.1    Turk, B.2
  • 89
    • 0036168150 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis
    • Adkison, A. M.; Raptis, S. Z.; Kelley, D. G.; Pham, C. T. Dipeptidyl peptidase I activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis. J. Clin. Invest., 2002, 109, 363-371.
    • (2002) J. Clin. Invest , vol.109 , pp. 363-371
    • Adkison, A.M.1    Raptis, S.Z.2    Kelley, D.G.3    Pham, C.T.4
  • 90
    • 34547133013 scopus 로고    scopus 로고
    • Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme processing
    • Méthot, N.; Rubin, J.; Guay, D.; Beaulieu, C.; Ethier, D.; Reddy, T. J.; Riendeau, D.; Percival, M. D. Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme processing. J. Biol. Chem., 2007, 282, 20836-20846.
    • (2007) J. Biol. Chem , vol.282 , pp. 20836-20846
    • Méthot, N.1    Rubin, J.2    Guay, D.3    Beaulieu, C.4    Ethier, D.5    Reddy, T.J.6    Riendeau, D.7    Percival, M.D.8
  • 91
    • 33947604810 scopus 로고    scopus 로고
    • Emerging roles of cysteine cathepsins in disease and their potential as drug targets
    • Vasiljeva, O.; Reinheckel, T.; Peters, C.; Turk, D.; Turk, V.; Turk, B. Emerging roles of cysteine cathepsins in disease and their potential as drug targets. Curr. Pharm. Des., 2007, 13, 387-403.
    • (2007) Curr. Pharm. Des , vol.13 , pp. 387-403
    • Vasiljeva, O.1    Reinheckel, T.2    Peters, C.3    Turk, D.4    Turk, V.5    Turk, B.6
  • 92
    • 1542604677 scopus 로고    scopus 로고
    • Cysteine proteases as disease markers
    • Berdowska, I. Cysteine proteases as disease markers. Clin. Chim. Acta, 2004, 342, 41-69.
    • (2004) Clin. Chim. Acta , vol.342 , pp. 41-69
    • Berdowska, I.1
  • 93
    • 34548594517 scopus 로고    scopus 로고
    • Lysosomal cysteine proteinase cathepsin S as a potential target for anti-cancer therapy
    • Chang, W. S. W.; Wu, H. R.; Yeh, C. T.; Wu, C. W.; Chang, J. Y. Lysosomal cysteine proteinase cathepsin S as a potential target for anti-cancer therapy. J. Cancer Mol., 2007, 3, 5-14.
    • (2007) J. Cancer Mol , vol.3 , pp. 5-14
    • Chang, W.S.W.1    Wu, H.R.2    Yeh, C.T.3    Wu, C.W.4    Chang, J.Y.5
  • 94
    • 33846643454 scopus 로고    scopus 로고
    • Cysteine cathepsins and the cutting edge of cancer invasion
    • Gocheva, V.; Joyce, J. A. Cysteine cathepsins and the cutting edge of cancer invasion. Cell Cycle, 2007, 6, 60-64.
    • (2007) Cell Cycle , vol.6 , pp. 60-64
    • Gocheva, V.1    Joyce, J.A.2
  • 95
    • 84858011122 scopus 로고    scopus 로고
    • Delineating protease functions during cancer development
    • Affara, N. I.; Andreu, P.; Coussens, L. M. Delineating protease functions during cancer development. Methods Mol. Biol., 2009, 539, 1-32.
    • (2009) Methods Mol. Biol , vol.539 , pp. 1-32
    • Affara, N.I.1    Andreu, P.2    Coussens, L.M.3
  • 96
    • 46749098502 scopus 로고    scopus 로고
    • The cathepsin family and their role in colorectal cancer
    • Kuester, D.; Lippert, H.; Roessner, A.; Krueger, S. The cathepsin family and their role in colorectal cancer. Pathol. Res. Pract., 2008, 204, 491-500.
    • (2008) Pathol. Res. Pract , vol.204 , pp. 491-500
    • Kuester, D.1    Lippert, H.2    Roessner, A.3    Krueger, S.4
  • 97
    • 37549070672 scopus 로고    scopus 로고
    • Cysteine cathepsin proteases as pharmacological targets in cancer
    • Palermo, C.; Joyce, J. A. Cysteine cathepsin proteases as pharmacological targets in cancer. Trends Pharmacol. Sci., 2008, 29, 22-28.
    • (2008) Trends Pharmacol. Sci , vol.29 , pp. 22-28
    • Palermo, C.1    Joyce, J.A.2
  • 98
    • 37549068912 scopus 로고    scopus 로고
    • Cathepsin K inhibitors: A novel target for osteoporosis therapy
    • Stoch, S. A.; Wagner, J. A. Cathepsin K inhibitors: a novel target for osteoporosis therapy. Clin. Pharmacol. Ther., 2008, 83, 172-175.
    • (2008) Clin. Pharmacol. Ther , vol.83 , pp. 172-175
    • Stoch, S.A.1    Wagner, J.A.2
  • 100
    • 52049085744 scopus 로고    scopus 로고
    • Cystatin C and cathepsins in cardiovascular disease
    • Bengtsson, E.; Nilsson, J.; Jovinge, S. Cystatin C and cathepsins in cardiovascular disease. Front. Biosci., 2008, 13, 5780-5786.
    • (2008) Front. Biosci , vol.13 , pp. 5780-5786
    • Bengtsson, E.1    Nilsson, J.2    Jovinge, S.3
  • 101
    • 18944365919 scopus 로고    scopus 로고
    • The role of cathepsins in osteoporosis and arthritis: Rationale for the design of new therapeutics
    • Yasuda, Y.; Kaleta, J.; Brömme, D. The role of cathepsins in osteoporosis and arthritis: rationale for the design of new therapeutics. Adv. Drug. Deliv. Rev., 2005, 57, 973-993.
    • (2005) Adv. Drug. Deliv. Rev , vol.57 , pp. 973-993
    • Yasuda, Y.1    Kaleta, J.2    Brömme, D.3
  • 103
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • Bidère, N.; Lorenzo, H. K.; Carmona, S.; Laforge, M.; Harper, F.; Dumont, C.; Senik, A. Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J. Biol. Chem., 2003, 278, 31401-31411.
    • (2003) J. Biol. Chem , vol.278 , pp. 31401-31411
    • Bidère, N.1    Lorenzo, H.K.2    Carmona, S.3    Laforge, M.4    Harper, F.5    Dumont, C.6    Senik, A.7
  • 104
    • 67449155856 scopus 로고    scopus 로고
    • Granulysin induces cathepsin B release from lysosomes of target tumor cells to attack mitochondria through processing of bid leading to necroptosis
    • Zhang, H.; Zhong, C.; Shi, L.; Guo, Y.; Fan, Z. Granulysin induces cathepsin B release from lysosomes of target tumor cells to attack mitochondria through processing of bid leading to necroptosis. J. Immunol., 2009, 182, 6993-7000.
    • (2009) J. Immunol , vol.182 , pp. 6993-7000
    • Zhang, H.1    Zhong, C.2    Shi, L.3    Guo, Y.4    Fan, Z.5
  • 106
    • 25844528025 scopus 로고    scopus 로고
    • The role of disturbed pH dynamics and the Na+/H+ exchanger in metastasis
    • Cardone, R. A.; Casavola, V.; Reshkin, S. J. The role of disturbed pH dynamics and the Na+/H+ exchanger in metastasis. Nat. Rev. Cancer, 2005, 5, 786-795.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 786-795
    • Cardone, R.A.1    Casavola, V.2    Reshkin, S.J.3
  • 107
    • 0029809357 scopus 로고    scopus 로고
    • Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency
    • Gelb, B. D.; Shi, G. P.; Chapman, H. A.; Desnick, R. J. Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency. Science, 1996, 273, 1236-1238.
    • (1996) Science , vol.273 , pp. 1236-1238
    • Gelb, B.D.1    Shi, G.P.2    Chapman, H.A.3    Desnick, R.J.4
  • 110
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D. J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev., 2001, 81, 741-766.
    • (2001) Physiol. Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 111
    • 57649221135 scopus 로고    scopus 로고
    • Amyloid precursor protein trafficking, processing, and function
    • Thinakaran, G.; Koo, E. H. Amyloid precursor protein trafficking, processing, and function. J. Biol. Chem., 2008, 283, 29615-29619.
    • (2008) J. Biol. Chem , vol.283 , pp. 29615-29619
    • Thinakaran, G.1    Koo, E.H.2
  • 112
    • 26844559355 scopus 로고    scopus 로고
    • Inhibition of cathepsin B reduces beta-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: Evidence for cathepsin B as a candidate β-secretase of Alzheimer's disease
    • Hook, V.; Toneff, T.; Bogyo, M.; Greenbaum, D.; Medzihradszky, K. F.; Neveu, J.; Lane, W.; Hook, G.; Reisine, T. Inhibition of cathepsin B reduces beta-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate β-secretase of Alzheimer's disease. Biol. Chem., 2005, 386, 931-940.
    • (2005) Biol. Chem , vol.386 , pp. 931-940
    • Hook, V.1    Toneff, T.2    Bogyo, M.3    Greenbaum, D.4    Medzihradszky, K.F.5    Neveu, J.6    Lane, W.7    Hook, G.8    Reisine, T.9
  • 114
    • 33846621573 scopus 로고    scopus 로고
    • Cysteine protease inhibitors effectively reduce in vivo levels of brain beta-amyloid related to Alzheimer's disease
    • Hook, V.; Kindy, M.; Hook, G. Cysteine protease inhibitors effectively reduce in vivo levels of brain beta-amyloid related to Alzheimer's disease. Biol. Chem., 2007, 388, 247-252.
    • (2007) Biol. Chem , vol.388 , pp. 247-252
    • Hook, V.1    Kindy, M.2    Hook, G.3
  • 115
    • 43149100823 scopus 로고    scopus 로고
    • Inhibitors of cathepsin B improve memory and reduce beta-amyloid in transgenic Alzheimer disease mice expressing the wild-type, but not the Swedish mutant, β-secretase site of the amyloid precursor protein
    • Hook, V. Y.; Kindy, M.; Hook, G. Inhibitors of cathepsin B improve memory and reduce beta-amyloid in transgenic Alzheimer disease mice expressing the wild-type, but not the Swedish mutant, β-secretase site of the amyloid precursor protein. J. Biol. Chem., 2008, 283, 7745-7753.
    • (2008) J. Biol. Chem , vol.283 , pp. 7745-7753
    • Hook, V.Y.1    Kindy, M.2    Hook, G.3
  • 116
    • 67649656100 scopus 로고    scopus 로고
    • Genetic cathepsin B deficiency reduces β-amyloid in transgenic mice expressing human wild-type amyloid precursor protein
    • Hook, V. Y.; Kindy, M.; Reinheckel, T.; Peters, C.; Hook, G. Genetic cathepsin B deficiency reduces β-amyloid in transgenic mice expressing human wild-type amyloid precursor protein. Biochem. Biophys. Res. Commun., 2009, 386, 284-288.
    • (2009) Biochem. Biophys. Res. Commun , vol.386 , pp. 284-288
    • Hook, V.Y.1    Kindy, M.2    Reinheckel, T.3    Peters, C.4    Hook, G.5
  • 117
    • 62449097363 scopus 로고    scopus 로고
    • Cathepsins B and L differentially regulate amyloid precursor protein processing
    • Klein, D. M.; Felsenstein, K. M.; Brenneman, D. E. Cathepsins B and L differentially regulate amyloid precursor protein processing. J. Pharmacol. Exp. Ther., 2009, 328, 813-821.
    • (2009) J. Pharmacol. Exp. Ther , vol.328 , pp. 813-821
    • Klein, D.M.1    Felsenstein, K.M.2    Brenneman, D.E.3
  • 118
    • 58149526807 scopus 로고    scopus 로고
    • Protease-mediated entry via the endosome of human coronavirus 229E
    • Kawase, M.; Shirato, K.; Matsuyama, S.; Taguchi, F. Protease-mediated entry via the endosome of human coronavirus 229E. J. Virol., 2009, 83, 712-721.
    • (2009) J. Virol , vol.83 , pp. 712-721
    • Kawase, M.1    Shirato, K.2    Matsuyama, S.3    Taguchi, F.4
  • 119
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran, K.; Sullivan, N. J.; Felbor, U.; Whelan, S. P.; Cunningham, J. M. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science, 2005, 308, 1643-1645.
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 120
    • 33645788357 scopus 로고    scopus 로고
    • Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein
    • Schornberg, K.; Matsuyama, S.; Kabsch, K.; Delos, S.; Bouton, A.; White, J. Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein. J. Virol., 2006, 80, 4174-4178.
    • (2006) J. Virol , vol.80 , pp. 4174-4178
    • Schornberg, K.1    Matsuyama, S.2    Kabsch, K.3    Delos, S.4    Bouton, A.5    White, J.6
  • 121
    • 0023792145 scopus 로고
    • The potential role of lysosomes in tissue distribution of weak bases
    • MacIntyre, A. C.; Cutler, D. J. The potential role of lysosomes in tissue distribution of weak bases. Biopharm. Drug Dispos., 1988, 9, 513-526.
    • (1988) Biopharm. Drug Dispos , vol.9 , pp. 513-526
    • MacIntyre, A.C.1    Cutler, D.J.2
  • 124
    • 70349471029 scopus 로고    scopus 로고
    • Pharmacological inhibitors to identify roles of cathepsin K in cell-based studies: A comparison of available tools
    • Desmarais, S.; Massé, F.; Percival, M. D. Pharmacological inhibitors to identify roles of cathepsin K in cell-based studies: a comparison of available tools. Biol. Chem., 2009, 390, 941-948.
    • (2009) Biol. Chem , vol.390 , pp. 941-948
    • Desmarais, S.1    Massé, F.2    Percival, M.D.3
  • 125
    • 33749664751 scopus 로고    scopus 로고
    • The consequences of lysosomotropism on the design of selective cathepsin K inhibitors
    • Black, W. C.; Percival, M. D. The consequences of lysosomotropism on the design of selective cathepsin K inhibitors. ChemBioChem, 2006, 7, 1525-1535.
    • (2006) ChemBioChem , vol.7 , pp. 1525-1535
    • Black, W.C.1    Percival, M.D.2
  • 127
    • 0034529448 scopus 로고    scopus 로고
    • Immunological principles of adverse drug reactions: The initiation and propagation of immune responses elicited by drug treatment
    • Naisbitt, D. J.; Gordon, S. F.; Pirmohamed, M.; Park, B. K. Immunological principles of adverse drug reactions: the initiation and propagation of immune responses elicited by drug treatment. Drug Saf., 2000, 23, 483-507.
    • (2000) Drug Saf , vol.23 , pp. 483-507
    • Naisbitt, D.J.1    Gordon, S.F.2    Pirmohamed, M.3    Park, B.K.4
  • 128
    • 1642281756 scopus 로고    scopus 로고
    • Drug-protein adducts: An industry perspective on minimizing the potential for drug bioactivation in drug discovery and development
    • Evans, D. C.; Watt, A. P.; Nicoll-Griffith, D. A.; Baillie T. A. Drug-protein adducts: an industry perspective on minimizing the potential for drug bioactivation in drug discovery and development. Chem. Res. Toxicol., 2004, 17, 3-16.
    • (2004) Chem. Res. Toxicol , vol.17 , pp. 3-16
    • Evans, D.C.1    Watt, A.P.2    Nicoll-Griffith, D.A.3    Baillie, T.A.4
  • 129
    • 64349093749 scopus 로고    scopus 로고
    • Covalent modifiers: An orthogonal approach to drug design
    • Potashman, M. H.; Duggan, M. E. Covalent modifiers: an orthogonal approach to drug design. J. Med. Chem., 2009, 52, 1231-1246.
    • (2009) J. Med. Chem , vol.52 , pp. 1231-1246
    • Potashman, M.H.1    Duggan, M.E.2
  • 130
    • 0032541311 scopus 로고    scopus 로고
    • Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection
    • Engel, J. C.; Doyle, P. S.; Hsieh, I.; McKerrow, J. H. Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection. J. Exp. Med., 1998, 188, 725-734.
    • (1998) J. Exp. Med , vol.188 , pp. 725-734
    • Engel, J.C.1    Doyle, P.S.2    Hsieh, I.3    McKerrow, J.H.4
  • 131
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine and threonine proteases
    • Powers, J. C.; Asgian, J. L.; Ekici, Ö. D.; James, K. E. Irreversible inhibitors of serine, cysteine and threonine proteases. Chem. Rev., 2002, 102, 4639-4750.
    • (2002) Chem. Rev , vol.102 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3    James, K.E.4
  • 132
  • 133
    • 0036260967 scopus 로고    scopus 로고
    • Thiol-dependent enzymes and their inhibitors: A review
    • Leung-Toung, R.; Li, W.; Tam, T. F.; Karimian, K. Thiol-dependent enzymes and their inhibitors: a review. Curr. Med. Chem., 2002, 9, 979-1002.
    • (2002) Curr. Med. Chem , vol.9 , pp. 979-1002
    • Leung-Toung, R.1    Li, W.2    Tam, T.F.3    Karimian, K.4
  • 136
    • 35048878659 scopus 로고    scopus 로고
    • Michael acceptors as cysteine protease inhibitors
    • Santos, M. M.; Moreira, R. Michael acceptors as cysteine protease inhibitors. Mini Rev. Med. Chem., 2007, 7, 1040-1050.
    • (2007) Mini Rev. Med. Chem , vol.7 , pp. 1040-1050
    • Santos, M.M.1    Moreira, R.2
  • 137
    • 0037528821 scopus 로고    scopus 로고
    • Non-peptidic inhibitors of cysteine proteases
    • Schirmeister, T., Kaeppler, U. Non-peptidic inhibitors of cysteine proteases. Min. Rev. Med. Chem., 2003, 3, 361-373.
    • (2003) Min. Rev. Med. Chem , vol.3 , pp. 361-373
    • Schirmeister, T.1    Kaeppler, U.2
  • 138
    • 0142142211 scopus 로고    scopus 로고
    • Cysteine protease inhibitors containing small rings
    • Schirmeister, T., Klockow, A. Cysteine protease inhibitors containing small rings. Min. Rev. Med. Chem., 2003, 3, 585-596.
    • (2003) Min. Rev. Med. Chem , vol.3 , pp. 585-596
    • Schirmeister, T.1    Klockow, A.2
  • 140
    • 0036679896 scopus 로고    scopus 로고
    • Recent advances in the synthesis, design and selection of cysteine protease inhibitors
    • Hernandez, A. A., Roush, W. R. Recent advances in the synthesis, design and selection of cysteine protease inhibitors. Curr. Opin. Chem. Biol., 2002, 6, 459-465.
    • (2002) Curr. Opin. Chem. Biol , vol.6 , pp. 459-465
    • Hernandez, A.A.1    Roush, W.R.2
  • 141
    • 0033910551 scopus 로고    scopus 로고
    • The therapeutic potential of advances in cysteine inhibitor design
    • Veber, D. F.; Thompson, S. K. The therapeutic potential of advances in cysteine inhibitor design. Curr. Opin. Drug Discov. Devel., 2000, 3, 362-369.
    • (2000) Curr. Opin. Drug Discov. Devel , vol.3 , pp. 362-369
    • Veber, D.F.1    Thompson, S.K.2
  • 142
    • 0343433408 scopus 로고    scopus 로고
    • Cysteine proteases and their inhibitors
    • Otto, H.-H.; Schirmeister, T. Cysteine proteases and their inhibitors. Chem. Rev., 1997, 97, 133-171.
    • (1997) Chem. Rev , vol.97 , pp. 133-171
    • Otto, H.-H.1    Schirmeister, T.2
  • 143
    • 0036882393 scopus 로고    scopus 로고
    • Human and parasitic papain-like cysteine proteases: Their role in physiology and pathology and recent developments in inhibitor design
    • Lecaille, F.; Kaleta, J.; Brömme, D. Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chem. Rev., 2002, 102, 4459-4488.
    • (2002) Chem. Rev , vol.102 , pp. 4459-4488
    • Lecaille, F.1    Kaleta, J.2    Brömme, D.3
  • 144
    • 0035986223 scopus 로고    scopus 로고
    • Thiol-dependent cathepsins: Pathophysiological implications and recent advances in inhibitor design
    • Brömme, D.; Kaleta, J. Thiol-dependent cathepsins: pathophysiological implications and recent advances in inhibitor design. Curr. Pharm. Des., 2002, 8, 1639-1658.
    • (2002) Curr. Pharm. Des , vol.8 , pp. 1639-1658
    • Brömme, D.1    Kaleta, J.2
  • 146
    • 33645051476 scopus 로고    scopus 로고
    • Design of cathepsin K inhibitors for osteoporosis
    • Deaton, D. N.; Tavares, F. X. Design of cathepsin K inhibitors for osteoporosis. Curr. Top. Med. Chem., 2005, 5, 1639-1675.
    • (2005) Curr. Top. Med. Chem , vol.5 , pp. 1639-1675
    • Deaton, D.N.1    Tavares, F.X.2
  • 147
    • 42949127288 scopus 로고    scopus 로고
    • The trifluoroethylamine function as peptide bond replacement
    • Sani, M.; Volonterio, A.; Zanda, M. The trifluoroethylamine function as peptide bond replacement. ChemMedChem, 2007, 2, 1693-1700.
    • (2007) ChemMedChem , vol.2 , pp. 1693-1700
    • Sani, M.1    Volonterio, A.2    Zanda, M.3
  • 148
    • 33646058296 scopus 로고    scopus 로고
    • Thiol proteases: Inhibitors and potential therapeutic targets
    • Leung-Toung, R.; Zhao, J.; Li, W.; Tam, T. F.; Karimian, K. Thiol proteases: inhibitors and potential therapeutic targets. Curr. Med. Chem., 2006, 13, 547-581.
    • (2006) Curr. Med. Chem , vol.13 , pp. 547-581
    • Leung-Toung, R.1    Zhao, J.2    Li, W.3    Tam, T.F.4    Karimian, K.5
  • 149
    • 0014644706 scopus 로고
    • The pH dependencies of individual rate constants in papain-catalyzed reactions
    • Lucas, E. C.; Williams, A. The pH dependencies of individual rate constants in papain-catalyzed reactions. Biochemistry, 1969, 8, 5125-5135.
    • (1969) Biochemistry , vol.8 , pp. 5125-5135
    • Lucas, E.C.1    Williams, A.2
  • 150
    • 0017747049 scopus 로고
    • Thiohemiacetal formation by inhibitory aldehydes at the active site of papain
    • Lewis, C. A. Jr.; Wolfenden R. Thiohemiacetal formation by inhibitory aldehydes at the active site of papain. Biochemistry, 1977, 16, 4890-4895.
    • (1977) Biochemistry , vol.16 , pp. 4890-4895
    • Lewis Jr., C.A.1    Wolfenden, R.2
  • 151
    • 0022607084 scopus 로고
    • Carboxyl-modified amino acids and peptides as protease inhibitors
    • Thompson, S. A.; Andrews, P. R.; Hanzlik, R. P. Carboxyl-modified amino acids and peptides as protease inhibitors. J. Med. Chem., 1986, 29, 104-111.
    • (1986) J. Med. Chem , vol.29 , pp. 104-111
    • Thompson, S.A.1    Andrews, P.R.2    Hanzlik, R.P.3
  • 152
    • 0001146727 scopus 로고
    • Reversible covalent inhibition of papain by a peptide nitrile. 13C-NMR evidence for a thioimidate ester adduct
    • Moon, J. B.; Coleman, R. S.; Hanzlik, R. P. Reversible covalent inhibition of papain by a peptide nitrile. 13C-NMR evidence for a thioimidate ester adduct. J. Am. Chem. Soc., 1986, 108, 1350-1351.
    • (1986) J. Am. Chem. Soc , vol.108 , pp. 1350-1351
    • Moon, J.B.1    Coleman, R.S.2    Hanzlik, R.P.3
  • 153
    • 0023098601 scopus 로고
    • Inhibition of papain by nitriles: Mechanistic studies using NMR and kinetic measurements
    • Liang, T. C.; Abeles, R. H.; Inhibition of papain by nitriles: mechanistic studies using NMR and kinetic measurements. Arch. Biochem. Biophys., 1987, 252, 626-634.
    • (1987) Arch. Biochem. Biophys , vol.252 , pp. 626-634
    • Liang, T.C.1    Abeles, R.H.2
  • 154
    • 0022977803 scopus 로고
    • Benzoylamidoacetonitrile is bound as a thioimidate in the active site of papain
    • Brisson, J.-R.; Carey, P. R.; Storer, A. C. Benzoylamidoacetonitrile is bound as a thioimidate in the active site of papain. J. Biol. Chem., 1986, 261, 9087-9089.
    • (1986) J. Biol. Chem , vol.261 , pp. 9087-9089
    • Brisson, J.-R.1    Carey, P.R.2    Storer, A.C.3
  • 155
    • 0035967769 scopus 로고    scopus 로고
    • 2-Alkylthio-4-oxo-3- quinazolineacetonitriles and analogous thieno[3,2-d] pyrimidineacetonitriles: Reaction with thiols via trapped thioimidates
    • Gütschow, M.; Powers, J. C. 2-Alkylthio-4-oxo-3- quinazolineacetonitriles and analogous thieno[3,2-d] pyrimidineacetonitriles: reaction with thiols via trapped thioimidates. J. Org. Chem., 2001, 66, 4723-4727.
    • (2001) J. Org. Chem , vol.66 , pp. 4723-4727
    • Gütschow, M.1    Powers, J.C.2
  • 156
    • 0025964131 scopus 로고
    • Reversible binding of peptide aldehydes to papain. Structure-activity relationships
    • Hanzlik, R. P.; Jacober, S. P.; Zygmunt, J. Reversible binding of peptide aldehydes to papain. Structure-activity relationships. Biochim. Biophys. Acta, 1991, 1073, 33-42.
    • (1991) Biochim. Biophys. Acta , vol.1073 , pp. 33-42
    • Hanzlik, R.P.1    Jacober, S.P.2    Zygmunt, J.3
  • 157
    • 0029146471 scopus 로고
    • Peptide aldehydes and nitriles as transition state analog inhibitors of cysteine proteases
    • Dufour, É.; Storer, A. C.; Ménard, R. Peptide aldehydes and nitriles as transition state analog inhibitors of cysteine proteases. Biochemistry, 1995, 34, 9136-9143.
    • (1995) Biochemistry , vol.34 , pp. 9136-9143
    • Dufour, E.1    Storer, A.C.2    Ménard, R.3
  • 159
    • 33847800887 scopus 로고
    • The hard soft acids bases (HSAB) principle and organic chemistry
    • Ho, T.-L. The hard soft acids bases (HSAB) principle and organic chemistry. Chem. Rev., 1975, 75, 2-20.
    • (1975) Chem. Rev , vol.75 , pp. 2-20
    • Ho, T.-L.1
  • 160
    • 0018118260 scopus 로고
    • Biochemical significance of the hard and soft acids ad bases principle
    • Ho, T.-L.; Ho, H. C.; Hamilton, L. D. Biochemical significance of the hard and soft acids ad bases principle. Chem. Biol. Interact., 1978, 23, 65-84.
    • (1978) Chem. Biol. Interact , vol.23 , pp. 65-84
    • Ho, T.-L.1    Ho, H.C.2    Hamilton, L.D.3
  • 161
    • 33947690115 scopus 로고    scopus 로고
    • Discovery of JANUVIA (sitagliptin), a selective dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes
    • Thornberry, N. A.; Weber, A. E. Discovery of JANUVIA (sitagliptin), a selective dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes. Curr. Top. Med. Chem., 2007, 7, 557-568.
    • (2007) Curr. Top. Med. Chem , vol.7 , pp. 557-568
    • Thornberry, N.A.1    Weber, A.E.2
  • 162
    • 20444406121 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl-peptidase IV catalyzed peptide truncation by Vildagliptin ((2S)-{[(3-hydroxyadamantan-1-yl)amino] acetyl}-pyrrolidine-2-carbonitrile)
    • Brandt, I.; Joossens, J.; Chen, X.; Maes, M.-B.; Scharpé, S.; De Meester, I.; Lambeir, A.-M. Inhibition of dipeptidyl-peptidase IV catalyzed peptide truncation by Vildagliptin ((2S)-{[(3-hydroxyadamantan-1-yl)amino] acetyl}-pyrrolidine-2-carbonitrile). Biochem. Pharmacol., 2005, 70, 134-143.
    • (2005) Biochem. Pharmacol , vol.70 , pp. 134-143
    • Brandt, I.1    Joossens, J.2    Chen, X.3    Maes, M.-B.4    Scharpé, S.5    De Meester, I.6    Lambeir, A.-M.7
  • 164
    • 0025345455 scopus 로고
    • Reversible covalent binding of peptide nitriles to papain
    • Hanzlik, R. P.; Zygmunt J.; Moon, J. B. Reversible covalent binding of peptide nitriles to papain. Biochim. Biophys. Acta, 1990, 1035, 62-70.
    • (1990) Biochim. Biophys. Acta , vol.1035 , pp. 62-70
    • Hanzlik, R.P.1    Zygmunt, J.2    Moon, J.B.3
  • 165
    • 0029590248 scopus 로고
    • Engineering nitrile hydratase activity into a cysteine protease by a single mutation
    • Dufour, É.; Storer, A. C.; Ménard, R. Engineering nitrile hydratase activity into a cysteine protease by a single mutation. Biochemistry, 1995, 34, 16382-16388.
    • (1995) Biochemistry , vol.34 , pp. 16382-16388
    • Dufour, E.1    Storer, A.C.2    Ménard, R.3
  • 166
    • 0037025152 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of nitriles by an engineered nitrile hydratase (papain Gln19Glu) in aqueous-organic media
    • Versari, A.; Ménard, R.; Lortie, R. Enzymatic hydrolysis of nitriles by an engineered nitrile hydratase (papain Gln19Glu) in aqueous-organic media. Biotechnol. Bioeng., 2002, 79, 9-14.
    • (2002) Biotechnol. Bioeng , vol.79 , pp. 9-14
    • Versari, A.1    Ménard, R.2    Lortie, R.3
  • 167
    • 0037032292 scopus 로고    scopus 로고
    • Protein engineering of nitrile hydratase activity of papain: Molecular dynamics study of a mutant and wild-type enzyme
    • Reddy, S. Y.; Kahn, K.; Zheng, Y. J.; Bruice, T. C. Protein engineering of nitrile hydratase activity of papain: molecular dynamics study of a mutant and wild-type enzyme. J. Am. Chem. Soc., 2002, 124, 12979-12990.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 12979-12990
    • Reddy, S.Y.1    Kahn, K.2    Zheng, Y.J.3    Bruice, T.C.4
  • 168
    • 0026156265 scopus 로고
    • Inhibition of papain by peptide nitriles: Reactions of external nucleophiles with the thioimidate ester adduct
    • Gour-Salin, B. J.; Storer, A. C.; Castelhano, A.; Krantz, A.; Robinson, V. Inhibition of papain by peptide nitriles: reactions of external nucleophiles with the thioimidate ester adduct. Enzyme Microb. Technol., 1991, 13, 408-411.
    • (1991) Enzyme Microb. Technol , vol.13 , pp. 408-411
    • Gour-Salin, B.J.1    Storer, A.C.2    Castelhano, A.3    Krantz, A.4    Robinson, V.5
  • 171
    • 8644276353 scopus 로고    scopus 로고
    • Novel purine nitrile derived inhibitors of the cysteine protease cathepsin K
    • Altmann, E.; Cowan-Jacob, S. W.; Missbach, M. Novel purine nitrile derived inhibitors of the cysteine protease cathepsin K. J. Med. Chem., 2004, 47, 5833-5836.
    • (2004) J. Med. Chem , vol.47 , pp. 5833-5836
    • Altmann, E.1    Cowan-Jacob, S.W.2    Missbach, M.3
  • 172
    • 33846640469 scopus 로고    scopus 로고
    • Oballa, R. M.; Truchon, J. F.; Bayly, C. I.; Chauret, N.; Day, S.; Crane, S.; Berthelette, C. A. generally applicable method for assessing the electrophilicity and reactivity of diverse nitrile-containing compounds. Bioorg. Med. Chem. Lett., 2007, 17, 998-1002.
    • Oballa, R. M.; Truchon, J. F.; Bayly, C. I.; Chauret, N.; Day, S.; Crane, S.; Berthelette, C. A. generally applicable method for assessing the electrophilicity and reactivity of diverse nitrile-containing compounds. Bioorg. Med. Chem. Lett., 2007, 17, 998-1002.
  • 173
    • 59849088616 scopus 로고    scopus 로고
    • A simple in vitro assay for assessing the reactivity of nitrile containing compounds
    • MacFaul, P. A.; Morley, A. D.; Crawford, J. J. A simple in vitro assay for assessing the reactivity of nitrile containing compounds. Bioorg. Med. Chem. Lett., 2009, 19, 1136-1138.
    • (2009) Bioorg. Med. Chem. Lett , vol.19 , pp. 1136-1138
    • MacFaul, P.A.1    Morley, A.D.2    Crawford, J.J.3
  • 174
    • 34547506020 scopus 로고    scopus 로고
    • Identification and characterization of 3-substituted pyrazolyl esters as alternate substrates for cathepsin B: The confounding effects of DTT and cysteine in biological assays
    • Myers, M. C.; Napper, A. D.; Motlekar, N.; Shah, P. P.; Chiu, C.-H.; Beavers, M. P.; Diamond, S. L.; Huryna, D. M.; Smith, A. B. III, Identification and characterization of 3-substituted pyrazolyl esters as alternate substrates for cathepsin B: the confounding effects of DTT and cysteine in biological assays. Bioorg. Med. Chem. Lett., 2007, 17, 4761-4766.
    • (2007) Bioorg. Med. Chem. Lett , vol.17 , pp. 4761-4766
    • Myers, M.C.1    Napper, A.D.2    Motlekar, N.3    Shah, P.P.4    Chiu, C.-H.5    Beavers, M.P.6    Diamond, S.L.7    Huryna, D.M.8    Smith III, A.B.9
  • 176
    • 0025259410 scopus 로고
    • Inhibition of bovine cathepsin B by amino acid-derived nitriles
    • Picken, P. P.; Guthrie, D. J. S.; Walker, B. Inhibition of bovine cathepsin B by amino acid-derived nitriles. Biochem. Soc. Trans., 1990, 18, 316.
    • (1990) Biochem. Soc. Trans , vol.18 , pp. 316
    • Picken, P.P.1    Guthrie, D.J.S.2    Walker, B.3
  • 177
    • 0021103783 scopus 로고
    • An exploration of the primary specificity site of cathepsin B
    • Shaw, E.; Wilkstrom, P.; Ruscica, J. An exploration of the primary specificity site of cathepsin B. Arch. Biochem. Biophys., 1983, 222, 424-429.
    • (1983) Arch. Biochem. Biophys , vol.222 , pp. 424-429
    • Shaw, E.1    Wilkstrom, P.2    Ruscica, J.3
  • 179
    • 0037028023 scopus 로고    scopus 로고
    • Ward, Y. D.; Thomson, D. S.; Frye, L. L.; Cywin, C. L.; Morwick, T.; Emmanuel, M. J.: Zindell, R.; McNeil, D.; Bekkali, Y.; Giradot, M.: Hrapchak, M.; DeTuri, M.; Crane, K.; White, D.; Pav, S.; Wang, Y.; Hao, M. H.; Grygon, C. A.; Labadia, M. E.; Freeman, D. M.; Davidson, W.; Hopkins, J. L.; Brown, M. L.; Spero, D. M. Design and synthesis of dipeptide nitriles as reversible and potent cathepsin S inhibitors. J. Med. Chem., 2002, 45, 5471-5482.
    • Ward, Y. D.; Thomson, D. S.; Frye, L. L.; Cywin, C. L.; Morwick, T.; Emmanuel, M. J.: Zindell, R.; McNeil, D.; Bekkali, Y.; Giradot, M.: Hrapchak, M.; DeTuri, M.; Crane, K.; White, D.; Pav, S.; Wang, Y.; Hao, M. H.; Grygon, C. A.; Labadia, M. E.; Freeman, D. M.; Davidson, W.; Hopkins, J. L.; Brown, M. L.; Spero, D. M. Design and synthesis of dipeptide nitriles as reversible and potent cathepsin S inhibitors. J. Med. Chem., 2002, 45, 5471-5482.
  • 180
    • 28144443719 scopus 로고    scopus 로고
    • Interaction of papain-like cysteine proteases with dipeptide-derived nitriles
    • Löser, R.; Schilling, K.; Dimmig, E.; Gütschow, M. Interaction of papain-like cysteine proteases with dipeptide-derived nitriles. J. Med. Chem., 2005, 48, 7688-7707.
    • (2005) J. Med. Chem , vol.48 , pp. 7688-7707
    • Löser, R.1    Schilling, K.2    Dimmig, E.3    Gütschow, M.4
  • 181
    • 34047228186 scopus 로고    scopus 로고
    • Microplate assay for quantitative determination of cathepsin activities in viable cells using derivatives of 4-methoxy-beta-naphthylamide
    • Rüttger, A.; Mollenhauer, J.; Löser, R.; Gütschow, M.; Wiederanders, B. Microplate assay for quantitative determination of cathepsin activities in viable cells using derivatives of 4-methoxy-beta-naphthylamide. Biotechniques, 2006, 41, 469-473.
    • (2006) Biotechniques , vol.41 , pp. 469-473
    • Rüttger, A.1    Mollenhauer, J.2    Löser, R.3    Gütschow, M.4    Wiederanders, B.5
  • 182
    • 38149135837 scopus 로고    scopus 로고
    • Cathepsins B, K, and L are regulated by a defined collagen type II peptide via activation of classical protein kinase C and p38 MAP kinase in articular chondrocytes
    • Ruettger, A.; Schueler, S.; Mollenhauer, J. A.; Wiederanders, B. Cathepsins B, K, and L are regulated by a defined collagen type II peptide via activation of classical protein kinase C and p38 MAP kinase in articular chondrocytes. J. Biol. Chem., 2008, 283, 1043-1051.
    • (2008) J. Biol. Chem , vol.283 , pp. 1043-1051
    • Ruettger, A.1    Schueler, S.2    Mollenhauer, J.A.3    Wiederanders, B.4
  • 183
    • 33750125526 scopus 로고    scopus 로고
    • Identification of selective, nonpeptidic nitrile inhibitors of cathepsin S using the substrate activity screening method
    • Patterson, A. W.; Wood, W. J.; Hornsby, M.; Lesley, S.; Spraggon, G.; Ellman, J. A. Identification of selective, nonpeptidic nitrile inhibitors of cathepsin S using the substrate activity screening method. J. Med. Chem., 2006, 49, 6298-6307.
    • (2006) J. Med. Chem , vol.49 , pp. 6298-6307
    • Patterson, A.W.1    Wood, W.J.2    Hornsby, M.3    Lesley, S.4    Spraggon, G.5    Ellman, J.A.6
  • 184
    • 27644555726 scopus 로고    scopus 로고
    • Substrate activity screening: A fragment-based method for the rapid identification of nonpeptidic protease inhibitors
    • Wood, W. J. L.; Patterson, A. W.; Tsuruoka, H.; Jain, R. K.; Ellman, J. A. Substrate activity screening: a fragment-based method for the rapid identification of nonpeptidic protease inhibitors. J. Am. Chem. Soc., 2005, 127, 15521-15527.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 15521-15527
    • Wood, W.J.L.1    Patterson, A.W.2    Tsuruoka, H.3    Jain, R.K.4    Ellman, J.A.5
  • 188
    • 46749119861 scopus 로고    scopus 로고
    • Azadipeptide nitriles: Highly potent and proteolytically stable inhibitors of papain-like cysteine proteases
    • Löser, R.; Frizler, M.; Schilling, K.; Gütschow, M. Azadipeptide nitriles: highly potent and proteolytically stable inhibitors of papain-like cysteine proteases. Angew. Chem. Int. Ed., 2008, 47, 4331-4334.
    • (2008) Angew. Chem. Int. Ed , vol.47 , pp. 4331-4334
    • Löser, R.1    Frizler, M.2    Schilling, K.3    Gütschow, M.4
  • 193
    • 0036332842 scopus 로고    scopus 로고
    • Peptidic 1-cyanopyrrolidines: Synthesis and SAR of a series of potent, selective cathepsin inhibitors
    • Rydzewski, R. M.; Bryant, C.; Oballa, R.; Wesolowski, G.; Rodan, S. B.; Bass, K. E.; Wong, D. H. Peptidic 1-cyanopyrrolidines: synthesis and SAR of a series of potent, selective cathepsin inhibitors. Bioorg. Med. Chem., 2002, 10, 3277-3284.
    • (2002) Bioorg. Med. Chem , vol.10 , pp. 3277-3284
    • Rydzewski, R.M.1    Bryant, C.2    Oballa, R.3    Wesolowski, G.4    Rodan, S.B.5    Bass, K.E.6    Wong, D.H.7
  • 196
    • 28144433007 scopus 로고    scopus 로고
    • Palmer, J. T.; Bryant, C.; Wang, D. X.; Davis, D. E.; Setti, E. L.; Rydzewski, R. M.; Venkatraman, S.; Tian, Z. Q.; Burrill, L. C.; Mendonca, R. V.; Springman, E.; McCarter, J.; Chung, T.; Cheung, H.; Janc, J. W.; McGrath, M.; Somoza, J. R.; Enriquez, P.; Yu, Z. W.; Strickley, R. M.; Liu, L.; Venuti, M. C.; Percival, M. D.; Falgueyret, J. P.; Prasit, P.; Oballa, R.; Riendeau, D.; Young, R. N.; Wesolowski, G.; Rodan, S. B.; Johnson, C.; Kimmel, D. B.; Rodan, G. Design and synthesis of tri-ring P3 benzamide-containing aminonitriles as potent, selective, orally effective inhibitors of cathepsin K. J. Med. Chem., 2005, 48, 7520-7534.
    • Palmer, J. T.; Bryant, C.; Wang, D. X.; Davis, D. E.; Setti, E. L.; Rydzewski, R. M.; Venkatraman, S.; Tian, Z. Q.; Burrill, L. C.; Mendonca, R. V.; Springman, E.; McCarter, J.; Chung, T.; Cheung, H.; Janc, J. W.; McGrath, M.; Somoza, J. R.; Enriquez, P.; Yu, Z. W.; Strickley, R. M.; Liu, L.; Venuti, M. C.; Percival, M. D.; Falgueyret, J. P.; Prasit, P.; Oballa, R.; Riendeau, D.; Young, R. N.; Wesolowski, G.; Rodan, S. B.; Johnson, C.; Kimmel, D. B.; Rodan, G. Design and synthesis of tri-ring P3 benzamide-containing aminonitriles as potent, selective, orally effective inhibitors of cathepsin K. J. Med. Chem., 2005, 48, 7520-7534.
  • 199
    • 38749144762 scopus 로고    scopus 로고
    • Gauthier, J. Y.; Chauret, N.; Cromlish, W.; Desmarais, S.; Duong le, T:, Falgueyret, J. P.; Kimmel, D. B.; Lamontagne, S.; Léger, S.; LeRiche, T.; Li, C. S.; Massé, F.; McKay, D. J.; Nicoll-Griffith, D. A.; Oballa, R. M.; Palmer, J. T.; Percival, M. D.; Riendeau, D.; Robichaud, J.; Rodan, G. A.; Rodan, S. B.; Seto, C.; Thérien, M.; Truong, V. L.; Venuti, M. C.; Wesolowski, G.; Young, R. N.; Zamboni, R.; Black, W. C. The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K. Bioorg. Med. Chem. Lett., 2008, 18, 923-928.
    • Gauthier, J. Y.; Chauret, N.; Cromlish, W.; Desmarais, S.; Duong le, T:, Falgueyret, J. P.; Kimmel, D. B.; Lamontagne, S.; Léger, S.; LeRiche, T.; Li, C. S.; Massé, F.; McKay, D. J.; Nicoll-Griffith, D. A.; Oballa, R. M.; Palmer, J. T.; Percival, M. D.; Riendeau, D.; Robichaud, J.; Rodan, G. A.; Rodan, S. B.; Seto, C.; Thérien, M.; Truong, V. L.; Venuti, M. C.; Wesolowski, G.; Young, R. N.; Zamboni, R.; Black, W. C. The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K. Bioorg. Med. Chem. Lett., 2008, 18, 923-928.
  • 200
    • 77949458551 scopus 로고    scopus 로고
    • Molecular Operating Environment (MOE), Chemical Computing Group, Montreal, Canada. 2007.
    • Molecular Operating Environment (MOE), Chemical Computing Group, Montreal, Canada. 2007.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.