메뉴 건너뛰기




Volumn 62, Issue 5, 2010, Pages 563-576

Proteases implicated in apoptosis: Old and new

Author keywords

Apoptosis; Diphenyl phosphonate; Protease; Proteolytic; Serine

Indexed keywords

ASPARTIC PROTEINASE; AUTOPHAGY PROTEIN 5; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CALPAIN; CALPASTATIN; CASPASE; CASPASE INHIBITOR; CATHEPSIN; CYSTATIN; CYSTEINE PROTEINASE; GRANZYME A; GRANZYME B; LACTACYSTIN; METALLOPROTEINASE; PROTEASOME; PROTEINASE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SERINE PROTEINASE OMI; STEFIN; THREONINE PROTEINASE; THROMBIN; X LINKED INHIBITOR OF APOPTOSIS;

EID: 84940570573     PISSN: 00223573     EISSN: None     Source Type: Journal    
DOI: 10.1211/jpp.62.05.0002     Document Type: Review
Times cited : (19)

References (148)
  • 1
    • 0030016329 scopus 로고    scopus 로고
    • Apoptosis induction resulting from Proteasome inhibition
    • Shinohara K et al. Apoptosis induction resulting from Proteasome inhibition. J Biochem 1996 317 : 385 388.
    • (1996) J Biochem , vol.317 , pp. 385-388
    • Shinohara, K.1
  • 2
    • 0032512622 scopus 로고    scopus 로고
    • Protease inhibitors protect macrophages from lipopolysaccharide-induced cytotoxicity: Possible role for NF- kappa B
    • Abate A, Schroder H. Protease inhibitors protect macrophages from lipopolysaccharide-induced cytotoxicity: possible role for NF- kappa B. Life Sci 1998 62 : 1081 1088.
    • (1998) Life Sci , vol.62 , pp. 1081-1088
    • Abate, A.1    Schroder, H.2
  • 3
    • 0036753558 scopus 로고    scopus 로고
    • In situ activation of caspases and serine proteases during apoptosis detected by affinity labeling their enzyme active centers with fluorochrome-tagged inhibitors
    • Grabarek J, Darzynkiewicz Z. In situ activation of caspases and serine proteases during apoptosis detected by affinity labeling their enzyme active centers with fluorochrome-tagged inhibitors. Exp Hematol 2002 30 : 982 989.
    • (2002) Exp Hematol , vol.30 , pp. 982-989
    • Grabarek, J.1    Darzynkiewicz, Z.2
  • 4
    • 0041825824 scopus 로고    scopus 로고
    • A novel serine protease predominately expressed in macrophages
    • Chen C et al. A novel serine protease predominately expressed in macrophages. J Biochem 2003 374 : 97 107.
    • (2003) J Biochem , vol.374 , pp. 97-107
    • Chen, C.1
  • 5
    • 27944454061 scopus 로고    scopus 로고
    • Characterization of a serine protease-mediated cell death program activated in human leukemia cells
    • O'Connell AR et al. Characterization of a serine protease-mediated cell death program activated in human leukemia cells. Exp Cell Res 2006 312 : 27 39.
    • (2006) Exp Cell Res , vol.312 , pp. 27-39
    • O'Connell, A.R.1
  • 8
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • Chapman HA et al. 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
  • 9
    • 0029060166 scopus 로고
    • Proteasome from Thermoplasma acidophilum: A threonine protease
    • Seemuller E et al. Proteasome from Thermoplasma acidophilum: a threonine protease. Science 1995 268 : 579.
    • (1995) Science , vol.268 , pp. 579
    • Seemuller, E.1
  • 10
  • 12
    • 0642345204 scopus 로고    scopus 로고
    • In the cut and thrust of apoptosis, serine proteases come of age
    • Stenson-Cox C et al. In the cut and thrust of apoptosis, serine proteases come of age. Biochem Pharmacol 2003 66 : 1469 1474.
    • (2003) Biochem Pharmacol , vol.66 , pp. 1469-1474
    • Stenson-Cox, C.1
  • 14
    • 0029962944 scopus 로고    scopus 로고
    • Conservation and variability in the structures of serine proteinases of the chymotrypsin family
    • Lesk AM, Fordham WD. Conservation and variability in the structures of serine proteinases of the chymotrypsin family. J Mol Biol 1996 258 : 501 537.
    • (1996) J Mol Biol , vol.258 , pp. 501-537
    • Lesk, A.M.1    Fordham, W.D.2
  • 15
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona JJ, Craik CS. Structural basis of substrate specificity in the serine proteases. Protein Sci 1995 4 : 337 360.
    • (1995) Protein Sci , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 16
    • 0032250184 scopus 로고    scopus 로고
    • Serpins and regulation of cell death
    • Bird PI. Serpins and regulation of cell death. Results Probl Cell Differ 1998 24 : 63 89.
    • (1998) Results Probl Cell Differ , vol.24 , pp. 63-89
    • Bird, P.I.1
  • 17
    • 0035500490 scopus 로고    scopus 로고
    • The many faces of metalloproteases: Cell growth, invasion, angiogenesis and metastasis
    • Chang C, Werb Z. The many faces of metalloproteases: cell growth, invasion, angiogenesis and metastasis. Trends Cell Biol 2001 11 : S37 43.
    • (2001) Trends Cell Biol , vol.11 , pp. 37-43
    • Chang, C.1    Werb, Z.2
  • 18
    • 0028073883 scopus 로고
    • The role of matrix metalloproteases and their inhibitors in tumour invasion, metastasis and angiogenesis
    • Ray JM, Stetler-Stevenson WG. The role of matrix metalloproteases and their inhibitors in tumour invasion, metastasis and angiogenesis. Eur Respir J 1994 7 : 2062 2072.
    • (1994) Eur Respir J , vol.7 , pp. 2062-2072
    • Ray, J.M.1    Stetler-Stevenson, W.G.2
  • 19
    • 0035188727 scopus 로고    scopus 로고
    • How metalloproteases regulate cell behaviour
    • Sternlicht MD, Werb Z. How metalloproteases regulate cell behaviour. Annu Rev Cell Dev Biol 2001 17 : 463 516.
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 20
    • 0023477907 scopus 로고
    • Human immunodeficiency virus protease expressed in Escherichia coli exhibits autoprocessing and specific maturation of the gag precursor
    • Debouck C et al. Human immunodeficiency virus protease expressed in Escherichia coli exhibits autoprocessing and specific maturation of the gag precursor. Proc Nat Acad Sci U S A 1987 84 : 8903 8906.
    • (1987) Proc Nat Acad Sci U S A , vol.84 , pp. 8903-8906
    • Debouck, C.1
  • 21
    • 1542723495 scopus 로고    scopus 로고
    • The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum
    • Fujinaga M et al. The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum. Proc Nat Acad Sci U S A 2004 101 : 3364 3369.
    • (2004) Proc Nat Acad Sci U S A , vol.101 , pp. 3364-3369
    • Fujinaga, M.1
  • 22
    • 4644324164 scopus 로고    scopus 로고
    • Glutamic protease distribution is limited to filamentous fungi
    • Sims AH et al. Glutamic protease distribution is limited to filamentous fungi. FEMS Microbiol Lett 2004 239 : 95 101.
    • (2004) FEMS Microbiol Lett , vol.239 , pp. 95-101
    • Sims, A.H.1
  • 23
    • 0037138438 scopus 로고    scopus 로고
    • Lysosomal proteases as potential targets for the induction of apoptotic cell death in human neuroblastomas
    • Castino R et al. Lysosomal proteases as potential targets for the induction of apoptotic cell death in human neuroblastomas. Int J Cancer 2002 97 : 775 779.
    • (2002) Int J Cancer , vol.97 , pp. 775-779
    • Castino, R.1
  • 24
    • 0033832629 scopus 로고    scopus 로고
    • Noncaspase proteases in apoptosis
    • Johnson DE. Noncaspase proteases in apoptosis. Leukemia 2000 14 : 1695 1703.
    • (2000) Leukemia , vol.14 , pp. 1695-1703
    • Johnson, D.E.1
  • 25
    • 0032806132 scopus 로고    scopus 로고
    • Ionizing radiation-induced, Bax-mediated cell death is dependent on activation of cysteine and serine proteases
    • Gong B et al. Ionizing radiation-induced, Bax-mediated cell death is dependent on activation of cysteine and serine proteases. Cell Growth Diff 1999 10 : 491 502.
    • (1999) Cell Growth Diff , vol.10 , pp. 491-502
    • Gong, B.1
  • 26
    • 0141893341 scopus 로고    scopus 로고
    • Serine proteases mediate apoptosis-like cell death and phagocytosis under caspase-inhibiting conditions
    • Egger L et al. Serine proteases mediate apoptosis-like cell death and phagocytosis under caspase-inhibiting conditions. Cell Death Diff 2003 10 : 1188 1203.
    • (2003) Cell Death Diff , vol.10 , pp. 1188-1203
    • Egger, L.1
  • 27
    • 33749162486 scopus 로고    scopus 로고
    • Calpain-mediated cleavage of Atg5 switches autophagy to apoptosis
    • Yousefi S et al. Calpain-mediated cleavage of Atg5 switches autophagy to apoptosis. Nat Cell Biol 2006 8 : 1124 1132.
    • (2006) Nat Cell Biol , vol.8 , pp. 1124-1132
    • Yousefi, S.1
  • 28
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: A potential molecular basis for neuronal degeneration
    • Saito K et al. Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. Proc Natl Acad Sci U S A 1993 90 : 2628 2632.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2628-2632
    • Saito, K.1
  • 29
    • 0029782494 scopus 로고    scopus 로고
    • Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha
    • Deiss LP et al. Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha. EMBO J 1996 15 : 3861 3870.
    • (1996) EMBO J , vol.15 , pp. 3861-3870
    • Deiss, L.P.1
  • 30
    • 0032580334 scopus 로고    scopus 로고
    • Potential role for cathepsin D in p53-dependent tumor suppression and chemosensitivity
    • Wu GS et al. Potential role for cathepsin D in p53-dependent tumor suppression and chemosensitivity. Oncogene 1998 16 : 2177 2183.
    • (1998) Oncogene , vol.16 , pp. 2177-2183
    • Wu, G.S.1
  • 31
    • 0032500842 scopus 로고    scopus 로고
    • Participation of cathepsins B and D in apoptosis of PC12 cells following serum deprivation
    • Shibata M et al. Participation of cathepsins B and D in apoptosis of PC12 cells following serum deprivation. Biochem Biophys Res Commun 1998 251 : 199 203.
    • (1998) Biochem Biophys Res Commun , vol.251 , pp. 199-203
    • Shibata, M.1
  • 32
    • 0033756474 scopus 로고    scopus 로고
    • Cathepsin B contributes to TNF-α-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c
    • Guicciardi ME et al. Cathepsin B contributes to TNF-α-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c. J Clin Invest 2000 106 : 1127 1137.
    • (2000) J Clin Invest , vol.106 , pp. 1127-1137
    • Guicciardi, M.E.1
  • 33
    • 0034025876 scopus 로고    scopus 로고
    • Z-Phe-Gly-NHO-Bz, an inhibitor of cysteine cathepsins, induces apoptosis in human cancer cells
    • Zhu D-M, Uckun FM. Z-Phe-Gly-NHO-Bz, an inhibitor of cysteine cathepsins, induces apoptosis in human cancer cells. Clin Cancer Res 2000 6 : 2064 2069.
    • (2000) Clin Cancer Res , vol.6 , pp. 2064-2069
    • Zhu, D.-M.1    Uckun, F.M.2
  • 34
    • 0034739734 scopus 로고    scopus 로고
    • Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates
    • Yamashima T. Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates. Prog Neurobiol 2000 62 : 273 295.
    • (2000) Prog Neurobiol , vol.62 , pp. 273-295
    • Yamashima, T.1
  • 35
    • 0028959720 scopus 로고
    • Cathepsin B in predicting the extent of the cervix carcinoma
    • Makarewicz R et al. Cathepsin B in predicting the extent of the cervix carcinoma. Neoplasma 1995 42 : 21 24.
    • (1995) Neoplasma , vol.42 , pp. 21-24
    • Makarewicz, R.1
  • 36
    • 0029838059 scopus 로고    scopus 로고
    • Biological and clinical significance of cathepsin D in breast cancer metastasis
    • Garcia M et al. Biological and clinical significance of cathepsin D in breast cancer metastasis. Stem Cells 1996 14 : 642 650.
    • (1996) Stem Cells , vol.14 , pp. 642-650
    • Garcia, M.1
  • 37
    • 0037969805 scopus 로고    scopus 로고
    • The clinical significance of cathepsin S expression in human astrocytomas
    • Flannery T et al. The clinical significance of cathepsin S expression in human astrocytomas. Am J Pathol 2003 163 : 175 182.
    • (2003) Am J Pathol , vol.163 , pp. 175-182
    • Flannery, T.1
  • 38
    • 33745918920 scopus 로고    scopus 로고
    • Cathepsin S expression: An independent prognostic factor in glioblastoma tumours - A pilot study
    • Flannery T et al. Cathepsin S expression: an independent prognostic factor in glioblastoma tumours-a pilot study. Int J Cancer 2006 119 : 854 860.
    • (2006) Int J Cancer , vol.119 , pp. 854-860
    • Flannery, T.1
  • 39
    • 20044383567 scopus 로고    scopus 로고
    • Involvement of cathepsin D in chemotherapy-induced cytochrome c release, caspase activation, and cell death
    • Emert-Sedlak L et al. Involvement of cathepsin D in chemotherapy-induced cytochrome c release, caspase activation, and cell death. Mol Cancer Ther 2005 4 : 733 742.
    • (2005) Mol Cancer Ther , vol.4 , pp. 733-742
    • Emert-Sedlak, L.1
  • 40
    • 0028947294 scopus 로고
    • Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system
    • Cataldo AM et al. Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: evidence for early up-regulation of the endosomal-lysosomal system. Neuron 1995 14 : 671 680.
    • (1995) Neuron , vol.14 , pp. 671-680
    • Cataldo, A.M.1
  • 41
    • 0030862412 scopus 로고    scopus 로고
    • Cathepsin B contributes to bile salt-induced apoptosis of rat hepatocytes
    • Roberts LR et al. Cathepsin B contributes to bile salt-induced apoptosis of rat hepatocytes. Gastroenterology 1997 113 : 1714 1726.
    • (1997) Gastroenterology , vol.113 , pp. 1714-1726
    • Roberts, L.R.1
  • 42
    • 0037062449 scopus 로고    scopus 로고
    • Neuronal loss and brain atrophy in mice lacking cathepsins B and L
    • Felbor U et al. Neuronal loss and brain atrophy in mice lacking cathepsins B and L. Proc Natl Acad Sci U S A 2002 99 : 7883 7888.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 7883-7888
    • Felbor, U.1
  • 43
    • 2142773262 scopus 로고    scopus 로고
    • Cathepsin-dependent apoptosis triggered by supraoptimal activation of T lymphocytes: A possible mechanism of high dose tolerance
    • Michallet MC et al. Cathepsin-dependent apoptosis triggered by supraoptimal activation of T lymphocytes: a possible mechanism of high dose tolerance. J Immunol 2004 172 : 5405 5414.
    • (2004) J Immunol , vol.172 , pp. 5405-5414
    • Michallet, M.C.1
  • 44
    • 17344370810 scopus 로고    scopus 로고
    • Uptake of oxidized LDL by macrophages results in partial lysosomal enzyme inactivation and relocation
    • Li W et al. Uptake of oxidized LDL by macrophages results in partial lysosomal enzyme inactivation and relocation. Arterioscler Thromb Vasc Biol 1998 18 : 177 184.
    • (1998) Arterioscler Thromb Vasc Biol , vol.18 , pp. 177-184
    • Li, W.1
  • 45
    • 0031897739 scopus 로고    scopus 로고
    • Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes
    • Roberg K, Ollinger K. Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes. Am J Pathol 1998 152 : 1151 1156.
    • (1998) Am J Pathol , vol.152 , pp. 1151-1156
    • Roberg, K.1    Ollinger, K.2
  • 46
    • 0031793017 scopus 로고    scopus 로고
    • Atractyloside-induced release of cathepsin B, a protease with caspase-processing activity
    • Vancompernolle K et al. Atractyloside-induced release of cathepsin B, a protease with caspase-processing activity. FEBS Lett 1998 438 : 150 158.
    • (1998) FEBS Lett , vol.438 , pp. 150-158
    • Vancompernolle, K.1
  • 47
    • 0242609099 scopus 로고    scopus 로고
    • Cathepsin D mediates cytochrome c release and caspase activation in human fibroblast apoptosis induced by staurosporine
    • Johansson AC et al. Cathepsin D mediates cytochrome c release and caspase activation in human fibroblast apoptosis induced by staurosporine. Cell Death Differ 2003 10 : 1253 1259.
    • (2003) Cell Death Differ , vol.10 , pp. 1253-1259
    • Johansson, A.C.1
  • 48
    • 34247849157 scopus 로고    scopus 로고
    • Cathepsin-cleaved Bid promotes apoptosis in human neutrophils via oxidative stress-induced lysosomal membrane permeabilization
    • Blomgran R et al. Cathepsin-cleaved Bid promotes apoptosis in human neutrophils via oxidative stress-induced lysosomal membrane permeabilization. J Leukocyte Biol 2007 81 : 1213 1223.
    • (2007) J Leukocyte Biol , vol.81 , pp. 1213-1223
    • Blomgran, R.1
  • 49
    • 0023905240 scopus 로고
    • Identification of latent procathepsins B and L in microsomal lumen: Characterization of enzymatic activation and proteolytic processing in vitro
    • Nishimura Y et al. Identification of latent procathepsins B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro. Arch Biochem Biophys 1988 61 : 64 71.
    • (1988) Arch Biochem Biophys , vol.61 , pp. 64-71
    • Nishimura, Y.1
  • 50
    • 0026664252 scopus 로고
    • Rat procathepsin B. Proteolytic processing to the mature form in vitro
    • Rowan AD et al. Rat procathepsin B. Proteolytic processing to the mature form in vitro. J Biol Chem 1992 267 : 15993 15999.
    • (1992) J Biol Chem , vol.267 , pp. 15993-15999
    • Rowan, A.D.1
  • 51
    • 0035793580 scopus 로고    scopus 로고
    • Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route
    • Stoka V et al. Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route. J Biol Chem 2001 276 : 3149 3157.
    • (2001) J Biol Chem , vol.276 , pp. 3149-3157
    • Stoka, V.1
  • 52
    • 0030970351 scopus 로고    scopus 로고
    • Activation of pro-caspase-7 by serine proteases includes a non-canonical specificity
    • Zhou Q, Salvesen GS. Activation of pro-caspase-7 by serine proteases includes a non-canonical specificity. Biochem J 1997 324 : 361 364.
    • (1997) Biochem J , vol.324 , pp. 361-364
    • Zhou, Q.1    Salvesen, G.S.2
  • 53
    • 0034485661 scopus 로고    scopus 로고
    • Cathepsin inhibition induces apoptotic death in human leukemia and lymphoma cells
    • Zhu DM, Uckun FM. Cathepsin inhibition induces apoptotic death in human leukemia and lymphoma cells. Leuk Lymphoma 2000 39 : 343 354.
    • (2000) Leuk Lymphoma , vol.39 , pp. 343-354
    • Zhu, D.M.1    Uckun, F.M.2
  • 54
    • 0025817602 scopus 로고
    • The cystatins: Protein inhibitors of cysteine proteinases
    • Turk V, Bode W. The cystatins: protein inhibitors of cysteine proteinases. FEBS Lett 1991 285 : 213 219.
    • (1991) FEBS Lett , vol.285 , pp. 213-219
    • Turk, V.1    Bode, W.2
  • 55
    • 33751251999 scopus 로고    scopus 로고
    • Lysosomal destabilization contributes to apoptosis of germinal center B-lymphocytes
    • van Nierop K et al. Lysosomal destabilization contributes to apoptosis of germinal center B-lymphocytes. J Histochem Cytochem 2006 54 : 1425 1435.
    • (2006) J Histochem Cytochem , vol.54 , pp. 1425-1435
    • Van Nierop, K.1
  • 56
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • Turk B et al. Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol Chem 1997 378 : 141 150.
    • (1997) Biol Chem , vol.378 , pp. 141-150
    • Turk, B.1
  • 57
    • 0026570448 scopus 로고
    • Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin
    • Lindahl P et al. Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin. Biochem J 1992 281 : 49 55.
    • (1992) Biochem J , vol.281 , pp. 49-55
    • Lindahl, P.1
  • 58
    • 15944426682 scopus 로고    scopus 로고
    • Inhibitory properties of cystatin F and its localization in U937 promonocyte cells
    • Langerholc T et al. Inhibitory properties of cystatin F and its localization in U937 promonocyte cells. FEBS J 2005 272 : 1535 1545.
    • (2005) FEBS J , vol.272 , pp. 1535-1545
    • Langerholc, T.1
  • 59
    • 0036077458 scopus 로고    scopus 로고
    • Cysteine peptidases of mammals: Their biological roles and potential effects in the oral cavity and other tissues in health and disease
    • Dickinson DP. Cysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease. Crit Rev Oral Biol Med 2002 13 : 238 275.
    • (2002) Crit Rev Oral Biol Med , vol.13 , pp. 238-275
    • Dickinson, D.P.1
  • 60
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen GM. Caspases: the executioners of apoptosis. J Biochem 1997 326 : 1 16.
    • (1997) J Biochem , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 61
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry NA, Lazebnik Y. Caspases: enemies within. Science 1998 281 : 1312 1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 62
    • 0028168514 scopus 로고
    • Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition
    • Komiyama T et al. Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition. J Biol Chem 1994 269 : 19331 19337.
    • (1994) J Biol Chem , vol.269 , pp. 19331-19337
    • Komiyama, T.1
  • 63
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Deveraux QL et al. X-linked IAP is a direct inhibitor of cell-death proteases. Nature 1997 388 : 300 304.
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1
  • 64
    • 0030698127 scopus 로고    scopus 로고
    • The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
    • Roy N et al. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J 1997 16 : 6914 6925.
    • (1997) EMBO J , vol.16 , pp. 6914-6925
    • Roy, N.1
  • 65
    • 0029056059 scopus 로고
    • Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein
    • Xue D, Horvitz HR. Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein. Nature 1995 377 : 248 251.
    • (1995) Nature , vol.377 , pp. 248-251
    • Xue, D.1    Horvitz, H.R.2
  • 66
    • 0028817947 scopus 로고
    • Inhibition of ICE family proteases by baculovirus antiapoptotic protein p35
    • Bump NJ et al. Inhibition of ICE family proteases by baculovirus antiapoptotic protein p35. Science 1995 269 : 1885 1888.
    • (1995) Science , vol.269 , pp. 1885-1888
    • Bump, N.J.1
  • 67
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins - Suppressors of apoptosis
    • Deveraux QL, Reed JC. IAP family proteins - suppressors of apoptosis. Genes Dev 1999 13 : 239 252.
    • (1999) Genes Dev , vol.13 , pp. 239-252
    • Deveraux, Q.L.1    Reed, J.C.2
  • 68
    • 0027990727 scopus 로고
    • Control of programmed cell death by the baculovirus genes p35 and iap
    • Clem RJ, Miller LK. Control of programmed cell death by the baculovirus genes p35 and iap. Mol Cell Biol 1994 14 : 5212 5222.
    • (1994) Mol Cell Biol , vol.14 , pp. 5212-5222
    • Clem, R.J.1    Miller, L.K.2
  • 69
    • 0024413057 scopus 로고
    • ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to Ubiquitin
    • Eytan E et al. ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to Ubiquitin. Proc Natl Acad Sci U S A 1989 86 : 7751 7755.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 7751-7755
    • Eytan, E.1
  • 70
    • 0027771443 scopus 로고
    • Structural features of the 26 S proteasome complex
    • Peters JM et al. Structural features of the 26 S proteasome complex. J Mol Biol 1993 234 : 932 937.
    • (1993) J Mol Biol , vol.234 , pp. 932-937
    • Peters, J.M.1
  • 71
    • 0028234770 scopus 로고
    • Distinct 19 S and 20 S subcomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm
    • Peters JM et al. Distinct 19 S and 20 S subcomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm. J Biol Chem 1994 269 : 7709 7718.
    • (1994) J Biol Chem , vol.269 , pp. 7709-7718
    • Peters, J.M.1
  • 72
    • 33745728140 scopus 로고    scopus 로고
    • Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132
    • Crawford LJ et al. Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132. Cancer Res 2006 66 : 6379 6386.
    • (2006) Cancer Res , vol.66 , pp. 6379-6386
    • Crawford, L.J.1
  • 73
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 A resolution
    • Groll M et al. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 1997 386 : 463 471.
    • (1997) Nature , vol.386 , pp. 463-471
    • Groll, M.1
  • 74
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser M. Ubiquitin-dependent protein degradation. Ann Rev Genet 1996 30 : 405 439.
    • (1996) Ann Rev Genet , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 75
    • 0030724422 scopus 로고    scopus 로고
    • Roles of ubiquitin-mediated proteolysis in cell cycle control
    • Hershko A. Roles of ubiquitin-mediated proteolysis in cell cycle control. Curr Opin Cell Biol 1997 9 : 788 799.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 788-799
    • Hershko, A.1
  • 76
    • 0030772933 scopus 로고    scopus 로고
    • Targeting of substrates to the 26S proteasome
    • Pickart CM. Targeting of substrates to the 26S proteasome. FASEB J 1997 11 : 1055 1066.
    • (1997) FASEB J , vol.11 , pp. 1055-1066
    • Pickart, C.M.1
  • 77
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O et al. Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem 1996 65 : 801 847.
    • (1996) Annu Rev Biochem , vol.65 , pp. 801-847
    • Coux, O.1
  • 79
    • 0033563113 scopus 로고    scopus 로고
    • Inhibition of ubiquitin-proteasome pathway activates a caspase-3-like protease and induces Bcl-2 cleavage in human M-07e leukaemic cells
    • Zhang X-M et al. Inhibition of ubiquitin-proteasome pathway activates a caspase-3-like protease and induces Bcl-2 cleavage in human M-07e leukaemic cells. J Biochem 1999 340 : 127 133.
    • (1999) J Biochem , vol.340 , pp. 127-133
    • Zhang, X.-M.1
  • 80
    • 0025109563 scopus 로고
    • Proteasomes are essential for yeast proliferation. cDNA cloning and gene disruption of two major subunits
    • Fujiwara T et al. Proteasomes are essential for yeast proliferation. cDNA cloning and gene disruption of two major subunits. J Biol Chem 1990 265 : 16604 16613.
    • (1990) J Biol Chem , vol.265 , pp. 16604-16613
    • Fujiwara, T.1
  • 81
    • 0029564960 scopus 로고
    • Lactacystin, a specific inhibitor of the Proteasome, induces apoptosis in human monoblast U937 Cells
    • Imajoh-Ohmi S et al. Lactacystin, a specific inhibitor of the Proteasome, induces apoptosis in human monoblast U937 Cells. Biochem Biophys Res Commun 1995 217 : 1070 1077.
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 1070-1077
    • Imajoh-Ohmi, S.1
  • 82
    • 0029762871 scopus 로고    scopus 로고
    • Proteasomes play an essential role in thymocyte apoptosis
    • Grimm LM et al. Proteasomes play an essential role in thymocyte apoptosis. EMBO J 1996 15 : 3835 3844.
    • (1996) EMBO J , vol.15 , pp. 3835-3844
    • Grimm, L.M.1
  • 83
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G et al. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 1995 268 : 726 731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1
  • 84
    • 0036240701 scopus 로고    scopus 로고
    • The proteasome: A novel target for cancer chemotherapy
    • Almond JB, Cohen GM. The proteasome: a novel target for cancer chemotherapy. Leukemia 2002 16 : 433 443.
    • (2002) Leukemia , vol.16 , pp. 433-443
    • Almond, J.B.1    Cohen, G.M.2
  • 85
    • 0345447210 scopus 로고    scopus 로고
    • Velcade: U.S. FDA approval for the treatment of multiple myeloma progressing on prior therapy
    • Kane RC et al. Velcade: U.S. FDA approval for the treatment of multiple myeloma progressing on prior therapy. Oncologist 2003 8 : 508 513.
    • (2003) Oncologist , vol.8 , pp. 508-513
    • Kane, R.C.1
  • 86
    • 0032539571 scopus 로고    scopus 로고
    • Inhibitors of the chymotrypsin-like activity of proteasome based on di- and tri-peptidyl alpha-keto aldehydes (glyoxals)
    • Lynas JF et al. Inhibitors of the chymotrypsin-like activity of proteasome based on di- and tri-peptidyl alpha-keto aldehydes (glyoxals). Bioorg Med Chem Lett 1998 8 : 373 378.
    • (1998) Bioorg Med Chem Lett , vol.8 , pp. 373-378
    • Lynas, J.F.1
  • 87
    • 0027302689 scopus 로고
    • Peptide glyoxals: A novel class of inhibitor for serine and cysteine proteinases
    • Walker B et al. Peptide glyoxals: a novel class of inhibitor for serine and cysteine proteinases. Biochem J 1993 293 : 321 323.
    • (1993) Biochem J , vol.293 , pp. 321-323
    • Walker, B.1
  • 88
    • 0033863365 scopus 로고    scopus 로고
    • Caspase and proteasome activity during staurosporine-induced apoptosis in lens epithelial cells
    • Andersson M et al. Caspase and proteasome activity during staurosporine-induced apoptosis in lens epithelial cells. Invest. Ophthalmol Vis Sci 2000 41 : 2623 2632.
    • (2000) Invest. Ophthalmol Vis Sci , vol.41 , pp. 2623-2632
    • Andersson, M.1
  • 89
    • 0023272405 scopus 로고
    • Protection from tumor necrosis factor cytotoxicity by protease inhibitors
    • Ruggiero V et al. Protection from tumor necrosis factor cytotoxicity by protease inhibitors. Cell Immunol 1987 107 : 317 325.
    • (1987) Cell Immunol , vol.107 , pp. 317-325
    • Ruggiero, V.1
  • 90
    • 0028149332 scopus 로고
    • Apoptotic cell death induced by intracellular proteolysis
    • Williams MS, Henkart PA. Apoptotic cell death induced by intracellular proteolysis. J Immunol 1994 153 : 4247 4255.
    • (1994) J Immunol , vol.153 , pp. 4247-4255
    • Williams, M.S.1    Henkart, P.A.2
  • 91
    • 0034194258 scopus 로고    scopus 로고
    • Serine protease inhibitors suppress cytochrome c-mediated caspase-9 activation and apoptosis during hypoxia-reoxygenation
    • Dong Z et al. Serine protease inhibitors suppress cytochrome c-mediated caspase-9 activation and apoptosis during hypoxia-reoxygenation. Biochem J 2000 347 : 669 677.
    • (2000) Biochem J , vol.347 , pp. 669-677
    • Dong, Z.1
  • 92
    • 33646826676 scopus 로고    scopus 로고
    • Caspase-dependant activation of chymotrypsin-like proteases mediates nuclear events during Jurkat T cell apoptosis
    • O'Connell AR et al. Caspase-dependant activation of chymotrypsin-like proteases mediates nuclear events during Jurkat T cell apoptosis. Biochem Biophys Res Commun 2006 345 : 608 616.
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 608-616
    • O'Connell, A.R.1
  • 93
    • 7944233607 scopus 로고    scopus 로고
    • Internucleosomal DNA cleavage in apoptotic WEHI 231 cells is mediated by a chymotrypsin-like protease
    • Murn J et al. Internucleosomal DNA cleavage in apoptotic WEHI 231 cells is mediated by a chymotrypsin-like protease. Genes Cells 2004 9 : 1103 1111.
    • (2004) Genes Cells , vol.9 , pp. 1103-1111
    • Murn, J.1
  • 94
    • 0035717034 scopus 로고    scopus 로고
    • A family of lymphocyte granule serine proteases
    • Trapani, Granzymes JA. a family of lymphocyte granule serine proteases. Genome Biol 2001 2 : 3014.1 3014.7.
    • (2001) Genome Biol , vol.2 , pp. 30141-30147
    • Trapani1    Granzymes, J.A.2
  • 95
    • 0035831462 scopus 로고    scopus 로고
    • Granzyme B induces BID-mediated cytochrome c release and mitochondrial permeability transition
    • Alimonti JB et al. Granzyme B induces BID-mediated cytochrome c release and mitochondrial permeability transition. J Biol Chem 2001 276 : 6974 6982.
    • (2001) J Biol Chem , vol.276 , pp. 6974-6982
    • Alimonti, J.B.1
  • 96
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
    • Thornberry NA et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J Biol Chem 1997 272 : 17907 17911.
    • (1997) J Biol Chem , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1
  • 97
    • 0026353348 scopus 로고
    • Granzyme A binding to target cell proteins. Granzyme A binds to and cleaves nucleolin in vitro
    • Pasternack MS et al. Granzyme A binding to target cell proteins. Granzyme A binds to and cleaves nucleolin in vitro. J Biol Chem 1991 266 : 14703 14708.
    • (1991) J Biol Chem , vol.266 , pp. 14703-14708
    • Pasternack, M.S.1
  • 98
    • 0028988261 scopus 로고
    • Granzyme A is an interleukin 1 beta-converting enzyme
    • Irmler M et al. Granzyme A is an interleukin 1 beta-converting enzyme. J Exp Med 1995 181 : 1917 1922.
    • (1995) J Exp Med , vol.181 , pp. 1917-1922
    • Irmler, M.1
  • 99
    • 0024416820 scopus 로고
    • Induction of target cell DNA release by the cytotoxic T lymphocyte granule protease granzyme A
    • Hayes MP et al. Induction of target cell DNA release by the cytotoxic T lymphocyte granule protease granzyme A. J Exp Med 1989 170 : 933 946.
    • (1989) J Exp Med , vol.170 , pp. 933-946
    • Hayes, M.P.1
  • 100
    • 0030777366 scopus 로고    scopus 로고
    • Activation of CPP32-like proteases is not sufficient to trigger apoptosis: Inhibition of apoptosis by agents that suppress activation of AP24, but not CPP32-like activity
    • Wright SC et al. Activation of CPP32-like proteases is not sufficient to trigger apoptosis: inhibition of apoptosis by agents that suppress activation of AP24, but not CPP32-like activity. J Exp Med 1997 186 : 1107 1117.
    • (1997) J Exp Med , vol.186 , pp. 1107-1117
    • Wright, S.C.1
  • 101
    • 18544386724 scopus 로고    scopus 로고
    • Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction
    • Hegde R et al. Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction. J Biol Chem 2002 277 : 432 438.
    • (2002) J Biol Chem , vol.277 , pp. 432-438
    • Hegde, R.1
  • 102
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess C et al. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 1999 97 : 339 347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1
  • 103
    • 0344391918 scopus 로고    scopus 로고
    • HtrA2/Omi, a sheep in wolf's clothing
    • Vaux DL, Silke J. HtrA2/Omi, a sheep in wolf's clothing. Cell 2003 115 : 251 253.
    • (2003) Cell , vol.115 , pp. 251-253
    • Vaux, D.L.1    Silke, J.2
  • 104
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki Y et al. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol Cell 2001 8 : 613 621.
    • (2001) Mol Cell , vol.8 , pp. 613-621
    • Suzuki, Y.1
  • 105
    • 0037016686 scopus 로고    scopus 로고
    • HtrA2 promotes cell death through Its serine protease activity and its ability to antagonize Inhibitor of Apoptosis Proteins
    • Verhagen AM et al. HtrA2 promotes cell death through Its serine protease activity and its ability to antagonize Inhibitor of Apoptosis Proteins. J Biol Chem 2002 277 : 445 454.
    • (2002) J Biol Chem , vol.277 , pp. 445-454
    • Verhagen, A.M.1
  • 106
    • 0021100126 scopus 로고
    • Tripeptidyl aminopeptidase in the extralysosomal fraction of rat liver
    • Balow RM et al. Tripeptidyl aminopeptidase in the extralysosomal fraction of rat liver. J Biol Chem 1983 258 : 11622 11628.
    • (1983) J Biol Chem , vol.258 , pp. 11622-11628
    • Balow, R.M.1
  • 109
    • 0033548055 scopus 로고    scopus 로고
    • A giant protease with potential to substitute for some functions of the proteasome
    • Geier E et al. A giant protease with potential to substitute for some functions of the proteasome. Science 1999 283 : 978 981.
    • (1999) Science , vol.283 , pp. 978-981
    • Geier, E.1
  • 110
    • 0023229578 scopus 로고
    • Supramolecular structure of tripeptidyl peptidase II from human erythrocytes as studied by electron microscopy, and its correlation to enzyme activity
    • Macpherson E et al. Supramolecular structure of tripeptidyl peptidase II from human erythrocytes as studied by electron microscopy, and its correlation to enzyme activity. Biochem J 1987 248 : 259 263.
    • (1987) Biochem J , vol.248 , pp. 259-263
    • MacPherson, E.1
  • 111
    • 77952757807 scopus 로고    scopus 로고
    • Tripeptidyl-peptidase II
    • 2nd edn. Barrett, A.J.*et al. eds.
    • Tomkinson, B. Tripeptidyl-peptidase II. In : Barrett AJ et al., eds. Handbook of Proteolytic Enzymes, 2nd edn.
    • Handbook of Proteolytic Enzymes
    • Tomkinson, B.1
  • 112
    • 0035097842 scopus 로고    scopus 로고
    • C-myc overexpression activates alternative pathways for intracellular proteolysis in lymphoma cells
    • Gavioli R et al. c-myc overexpression activates alternative pathways for intracellular proteolysis in lymphoma cells. Nat Cell Biol 2001 3 : 283 288.
    • (2001) Nat Cell Biol , vol.3 , pp. 283-288
    • Gavioli, R.1
  • 113
    • 0036036450 scopus 로고    scopus 로고
    • Tripeptidyl-peptidase II expression and activity are increased in skeletal muscle during sepsis
    • Wray CJ et al. Tripeptidyl-peptidase II expression and activity are increased in skeletal muscle during sepsis. Biochem Biophys Res Commun 2002 296 : 41 47.
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 41-47
    • Wray, C.J.1
  • 114
    • 0036295676 scopus 로고    scopus 로고
    • Molecular regulation of muscle cachexia: It may be more than the proteasome
    • Hasselgren PO et al. Molecular regulation of muscle cachexia: it may be more than the proteasome. Biochem Biophys Res Commun 2002 290 : 1 10.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 1-10
    • Hasselgren, P.O.1
  • 115
    • 12844268167 scopus 로고    scopus 로고
    • Effect of cancer cachexia on the activity of tripeptidyl-peptidase II in skeletal muscle
    • Chand A et al. Effect of cancer cachexia on the activity of tripeptidyl-peptidase II in skeletal muscle. Cancer Lett 2005 218 : 215 222.
    • (2005) Cancer Lett , vol.218 , pp. 215-222
    • Chand, A.1
  • 116
    • 0033796540 scopus 로고    scopus 로고
    • Tripeptidyl Peptidase II promotes maturation of caspase-1 in Shigella flexneri-induced macrophage apoptosis
    • Hilbi H et al. Tripeptidyl Peptidase II promotes maturation of caspase-1 in Shigella flexneri-induced macrophage apoptosis. Infect Immun 2000 68 : 5502 5508.
    • (2000) Infect Immun , vol.68 , pp. 5502-5508
    • Hilbi, H.1
  • 117
    • 0037529368 scopus 로고    scopus 로고
    • Tumors acquire inhibitor of apoptosis protein (IAP)-mediated apoptosis resistance through altered specificity of cytosolic proteolysis
    • Hong X et al. Tumors acquire inhibitor of apoptosis protein (IAP)-mediated apoptosis resistance through altered specificity of cytosolic proteolysis. J Exp Med 2003 197 : 1731 1743.
    • (2003) J Exp Med , vol.197 , pp. 1731-1743
    • Hong, X.1
  • 118
    • 1842785206 scopus 로고    scopus 로고
    • A major role for TPPII in trimming proteasomal degradation products for MHC Class i antigen presentation
    • Reits E et al. A major role for TPPII in trimming proteasomal degradation products for MHC Class I antigen presentation. Immunity 2004 20 : 495 506.
    • (2004) Immunity , vol.20 , pp. 495-506
    • Reits, E.1
  • 119
    • 33746215297 scopus 로고    scopus 로고
    • Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class i antigen presentation
    • York IA et al. Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentation. J Immunol 2006 177 : 1434 1443.
    • (2006) J Immunol , vol.177 , pp. 1434-1443
    • York, I.A.1
  • 120
    • 10744230904 scopus 로고    scopus 로고
    • AAF-cmk sensitizes tumor cells to trail-mediated apoptosis
    • Mllnarczuk I et al. AAF-cmk sensitizes tumor cells to trail-mediated apoptosis. Leuk Res 2004 28 : 53 61.
    • (2004) Leuk Res , vol.28 , pp. 53-61
    • Mllnarczuk, I.1
  • 121
    • 0036957579 scopus 로고    scopus 로고
    • Serine protease inhibitor Spi2 mediated apoptosis of olfactory neurons
    • Thiemmara V et al. Serine protease inhibitor Spi2 mediated apoptosis of olfactory neurons. Cell Death Differ 2002 9 : 1343 1351.
    • (2002) Cell Death Differ , vol.9 , pp. 1343-1351
    • Thiemmara, V.1
  • 122
    • 0014423833 scopus 로고
    • Chemical modification of papain. I. Reaction with the chloromethyl ketones of phenylalanine and lysine and with phenylmethylsulfonyl fluoride
    • Whitaker JR, Perez-Villasenor J. Chemical modification of papain. I. Reaction with the chloromethyl ketones of phenylalanine and lysine and with phenylmethylsulfonyl fluoride. Arch Biochem Biophys 1968 124 : 70 78.
    • (1968) Arch Biochem Biophys , vol.124 , pp. 70-78
    • Whitaker, J.R.1    Perez-Villasenor, J.2
  • 123
    • 0014766277 scopus 로고
    • Selective chemical modification of proteins
    • Shaw E. Selective chemical modification of proteins. Physiol Rev 1970 50 : 244 296.
    • (1970) Physiol Rev , vol.50 , pp. 244-296
    • Shaw, E.1
  • 124
    • 0033570275 scopus 로고    scopus 로고
    • Crystal structure of gingipain R: An Arg-specific bacterial cysteine proteinase with a caspase-like fold
    • Eichinger A et al. Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold. EMBO J 1999 18 : 5453 5462.
    • (1999) EMBO J , vol.18 , pp. 5453-5462
    • Eichinger, A.1
  • 125
    • 12444315984 scopus 로고    scopus 로고
    • Inhibition of papain-like cysteine proteases and legumain by "caspase-specific" inhibitors: When reaction mechanism is more important than specificity
    • Rozman-Pungerčar J et al. Inhibition of papain-like cysteine proteases and legumain by "caspase-specific" inhibitors: when reaction mechanism is more important than specificity. Cell Death Differ 2003 10 : 881 888.
    • (2003) Cell Death Differ , vol.10 , pp. 881-888
    • Rozman-Pungerčar, J.1
  • 126
    • 0016152114 scopus 로고
    • Inhibition of macromolecular synthesis in Escherichia coli by protease inhibitors. Specific reversal by glutathione of the effects of chloromethyl ketones
    • Rossman T et al. Inhibition of macromolecular synthesis in Escherichia coli by protease inhibitors. Specific reversal by glutathione of the effects of chloromethyl ketones. J Biol Chem 1974 249 : 3412 3417.
    • (1974) J Biol Chem , vol.249 , pp. 3412-3417
    • Rossman, T.1
  • 127
    • 0020641260 scopus 로고
    • Inhibition of neutrophil sulfhydryl groups by chloromethyl ketones. A mechanism for their inhibition of superoxide production
    • Tsan MF. Inhibition of neutrophil sulfhydryl groups by chloromethyl ketones. A mechanism for their inhibition of superoxide production. Biochem Biophys Res Commun 1983 112 : 671 677.
    • (1983) Biochem Biophys Res Commun , vol.112 , pp. 671-677
    • Tsan, M.F.1
  • 128
    • 0000700968 scopus 로고
    • Evidence for an active-center histidine in trypsin through use of a specific reagent, 1-chloro-3-tosylamido-7-amino-2-heptanone, the chloromethyl ketone derived from Nα-tosyl-L-lysine
    • Shaw E et al. Evidence for an active-center histidine in trypsin through use of a specific reagent, 1-chloro-3-tosylamido-7-amino-2-heptanone, the chloromethyl ketone derived from Nα-tosyl-L-lysine. Biochemistry 1965 4 : 2219 2224.
    • (1965) Biochemistry , vol.4 , pp. 2219-2224
    • Shaw, E.1
  • 129
    • 0015950980 scopus 로고
    • Affinity labelling of proteinases with tryptic specificity by peptides with C-terminal lysine chloromethyl ketone
    • Coggins JR et al. Affinity labelling of proteinases with tryptic specificity by peptides with C-terminal lysine chloromethyl ketone. Biochem J 1974 137 : 579 585.
    • (1974) Biochem J , vol.137 , pp. 579-585
    • Coggins, J.R.1
  • 130
    • 0001244705 scopus 로고
    • Direct evidence for the presence of histidine in the active center of chymotrypsin
    • Schoellmann G, Shaw E. Direct evidence for the presence of histidine in the active center of chymotrypsin. Biochemistry 1963 2 : 252 255.
    • (1963) Biochemistry , vol.2 , pp. 252-255
    • Schoellmann, G.1    Shaw, E.2
  • 131
    • 15944363451 scopus 로고    scopus 로고
    • Another biological effect of tosylphenylalanylchloromethane (TPCK): It prevents p47phox phosphorylation and translocation upon neutrophil stimulation
    • Gillibert M et al. Another biological effect of tosylphenylalanylchloromethane (TPCK): it prevents p47phox phosphorylation and translocation upon neutrophil stimulation. Biochem J 2005 386 : 549 556.
    • (2005) Biochem J , vol.386 , pp. 549-556
    • Gillibert, M.1
  • 132
    • 17144378200 scopus 로고    scopus 로고
    • Pro- and anti-apoptotic effects of an inhibitor of chymotrypsin-like serine proteases
    • King MA et al. Pro- and anti-apoptotic effects of an inhibitor of chymotrypsin-like serine proteases. Cell Cycle 2004 3 : 1566 1571.
    • (2004) Cell Cycle , vol.3 , pp. 1566-1571
    • King, M.A.1
  • 133
    • 0027255417 scopus 로고
    • Specific proteolytic cleavage of poly(ADP-ribose) polymerase: An early marker of chemotherapy-induced apoptosis
    • Kaufmann SH et al. Specific proteolytic cleavage of poly(ADP-ribose) polymerase: an early marker of chemotherapy-induced apoptosis. Cancer Res 1993 53 : 3976 3985.
    • (1993) Cancer Res , vol.53 , pp. 3976-3985
    • Kaufmann, S.H.1
  • 134
    • 0022246323 scopus 로고
    • N-alpha-Tosyl-L-lysine chloromethyl ketone and N-alpha-tosyl-L- phenylalanine chloromethyl ketone inhibit protein kinase C
    • Solomon DH et al. N-alpha-Tosyl-L-lysine chloromethyl ketone and N-alpha-tosyl-L-phenylalanine chloromethyl ketone inhibit protein kinase C. FEBS Lett 1985 190 : 342 344.
    • (1985) FEBS Lett , vol.190 , pp. 342-344
    • Solomon, D.H.1
  • 135
    • 0020491337 scopus 로고
    • Calcium-activated, phospholipid-dependent protein kinase from rat brain. Subcellular distribution, purification, and properties
    • Kikkawa U et al. Calcium-activated, phospholipid-dependent protein kinase from rat brain. Subcellular distribution, purification, and properties. J Biol Chem 1982 257 : 13341 13348.
    • (1982) J Biol Chem , vol.257 , pp. 13341-13348
    • Kikkawa, U.1
  • 136
    • 20844442967 scopus 로고    scopus 로고
    • Can application of serine protease inhibitors TPCK and TLCK provide evidence for possible involvement of serine protease Omi/HtrA2 in imatinib mesylate-induced cell death of BCR-ABL-positive human leukemia cells
    • Mlejnek P. Can application of serine protease inhibitors TPCK and TLCK provide evidence for possible involvement of serine protease Omi/HtrA2 in imatinib mesylate-induced cell death of BCR-ABL-positive human leukemia cells Leukemia 2005 19 : 1085 1087.
    • (2005) Leukemia , vol.19 , pp. 1085-1087
    • Mlejnek, P.1
  • 137
    • 0028172869 scopus 로고
    • Inducible phosphorylation of i kappa B alpha is not sufficient for its dissociation from NF-kappa B and is inhibited by protease inhibitors
    • Finco TS et al. Inducible phosphorylation of I kappa B alpha is not sufficient for its dissociation from NF-kappa B and is inhibited by protease inhibitors. Proc Natl Acad Sci U S A 1994 91 : 11884 11888.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 11884-11888
    • Finco, T.S.1
  • 138
    • 0029091469 scopus 로고
    • Protease inhibitors differentially regulate tumor necrosis factor-induced apoptosis, nuclear factor-kappa B activation, cytotoxicity, and differentiation
    • Higuchi M et al. Protease inhibitors differentially regulate tumor necrosis factor-induced apoptosis, nuclear factor-kappa B activation, cytotoxicity, and differentiation. Blood 1995 86 : 2248 2256.
    • (1995) Blood , vol.86 , pp. 2248-2256
    • Higuchi, M.1
  • 140
    • 0028557348 scopus 로고
    • Tumor necrosis factor alpha-induced phosphorylation of i kappa B alpha is a signal for its degradation but not dissociation from NF-kappa B
    • Miyamoto S et al. Tumor necrosis factor alpha-induced phosphorylation of I kappa B alpha is a signal for its degradation but not dissociation from NF-kappa B. Proc Natl Acad Sci U S A 1994 91 : 12740 12744.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 12740-12744
    • Miyamoto, S.1
  • 141
    • 0028981050 scopus 로고
    • Activation of NF-kappa B requires proteolysis of the inhibitor i kappa B-alpha: Signal-induced phosphorylation of i kappa B-alpha alone does not release active NF-kappa B
    • Lin Y et al. Activation of NF-kappa B requires proteolysis of the inhibitor I kappa B-alpha: signal-induced phosphorylation of I kappa B-alpha alone does not release active NF-kappa B. Proc Natl Acad Sci U S A 1995 92 : 552 556.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 552-556
    • Lin, Y.1
  • 142
    • 0028985190 scopus 로고
    • Phosphorylation of i kappa B alpha precedes but is not sufficient for its dissociation from NF-kappa B
    • DiDonato JA et al. Phosphorylation of I kappa B alpha precedes but is not sufficient for its dissociation from NF-kappa B. Mol Cell Biol 1995 15 : 1302 1311.
    • (1995) Mol Cell Biol , vol.15 , pp. 1302-1311
    • Didonato, J.A.1
  • 143
    • 0027367970 scopus 로고
    • Purification and characterization of a tripeptidyl peptidase i from human osteoclastomas: Evidence for its role in bone resorption
    • Page AE et al. Purification and characterization of a tripeptidyl peptidase I from human osteoclastomas: evidence for its role in bone resorption. Arch Biochem Biophys 1993 306 : 354 359.
    • (1993) Arch Biochem Biophys , vol.306 , pp. 354-359
    • Page, A.E.1
  • 144
    • 0025979246 scopus 로고
    • Irreversible inhibition of serine proteases by peptide derivatives of (alpha-aminoalkyl)phosphonate diphenyl esters
    • Oleksyszyn J, Powers JC. Irreversible inhibition of serine proteases by peptide derivatives of (alpha-aminoalkyl)phosphonate diphenyl esters. Biochemistry 1991 30 : 485 493.
    • (1991) Biochemistry , vol.30 , pp. 485-493
    • Oleksyszyn, J.1    Powers, J.C.2
  • 145
    • 0028057482 scopus 로고
    • Novel amidine-containing peptidyl phosphonates as irreversible inhibitors for blood coagulation and related serine proteases
    • Oleksyszyn J et al. Novel amidine-containing peptidyl phosphonates as irreversible inhibitors for blood coagulation and related serine proteases. J Med Chem 1994 37 : 226 231.
    • (1994) J Med Chem , vol.37 , pp. 226-231
    • Oleksyszyn, J.1
  • 146
    • 0033602521 scopus 로고    scopus 로고
    • Structure-activity relationship of diaryl phosphonate esters as potent irreversible dipeptidyl peptidase IV inhibitors
    • Belyaev A et al. Structure-activity relationship of diaryl phosphonate esters as potent irreversible dipeptidyl peptidase IV inhibitors. J Med Chem 1999 42 : 1041 1052.
    • (1999) J Med Chem , vol.42 , pp. 1041-1052
    • Belyaev, A.1
  • 147
    • 0028672813 scopus 로고
    • Amino acid and peptide phosphonate derivatives as specific inhibitors of serine peptidases
    • Oleksyszyn J, Powers JC. Amino acid and peptide phosphonate derivatives as specific inhibitors of serine peptidases. Methods Enzymol 1994 244 : 423 441.
    • (1994) Methods Enzymol , vol.244 , pp. 423-441
    • Oleksyszyn, J.1    Powers, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.