메뉴 건너뛰기




Volumn 15, Issue 1, 2002, Pages 43-51

A possible intermediate step during apoptotic execution

Author keywords

[No Author keywords available]

Indexed keywords

BENZYLOXYCARBONYLLEUCYL LEUCYL LEUCINE ALDEHYDE; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; CASPASE; DNA FRAGMENT; FAS ANTIGEN; LEUPEPTIN; MONOCLONAL ANTIBODY; PEPTIDE CHLOROMETHYL KETONE;

EID: 0036516901     PISSN: 09147470     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1749-0774.2002.tb00098.x     Document Type: Article
Times cited : (1)

References (40)
  • 1
    • 0028018268 scopus 로고
    • The ubiquitin‐proteasome proteolytic pathway
    • Ciechanover A: The ubiquitin‐proteasome proteolytic pathway. Cell 79: 13–21, 1994.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A1
  • 2
    • 0027358723 scopus 로고
    • Ubiquitin‐protein ligase in the ubiquitination of p53
    • Scheffner M, Huibregtse J M, Vierstra R.D. et al: Ubiquitin‐protein ligase in the ubiquitination of p53. Cell 75: 495–505, 1993.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M1    Huibregtse, J M2    Vierstra, R.D.3
  • 3
    • 0028985013 scopus 로고
    • Ubiquitination of the G1 cyclin Cln2p by a Cdc34p‐dependent pathway
    • Deshaies R J, Chau V, Kirschner M: Ubiquitination of the G1 cyclin Cln2p by a Cdc34p‐dependent pathway. EMBO J. 14: 303–312, 1995.
    • (1995) EMBO J. , vol.14 , pp. 303-312
    • Deshaies, R J1    Chau, V2    Kirschner, M3
  • 4
    • 0028983369 scopus 로고
    • p34Cdc28‐mediated control of Cln3 cyclin degradation
    • Yaglom J, Linskens M H K, Sadis S. et al: p34Cdc28‐mediated control of Cln3 cyclin degradation. Mol. Cell. Biol. 15: 731–741, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 731-741
    • Yaglom, J1    Linskens, M H K2    Sadis, S.3
  • 5
    • 0028171039 scopus 로고
    • G1 cyclin degradation: the PEST motif of yeast Cln2 is necessary, but not sufficient, for rapid protein turnover
    • Salama S R, Hendricks K B, Thorner J: G1 cyclin degradation: the PEST motif of yeast Cln2 is necessary, but not sufficient, for rapid protein turnover. Mol. Cell. Biol. 14: 7953–7966, 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7953-7966
    • Salama, S R1    Hendricks, K B2    Thorner, J3
  • 6
    • 0028967267 scopus 로고
    • Role of a ubiquitin‐conjugating enzyme in degradation of S‐ and M‐phase cyclins
    • Seufert W, Futcher B, Jentsch S: Role of a ubiquitin‐conjugating enzyme in degradation of S‐ and M‐phase cyclins. Nature 373: 78–81, 1995.
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W1    Futcher, B2    Jentsch, S3
  • 7
    • 0029024015 scopus 로고
    • Role of the ubiquitin‐proteasome pathway in regulating abundance of the cyclin‐dependent kinase inhibitor p27
    • Pagano M, Tarn S W, Theodoras A.M. et al: Role of the ubiquitin‐proteasome pathway in regulating abundance of the cyclin‐dependent kinase inhibitor p27. Science 269: 682–685, 1995.
    • (1995) Science , vol.269 , pp. 682-685
    • Pagano, M1    Tarn, S W2    Theodoras, A.M.3
  • 9
    • 0030962262 scopus 로고    scopus 로고
    • : p53‐dependent induction of apoptosis by proteasome inhibitors
    • Lopes, U. G., Erhardt, P., Yao, R, and Cooper, G. M.:: p53‐dependent induction of apoptosis by proteasome inhibitors. J. Biol. Chem. 272: 12893–12896, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12893-12896
    • Lopes, U.G.1    Erhardt, P.2    Yao, R3    Cooper, G.M.4
  • 10
    • 0031034160 scopus 로고    scopus 로고
    • : Activation of the cell death program by inhibition of proteasome function
    • Drexler, H. C. A.:: Activation of the cell death program by inhibition of proteasome function. Proc. Natl. Acad. Sci. USA 94: 855–860, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 855-860
    • Drexler, H.C.A.1
  • 13
    • 0030134624 scopus 로고    scopus 로고
    • The cell‐death machine
    • Chinnaiyan A M, Dixit V M: The cell‐death machine. Curr. Biol. 6: 555–562, 1996.
    • (1996) Curr. Biol. , vol.6 , pp. 555-562
    • Chinnaiyan, A M1    Dixit, V M2
  • 14
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL‐1 beta‐converting enzyme, a mammalian homolog of the C. elegans cell death gene ced‐3
    • Miura M, Zhu H, Rotello R. et al: Induction of apoptosis in fibroblasts by IL‐1 beta‐converting enzyme, a mammalian homolog of the C. elegans cell death gene ced‐3. Cell 75: 653–660, 1993.
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M1    Zhu, H2    Rotello, R.3
  • 15
    • 0027989510 scopus 로고
    • Chromatin condensation during apoptosis is accompanied by degradation of lamin A+B, without enhanced activation of cdc2 kinase
    • Oberhammer F A, Hochegger K, Froschl G. et al: Chromatin condensation during apoptosis is accompanied by degradation of lamin A+B, without enhanced activation of cdc2 kinase. J. Cell Biol. 126: 827–837, 1994.
    • (1994) J. Cell Biol. , vol.126 , pp. 827-837
    • Oberhammer, F A1    Hochegger, K2    Froschl, G.3
  • 16
    • 0029610432 scopus 로고
    • Identification of actin as a substrate of ICE and an ICE‐like protease and involvement of an ICE‐like protease but not ICE in VP‐16‐induced U937 apoptosis
    • Mashima T, Naito M, Fujita N. et al: Identification of actin as a substrate of ICE and an ICE‐like protease and involvement of an ICE‐like protease but not ICE in VP‐16‐induced U937 apoptosis. Biochem. Biophvs. Res. Commun. 217: 1185–1192, 1995.
    • (1995) Biochem. Biophvs. Res. Commun. , vol.217 , pp. 1185-1192
    • Mashima, T1    Naito, M2    Fujita, N.3
  • 17
    • 0028788309 scopus 로고
    • Microfilament reorganization during apoptosis: the role of Gas2, a possible substrate for ICE‐like proteases
    • Brancolini C, Benedetti M, Schneider C: Microfilament reorganization during apoptosis: the role of Gas2, a possible substrate for ICE‐like proteases. EMBO J. 14: 5179–5190, 1995.
    • (1995) EMBO J. , vol.14 , pp. 5179-5190
    • Brancolini, C1    Benedetti, M2    Schneider, C3
  • 18
    • 0031888955 scopus 로고    scopus 로고
    • A caspase‐activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M, Sakahira H, Yokoyama H. et al: A caspase‐activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391: 43–50, 1998.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M1    Sakahira, H2    Yokoyama, H.3
  • 19
    • 0029877917 scopus 로고    scopus 로고
    • Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di‐Ieucine and tri‐leucine
    • Tsubuki S, Saito Y, Tomioka M. et al: Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di‐Ieucine and tri‐leucine. J. Biochem. 119: 572–576, 1996.
    • (1996) J. Biochem. , vol.119 , pp. 572-576
    • Tsubuki, S1    Saito, Y2    Tomioka, M.3
  • 20
    • 0016805556 scopus 로고
    • Synthetic study of peptide aldehydes
    • Ito A, Takahashi R, Miura C. et al: Synthetic study of peptide aldehydes. Chem. Pharm. Bull 23: 3106–3113, 1975.
    • (1975) Chem. Pharm. Bull , vol.23 , pp. 3106-3113
    • Ito, A1    Takahashi, R2    Miura, C.3
  • 21
    • 0027942467 scopus 로고
    • X‐ray‐induced cell death: apoptosis and necrosis
    • Nakano H, Shinohara K: X‐ray‐induced cell death: apoptosis and necrosis. Rad. Res 140: 1–9, 1994.
    • (1994) Rad. Res , vol.140 , pp. 1-9
    • Nakano, H1    Shinohara, K2
  • 22
    • 0021990666 scopus 로고
    • The orientation of nucleus, nucleus‐associated body and protruding nucleolus in aggregating Dictyostelium discoideum
    • Sameshima M: The orientation of nucleus, nucleus‐associated body and protruding nucleolus in aggregating Dictyostelium discoideum. Exp. Cell Res 156: 341–350, 1985.
    • (1985) Exp. Cell Res , vol.156 , pp. 341-350
    • Sameshima, M1
  • 23
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP‐ribose) polymerase by a proteinase with properties like ICE
    • Lazebnik Y A, Kaufmann S H, Desnoyers S. et al: Cleavage of poly(ADP‐ribose) polymerase by a proteinase with properties like ICE. Nature 371: 346–347, 1994.
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y A1    Kaufmann, S H2    Desnoyers, S.3
  • 24
    • 0031033274 scopus 로고    scopus 로고
    • Inhibition of Ced‐3/ICE‐related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl‐2 homologue Bak
    • McCarthy N J, Whyte M K B, Gilbert C.S. et al: Inhibition of Ced‐3/ICE‐related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl‐2 homologue Bak. J. Cell Biol 136: 215–227, 1997.
    • (1997) J. Cell Biol , vol.136 , pp. 215-227
    • McCarthy, N J1    Whyte, M K B2    Gilbert, C.S.3
  • 25
    • 0029906828 scopus 로고    scopus 로고
    • BAX‐induced cell death may not require interleukin 1 beta‐converting enzyme‐like proteases
    • Xiang, J, Chao D T, Korsmeyer S J: BAX‐induced cell death may not require interleukin 1 beta‐converting enzyme‐like proteases. Proc. Natl. Acad. Sci. USA 93: 14559–14563, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14559-14563
    • Xiang, J1    Chao, D T2    Korsmeyer, S J3
  • 26
    • 0032561352 scopus 로고    scopus 로고
    • Efficient nuclear targeting of granzyme B and the nuclear consequences of apoptosis induced by granzyme B and perforin are caspase‐dependent, but cell death is caspase‐independent
    • Trapani J A, Jans D A, Jans P.J. et al: Efficient nuclear targeting of granzyme B and the nuclear consequences of apoptosis induced by granzyme B and perforin are caspase‐dependent, but cell death is caspase‐independent. J. Biol. Chem 273: 27934–27938, 1998.
    • (1998) J. Biol. Chem , vol.273 , pp. 27934-27938
    • Trapani, J A1    Jans, D A2    Jans, P.J.3
  • 27
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S: Apoptosis by death factor. Cell 88: 355–365, 1997.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S1
  • 28
    • 0029068871 scopus 로고
    • Identification and inhibition of the ICE/CED‐3 protease necessary for mammalian apoptosis
    • Nicholson D W, Ali A, Thornberry N.A. et al: Identification and inhibition of the ICE/CED‐3 protease necessary for mammalian apoptosis. Nature 376: 3743, 1995.
    • (1995) Nature , vol.376 , pp. 3743
    • Nicholson, D W1    Ali, A2    Thornberry, N.A.3
  • 29
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD‐interacting protease, in Fas/APO‐1‐ and TNF receptor‐induced cell death
    • Boldin M P, Goncharov T M., Goltsev Y.V. et al: Involvement of MACH, a novel MORT1/FADD‐interacting protease, in Fas/APO‐1‐ and TNF receptor‐induced cell death. Cell 85: 803–815, 1996.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M P1    Goncharov, T M.2    Goltsev, Y.V.3
  • 30
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD‐homologous ICE/CED‐3‐like protease, is recruited to the CD95 (Fas/APO‐1) death‐inducing signaling complex
    • Muzio M, Chinnaiyan A M., Kischkel F.C. et al: FLICE, a novel FADD‐homologous ICE/CED‐3‐like protease, is recruited to the CD95 (Fas/APO‐1) death‐inducing signaling complex. Cell 85: 817–827, 1996.
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M1    Chinnaiyan, A M.2    Kischkel, F.C.3
  • 31
    • 0032571567 scopus 로고    scopus 로고
    • Inhibition of caspase activity induces a switch from apoptosis to necrosis
    • Lemaire C, Andreau K, Souvannavong V. et al: Inhibition of caspase activity induces a switch from apoptosis to necrosis. FEBS Lett 25: 266–270, 1998.
    • (1998) FEBS Lett , vol.25 , pp. 266-270
    • Lemaire, C1    Andreau, K2    Souvannavong, V.3
  • 32
    • 0029619221 scopus 로고
    • Protease inhibitors block apoptosis at intermediate stages: a compared analysis of DNA fragmentation and apoptotic nuclear morphology
    • Ghibelli L, Maresca V, Coppola S. et al: Protease inhibitors block apoptosis at intermediate stages: a compared analysis of DNA fragmentation and apoptotic nuclear morphology. FEBS Lett 377: 9–14, 1995.
    • (1995) FEBS Lett , vol.377 , pp. 9-14
    • Ghibelli, L1    Maresca, V2    Coppola, S.3
  • 33
    • 0027936115 scopus 로고
    • Zinc inhibits UV radiation‐induced apoptosis but fails to prevent subsequent cell death
    • McGowan A J, Fernandes R S, Verhaegen S. et al: Zinc inhibits UV radiation‐induced apoptosis but fails to prevent subsequent cell death. Int. T. Rad. Biol 66: 343–349, 1994.
    • (1994) Int. T. Rad. Biol , vol.66 , pp. 343-349
    • McGowan, A J1    Fernandes, R S2    Verhaegen, S.3
  • 34
    • 0030984171 scopus 로고    scopus 로고
    • Inhibitors of trypsin‐like serine proteases inhibit processing of the caspase Nedd‐2 and protect PC12 cells and sympathetic neurons from death evoked by withdrawal of trophic support
    • Stefanis L, Troy C M, Qi H. et al: Inhibitors of trypsin‐like serine proteases inhibit processing of the caspase Nedd‐2 and protect PC12 cells and sympathetic neurons from death evoked by withdrawal of trophic support. J. Neurochem 69: 1425–1437, 1997.
    • (1997) J. Neurochem , vol.69 , pp. 1425-1437
    • Stefanis, L1    Troy, C M2    Qi, H.3
  • 35
    • 0030855488 scopus 로고    scopus 로고
    • Zinc is a potent inhibitor of the apoptotic protease, caspase‐3. A novel target for zinc in the inhibition of apoptosis
    • Perry D K, Smyth M J, Stennicke H.R. et al: Zinc is a potent inhibitor of the apoptotic protease, caspase‐3. A novel target for zinc in the inhibition of apoptosis. J. Biol. Chem. 272: 18530–18533, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18530-18533
    • Perry, D K1    Smyth, M J2    Stennicke, H.R.3
  • 36
    • 0032583164 scopus 로고    scopus 로고
    • Caspase‐independent cell killing by Fas‐associated protein with death domain
    • Kawahara A, Ohsawa Y, Matsumura H. et al: Caspase‐independent cell killing by Fas‐associated protein with death domain. J. Cell. Biol 143: 1353–1360, 1998.
    • (1998) J. Cell. Biol , vol.143 , pp. 1353-1360
    • Kawahara, A1    Ohsawa, Y2    Matsumura, H.3
  • 37
    • 0030815584 scopus 로고    scopus 로고
    • Volume expression‐sensing outward‐rectifier C1‐channel: fresh start to the molecular identity and volume sensor
    • Okada Y: Volume expression‐sensing outward‐rectifier C1‐channel: fresh start to the molecular identity and volume sensor. Am. J. Physiol. 273: C755–789. 1997.
    • (1997) Am. J. Physiol , vol.273 , pp. C755-789
    • Okada, Y1
  • 38
    • 0032983795 scopus 로고    scopus 로고
    • Cell volume regulatory mechanisms in apoptotic cell death
    • Lang F, Uhlemann A C, Lepple‐Wienhues, A, et al: Cell volume regulatory mechanisms in apoptotic cell death. Hexz 24: 232–235, 1999.
    • (1999) Hexz , vol.24 , pp. 232-235
    • Lang, F1    Uhlemann, A C2    Lepple‐Wienhues, A3
  • 39
    • 0029943886 scopus 로고    scopus 로고
    • Apoptosis in vascular smooth muscle cells: role of cell shrinkage. Biochem
    • Orlov S N, Dam T V, Tremblay J. et al: Apoptosis in vascular smooth muscle cells: role of cell shrinkage. Biochem. Biophys. Res. Commun 221: 708–715, 1996.
    • (1996) Biophys. Res. Commun , vol.221 , pp. 708-715
    • Orlov, S N1    Dam, T V2    Tremblay, J.3
  • 40
    • 0031773579 scopus 로고    scopus 로고
    • A necessary role for cell shrinkage in apoptosis
    • Bortner C D, Cidlowski J A: A necessary role for cell shrinkage in apoptosis. Biochem. Pharmacol 56: 1549–1559, 1998.
    • (1998) Biochem. Pharmacol , vol.56 , pp. 1549-1559
    • Bortner, C D1    Cidlowski, J A2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.