메뉴 건너뛰기




Volumn 4, Issue 2, 2005, Pages 305-315

Phosphorothioate oligodeoxynucleotides and G3139 induce apoptosis in 518A2 melanoma cells

Author keywords

[No Author keywords available]

Indexed keywords

4',6 DIAMIDINO 2 PHENYLINDOLE; CASPASE 3; CASPASE INHIBITOR; CYTOCHROME C; G 4126; G 4146; LIPOCORTIN 5; LIPOFECTAMINE; OBLIMERSEN; OLIGODEOXYNUCLEOTIDE PHOSPHOROTHIOATE; POLY(ADENOSINE DIPHOSPHATE RIBOSE); PROTEIN BCL 2; PROTEIN BID; UNCLASSIFIED DRUG;

EID: 14844294993     PISSN: 15357163     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (34)

References (58)
  • 1
    • 0031032294 scopus 로고    scopus 로고
    • L antagonize the mitochondrial dysfunction preceding nuclear apoptosis induced by chemotherapeutic agents
    • L antagonize the mitochondrial dysfunction preceding nuclear apoptosis induced by chemotherapeutic agents. Cancer Res 1997;57:62-7.
    • (1997) Cancer Res. , vol.57 , pp. 62-67
    • Decaudin, D.1    Geley, S.2    Hirsch, T.3
  • 2
    • 0027892521 scopus 로고
    • Bcl-2 protein inhibits etoposide-induced apoptosis through its effects on events subsequent to topoisomerase II-induced DNA strand breaks and their repair
    • Kamesaki S, Kamesaki H, Jorgensen TJ, et al. Bcl-2 protein inhibits etoposide-induced apoptosis through its effects on events subsequent to topoisomerase II-induced DNA strand breaks and their repair. Cancer Res 1993;53:4251-6.
    • (1993) Cancer Res. , vol.53 , pp. 4251-4256
    • Kamesaki, S.1    Kamesaki, H.2    Jorgensen, T.J.3
  • 3
    • 0027389763 scopus 로고
    • Bcl-2 oncoprotein blocks chemotherapy-induced apoptosis in a human leukemia cell line
    • Miyashita T, Reed JC. Bcl-2 oncoprotein blocks chemotherapy-induced apoptosis in a human leukemia cell line. Blood 1993;81:151-7.
    • (1993) Blood , vol.81 , pp. 151-157
    • Miyashita, T.1    Reed, J.C.2
  • 4
    • 0029077281 scopus 로고
    • Overexpression of bcl-2 protects prostate cancer cells from apoptosis in vitro and confers resistance to androgen depletion in vivo
    • Raffo AJ, Perlman H, Chen MW, et al. Overexpression of bcl-2 protects prostate cancer cells from apoptosis in vitro and confers resistance to androgen depletion in vivo. Cancer Res 1995;55:4438-45.
    • (1995) Cancer Res. , vol.55 , pp. 4438-4445
    • Raffo, A.J.1    Perlman, H.2    Chen, M.W.3
  • 5
    • 0029157380 scopus 로고
    • Estrogen promotes chemotherapeutic drug resistance by a mechanism involving Bcl-2 proto-oncogene expression in human breast cancer cells
    • Teixeira C, Reed JC, Pratt MA. Estrogen promotes chemotherapeutic drug resistance by a mechanism involving Bcl-2 proto-oncogene expression in human breast cancer cells. Cancer Res 1995;55:3902-7.
    • (1995) Cancer Res. , vol.55 , pp. 3902-3907
    • Teixeira, C.1    Reed, J.C.2    Pratt, M.A.3
  • 6
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J, Liu X, Bhalla K, et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 1997;275: 1129-32.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 7
    • 0035910754 scopus 로고    scopus 로고
    • Control of mitochondrial membrane permeabilization by adenine nucleotide translocator interacting with HIV-1 viral protein rR and Bcl-2
    • Jacotot E, Ferri KF, El Hamel C, et al. Control of mitochondrial membrane permeabilization by adenine nucleotide translocator interacting with HIV-1 viral protein rR and Bcl-2. J Exp Med 2001;193:509-19.
    • (2001) J. Exp. Med. , vol.193 , pp. 509-519
    • Jacotot, E.1    Ferri, K.F.2    El Hamel, C.3
  • 8
    • 0033939697 scopus 로고    scopus 로고
    • Selective localization of Bcl-2 to the inner mitochondrial and smooth endoplasmic reticulum membranes in mammalian cells
    • Gotow T, Shibata M, Kanamori S, et al. Selective localization of Bcl-2 to the inner mitochondrial and smooth endoplasmic reticulum membranes in mammalian cells. Cell Death Differ 2000;7:666-74.
    • (2000) Cell Death Differ. , vol.7 , pp. 666-674
    • Gotow, T.1    Shibata, M.2    Kanamori, S.3
  • 9
    • 0032575606 scopus 로고    scopus 로고
    • Bcl-2 is located predominantly in the inner membrane and crista of mitochondria in rat liver
    • Motoyama S, Kitamura M, Saito S, et al. Bcl-2 is located predominantly in the inner membrane and crista of mitochondria in rat liver. Biochem Biophys Res Commun 1998;249:628-36.
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 628-636
    • Motoyama, S.1    Kitamura, M.2    Saito, S.3
  • 10
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • Antonsson B, Montessuit S, Sanchez B, Martinou JC. Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. J Biol Chem 2001;276:11615-23.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 11
    • 0035947596 scopus 로고    scopus 로고
    • Bcl-2 prevents Bax oligomerization in the mitochondrial outer membrane
    • Mikhailov V, Mikhailova M, Pulkrabek DJ, et al. Bcl-2 prevents Bax oligomerization in the mitochondrial outer membrane. J Biol Chem 2001;276:18361-74.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18361-18374
    • Mikhailov, V.1    Mikhailova, M.2    Pulkrabek, D.J.3
  • 12
    • 0034253592 scopus 로고    scopus 로고
    • BAX-dependent transport of cytochrome c reconstituted in pure liposomes
    • Saito M, Korsmeyer SJ, Schlesinger PH. BAX-dependent transport of cytochrome c reconstituted in pure liposomes. Nat Cell Biol 2000;2: 553-5.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 553-555
    • Saito, M.1    Korsmeyer, S.J.2    Schlesinger, P.H.3
  • 13
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 1996;86:147-57.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 15
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • Bossy-Wetzel E, Newmeyer DD, Green DR. Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO J 1998;17:37-49.
    • (1998) EMBO J. , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 17
    • 0036850631 scopus 로고    scopus 로고
    • Potential roles of antisense oligonucleotides in cancer therapy. The example of Bcl-2 antisense oligonucleotides
    • Dias N, Stein CA. Potential roles of antisense oligonucleotides in cancer therapy. The example of Bcl-2 antisense oligonucleotides. Eur J Pharm Biopharm 2002;54:263-9.
    • (2002) Eur. J. Pharm. Biopharm. , vol.54 , pp. 263-269
    • Dias, N.1    Stein, C.A.2
  • 18
    • 0242500957 scopus 로고    scopus 로고
    • The BCL2-family of protein ligands as cancer drugs: The next generation of therapeutics
    • Liu W, Bulgaru A, Haigentz M, et al. The BCL2-family of protein ligands as cancer drugs: the next generation of therapeutics. Curr Med Chem Anti-Canc Agents 2003;3:217-23.
    • (2003) Curr. Med. Chem. Anti-Canc. Agents , vol.3 , pp. 217-223
    • Liu, W.1    Bulgaru, A.2    Haigentz, M.3
  • 19
    • 0035942324 scopus 로고    scopus 로고
    • Biophysical characterization of recombinant human Bcl-2 and its interactions with an inhibitory ligand, antimycin A
    • Kim KM, Giedt CD, Basanez G, et al. Biophysical characterization of recombinant human Bcl-2 and its interactions with an inhibitory ligand, antimycin A. Biochemistry 2001;40:4911-22.
    • (2001) Biochemistry , vol.40 , pp. 4911-4922
    • Kim, K.M.1    Giedt, C.D.2    Basanez, G.3
  • 20
    • 0032817236 scopus 로고    scopus 로고
    • A recombinant defective adenoviral agent expressing anti-bcl-2 ribozyme promotes apoptosis of bcl-2-expressing human prostate cancer cells
    • Dorai T, Perlman H, Walsh K, et al. A recombinant defective adenoviral agent expressing anti-bcl-2 ribozyme promotes apoptosis of bcl-2-expressing human prostate cancer cells. Int J Cancer 1999;82: 846-52.
    • (1999) Int. J. Cancer , vol.82 , pp. 846-852
    • Dorai, T.1    Perlman, H.2    Walsh, K.3
  • 21
    • 2442478364 scopus 로고    scopus 로고
    • Antisense RNA down-regulation of bcl-2 expression in DU145 prostate cancer cells does not diminish the cytostatic effects of G3139 (Oblimersen)
    • Raffo A, Lai JC, Stein CA, et al. Antisense RNA down-regulation of bcl-2 expression in DU145 prostate cancer cells does not diminish the cytostatic effects of G3139 (Oblimersen). Clin Cancer Res 2004;10:3195-206.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 3195-3206
    • Raffo, A.1    Lai, J.C.2    Stein, C.A.3
  • 22
    • 2542576435 scopus 로고    scopus 로고
    • Changes in gene expression induced by phosphorothioate oligodeoxynucleotides (including G3139) in PC3 prostate carcinoma cells are recapitulated at least in part by treatment with interferon-β and γ
    • Benimetskaya L, Wittenberger T, Stein CA, et al. Changes in gene expression induced by phosphorothioate oligodeoxynucleotides (including G3139) in PC3 prostate carcinoma cells are recapitulated at least in part by treatment with interferon-β and γ. Clin Cancer Res 2004;10:3678-88.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 3678-3688
    • Benimetskaya, L.1    Wittenberger, T.2    Stein, C.A.3
  • 23
    • 1042275580 scopus 로고    scopus 로고
    • G3139 (Oblimersen) may inhibit prostate cancer cell growth in a partially bis-CpG-dependent non-antisense manner
    • Lai JC, Benimetskaya L, Santella RM, et al. G3139 (Oblimersen) may inhibit prostate cancer cell growth in a partially bis-CpG-dependent non-antisense manner. Mol Cancer Ther 2003;2:1031-43.
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 1031-1043
    • Lai, J.C.1    Benimetskaya, L.2    Santella, R.M.3
  • 24
    • 0035869667 scopus 로고    scopus 로고
    • Synergistic chemosensitization and inhibition of progression to androgen independence by antisense Bcl-2 oligodeoxynucleotide and paclitaxel in the LNCaP prostate tumor model
    • Leung S, Miyake H, Zellweger T, Tolcher A, Gleave ME. Synergistic chemosensitization and inhibition of progression to androgen independence by antisense Bcl-2 oligodeoxynucleotide and paclitaxel in the LNCaP prostate tumor model. Int J Cancer 2001;91:846-50.
    • (2001) Int. J. Cancer , vol.91 , pp. 846-850
    • Leung, S.1    Miyake, H.2    Zellweger, T.3    Tolcher, A.4    Gleave, M.E.5
  • 26
    • 0033567003 scopus 로고    scopus 로고
    • Antisense Bcl-2 oligodeoxynucleotides inhibit progression to androgen-independence after castration in the Shionogi tumor model
    • Miyake H, Tolcher A, Gleave ME. Antisense Bcl-2 oligodeoxynucleotides inhibit progression to androgen-independence after castration in the Shionogi tumor model. Cancer Res 1999;59:4030-4.
    • (1999) Cancer Res. , vol.59 , pp. 4030-4034
    • Miyake, H.1    Tolcher, A.2    Gleave, M.E.3
  • 27
    • 0027217846 scopus 로고
    • Investigations of antisense oligonucleotides targeted against bcl-2 RNAs
    • Kitada S, Miyashita T, Tanaka S, Reed JC. Investigations of antisense oligonucleotides targeted against bcl-2 RNAs. Antisense Res Dev 1993;3:157-69.
    • (1993) Antisense Res. Dev. , vol.3 , pp. 157-169
    • Kitada, S.1    Miyashita, T.2    Tanaka, S.3    Reed, J.C.4
  • 28
    • 0028060247 scopus 로고
    • Reversal of chemoresistance of lymphoma cells by antisense-mediated reduction of bcl-2 gene expression
    • Kitada S, Takayama S, De Riel K, Tanaka S, Reed JC. Reversal of chemoresistance of lymphoma cells by antisense-mediated reduction of bcl-2 gene expression. Antisense Res Dev 1994;4:71-9.
    • (1994) Antisense Res. Dev. , vol.4 , pp. 71-79
    • Kitada, S.1    Takayama, S.2    De Riel, K.3    Tanaka, S.4    Reed, J.C.5
  • 29
    • 0034684471 scopus 로고    scopus 로고
    • Chemosensitisation of malignant melanoma by BCL2 antisense therapy
    • Jansen B, Wacheck V, Heere-Ress E, et al. Chemosensitisation of malignant melanoma by BCL2 antisense therapy. Lancet 2000;356: 1728-33.
    • (2000) Lancet , vol.356 , pp. 1728-1733
    • Jansen, B.1    Wacheck, V.2    Heere-Ress, E.3
  • 30
    • 0031907428 scopus 로고    scopus 로고
    • bcl-2 antisense therapy chemosensitizes human melanoma in SCID mice
    • Jansen B, Schlagbauer-Wadl H, Brown BD, et al. bcl-2 antisense therapy chemosensitizes human melanoma in SCID mice. Nat Med 1998;4: 232-4.
    • (1998) Nat. Med. , vol.4 , pp. 232-234
    • Jansen, B.1    Schlagbauer-Wadl, H.2    Brown, B.D.3
  • 31
    • 0029592738 scopus 로고
    • Phosphorothioate oligonucleotides reduce melanoma growth in a SCID-hu mouse model by a nonantisense mechanism
    • Jansen B, Wadl H, Inoue SA, et al. Phosphorothioate oligonucleotides reduce melanoma growth in a SCID-hu mouse model by a nonantisense mechanism. Antisense Res Dev 1995;5:271-7.
    • (1995) Antisense Res. Dev. , vol.5 , pp. 271-277
    • Jansen, B.1    Wadl, H.2    Inoue, S.A.3
  • 32
    • 0033748335 scopus 로고    scopus 로고
    • Effects of Bcl-2 modulation with G3139 antisense oligonucleotide on human breast cancer cells are independent of inherent Bcl-2 protein expression
    • Chi KC, Wallis AE, Lee CH, et al. Effects of Bcl-2 modulation with G3139 antisense oligonucleotide on human breast cancer cells are independent of inherent Bcl-2 protein expression. Breast Cancer Res Treat 2000;63:199-212.
    • (2000) Breast Cancer Res. Treat. , vol.63 , pp. 199-212
    • Chi, K.C.1    Wallis, A.E.2    Lee, C.H.3
  • 33
    • 0028815149 scopus 로고
    • Phosphorothioate oligodeoxynucleotides bind to basic fibroblast growth factor, inhibit its binding to cell surface receptors, and remove it from low affinity binding sites an extracellular matrix
    • Guvakova MA, Yakubov LA, Vlodavsky I, Tonkinson JL, Stein CA. Phosphorothioate oligodeoxynucleotides bind to basic fibroblast growth factor, inhibit its binding to cell surface receptors, and remove it from low affinity binding sites an extracellular matrix. J Biol Chem 1995;270: 2620-7.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2620-2627
    • Guvakova, M.A.1    Yakubov, L.A.2    Vlodavsky, I.3    Tonkinson, J.L.4    Stein, C.A.5
  • 34
    • 0030987371 scopus 로고    scopus 로고
    • Cell-surface perturbations of the epidermal growth factor and vascular endothelial growth factor receptors by phosphorothioate oligodeoxynucleotides
    • Rockwell P, O'Connor WJ, King K, et al. Cell-surface perturbations of the epidermal growth factor and vascular endothelial growth factor receptors by phosphorothioate oligodeoxynucleotides. Proc Natl Acad Sci U S A 1997;94:6523-8.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 6523-6528
    • Rockwell, P.1    O'Connor, W.J.2    King, K.3
  • 35
    • 0029919656 scopus 로고    scopus 로고
    • Multiple mechanisms may contribute to the cellular anti-adhesive effects of phosphorothioate oligodeoxynucleotides
    • Khaled Z, Benimetskaya L, Zeltser R, et al. Multiple mechanisms may contribute to the cellular anti-adhesive effects of phosphorothioate oligodeoxynucleotides. Nucleic Acids Res 1996;24:737-45.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 737-745
    • Khaled, Z.1    Benimetskaya, L.2    Zeltser, R.3
  • 36
    • 0034737298 scopus 로고    scopus 로고
    • RNAi: Double-stranded RNA directs the ATP-dependent cleavage of mRNA at 21 to 23 nucleotide intervals
    • Zamora PD, Tuschl T, Sharp PA, Bartel DP. RNAi: double-stranded RNA directs the ATP-dependent cleavage of mRNA at 21 to 23 nucleotide intervals. Cell 2000;101:25-33.
    • (2000) Cell , vol.101 , pp. 25-33
    • Zamora, P.D.1    Tuschl, T.2    Sharp, P.A.3    Bartel, D.P.4
  • 37
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbashir SM, Harborth J, Lendeckel W, et al. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 2001;411:494-8.
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3
  • 38
    • 11144220793 scopus 로고    scopus 로고
    • Relative bcl-2 independence of drug-induced cytotoxicity and resistance in 518A2 melanoma cells
    • Benimetskaya L, Lai JC, Khvorova A, et al. Relative bcl-2 independence of drug-induced cytotoxicity and resistance in 518A2 melanoma cells. Clin Cancer Res 2004;10:8371-96.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 8371-8396
    • Benimetskaya, L.1    Lai, J.C.2    Khvorova, A.3
  • 39
    • 0035865470 scopus 로고    scopus 로고
    • Role of Bcl-2 and its posttranscriptional modification in response to antitumor therapy
    • Pratesi G, Perego P, Zunino F. Role of Bcl-2 and its posttranscriptional modification in response to antitumor therapy. Biochem Pharmacol 2001;61:381-6.
    • (2001) Biochem. Pharmacol. , vol.61 , pp. 381-386
    • Pratesi, G.1    Perego, P.2    Zunino, F.3
  • 40
    • 0027427492 scopus 로고
    • Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair
    • Veis DJ, Sorenson CM, Shutter JR, Korsmeyer SJ. Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair. Cell 1993;75:229-40.
    • (1993) Cell , vol.75 , pp. 229-240
    • Veis, D.J.1    Sorenson, C.M.2    Shutter, J.R.3    Korsmeyer, S.J.4
  • 42
    • 0142029990 scopus 로고    scopus 로고
    • The role of Bcl-2 family members in the progression of cutaneous melanoma
    • Bush JA, Li G. The role of Bcl-2 family members in the progression of cutaneous melanoma. Clin Exp Metastasis 2003;20:531-9.
    • (2003) Clin. Exp. Metastasis , vol.20 , pp. 531-539
    • Bush, J.A.1    Li, G.2
  • 43
    • 0029748608 scopus 로고    scopus 로고
    • Bcl-2 expression in malignant melanoma and its prognostic significance
    • Grover R, Wilson GD. Bcl-2 expression in malignant melanoma and its prognostic significance. Eur J Surg Oncol 1996;22:347-9.
    • (1996) Eur. J. Surg. Oncol. , vol.22 , pp. 347-349
    • Grover, R.1    Wilson, G.D.2
  • 44
    • 1442359881 scopus 로고    scopus 로고
    • Bcl-2 family members: Intracellular targeting, membrane-insertion, and changes in subcellular localization
    • Schinzel A, Kaufmann T, Borner C. Bcl-2 family members: intracellular targeting, membrane-insertion, and changes in subcellular localization. Biochim Biophys Acta 2004;1644:95-105.
    • (2004) Biochim. Biophys. Acta , vol.1644 , pp. 95-105
    • Schinzel, A.1    Kaufmann, T.2    Borner, C.3
  • 45
    • 0027977928 scopus 로고
    • The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane
    • Lithgow T, van Driel R, Bertram JF, Strasser A. The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane. Cell Growth Differ 1994;5:411-7.
    • (1994) Cell Growth Differ. , vol.5 , pp. 411-417
    • Lithgow, T.1    van Driel, R.2    Bertram, J.F.3    Strasser, A.4
  • 46
    • 0034123026 scopus 로고    scopus 로고
    • Cleavage of BID during cytotoxic drug and UV radiation-induced apoptosis occurs downstream of the point of Bcl-2 action and is catalysed by caspase-3: A potential feedback loop for amplification of apoptosis-associated mitochondrial cytochrome c release
    • Slee EA, Keogh SA, Martin SJ. Cleavage of BID during cytotoxic drug and UV radiation-induced apoptosis occurs downstream of the point of Bcl-2 action and is catalysed by caspase-3: a potential feedback loop for amplification of apoptosis-associated mitochondrial cytochrome c release. Cell Death Differ 2000;7:556-65.
    • (2000) Cell Death Differ. , vol.7 , pp. 556-565
    • Slee, E.A.1    Keogh, S.A.2    Martin, S.J.3
  • 47
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 1998;94:491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 48
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X, Budihardjo I, Zou H, Slaughter C, Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998;94: 481-90.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 49
    • 0033597785 scopus 로고    scopus 로고
    • Caspase-3-dependent cleavage of Bcl-2 promotes release of cytochrome c
    • Kirsch DG, Doseff A, Chau BN, et al. Caspase-3-dependent cleavage of Bcl-2 promotes release of cytochrome c. J Biol Chem 1999;274: 21155-61.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21155-21161
    • Kirsch, D.G.1    Doseff, A.2    Chau, B.N.3
  • 50
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes R, Desagher S, Antonsson B, Martinou JC. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol Cell Biol 2000;20:929-35.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 51
    • 0034663829 scopus 로고    scopus 로고
    • tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
    • Wei MC, Lindsten T, Mootha VK, et al. tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. Genes Dev 2000;14:2060-71.
    • (2000) Genes Dev. , vol.14 , pp. 2060-2071
    • Wei, M.C.1    Lindsten, T.2    Mootha, V.K.3
  • 52
    • 1442335318 scopus 로고    scopus 로고
    • Control of mitochondrial permeability by Bcl-2 family members
    • Sharpe JC, Arnoult D, Youle RJ. Control of mitochondrial permeability by Bcl-2 family members. Biochim Biophys Acta 2004;1644:107-13.
    • (2004) Biochim. Biophys. Acta , vol.1644 , pp. 107-113
    • Sharpe, J.C.1    Arnoult, D.2    Youle, R.J.3
  • 53
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • Kuwana T, Mackey MR, Perkins G, et al. Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 2002;111:331-42.
    • (2002) Cell , vol.111 , pp. 331-342
    • Kuwana, T.1    Mackey, M.R.2    Perkins, G.3
  • 54
    • 0032574761 scopus 로고    scopus 로고
    • Bax directly induces release of cytochrome c from isolated mitochondria
    • Jurgensmeier JM, Xie Z, Deveraux Q, et al. Bax directly induces release of cytochrome c from isolated mitochondria. Proc Natl Acad Sci U S A 1998;95:4997-5002.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 4997-5002
    • Jurgensmeier, J.M.1    Xie, Z.2    Deveraux, Q.3
  • 55
    • 0034671720 scopus 로고    scopus 로고
    • Bid-induced cytochrome c release is mediated by a pathway independent of mitochondrial permeability transition pore and Bax
    • Kim TH, Zhao Y, Barber MJ, Kuharsky DK, Yin XM. Bid-induced cytochrome c release is mediated by a pathway independent of mitochondrial permeability transition pore and Bax. J Biol Chem 2000;275:39474-81.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39474-39481
    • Kim, T.H.1    Zhao, Y.2    Barber, M.J.3    Kuharsky, D.K.4    Yin, X.M.5
  • 56
    • 17844362452 scopus 로고    scopus 로고
    • Bid acts on the permeability transition pore complex to induce apoptosis
    • Zamzami N, El Hamel C, Maisse C, et al. Bid acts on the permeability transition pore complex to induce apoptosis. Oncogene 2000;19:6342-50.
    • (2000) Oncogene , vol.19 , pp. 6342-6350
    • Zamzami, N.1    El Hamel, C.2    Maisse, C.3
  • 57
    • 0034605121 scopus 로고    scopus 로고
    • Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release
    • von Ahsen O, Renken C, Perkins G, et al. Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release. J Cell Biol 2000;150:1027-36.
    • (2000) J. Cell Biol. , vol.150 , pp. 1027-1036
    • von Ahsen, O.1    Renken, C.2    Perkins, G.3
  • 58
    • 0034681110 scopus 로고    scopus 로고
    • Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity
    • Shimizu S, Tsujimoto Y. Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity. Proc Natl Acad Sci U S A 2000;97:577-82.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 577-582
    • Shimizu, S.1    Tsujimoto, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.