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Volumn 64, Issue 1, 2004, Pages 85-93

Cyclophilin D, a Component of the Permeability Transition-Pore, Is an Apoptosis Repressor

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE; ANION CHANNEL; BONGKREKIC ACID; CHAPERONE; CYCLOPHILIN; CYCLOPHILIN D; DNA; PROTEIN; UNCLASSIFIED DRUG;

EID: 1542332908     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-03-0476     Document Type: Article
Times cited : (106)

References (69)
  • 1
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green, D. R., and Reed, J. C. Mitochondria and apoptosis. Science (Wash. DC). 281: 1369-1312, 1998.
    • (1998) Science (Wash. DC) , vol.281 , pp. 1369-1312
    • Green, D.R.1    Reed, J.C.2
  • 2
    • 0033290850 scopus 로고    scopus 로고
    • The mitochondrial permeability transition: Its molecular mechanism and role in reperfusion injury
    • Halestrap, A. P. The mitochondrial permeability transition: its molecular mechanism and role in reperfusion injury. Biochem. Soc. Symp., 66: 181-203, 1999.
    • (1999) Biochem. Soc. Symp. , vol.66 , pp. 181-203
    • Halestrap, A.P.1
  • 3
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton, M. The mitochondrial permeability transition pore and its role in cell death. Biochem. J., 341: 233-249, 1999.
    • (1999) Biochem. J. , vol.341 , pp. 233-249
    • Crompton, M.1
  • 5
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu, S., Narita, M., and Tsujimoto, Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature (Lond.), 399: 483-487, 1999.
    • (1999) Nature (Lond.) , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 9
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing 1AP proteins
    • Verhagen, A. M., Ekert, P. G., Pakusch, M., Silke, J., Connolly, L. M., Reid, G. E., Moritz, R. L., Simpson, R. J., and Vaux, D. L. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing 1AP proteins. Cell. 102: 43-53, 2000.
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3    Silke, J.4    Connolly, L.M.5    Reid, G.E.6    Moritz, R.L.7    Simpson, R.J.8    Vaux, D.L.9
  • 10
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating 1AP inhibition
    • Du, C., Fang, M., Li, Y., Li, L., and Wang, X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating 1AP inhibition. Cell, 102: 33-42, 2000.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 11
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu, X., Kim, C. N., Yang, J., Jemmerson, R., and Wang, X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell, 86: 147-157, 1996.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 12
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D., and Weinberg, R. A. The hallmarks of cancer. Cell, 100: 57-70, 2000.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 14
    • 0031018674 scopus 로고    scopus 로고
    • Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype
    • Rampino, N., Yamamoto, H., Ionov, Y., Li, Y., Sawai, H., Reed, J. C., and Perucho, M. Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype. Science (Wash. DC), 275: 967-969, 1997.
    • (1997) Science (Wash. DC) , vol.275 , pp. 967-969
    • Rampino, N.1    Yamamoto, H.2    Ionov, Y.3    Li, Y.4    Sawai, H.5    Reed, J.C.6    Perucho, M.7
  • 15
    • 0023786047 scopus 로고
    • Bcl-2 gene promotes haemopmetic cell survival and cooperates with c-myc to immortalize pre-B cells
    • Vaux, D. L., Cory, S., and Adams, J. M. Bcl-2 gene promotes haemopmetic cell survival and cooperates with c-myc to immortalize pre-B cells. Nature (Lond.), 335: 440-442, 1988.
    • (1988) Nature (Lond.) , vol.335 , pp. 440-442
    • Vaux, D.L.1    Cory, S.2    Adams, J.M.3
  • 16
    • 0030959526 scopus 로고    scopus 로고
    • An apoptosis-inducing isoform of neu differentiation factor (NDF) identified using a novel screen for dominant, apoptosis-inducing genes
    • Grimm, S., and Leder, P. An apoptosis-inducing isoform of neu differentiation factor (NDF) identified using a novel screen for dominant, apoptosis-inducing genes. J. Exp. Med., 185: 1137-1142, 1997.
    • (1997) J. Exp. Med. , vol.185 , pp. 1137-1142
    • Grimm, S.1    Leder, P.2
  • 17
    • 0033611057 scopus 로고    scopus 로고
    • Adenine nucleotide translocase-1, a component of the permeability transition pore, can dominantly induce apoptosis
    • Bauer, M. K. A., Schubert, A., Rocks, O., and Grimm, S. Adenine nucleotide translocase-1, a component of the permeability transition pore, can dominantly induce apoptosis. J. Cell Biol. 147: 1493-1502, 1999.
    • (1999) J. Cell Biol. , vol.147 , pp. 1493-1502
    • Bauer, M.K.A.1    Schubert, A.2    Rocks, O.3    Grimm, S.4
  • 18
    • 0035891212 scopus 로고    scopus 로고
    • Adenine nucleotide translocator mediates the mitochondrial membrane permeabilization induced by lonidamine, arsenite and CD437
    • Belzacq, A. S., El Hamel, C., Vieira, H. L., Cohen, I., Haouzi, D., Metivier, D., Marchetti, P., Brenner, C., and Kroemer, G. Adenine nucleotide translocator mediates the mitochondrial membrane permeabilization induced by lonidamine, arsenite and CD437. Oncogene, 20: 7579-7587, 2001.
    • (2001) Oncogene , vol.20 , pp. 7579-7587
    • Belzacq, A.S.1    El Hamel, C.2    Vieira, H.L.3    Cohen, I.4    Haouzi, D.5    Metivier, D.6    Marchetti, P.7    Brenner, C.8    Kroemer, G.9
  • 19
    • 0030853574 scopus 로고    scopus 로고
    • Adenine nucleotide translocator in dilated cardiomyopathy: Pathophysiological alterations in expression and function
    • Dorner, A., Schulze, K., Rauch, U., and Schultheiss, H. P. Adenine nucleotide translocator in dilated cardiomyopathy: pathophysiological alterations in expression and function. Mol. Cell. Biochem., 174: 261-269, 1997.
    • (1997) Mol. Cell. Biochem. , vol.174 , pp. 261-269
    • Dorner, A.1    Schulze, K.2    Rauch, U.3    Schultheiss, H.P.4
  • 21
    • 0024448458 scopus 로고
    • Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation
    • King, M. P., and Attardi, G. Human cells lacking mtDNA: repopulation with exogenous mitochondria by complementation. Science (Wash. DC), 246: 500-503, 1989.
    • (1989) Science (Wash. DC) , vol.246 , pp. 500-503
    • King, M.P.1    Attardi, G.2
  • 22
    • 0029054725 scopus 로고
    • RIP a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death
    • Stanger, B. Z., Leder, P., Lee, T. H., Kim, E., and Seed, B. RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell, 81: 513-523, 1995.
    • (1995) Cell , vol.81 , pp. 513-523
    • Stanger, B.Z.1    Leder, P.2    Lee, T.H.3    Kim, E.4    Seed, B.5
  • 23
    • 0032889531 scopus 로고    scopus 로고
    • Sendai virus infection induces apoptosis through activation of caspase-8 (FLICE) and caspase-3 (CPP32)
    • Bitzer, M., Prinz, F., Bauer, M., Spiegel, M., Neubert, W. J., Gregor, M., Schulze-Osthoff, K., and Lauer, U. Sendai virus infection induces apoptosis through activation of caspase-8 (FLICE) and caspase-3 (CPP32). J. Virol., 73: 702-708, 1999.
    • (1999) J. Virol. , vol.73 , pp. 702-708
    • Bitzer, M.1    Prinz, F.2    Bauer, M.3    Spiegel, M.4    Neubert, W.J.5    Gregor, M.6    Schulze-Osthoff, K.7    Lauer, U.8
  • 26
    • 0028023680 scopus 로고
    • Structure-function relationships of the ADP/ATP carrier
    • Klingenberg, M., and Nelson, D. R. Structure-function relationships of the ADP/ATP carrier. Biochim. Biophys. Acta, 1187: 241-244, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1187 , pp. 241-244
    • Klingenberg, M.1    Nelson, D.R.2
  • 27
    • 0034468736 scopus 로고    scopus 로고
    • Role of reactive oxygen species (ROS) in apoptosis induction
    • Simon, H. U., Haj-Yehia, A., and Levi-Schaffer, F. Role of reactive oxygen species (ROS) in apoptosis induction. Apoptosis. 5: 415-418, 2000.
    • (2000) Apoptosis , vol.5 , pp. 415-418
    • Simon, H.U.1    Haj-Yehia, A.2    Levi-Schaffer, F.3
  • 33
    • 0027071803 scopus 로고
    • Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition
    • Zydowsky, L. D., Etzkorn, F. A., Chang, H. Y., Ferguson, S. B., Stolz, L. A., Ho, S. I., and Walsh, C. T. Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition. Protein Sci., 1: 1092-1099, 1992.
    • (1992) Protein Sci. , vol.1 , pp. 1092-1099
    • Zydowsky, L.D.1    Etzkorn, F.A.2    Chang, H.Y.3    Ferguson, S.B.4    Stolz, L.A.5    Ho, S.I.6    Walsh, C.T.7
  • 34
    • 0030927540 scopus 로고    scopus 로고
    • The role of molecular chaperones in mitochondrial protein import and folding
    • Ryan, M. T., Naylor, D. J., Hoj, P. B., Clark, M. S., and Hoogenraad, N. J. The role of molecular chaperones in mitochondrial protein import and folding. Int. Rev. Cytol., 174: 127-193, 1997.
    • (1997) Int. Rev. Cytol. , vol.174 , pp. 127-193
    • Ryan, M.T.1    Naylor, D.J.2    Hoj, P.B.3    Clark, M.S.4    Hoogenraad, N.J.5
  • 35
    • 0032580361 scopus 로고    scopus 로고
    • Subcellular and submitochondrial mode of action of Bcl-2-like oncoproteins
    • Zamzami, N., Brenner, C., Marzo, I., Susin, S. A., and Kroemer, G. Subcellular and submitochondrial mode of action of Bcl-2-like oncoproteins. Oncogene, 16: 2265-2282, 1998.
    • (1998) Oncogene , vol.16 , pp. 2265-2282
    • Zamzami, N.1    Brenner, C.2    Marzo, I.3    Susin, S.A.4    Kroemer, G.5
  • 36
    • 0014941307 scopus 로고
    • On the inhibition of the adenine nucleotide translocation by bongkrekic acid
    • Klingenberg, M., Grebe, K., and Heldt, H. W. On the inhibition of the adenine nucleotide translocation by bongkrekic acid. Biochem. Biophys. Res. Commun., 39: 344-351, 1970.
    • (1970) Biochem. Biophys. Res. Commun. , vol.39 , pp. 344-351
    • Klingenberg, M.1    Grebe, K.2    Heldt, H.W.3
  • 38
    • 0030915095 scopus 로고    scopus 로고
    • Functional activation of Nedd2/ICH-1 (caspase-2) is an early process in apoptosis
    • Harvey, N. L., Butt, A. J., and Kumar, S. Functional activation of Nedd2/ICH-1 (caspase-2) is an early process in apoptosis. J. Biol. Chem., 272: 13134-13139, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13134-13139
    • Harvey, N.L.1    Butt, A.J.2    Kumar, S.3
  • 39
    • 0037162833 scopus 로고    scopus 로고
    • Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization
    • Lassus, P., Opitz-Araya, X., and Lazebnik, Y. Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization. Science (Wash. DC), 297: 1352-1354, 2002.
    • (2002) Science (Wash. DC) , vol.297 , pp. 1352-1354
    • Lassus, P.1    Opitz-Araya, X.2    Lazebnik, Y.3
  • 40
    • 0032910169 scopus 로고    scopus 로고
    • Apoptosis control by death and decoy receptors
    • Ashkenazi, A., and Dixit, V. M. Apoptosis control by death and decoy receptors. Curr. Opin. Cell Biol., 11: 255-260, 1999.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 255-260
    • Ashkenazi, A.1    Dixit, V.M.2
  • 41
    • 0030705234 scopus 로고    scopus 로고
    • p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum
    • Ng, F. W., Nguyen, M., Kwan, T., Branton, P. E., Nicholson, D. W., Cromlish, J. A., and Shore, G. C. p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum. J. Cell Biol., 139: 327-338, 1997.
    • (1997) J. Cell Biol. , vol.139 , pp. 327-338
    • Ng, F.W.1    Nguyen, M.2    Kwan, T.3    Branton, P.E.4    Nicholson, D.W.5    Cromlish, J.A.6    Shore, G.C.7
  • 42
  • 43
    • 0035853767 scopus 로고    scopus 로고
    • Arachidonic acid causes cell death through the mitochondrial permeability transition. Implications for tumor necrosis factor-α apoptotic signaling
    • Scorrano, L., Penzo, D., Petronilli, V., Pagano, F., and Bernardi, P. Arachidonic acid causes cell death through the mitochondrial permeability transition. Implications for tumor necrosis factor-α apoptotic signaling. J. Biol. Chem., 276: 12035-12040, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12035-12040
    • Scorrano, L.1    Penzo, D.2    Petronilli, V.3    Pagano, F.4    Bernardi, P.5
  • 46
    • 0036087028 scopus 로고    scopus 로고
    • Role of Bcl-2 family of proteins in malignancy
    • Baliga, B. C., and Kumar, S. Role of Bcl-2 family of proteins in malignancy. Hematol. Oncol., 20: 63-74, 2002.
    • (2002) Hematol. Oncol. , vol.20 , pp. 63-74
    • Baliga, B.C.1    Kumar, S.2
  • 47
    • 0032410818 scopus 로고    scopus 로고
    • The inhibitors of apoptosis (IAPs) and their emerging role in cancer
    • LaCasse, E. C., Baird, S., Korneluk, R. G., and MacKenzie, A. E. The inhibitors of apoptosis (IAPs) and their emerging role in cancer. Oncogene, 17: 3247-3259, 1998.
    • (1998) Oncogene , vol.17 , pp. 3247-3259
    • LaCasse, E.C.1    Baird, S.2    Korneluk, R.G.3    MacKenzie, A.E.4
  • 48
    • 0037390872 scopus 로고    scopus 로고
    • Spike, a novel BH3-only protein, regulates apoptosis at the endoplasmic reticulum
    • Mund, T., Gewies, A., Schoenfeld, N., Bauer, M. K., and Grimm, S. Spike, a novel BH3-only protein, regulates apoptosis at the endoplasmic reticulum. FASEB J., 17: 696-698, 2003.
    • (2003) FASEB J. , vol.17 , pp. 696-698
    • Mund, T.1    Gewies, A.2    Schoenfeld, N.3    Bauer, M.K.4    Grimm, S.5
  • 49
    • 25344466226 scopus 로고    scopus 로고
    • The metastasis suppressor gene C33/CD82/KA11 induces apoptosis through reactive oxygen intermediates
    • in press
    • Schoenfeld, N., Bauer, M. K. A., and Grimm, S. The metastasis suppressor gene C33/CD82/KA11 induces apoptosis through reactive oxygen intermediates. FASEB J., in press, 2003.
    • (2003) FASEB J.
    • Schoenfeld, N.1    Bauer, M.K.A.2    Grimm, S.3
  • 50
    • 0032401567 scopus 로고    scopus 로고
    • Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore
    • Crompton, M., Virji, S., and Ward, J. M. Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore. Eur. J. Biochem., 258: 729-735, 1998.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 729-735
    • Crompton, M.1    Virji, S.2    Ward, J.M.3
  • 51
    • 0036142850 scopus 로고    scopus 로고
    • Modulation of cyctophilin gene expression by N-4-(hydroxyphenyl)retinamide: Association with reactive oxygen species generation and apoptosis
    • Hursting, S. D., Shen, J. C., Sun, X. Y., Wang, T. T., Phang, J. M., and Perkins, S. N. Modulation of cyctophilin gene expression by N-4-(hydroxyphenyl)retinamide: association with reactive oxygen species generation and apoptosis. Mol. Carcinog., 33: 16-24, 2002.
    • (2002) Mol. Carcinog. , vol.33 , pp. 16-24
    • Hursting, S.D.1    Shen, J.C.2    Sun, X.Y.3    Wang, T.T.4    Phang, J.M.5    Perkins, S.N.6
  • 52
    • 0025193488 scopus 로고
    • 2+-induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adenine nucleotide translocase
    • 2+-induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adenine nucleotide translocase Biochem. J., 268: 153-160, 1990.
    • (1990) Biochem. J. , vol.268 , pp. 153-160
    • Halestrap, A.P.1    Davidson, A.M.2
  • 56
    • 0028290446 scopus 로고
    • Identification of immunosuppressant-induced apoptosis in a murine B-cell line and its prevention by bcl-x but not bcl-2
    • Gottschalk, A. R., Boise, L. H., Thompson, C. B., and Quintans, J. Identification of immunosuppressant-induced apoptosis in a murine B-cell line and its prevention by bcl-x but not bcl-2. Proc. Natl. Acad. Sci. USA, 91: 7350-7354, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7350-7354
    • Gottschalk, A.R.1    Boise, L.H.2    Thompson, C.B.3    Quintans, J.4
  • 58
    • 0037163117 scopus 로고    scopus 로고
    • Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization
    • Lin, D. T., and Lechleiter, J. D. Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization. J. Biol. Chem., 277: 31134-31141, 2002.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31134-31141
    • Lin, D.T.1    Lechleiter, J.D.2
  • 59
    • 0033603889 scopus 로고    scopus 로고
    • Collapse of the inner mitochondrial transmembrane potential is not required for apoptosis of HL60 cells
    • Finucane, D. M., Waterhouse, N. J., Amarante-Mendes, G. P., Cotter, T. G., and Green, D. R. Collapse of the inner mitochondrial transmembrane potential is not required for apoptosis of HL60 cells. Exp. Cell Res., 251: 166-174, 1999.
    • (1999) Exp. Cell Res. , vol.251 , pp. 166-174
    • Finucane, D.M.1    Waterhouse, N.J.2    Amarante-Mendes, G.P.3    Cotter, T.G.4    Green, D.R.5
  • 60
    • 0036168738 scopus 로고    scopus 로고
    • Trans-complementation rescue of cyclophilin A-deficient viruses reveals that the requirement for cyclophilin A in human immunodeficiency virus type 1 replication is independent of its isomerase activity
    • Saphire, A. C., Bobardt, M. D., and Gallay, P. A. Trans-complementation rescue of cyclophilin A-deficient viruses reveals that the requirement for cyclophilin A in human immunodeficiency virus type 1 replication is independent of its isomerase activity. J. Virol., 76: 2255-2262, 2002.
    • (2002) J. Virol. , vol.76 , pp. 2255-2262
    • Saphire, A.C.1    Bobardt, M.D.2    Gallay, P.A.3
  • 61
    • 0034774703 scopus 로고    scopus 로고
    • Chaperone-like activity of peptidyl-prolyl cis-trans isomerase during creatine kinase refolding
    • Ou, W. B., Luo, W., Park, Y. D., and Zhou, H. M. Chaperone-like activity of peptidyl-prolyl cis-trans isomerase during creatine kinase refolding. Protein Sci., 10: 2346-2353, 2001.
    • (2001) Protein Sci. , vol.10 , pp. 2346-2353
    • Ou, W.B.1    Luo, W.2    Park, Y.D.3    Zhou, H.M.4
  • 62
    • 0034006323 scopus 로고
    • Protective effect of the energy precursor creatine against toxicity of glutamate and β-amyloid in rat hippocampal neurons
    • Brewer, G. J., and Wallimann, T. W. Protective effect of the energy precursor creatine against toxicity of glutamate and β-amyloid in rat hippocampal neurons. J. Neurochem., 74: 1968-1978, 1968.
    • (1968) J. Neurochem. , vol.74 , pp. 1968-1978
    • Brewer, G.J.1    Wallimann, T.W.2
  • 64
    • 0034737380 scopus 로고    scopus 로고
    • Neuroprotective effects of creatine administration against NMDA and malonate toxicity
    • Malcon, C., Kaddurah-Daouk, R., and Beal, M. F. Neuroprotective effects of creatine administration against NMDA and malonate toxicity. Brain Res., 860: 195-198, 2000.
    • (2000) Brain Res. , vol.860 , pp. 195-198
    • Malcon, C.1    Kaddurah-Daouk, R.2    Beal, M.F.3
  • 65
    • 0032920451 scopus 로고    scopus 로고
    • Apoptosis in breast cancer: Relationship with other pathological parameters
    • Lipponen, P. Apoptosis in breast cancer: relationship with other pathological parameters. Endocr. Relat. Cancer, 6: 13-16, 1999.
    • (1999) Endocr. Relat. Cancer , vol.6 , pp. 13-16
    • Lipponen, P.1
  • 66
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson, C. B. Apoptosis in the pathogenesis and treatment of disease. Science (Wash. DC), 267: 1456-1462, 1995.
    • (1995) Science (Wash. DC) , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 67
    • 0034809942 scopus 로고    scopus 로고
    • Estradiol-regulated expression of the immunophilins cyclophilin 40 and FKBP52 in MCF-7 breast cancer cells
    • Kumar, P., Mark, P. J., Ward, B. K., Minchin, R. F., and Ratajczak. T. Estradiol-regulated expression of the immunophilins cyclophilin 40 and FKBP52 in MCF-7 breast cancer cells. Biochem. Biophys. Res. Commun., 284: 219-225, 2001.
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 219-225
    • Kumar, P.1    Mark, P.J.2    Ward, B.K.3    Minchin, R.F.4    Ratajczak, T.5
  • 68
    • 0036315162 scopus 로고    scopus 로고
    • PIN1 is an E2F target gene essential for Neu/Ras-induced transformation of mammary epithelial cells
    • Ryo, A., Liou, Y. C., Wulf, G., Nakamura, M., Lee, S. W., and Lu, K. P. PIN1 is an E2F target gene essential for Neu/Ras-induced transformation of mammary epithelial cells. Mol. Cell. Biol., 22: 5281-5295. 2002.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5281-5295
    • Ryo, A.1    Liou, Y.C.2    Wulf, G.3    Nakamura, M.4    Lee, S.W.5    Lu, K.P.6
  • 69
    • 0032572805 scopus 로고    scopus 로고
    • Co-amplification of a novel cyclophilin-like gene (PPIE) with L-myc in small cell lung cancer cell lines
    • Kim, J. O., Nau, M. M., Allikian, K. A., Makela, T. P., Alitalo, K., Johnson, B. E., and Kelley, M. J. Co-amplification of a novel cyclophilin-like gene (PPIE) with L-myc in small cell lung cancer cell lines. Oncogene, 17: 1019-1026, 1998.
    • (1998) Oncogene , vol.17 , pp. 1019-1026
    • Kim, J.O.1    Nau, M.M.2    Allikian, K.A.3    Makela, T.P.4    Alitalo, K.5    Johnson, B.E.6    Kelley, M.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.