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Volumn 8, Issue 11, 1997, Pages 1151-1160

Inactivation of MyoD-mediated expression of p21 in tumor cell lines

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE INHIBITOR; DNA; HELIX LOOP HELIX PROTEIN; PROTEIN P21;

EID: 0030778399     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (44)

References (79)
  • 2
    • 0029739541 scopus 로고    scopus 로고
    • Retinoblastoma protein family in cell cycle and cancer: A review
    • Paggi, M. G., Baldi, A., Bonetto, F., and Giordano, A. Retinoblastoma protein family in cell cycle and cancer: a review. J. Cell. Biochem., 62; 418-430, 1996.
    • (1996) J. Cell. Biochem. , vol.62 , pp. 418-430
    • Paggi, M.G.1    Baldi, A.2    Bonetto, F.3    Giordano, A.4
  • 3
    • 0030299866 scopus 로고    scopus 로고
    • INK4 genes in hematologic malignancies
    • INK4 genes in hematologic malignancies. Leuk. Lymphoma, 23: 235-245, 1996.
    • (1996) Leuk. Lymphoma , vol.23 , pp. 235-245
    • Heyman, M.1    Einhorn, S.2
  • 4
    • 0027959641 scopus 로고
    • Tumor suppressor genes and their roles in breast cancer
    • Cox, L. A., Chen, G., and Lee, E. Y. Tumor suppressor genes and their roles in breast cancer. Breast Cancer Res. Treat., 32: 19-38, 1994.
    • (1994) Breast Cancer Res. Treat. , vol.32 , pp. 19-38
    • Cox, L.A.1    Chen, G.2    Lee, E.Y.3
  • 5
    • 0027239898 scopus 로고
    • The regulation and function of the helix-loop-helix gene, asense, in Drosophila neural precursors
    • Camb.
    • Jarman, A. P., Brand, Wl., Jan, L. Y., and Jan, Y. N. The regulation and function of the helix-loop-helix gene, asense, in Drosophila neural precursors. Development (Camb.), 119: 19-29, 1993.
    • (1993) Development , vol.119 , pp. 19-29
    • Jarman, A.P.1    Brand, W.2    Jan, L.Y.3    Jan, Y.N.4
  • 7
    • 0028148938 scopus 로고
    • The helix-loop-helix gene E2A is required for B cell formation
    • Zhuang, Y., Soriano, P., and Weintraub, H. The helix-loop-helix gene E2A is required for B cell formation. Cell, 79: 875-884, 1994.
    • (1994) Cell , vol.79 , pp. 875-884
    • Zhuang, Y.1    Soriano, P.2    Weintraub, H.3
  • 8
    • 0028966222 scopus 로고
    • Proneural genes influence gliogenesis in Drosophila
    • Camb.
    • Giangrande, A. Proneural genes influence gliogenesis in Drosophila. Development (Camb.), 121: 429-438, 1995.
    • (1995) Development , vol.121 , pp. 429-438
    • Giangrande, A.1
  • 9
    • 0029068316 scopus 로고
    • Conversion of Xenopus ectoderm into neurons by NeuroD, a basic helix-loop-helix protein
    • Washington DC
    • Lee, J. E., Hollenberg, S. M., Snider, L., Turner, D. L., Lipnick, N, and Weintraub, H. Conversion of Xenopus ectoderm into neurons by NeuroD, a basic helix-loop-helix protein. Science (Washington DC), 268; 836-844, 1995.
    • (1995) Science , vol.268 , pp. 836-844
    • Lee, J.E.1    Hollenberg, S.M.2    Snider, L.3    Turner, D.L.4    Lipnick, N.5    Weintraub, H.6
  • 10
    • 0029557587 scopus 로고
    • Analysis of the rale of basic helix-loop-helix transcription factors in the development of neural lineages in the mouse
    • Guillemot, F. Analysis of the rale of basic helix-loop-helix transcription factors in the development of neural lineages in the mouse. Biol. Cell, 84: 3-6, 1995.
    • (1995) Biol. Cell , vol.84 , pp. 3-6
    • Guillemot, F.1
  • 12
    • 0028897842 scopus 로고
    • Scleraxis: A basic helix-loop-helix protein that prefigures skeletal formation during mouse embry-ogenesis
    • Camb.
    • Cserjesi, P., Brown, D., Ligon, K. L., Lyons, G. E., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., and Olson, E. N. Scleraxis: a basic helix-loop-helix protein that prefigures skeletal formation during mouse embry-ogenesis. Development (Camb.), 121: 1099-1110, 1995.
    • (1995) Development , vol.121 , pp. 1099-1110
    • Cserjesi, P.1    Brown, D.2    Ligon, K.L.3    Lyons, G.E.4    Copeland, N.G.5    Gilbert, D.J.6    Jenkins, N.A.7    Olson, E.N.8
  • 13
    • 0030030944 scopus 로고    scopus 로고
    • Myf-5 and myoD genes are activated in distinct mesenchymal stem cells and determine different skeletal muscle cell lineages
    • Braun, T., and Arnold, H. H. Myf-5 and myoD genes are activated in distinct mesenchymal stem cells and determine different skeletal muscle cell lineages. EMBO J., 15: 310-318, 1996.
    • (1996) EMBO J. , vol.15 , pp. 310-318
    • Braun, T.1    Arnold, H.H.2
  • 14
    • 0025944330 scopus 로고
    • Muscle-specific gene expression in rhabdomyosarcomas and stages of human fetal skeletal muscle development
    • Tonin, P. N., Scrable, H., Shimada, H., and Cavenee, W. K. Muscle-specific gene expression in rhabdomyosarcomas and stages of human fetal skeletal muscle development. Cancer Res., 51: 5100-5106, 1991.
    • (1991) Cancer Res. , vol.51 , pp. 5100-5106
    • Tonin, P.N.1    Scrable, H.2    Shimada, H.3    Cavenee, W.K.4
  • 15
    • 0027414452 scopus 로고
    • Deficiency in rhabdomyosarcomas of a factor required for MyoD activity and myogenesis
    • Washington DC
    • Tapscott, S. J., Thayer, M. J., and Weintraub, H. Deficiency in rhabdomyosarcomas of a factor required for MyoD activity and myogenesis. Science (Washington DC), 259; 1450-1453, 1993.
    • (1993) Science , vol.259 , pp. 1450-1453
    • Tapscott, S.J.1    Thayer, M.J.2    Weintraub, H.3
  • 16
    • 0026649648 scopus 로고
    • The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
    • Momand, J., Zambetti, G. P., Olson, D. C., George, D., and Levine, A. J. The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell, 69; 1237-1245, 1992.
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 17
    • 0029743891 scopus 로고    scopus 로고
    • Amplification of MDM2 inhibits MyoD-mediated myogenesis
    • Fiddler, T. A., Smith, L., Tapscott, S. J., and Thayer, M. J. Amplification of MDM2 inhibits MyoD-mediated myogenesis. Mol. Cell. Biol., 16: 5048-5057, 1996.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5048-5057
    • Fiddler, T.A.1    Smith, L.2    Tapscott, S.J.3    Thayer, M.J.4
  • 18
    • 0023663888 scopus 로고
    • Expression of a single transfected cDNA converts fibroblasts to myoblasts
    • Davis, R. L, Weintraub, H., and Lassar, A. B. Expression of a single transfected cDNA converts fibroblasts to myoblasts. Cell, 51: 987-1000, 1987.
    • (1987) Cell , vol.51 , pp. 987-1000
    • Davis, R.L.1    Weintraub, H.2    Lassar, A.B.3
  • 19
    • 0024381667 scopus 로고
    • Activation of muscle-specific genes in pigment, nerve, fat, liver, and fibroblast cell lines by forced expression of MyoD
    • Weintraub, H., Tapscott, S. J., Davis, R. L., Thayer, M. J., Adam, M. A., Lassar, A. B., and Miller, A. D. Activation of muscle-specific genes in pigment, nerve, fat, liver, and fibroblast cell lines by forced expression of MyoD. Proc. Natl. Acad. Sci. USA, 86: 5434-5438, 1989.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5434-5438
    • Weintraub, H.1    Tapscott, S.J.2    Davis, R.L.3    Thayer, M.J.4    Adam, M.A.5    Lassar, A.B.6    Miller, A.D.7
  • 20
    • 0027177830 scopus 로고
    • Analysis of dystrophin expression after activation of myogenesis in amniocytes, chorionic-villus cells, and fibroblasts. A new method for diagnosing Duchenne's muscular dystrophy
    • Sancho, S., Mongini, T., Tanji, K., Tapscott, S. J., Walker, W. F., Weintraub, H., Miller, A. D., and Miranda, A. F. Analysis of dystrophin expression after activation of myogenesis in amniocytes, chorionic-villus cells, and fibroblasts. A new method for diagnosing Duchenne's muscular dystrophy. N. Engl. J. Med., 329: 915-920, 1993.
    • (1993) N. Engl. J. Med. , vol.329 , pp. 915-920
    • Sancho, S.1    Mongini, T.2    Tanji, K.3    Tapscott, S.J.4    Walker, W.F.5    Weintraub, H.6    Miller, A.D.7    Miranda, A.F.8
  • 21
    • 0025114455 scopus 로고
    • MyoD converts primary dermal fibroblasts, chondroblasts, smooth muscle, and retinal pigmented epithelial cells into striated mononucleated myoblasts and multinucleated myotubes
    • Choi, J., Costa, M. L., Mermelstein, C. S., Chagas, C., Holtzer, S., and Holtzer, H. MyoD converts primary dermal fibroblasts, chondroblasts, smooth muscle, and retinal pigmented epithelial cells into striated mononucleated myoblasts and multinucleated myotubes. Proc. Natl. Acad. Sci. USA, 87: 7988-7992, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7988-7992
    • Choi, J.1    Costa, M.L.2    Mermelstein, C.S.3    Chagas, C.4    Holtzer, S.5    Holtzer, H.6
  • 22
    • 0029980077 scopus 로고    scopus 로고
    • Tumor cell complementation groups based on myogenic potential: Evidence for inactivation of loci required for basic helix-loop-helix protein activity
    • Gerber, A. N., and Tapscott, S. J. Tumor cell complementation groups based on myogenic potential: evidence for inactivation of loci required for basic helix-loop-helix protein activity. Mol. Cell. Biol., 76: 3901-3908, 1996.
    • (1996) Mol. Cell. Biol. , vol.76 , pp. 3901-3908
    • Gerber, A.N.1    Tapscott, S.J.2
  • 23
    • 0025277030 scopus 로고
    • Cell proliferation inhibited by MyoD1 independently of myogenic differentiation
    • Sorrentino, V., Pepperkok, R., Davis, R. L., Ansorge, W., and Philipson, L. Cell proliferation inhibited by MyoD1 independently of myogenic differentiation. Nature (Lond.), 345: 813-815, 1990.
    • (1990) Nature (Lond.) , vol.345 , pp. 813-815
    • Sorrentino, V.1    Pepperkok, R.2    Davis, R.L.3    Ansorge, W.4    Philipson, L.5
  • 25
    • 0027293918 scopus 로고
    • MyoD-induced cell cycle arrest is associated with increased nuclear affinity of the Rb protein
    • Thorburn, A. M., Walton, P. A., and Feramisco, J. R. MyoD-induced cell cycle arrest is associated with increased nuclear affinity of the Rb protein. Mol. Biol. Cell, 4: 705-713, 1993.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 705-713
    • Thorburn, A.M.1    Walton, P.A.2    Feramisco, J.R.3
  • 26
    • 0025201585 scopus 로고
    • Increased retinoblastoma gene expression is associated with late stages of differentiation in many different cell types
    • Coppola, J. A., Lewis, B. A., and Cole, M. D. Increased retinoblastoma gene expression is associated with late stages of differentiation in many different cell types. Oncogene, 5: 1731-1733, 1990.
    • (1990) Oncogene , vol.5 , pp. 1731-1733
    • Coppola, J.A.1    Lewis, B.A.2    Cole, M.D.3
  • 28
    • 0027499060 scopus 로고
    • Interaction of myogenic factors and the retinoblastoma protein mediates muscle cell commitment and differentiation
    • Gu, W., Schneider, J. W., Condorelli, G., Kaushal, S., Mahdavi, V., and Nadal-Ginard, B. Interaction of myogenic factors and the retinoblastoma protein mediates muscle cell commitment and differentiation. Cell, 72: 309-324, 1993.
    • (1993) Cell , vol.72 , pp. 309-324
    • Gu, W.1    Schneider, J.W.2    Condorelli, G.3    Kaushal, S.4    Mahdavi, V.5    Nadal-Ginard, B.6
  • 29
    • 0027336491 scopus 로고
    • 1 cyclins
    • 1 cyclins. Cell, 73: 1059-1065, 1993.
    • (1993) Cell , vol.73 , pp. 1059-1065
    • Sherr, C.J.1
  • 34
    • 0028342664 scopus 로고
    • Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen
    • Noda, A., Ning, Y., Venable, S. F., Pereira-Smith, O. M., and Smith, J. R. Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen. Exp. Cell Res., 277: 90-98, 1994.
    • (1994) Exp. Cell Res. , vol.277 , pp. 90-98
    • Noda, A.1    Ning, Y.2    Venable, S.F.3    Pereira-Smith, O.M.4    Smith, J.R.5
  • 35
    • 0027731971 scopus 로고
    • Inhibition of CDK2 activity in vivo by an associated 20K regulatory subunit
    • Gu, Y., Turck, C. W., and Morgan, D. O. Inhibition of CDK2 activity in vivo by an associated 20K regulatory subunit. Nature (Lond.), 366: 707-710, 1993.
    • (1993) Nature (Lond.) , vol.366 , pp. 707-710
    • Gu, Y.1    Turck, C.W.2    Morgan, D.O.3
  • 38
    • 0028363519 scopus 로고
    • 1 cyclin-Cdk protein kinase activity, is related to p21
    • 1 cyclin-Cdk protein kinase activity, is related to p21. Cell, 78: 67-74, 1994.
    • (1994) Cell , vol.78 , pp. 67-74
    • Toyoshima, H.1    Hunter, T.2
  • 39
    • 0028988158 scopus 로고
    • KIP2, a cyclin-dependent kinase inhibitor with unique domain structure and tissue distribution
    • KIP2, a cyclin-dependent kinase inhibitor with unique domain structure and tissue distribution. Genes Dev., 9: 639-649, 1995.
    • (1995) Genes Dev. , vol.9 , pp. 639-649
    • Lee, M.H.1    Reynisdottir, I.2    Massague, J.3
  • 40
    • 0027769876 scopus 로고
    • A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4
    • Serrano, M., Hannon, G. J., and Beach, D. A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4. Nature (Lond.), 366: 704-707, 1993.
    • (1993) Nature (Lond.) , vol.366 , pp. 704-707
    • Serrano, M.1    Hannon, G.J.2    Beach, D.3
  • 41
    • 0028168242 scopus 로고
    • INK4B is a potential effector of TGF-β-induced cell cycle arrest
    • INK4B is a potential effector of TGF-β-induced cell cycle arrest. Nature (Lond.), 377: 257-261, 1994.
    • (1994) Nature (Lond.) , vol.377 , pp. 257-261
    • Hannon, G.J.1    Beach, D.2
  • 46
    • 0028941483 scopus 로고
    • Correlation of terminal cell cycle arrest of skeletal muscle with induction of p21 by MyoD
    • Washington DC
    • Halevy, O., Novitch, B. G., Spicer, D. B., Skapek, S. X., Rhee, J., Hannon, G. J., Beach, D., and Lassar, A. B. Correlation of terminal cell cycle arrest of skeletal muscle with induction of p21 by MyoD. Science (Washington DC), 267: 1018-1021, 1995.
    • (1995) Science , vol.267 , pp. 1018-1021
    • Halevy, O.1    Novitch, B.G.2    Spicer, D.B.3    Skapek, S.X.4    Rhee, J.5    Hannon, G.J.6    Beach, D.7    Lassar, A.B.8
  • 50
    • 0027305904 scopus 로고
    • Use of a conditional MyoD transcription factor in studies of MyoD trans-activation and muscle determination
    • Hollenberg, S. M., Cheng, P. F., and Weintraub, H. Use of a conditional MyoD transcription factor in studies of MyoD trans-activation and muscle determination. Proc. Natl. Acad. Sci. USA, 90: 8028-8032, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8028-8032
    • Hollenberg, S.M.1    Cheng, P.F.2    Weintraub, H.3
  • 54
    • 0028169236 scopus 로고
    • p21-containing cyclin kinases exist in both active and inactive states
    • Zhang, H., Hannon, G. J., and Beach, D. p21-containing cyclin kinases exist in both active and inactive states. Genes Dev., 8: 1750-1758, 1994.
    • (1994) Genes Dev. , vol.8 , pp. 1750-1758
    • Zhang, H.1    Hannon, G.J.2    Beach, D.3
  • 55
    • 0027301324 scopus 로고
    • Subunit rearrangement of the cyclin-dependent kinases is associated with cellular transformation
    • Xiong, Y., Zhang, H., and Beach, D. Subunit rearrangement of the cyclin-dependent kinases is associated with cellular transformation. Genes Dev., 7: 1572-1583, 1993.
    • (1993) Genes Dev. , vol.7 , pp. 1572-1583
    • Xiong, Y.1    Zhang, H.2    Beach, D.3
  • 58
    • 0025186232 scopus 로고
    • Morphological and molecular characterization of spontaneous myogenic differentiation in a human rhabdomyosarcoma cell line
    • Shapiro, D. N., Houghton, P. J., Hazelton, B. J., Germain, G. S., Murti, K. G., Rahman, A., and Houghton, J. A. Morphological and molecular characterization of spontaneous myogenic differentiation in a human rhabdomyosarcoma cell line. Cancer Res., 50: 6002-6009, 1990.
    • (1990) Cancer Res. , vol.50 , pp. 6002-6009
    • Shapiro, D.N.1    Houghton, P.J.2    Hazelton, B.J.3    Germain, G.S.4    Murti, K.G.5    Rahman, A.6    Houghton, J.A.7
  • 60
    • 0027981476 scopus 로고
    • Cdk-interacting protein 1 directly binds with proliferating cell nuclear antigen and inhibits DNA replication catalyzed by the DNA polymerase 8 holoenzyme
    • Flores-Rozas, H., Kelman, Z., Dean, F. B., Pan, Z. Q., Harper, J. W., Elledge, S. J., O'Donnell, M., and Hurwitz, J. Cdk-interacting protein 1 directly binds with proliferating cell nuclear antigen and inhibits DNA replication catalyzed by the DNA polymerase 8 holoenzyme. Proc. Natl. Acad. Sci. USA, 97: 8655-8659, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8655-8659
    • Flores-Rozas, H.1    Kelman, Z.2    Dean, F.B.3    Pan, Z.Q.4    Harper, J.W.5    Elledge, S.J.6    O'Donnell, M.7    Hurwitz, J.8
  • 61
    • 0028352434 scopus 로고
    • The p21 inhibitor of cyclin-dependent kinases controls DNA replication by interaction with PCNA
    • Waga, S., Hannon, G. J., Beach, D., and Stillman, B. The p21 inhibitor of cyclin-dependent kinases controls DNA replication by interaction with PCNA. Nature (Lond.), 369: 574-578, 1994.
    • (1994) Nature (Lond.) , vol.369 , pp. 574-578
    • Waga, S.1    Hannon, G.J.2    Beach, D.3    Stillman, B.4
  • 62
    • 0028074603 scopus 로고
    • Differential effects by the p21 CDK inhibitor on PCNA-dependent DNA replication and repair
    • Li, R., Waga, S., Hannon, G. J., Beach, D., and Stillman, B. Differential effects by the p21 CDK inhibitor on PCNA-dependent DNA replication and repair. Nature (Lond.), 377: 534-537, 1994.
    • (1994) Nature (Lond.) , vol.377 , pp. 534-537
    • Li, R.1    Waga, S.2    Hannon, G.J.3    Beach, D.4    Stillman, B.5
  • 63
    • 0028675510 scopus 로고
    • Cip1 inhibits DNA replication but not PCNA-dependent nucleotide excision repair
    • Shivji, M. K., Grey, S. J., Strausfeld, U. P., Wood, R. D., and Blow, J. J. Cip1 inhibits DNA replication but not PCNA-dependent nucleotide excision repair. Curr. Biol., 4: 1062-1068, 1994.
    • (1994) Curr. Biol. , vol.4 , pp. 1062-1068
    • Shivji, M.K.1    Grey, S.J.2    Strausfeld, U.P.3    Wood, R.D.4    Blow, J.J.5
  • 64
    • 0028928036 scopus 로고
    • Inhibition of myogenic differentiation in proliferating myoblasts by cyclin D1-dependent kinase
    • Washington DC
    • Skapek, S. X., Rhee, J., Spicer, D. B., and Lassar, A. B. Inhibition of myogenic differentiation in proliferating myoblasts by cyclin D1-dependent kinase. Science (Washington DC), 267: 1022-1024, 1995.
    • (1995) Science , vol.267 , pp. 1022-1024
    • Skapek, S.X.1    Rhee, J.2    Spicer, D.B.3    Lassar, A.B.4
  • 66
    • 0027247729 scopus 로고
    • The control of apoptosis in mammalian cells
    • Collins, M. K., and Lopez Rivas, A. The control of apoptosis in mammalian cells. Trends Biochem. Sci., 18: 307-309, 1993.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 307-309
    • Collins, M.K.1    Lopez Rivas, A.2
  • 67
    • 0029996726 scopus 로고    scopus 로고
    • Resistance to apoptosis conferred by CDK inhibitors during myocyte differentiation
    • Washington DC
    • Wang, J., and Walsh, K. Resistance to apoptosis conferred by CDK inhibitors during myocyte differentiation. Science (Washington DC), 273: 359-361, 1996.
    • (1996) Science , vol.273 , pp. 359-361
    • Wang, J.1    Walsh, K.2
  • 68
    • 0024460181 scopus 로고
    • Improved retroviral vectors for gene transfer and expression
    • Miller, A. D., and Rosman, G. J. Improved retroviral vectors for gene transfer and expression. Biotechniques, 7: 980-982, 984-986, 989-990, 1989.
    • (1989) Biotechniques , vol.7 , pp. 980-982
    • Miller, A.D.1    Rosman, G.J.2
  • 69
    • 0025217856 scopus 로고
    • The MyoD DNA binding domain contains a recognition code for muscle-specific gene activation
    • Davis, R. L., Cheng, P. F., Lassar, A. B., and Weintraub, H. The MyoD DNA binding domain contains a recognition code for muscle-specific gene activation. Cell, 60: 733-746, 1990.
    • (1990) Cell , vol.60 , pp. 733-746
    • Davis, R.L.1    Cheng, P.F.2    Lassar, A.B.3    Weintraub, H.4
  • 70
    • 0028306459 scopus 로고
    • Expression of achaete-scute homolog 3 in Xenopus embryos converts ectodermal cells to a neural fate
    • Turner, D. L., and Weintraub, H. Expression of achaete-scute homolog 3 in Xenopus embryos converts ectodermal cells to a neural fate. Genes Dev., 8: 1434-1447, 1994.
    • (1994) Genes Dev. , vol.8 , pp. 1434-1447
    • Turner, D.L.1    Weintraub, H.2
  • 71
    • 0028352113 scopus 로고
    • Xenopus embryos regulate the nuclear localization of XMyoD
    • Rupp, R. A., Snider, L., and Weintraub, H. Xenopus embryos regulate the nuclear localization of XMyoD. Genes Dev., 8: 1311-1323, 1994.
    • (1994) Genes Dev. , vol.8 , pp. 1311-1323
    • Rupp, R.A.1    Snider, L.2    Weintraub, H.3
  • 72
    • 0027742184 scopus 로고
    • Distinct roles for cyclin-dependent kinases in cell cycle control
    • Washington DC
    • van den Heuvel, S., and Harlow, E. Distinct roles for cyclin-dependent kinases in cell cycle control. Science (Washington DC), 262: 2050-2054, 1993.
    • (1993) Science , vol.262 , pp. 2050-2054
    • Van Den Heuvel, S.1    Harlow, E.2
  • 73
    • 0018751062 scopus 로고
    • Depletion of L-3,5,3′-triiodothyronine and L-thyroxine in euthyroid calf serum for use in cell culture studies of the action of thyroid hormone
    • Samuels, H. H., Stanley, F., and Casanova, J. Depletion of L-3,5,3′-triiodothyronine and L-thyroxine in euthyroid calf serum for use in cell culture studies of the action of thyroid hormone. Endocrinology, 105: 80-85, 1979.
    • (1979) Endocrinology , vol.105 , pp. 80-85
    • Samuels, H.H.1    Stanley, F.2    Casanova, J.3
  • 74
    • 0019023345 scopus 로고
    • Purification of mouse immunoglobulin heavy-chain messenger RNAs from total myeloma tumor RNA
    • Auffray, C., and Rougeon, F. Purification of mouse immunoglobulin heavy-chain messenger RNAs from total myeloma tumor RNA. Eur. J. Biochem., 707: 303-314, 1980.
    • (1980) Eur. J. Biochem. , vol.707 , pp. 303-314
    • Auffray, C.1    Rougeon, F.2
  • 75
    • 0028229732 scopus 로고
    • Inactivation of a Cdk2 inhibitor during interleukin 2-induced proliferation of human T lymphocytes
    • Firpo, E. J., Koff, A., Solomon, M. J., and Roberts, J. M. Inactivation of a Cdk2 inhibitor during interleukin 2-induced proliferation of human T lymphocytes. Mol. Cell. Biol., 14: 4889-4901, 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4889-4901
    • Firpo, E.J.1    Koff, A.2    Solomon, M.J.3    Roberts, J.M.4
  • 76
    • 0027090324 scopus 로고
    • Activation of the p34 CDC2 protein kinase at the start of S phase in the human cell cycle
    • Marraccino, R. L., Firpo, E. J., and Roberts, J. M. Activation of the p34 CDC2 protein kinase at the start of S phase in the human cell cycle. Mol. Biol. Cell, 3: 389-401, 1992.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 389-401
    • Marraccino, R.L.1    Firpo, E.J.2    Roberts, J.M.3
  • 77
    • 0027430658 scopus 로고
    • Screening patients for heterozygous p53 mutations using a functional assay in yeast
    • Ishioka, C., Frebourg, T., Yan, Y. X., Vidal, M., Friend, S. H., Schmidt, S., and Iggo, R. Screening patients for heterozygous p53 mutations using a functional assay in yeast. Nat. Genet., 5: 124-129, 1993.
    • (1993) Nat. Genet. , vol.5 , pp. 124-129
    • Ishioka, C.1    Frebourg, T.2    Yan, Y.X.3    Vidal, M.4    Friend, S.H.5    Schmidt, S.6    Iggo, R.7
  • 79
    • 0020530724 scopus 로고
    • A detergent-trypsin method for the preparation of nuclei for flow cytometric DNA analysis
    • Vindelov, L. L., Christensen, I. J., and Nissen, N. I. A detergent-trypsin method for the preparation of nuclei for flow cytometric DNA analysis. Cytometry, 3: 323-327, 1983.
    • (1983) Cytometry , vol.3 , pp. 323-327
    • Vindelov, L.L.1    Christensen, I.J.2    Nissen, N.I.3


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