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Volumn , Issue , 2010, Pages 35-68

Transcription factors and muscle differentiation

Author keywords

BHLH transcription factors; Cellular oncogenes; Myoblast differentiation; Retinoic acid receptors; T3 mitochondrial receptors; Triiodothyronine (T3) nuclear receptor

Indexed keywords


EID: 84865439205     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-60327-153-0_3     Document Type: Chapter
Times cited : (3)

References (196)
  • 1
    • 0037278616 scopus 로고    scopus 로고
    • The formation of skeletal muscle: From somite to limb
    • Buckingham M, Bajard L, Chang T, et al (2003) The formation of skeletal muscle: From somite to limb. J Anat 202(1):59-68
    • (2003) J Anat , vol.202 , Issue.1 , pp. 59-68
    • Buckingham, M.1    Bajard, L.2    Chang, T.3
  • 2
    • 0024453704 scopus 로고
    • A novel human muscle factor related to but distinct from MyoD1 induces myogenic conversion in 10T1/2 fibroblasts
    • Braun T, Buschhausen-Denker G, Bober E, Tannich E, Arnold HH (1989) A novel human muscle factor related to but distinct from MyoD1 induces myogenic conversion in 10T1/2 fibroblasts. Embo J 8(3):701-709
    • (1989) Embo J , vol.8 , Issue.3 , pp. 701-709
    • Braun, T.1    Buschhausen-Denker, G.2    Bober, E.3    Tannich, E.4    Arnold, H.H.5
  • 3
    • 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 ML, Mermelstein CS, Chagas C, Holtzer S, Holtzer H (1990) MyoD converts primary dermal fibroblasts, chondroblasts, smooth muscle, and retinal pigmented epithelial cells into striated mononucleated myoblasts and multinucleated myotubes. Proc Natl Acad Sci U S A 87(20):7988-7992
    • (1990) Proc Natl Acad Sci U S A , vol.87 , Issue.20 , pp. 7988-7992
    • Choi, J.1    Costa, M.L.2    Mermelstein, C.S.3    Chagas, C.4    Holtzer, S.5    Holtzer, H.6
  • 4
    • 0024821376 scopus 로고
    • Identification of MRF4: A new member of the muscle regulatory factor gene family
    • Rhodes SJ, Konieczny SF (1989) Identification of MRF4: A new member of the muscle regulatory factor gene family. Genes Dev 3(12B):2050-2061
    • (1989) Genes Dev , vol.3 , Issue.12 , pp. 2050-2061
    • Rhodes, S.J.1    Konieczny, S.F.2
  • 5
    • 0024294014 scopus 로고
    • MyoD1: A nuclear phosphoprotein requiring a Myc homology region to convert fibroblasts to myoblasts
    • Tapscott SJ, Davis RL, Thayer MJ, Cheng PF, Weintraub H, Lassar AB (1988) MyoD1: A nuclear phosphoprotein requiring a Myc homology region to convert fibroblasts to myoblasts. Science 242(4877):405-411
    • (1988) Science , vol.242 , Issue.4877 , pp. 405-411
    • Tapscott, S.J.1    Davis, R.L.2    Thayer, M.J.3    Cheng, P.F.4    Weintraub, H.5    Lassar, A.B.6
  • 6
    • 0024576880 scopus 로고
    • Myogenin, a factor regulating myogenesis, has a domain homologous to MyoD
    • Wright WE, Sassoon DA, Lin VK (1989) Myogenin, a factor regulating myogenesis, has a domain homologous to MyoD. Cell 56(4):607-617
    • (1989) Cell , vol.56 , Issue.4 , pp. 607-617
    • Wright, W.E.1    Sassoon, D.A.2    Lin, V.K.3
  • 8
    • 0027258162 scopus 로고
    • Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene
    • Hasty P, Bradley A, Morris JH, et al (1993) Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene. Nature 364(6437):501-506
    • (1993) Nature , vol.364 , Issue.6437 , pp. 501-506
    • Hasty, P.1    Bradley, A.2    Morris, J.H.3
  • 9
    • 0027297310 scopus 로고
    • Myogenin gene disruption results in perinatal lethality because of severe muscle defect
    • Nabeshima Y, Hanaoka K, Hayasaka M, et al (1993) Myogenin gene disruption results in perinatal lethality because of severe muscle defect. Nature 364(6437):532-535
    • (1993) Nature , vol.364 , Issue.6437 , pp. 532-535
    • Nabeshima, Y.1    Hanaoka, K.2    Hayasaka, M.3
  • 10
    • 0025830788 scopus 로고
    • The muscle regulatory gene, Myf-6, has a biphasic pattern of expression during early mouse development
    • Bober E, Lyons GE, Braun T, Cossu G, Buckingham M, Arnold HH (1991) The muscle regulatory gene, Myf-6, has a biphasic pattern of expression during early mouse development. J Cell Biol 113(6):1255-1265
    • (1991) J Cell Biol , vol.113 , Issue.6 , pp. 1255-1265
    • Bober, E.1    Lyons, G.E.2    Braun, T.3    Cossu, G.4    Buckingham, M.5    Arnold, H.H.6
  • 11
    • 4644280175 scopus 로고    scopus 로고
    • Mrf4 determines skeletal muscle identity in Myf5:Myod double-mutant mice
    • Kassar-Duchossoy L, Gayraud-Morel B, Gomes D, et al (2004) Mrf4 determines skeletal muscle identity in Myf5:Myod double-mutant mice. Nature 431(7007):466-471
    • (2004) Nature , vol.431 , Issue.7007 , pp. 466-471
    • Kassar-Duchossoy, L.1    Gayraud-Morel, B.2    Gomes, D.3
  • 12
    • 0029286496 scopus 로고
    • Transcriptional control by the retinoblastoma protein
    • Kouzarides T (1995) Transcriptional control by the retinoblastoma protein. Semin Cancer Biol 6(2):91-98
    • (1995) Semin Cancer Biol , vol.6 , Issue.2 , pp. 91-98
    • Kouzarides, T.1
  • 13
    • 0031016121 scopus 로고    scopus 로고
    • RB kinases and RB-binding proteins: New points of view
    • Taya Y (1997) RB kinases and RB-binding proteins: New points of view. Trends Biochem Sci 22(1):14-17
    • (1997) Trends Biochem Sci , vol.22 , Issue.1 , pp. 14-17
    • Taya, Y.1
  • 14
    • 0031935648 scopus 로고    scopus 로고
    • Control of pRB phosphorylation
    • Mittnacht S (1998) Control of pRB phosphorylation. Curr Opin Genet Dev 8(1):21-27
    • (1998) Curr Opin Genet Dev , vol.8 , Issue.1 , pp. 21-27
    • Mittnacht, S.1
  • 15
    • 0027499060 scopus 로고
    • Interaction of myogenic factors and the retinoblastoma protein mediates muscle cell commitment and differentiation
    • Gu W, Schneider JW, Condorelli G, Kaushal S, Mahdavi V, Nadal-Ginard B (1993) Interaction of myogenic factors and the retinoblastoma protein mediates muscle cell commitment and differentiation. Cell 72(3):309-324
    • (1993) Cell , vol.72 , Issue.3 , pp. 309-324
    • Gu, W.1    Schneider, J.W.2    Condorelli, G.3    Kaushal, S.4    Mahdavi, V.5    Nadal-Ginard, B.6
  • 16
    • 0033558347 scopus 로고    scopus 로고
    • Coupling of the cell cycle and myogenesis through the cyclin D1-dependent interaction of MyoD with cdk4
    • Zhang JM, Wei Q, Zhao X, Paterson BM (1999) Coupling of the cell cycle and myogenesis through the cyclin D1-dependent interaction of MyoD with cdk4. Embo J 18(4):926-933
    • (1999) Embo J , vol.18 , Issue.4 , pp. 926-933
    • Zhang, J.M.1    Wei, Q.2    Zhao, X.3    Paterson, B.M.4
  • 17
    • 0028145332 scopus 로고
    • Ectopic expression of cyclin D1 prevents activation of gene transcription by myogenic basic helix-loop-helix regulators
    • Rao SS, Chu C, Kohtz DS (1994) Ectopic expression of cyclin D1 prevents activation of gene transcription by myogenic basic helix-loop-helix regulators. Mol Cell Biol 14(8): 5259-5267
    • (1994) Mol Cell Biol , vol.14 , Issue.8 , pp. 5259-5267
    • Rao, S.S.1    Chu, C.2    Kohtz, D.S.3
  • 18
    • 0028928036 scopus 로고
    • Inhibition of myogenic differentiation in proliferating myoblasts by cyclin D1-dependent kinase
    • Skapek SX, Rhee J, Spicer DB, Lassar AB (1995) Inhibition of myogenic differentiation in proliferating myoblasts by cyclin D1-dependent kinase. Science 267(5200):1022-1024
    • (1995) Science , vol.267 , Issue.5200 , pp. 1022-1024
    • Skapek, S.X.1    Rhee, J.2    Spicer, D.B.3    Lassar, A.B.4
  • 19
    • 0025808242 scopus 로고
    • Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo
    • Lassar AB, Davis RL, Wright WE, et al (1991) Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo. Cell 66(2): 305-315
    • (1991) Cell , vol.66 , Issue.2 , pp. 305-315
    • Lassar, A.B.1    Davis, R.L.2    Wright, W.E.3
  • 20
    • 0025238437 scopus 로고
    • The protein Id: A negative regulator of helix-loop-helix DNA binding proteins
    • Benezra R, Davis RL, Lockshon D, Turner DL, Weintraub H (1990) The protein Id: A negative regulator of helix-loop-helix DNA binding proteins. Cell 61(1):49-59
    • (1990) Cell , vol.61 , Issue.1 , pp. 49-59
    • Benezra, R.1    Davis, R.L.2    Lockshon, D.3    Turner, D.L.4    Weintraub, H.5
  • 21
    • 0032473502 scopus 로고    scopus 로고
    • The basic helix-loop-helix transcription factor Mist1 functions as a transcriptional repressor of myoD
    • Lemercier C, To RQ, Carrasco RA, Konieczny SF (1998) The basic helix-loop-helix transcription factor Mist1 functions as a transcriptional repressor of myoD. Embo J 17(5):1412-1422
    • (1998) Embo J , vol.17 , Issue.5 , pp. 1412-1422
    • Lemercier, C.1    To, R.Q.2    Carrasco, R.A.3    Konieczny, S.F.4
  • 22
    • 13044258437 scopus 로고    scopus 로고
    • MyoR: A muscle-restricted basic helix-loophelix transcription factor that antagonizes the actions of MyoD
    • Lu J,Webb R, Richardson JA, Olson EN (1999) MyoR: A muscle-restricted basic helix-loophelix transcription factor that antagonizes the actions of MyoD. Proc Natl Acad Sci U S A 96(2):552-557
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.2 , pp. 552-557
    • Lu, J.1    Webb, R.2    Richardson, J.A.3    Olson, E.N.4
  • 23
    • 0027987346 scopus 로고
    • M-Twist is an inhibitor of muscle differentiation
    • Hebrok M,Wertz K, Fuchtbauer EM(1994) M-Twist is an inhibitor of muscle differentiation. Dev Biol 165(2):537-544
    • (1994) Dev Biol , vol.165 , Issue.2 , pp. 537-544
    • Hebrok, M.1    Wertz, K.2    Fuchtbauer, E.M.3
  • 24
    • 0030960196 scopus 로고    scopus 로고
    • ZEB, a vertebrate homolog of Drosophila Zfh-1, is a negative regulator of muscle differentiation
    • Postigo AA, Dean DC (1997) ZEB, a vertebrate homolog of Drosophila Zfh-1, is a negative regulator of muscle differentiation. Embo J 16(13):3935-3943
    • (1997) Embo J , vol.16 , Issue.13 , pp. 3935-3943
    • Postigo, A.A.1    Dean, D.C.2
  • 25
    • 0026328855 scopus 로고
    • C-myc inhibition of MyoD and myogenin-initiated myogenic differentiation
    • Miner JH, Wold BJ (1991) c-myc inhibition of MyoD and myogenin-initiated myogenic differentiation. Mol Cell Biol 11(5):2842-2851
    • (1991) Mol Cell Biol , vol.11 , Issue.5 , pp. 2842-2851
    • Miner, J.H.1    Wold, B.J.2
  • 26
    • 33644930340 scopus 로고    scopus 로고
    • Mitochondrial activity regulates myoblast differentiation by control of c-Myc expression
    • Seyer P, Grandemange S, Busson M, et al (2006) Mitochondrial activity regulates myoblast differentiation by control of c-Myc expression. J Cell Physiol 207(1):75-86
    • (2006) J Cell Physiol , vol.207 , Issue.1 , pp. 75-86
    • Seyer, P.1    Grandemange, S.2    Busson, M.3
  • 27
    • 0034723175 scopus 로고    scopus 로고
    • Mitochondrial activity is involved in the regulation of myoblast differentiation through myogenin expression and activity of myogenic factors
    • Rochard P, Rodier A, Casas F et al (2000) Mitochondrial activity is involved in the regulation of myoblast differentiation through myogenin expression and activity of myogenic factors. J Biol Chem 275(4):2733-2744
    • (2000) J Biol Chem , vol.275 , Issue.4 , pp. 2733-2744
    • Rochard, P.1    Rodier, A.2    Casas, F.3
  • 28
    • 0031045835 scopus 로고    scopus 로고
    • Molecular mechanisms of myogenic coactivation by p300: Direct interaction with the activation domain of MyoD and with the MADS box of MEF2C
    • Sartorelli V, Huang J, Hamamori Y, Kedes L (1997) Molecular mechanisms of myogenic coactivation by p300: Direct interaction with the activation domain of MyoD and with the MADS box of MEF2C. Mol Cell Biol 17(2):1010-1026
    • (1997) Mol Cell Biol , vol.17 , Issue.2 , pp. 1010-1026
    • Sartorelli, V.1    Huang, J.2    Hamamori, Y.3    Kedes, L.4
  • 29
    • 0029968939 scopus 로고    scopus 로고
    • Human p300 protein is a coactivator for the transcription factor MyoD
    • Yuan W, Condorelli G, Caruso M, Felsani A, Giordano A (1996) Human p300 protein is a coactivator for the transcription factor MyoD. J Biol Chem 271(15):9009-9013
    • (1996) J Biol Chem , vol.271 , Issue.15 , pp. 9009-9013
    • Yuan, W.1    Condorelli, G.2    Caruso, M.3    Felsani, A.4    Giordano, A.5
  • 30
    • 0031310741 scopus 로고    scopus 로고
    • Differential roles of p300 and PCAF acetyltransferases in muscle differentiation
    • Puri PL, Sartorelli V, Yang XJ et al (1997) Differential roles of p300 and PCAF acetyltransferases in muscle differentiation. Mol Cell 1(1):35-45
    • (1997) Mol Cell , vol.1 , Issue.1 , pp. 35-45
    • Puri, P.L.1    Sartorelli, V.2    Yang, X.J.3
  • 31
    • 0033231604 scopus 로고    scopus 로고
    • Acetylation of MyoD directed by PCAF is necessary for the execution of the muscle program
    • Sartorelli V, Puri PL, Hamamori Y et al (1999) Acetylation of MyoD directed by PCAF is necessary for the execution of the muscle program. Mol Cell 4(5):725-734
    • (1999) Mol Cell , vol.4 , Issue.5 , pp. 725-734
    • Sartorelli, V.1    Puri, P.L.2    Hamamori, Y.3
  • 32
    • 14944344859 scopus 로고    scopus 로고
    • Coactivation of nuclear receptors and myogenic factors induces the major BTG1 influence on muscle differentiation
    • Busson M, Carazo A, Seyer P, et al (2005) Coactivation of nuclear receptors and myogenic factors induces the major BTG1 influence on muscle differentiation. Oncogene 24(10):1698-1710
    • (2005) Oncogene , vol.24 , Issue.10 , pp. 1698-1710
    • Busson, M.1    Carazo, A.2    Seyer, P.3
  • 33
    • 0029149037 scopus 로고
    • Stimulation of avian myoblast differentiation by triiodothyronine: Possible involvement of the cAMP pathway
    • Marchal S, Cassar-Malek I, Magaud JP, Rouault JP, Wrutniak C, Cabello G (1995) Stimulation of avian myoblast differentiation by triiodothyronine: Possible involvement of the cAMP pathway. Exp Cell Res 220(1):1-10
    • (1995) Exp Cell Res , vol.220 , Issue.1 , pp. 1-10
    • Marchal, S.1    Cassar-Malek, I.2    Magaud, J.P.3    Rouault, J.P.4    Wrutniak, C.5    Cabello, G.6
  • 34
    • 0033563647 scopus 로고    scopus 로고
    • BTG1: A triiodothyronine target involved in the myogenic influence of the hormone
    • Rodier A, Marchal-Victorion S, Rochard P et al (1999) BTG1: A triiodothyronine target involved in the myogenic influence of the hormone. Exp Cell Res 249(2):337-348
    • (1999) Exp Cell Res , vol.249 , Issue.2 , pp. 337-348
    • Rodier, A.1    Marchal-Victorion, S.2    Rochard, P.3
  • 35
    • 0023845213 scopus 로고
    • Oncogene jun encodes a sequence-specific trans-Activator similar to AP-1
    • Angel P, Allegretto EA, Okino ST et al (1988) Oncogene jun encodes a sequence-specific trans-Activator similar to AP-1. Nature 332(6160):166-171
    • (1988) Nature , vol.332 , Issue.6160 , pp. 166-171
    • Angel, P.1    Allegretto, E.A.2    Okino, S.T.3
  • 36
    • 0023625090 scopus 로고
    • Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated trans-Acting factor
    • Angel P, Imagawa M, Chiu R, et al (1987) Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated trans-Acting factor. Cell 49(6):729-739
    • (1987) Cell , vol.49 , Issue.6 , pp. 729-739
    • Angel, P.1    Imagawa, M.2    Chiu, R.3
  • 37
    • 0023798751 scopus 로고
    • Fos and Jun: The AP-1 connection
    • Curran T, Franza BR Jr (1988) Fos and Jun: The AP-1 connection. Cell 55(3):395-397
    • (1988) Cell , vol.55 , Issue.3 , pp. 395-397
    • Curran, T.1    Franza Jr., B.R.2
  • 38
    • 0023771685 scopus 로고
    • C-Jun dimerizes with itself and with c-Fos, forming complexes of different DNA binding affinities
    • Halazonetis TD, Georgopoulos K, Greenberg ME, Leder P (1988) c-Jun dimerizes with itself and with c-Fos, forming complexes of different DNA binding affinities. Cell 55(5):917-924
    • (1988) Cell , vol.55 , Issue.5 , pp. 917-924
    • Halazonetis, T.D.1    Georgopoulos, K.2    Greenberg, M.E.3    Leder, P.4
  • 39
    • 0024766967 scopus 로고
    • Jun DNA-binding is modulated by mutations between the leucines or by direct interaction of fos with the TGACTCA sequence
    • Hirai S, Yaniv M (1989) Jun DNA-binding is modulated by mutations between the leucines or by direct interaction of fos with the TGACTCA sequence. New Biol 1(2):181-191
    • (1989) New Biol , vol.1 , Issue.2 , pp. 181-191
    • Hirai, S.1    Yaniv, M.2
  • 40
    • 0023718397 scopus 로고
    • Fos-Associated cellular p39 is related to nuclear transcription factor AP-1
    • Sassone-Corsi P, Lamph WW, Kamps M, Verma IM (1988) fos-Associated cellular p39 is related to nuclear transcription factor AP-1. Cell 54(4):553-560
    • (1988) Cell , vol.54 , Issue.4 , pp. 553-560
    • Sassone-Corsi, P.1    Lamph, W.W.2    Kamps, M.3    Verma, I.M.4
  • 41
    • 0025878233 scopus 로고
    • Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity
    • Hai T, Curran T (1991) Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity. Proc Natl Acad Sci U S A 88(9):3720-3724
    • (1991) Proc Natl Acad Sci U S A , vol.88 , Issue.9 , pp. 3720-3724
    • Hai, T.1    Curran, T.2
  • 42
    • 0027954409 scopus 로고
    • Maf nuclear oncoprotein recognizes sequences related to an AP-1 site and forms heterodimers with both Fos and Jun
    • Kataoka K, Noda M, Nishizawa M (1994) Maf nuclear oncoprotein recognizes sequences related to an AP-1 site and forms heterodimers with both Fos and Jun. Mol Cell Biol 14(1):700-712
    • (1994) Mol Cell Biol , vol.14 , Issue.1 , pp. 700-712
    • Kataoka, K.1    Noda, M.2    Nishizawa, M.3
  • 43
    • 0028154038 scopus 로고
    • Maf and Nrl can bind to AP-1 sites and form heterodimers with Fos and Jun
    • Kerppola TK, Curran T (1994) Maf and Nrl can bind to AP-1 sites and form heterodimers with Fos and Jun. Oncogene 9(3):675-684
    • (1994) Oncogene , vol.9 , Issue.3 , pp. 675-684
    • Kerppola, T.K.1    Curran, T.2
  • 44
    • 0024205841 scopus 로고
    • The role of the leucine zipper in the fos-jun interaction
    • Kouzarides T, Ziff E (1988) The role of the leucine zipper in the fos-jun interaction. Nature 336(6200):646-651
    • (1988) Nature , vol.336 , Issue.6200 , pp. 646-651
    • Kouzarides, T.1    Ziff, E.2
  • 45
    • 0024295767 scopus 로고
    • The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins
    • Landschulz WH, Johnson PF, McKnight SL (1988) The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins. Science 240(4860):1759-1764
    • (1988) Science , vol.240 , Issue.4860 , pp. 1759-1764
    • Landschulz, W.H.1    Johnson, P.F.2    McKnight, S.L.3
  • 46
    • 0035971517 scopus 로고    scopus 로고
    • The mammalian Jun proteins: Redundancy and specificity
    • Mechta-Grigoriou F, Gerald D, Yaniv M (2001) The mammalian Jun proteins: Redundancy and specificity. Oncogene 20(19):2378-2389
    • (2001) Oncogene , vol.20 , Issue.19 , pp. 2378-2389
    • Mechta-Grigoriou, F.1    Gerald, D.2    Yaniv, M.3
  • 47
    • 0027472176 scopus 로고
    • Heterodimer formation of cJun and ATF-2 is responsible for induction of c-jun by the 243 amino acid adenovirus E1A protein
    • van Dam H, Duyndam M, Rottier R et al (1993) Heterodimer formation of cJun and ATF-2 is responsible for induction of c-jun by the 243 amino acid adenovirus E1A protein. Embo J 12(2):479-487
    • (1993) Embo J , vol.12 , Issue.2 , pp. 479-487
    • Van Dam, H.1    Duyndam, M.2    Rottier, R.3
  • 48
    • 0027209916 scopus 로고
    • Adenovirus E1A negatively and positively modulates transcription of AP-1 dependent genes by dimer-specific regulation of the DNA binding and transactivation activities of Jun
    • Hagmeyer BM, Konig H, Herr I et al (1993) Adenovirus E1A negatively and positively modulates transcription of AP-1 dependent genes by dimer-specific regulation of the DNA binding and transactivation activities of Jun. Embo J 12(9):3559-3572
    • (1993) Embo J , vol.12 , Issue.9 , pp. 3559-3572
    • Hagmeyer, B.M.1    Konig, H.2    Herr, I.3
  • 49
    • 0026828017 scopus 로고
    • Ultraviolet-radiation induced c-jun gene transcription: Two AP-1 like binding sites mediate the response
    • Stein B, Angel P, van Dam H, et al (1992) Ultraviolet-radiation induced c-jun gene transcription: Two AP-1 like binding sites mediate the response. Photochem Photobiol 55(3):409-415
    • (1992) Photochem Photobiol , vol.55 , Issue.3 , pp. 409-415
    • Stein, B.1    Angel, P.2    Van Dam, H.3
  • 50
    • 0033008427 scopus 로고    scopus 로고
    • CD28-mediated regulation of the c-jun promoter involves the MEF2 transcription factor in Jurkat T cells
    • Shin HM, Han TH (1999) CD28-mediated regulation of the c-jun promoter involves the MEF2 transcription factor in Jurkat T cells. Mol Immunol 36(3):197-203
    • (1999) Mol Immunol , vol.36 , Issue.3 , pp. 197-203
    • Shin, H.M.1    Han, T.H.2
  • 51
    • 0037053385 scopus 로고    scopus 로고
    • Composition and function of AP-1 transcription complexes during muscle cell differentiation
    • Andreucci JJ, Grant D, Cox DM et al (2002) Composition and function of AP-1 transcription complexes during muscle cell differentiation. J Biol Chem 277(19):16426-16432
    • (2002) J Biol Chem , vol.277 , Issue.19 , pp. 16426-16432
    • Andreucci, J.J.1    Grant, D.2    Cox, D.M.3
  • 52
    • 0027361017 scopus 로고
    • Phosphorylation of the c-Fos transrepression domain by mitogen-Activated protein kinase and 90-kDa ribosomal S6 kinase
    • Chen RH, Abate C, Blenis J (1993) Phosphorylation of the c-Fos transrepression domain by mitogen-Activated protein kinase and 90-kDa ribosomal S6 kinase. Proc Natl Acad Sci U S A 90(23):10952-10956
    • (1993) Proc Natl Acad Sci U S A , vol.90 , Issue.23 , pp. 10952-10956
    • Chen, R.H.1    Abate, C.2    Blenis, J.3
  • 53
    • 0028144846 scopus 로고
    • C-Fos transcriptional activity stimulated by H-Ras-Activated protein kinase distinct from JNK and ERK
    • Deng T, KarinM (1994) c-Fos transcriptional activity stimulated by H-Ras-Activated protein kinase distinct from JNK and ERK. Nature 371(6493):171-175
    • (1994) Nature , vol.371 , Issue.6493 , pp. 171-175
    • Deng, T.1    Karin, M.2
  • 54
    • 0028935270 scopus 로고
    • Pro-inflammatory cytokines and environmental stress cause p38 mitogen-Activated protein kinase activation by dual phosphorylation on tyrosine and threonine
    • Raingeaud J, Gupta S, Rogers JS et al (1995) Pro-inflammatory cytokines and environmental stress cause p38 mitogen-Activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J Biol Chem 270(13):7420-7426
    • (1995) J Biol Chem , vol.270 , Issue.13 , pp. 7420-7426
    • Raingeaud, J.1    Gupta, S.2    Rogers, J.S.3
  • 55
    • 0029006550 scopus 로고
    • Intramolecular signal transduction in c-Jun
    • Papavassiliou AG, TreierM, Bohmann D (1995) Intramolecular signal transduction in c-Jun. Embo J 14(9):2014-2019
    • (1995) Embo J , vol.14 , Issue.9 , pp. 2014-2019
    • Papavassiliou, A.G.1    Treier, M.2    Bohmann, D.3
  • 56
    • 0028060030 scopus 로고
    • Activation of cAMP and mitogen responsive genes relies on a common nuclear factor
    • Arias J, Alberts AS, Brindle P et al (1994) Activation of cAMP and mitogen responsive genes relies on a common nuclear factor. Nature 370(6486):226-229
    • (1994) Nature , vol.370 , Issue.6486 , pp. 226-229
    • Arias, J.1    Alberts, A.S.2    Brindle, P.3
  • 57
    • 0029585553 scopus 로고
    • Stimulation of c-Jun activity by CBP: C-Jun residues Ser63/73 are required for CBP induced stimulation in vivo and CBP binding in vitro
    • Bannister AJ, Oehler T, Wilhelm D, Angel P, Kouzarides T (1995) Stimulation of c-Jun activity by CBP: C-Jun residues Ser63/73 are required for CBP induced stimulation in vivo and CBP binding in vitro. Oncogene 11(12):2509-2514
    • (1995) Oncogene , vol.11 , Issue.12 , pp. 2509-2514
    • Bannister, A.J.1    Oehler, T.2    Wilhelm, D.3    Angel, P.4    Kouzarides, T.5
  • 58
    • 0031023756 scopus 로고    scopus 로고
    • Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases
    • Musti AM, TreierM, Bohmann D (1997) Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases. Science 275(5298):400-402
    • (1997) Science , vol.275 , Issue.5298 , pp. 400-402
    • Musti, A.M.1    Treier, M.2    Bohmann, D.3
  • 59
    • 0025882879 scopus 로고
    • The jun and fos protein families are both required for cell cycle progression in fibroblasts
    • Kovary K, Bravo R (1991) The jun and fos protein families are both required for cell cycle progression in fibroblasts. Mol Cell Biol 11(9):4466-4472
    • (1991) Mol Cell Biol , vol.11 , Issue.9 , pp. 4466-4472
    • Kovary, K.1    Bravo, R.2
  • 60
    • 0026599596 scopus 로고
    • Transcription factor AP-1 activity is required for initiation of DNA synthesis and is lost during cellular aging
    • Riabowol K, Schiff J, Gilman MZ (1992) Transcription factor AP-1 activity is required for initiation of DNA synthesis and is lost during cellular aging. Proc Natl Acad Sci U S A 89(1):157-161
    • (1992) Proc Natl Acad Sci U S A , vol.89 , Issue.1 , pp. 157-161
    • Riabowol, K.1    Schiff, J.2    Gilman, M.Z.3
  • 61
    • 0028325891 scopus 로고
    • Mouse JunD negatively regulates fibroblast growth and antagonizes transformation by ras
    • Pfarr CM, Mechta F, Spyrou G, Lallemand D, Carillo S, Yaniv M (1994) Mouse JunD negatively regulates fibroblast growth and antagonizes transformation by ras. Cell 76(4): 747-760
    • (1994) Cell , vol.76 , Issue.4 , pp. 747-760
    • Pfarr, C.M.1    Mechta, F.2    Spyrou, G.3    Lallemand, D.4    Carillo, S.5    Yaniv, M.6
  • 62
    • 0034595423 scopus 로고    scopus 로고
    • Cell cycle-dependent variations in c-Jun and JunB phosphorylation: A role in the control of cyclin D1 expression
    • Bakiri L, Lallemand D, Bossy-Wetzel E, Yaniv M (2000) Cell cycle-dependent variations in c-Jun and JunB phosphorylation: A role in the control of cyclin D1 expression. Embo J 19(9):2056-2068
    • (2000) Embo J , vol.19 , Issue.9 , pp. 2056-2068
    • Bakiri, L.1    Lallemand, D.2    Bossy-Wetzel, E.3    Yaniv, M.4
  • 63
    • 0027219303 scopus 로고
    • A null mutation at the c-jun locus causes embryonic lethality and retarded cell growth in culture
    • Johnson RS, van Lingen B, Papaioannou VE, Spiegelman BM (1993) A null mutation at the c-jun locus causes embryonic lethality and retarded cell growth in culture. Genes Dev 7(7B):1309-1317
    • (1993) Genes Dev , vol.7 , Issue.7 , pp. 1309-1317
    • Johnson, R.S.1    Van Lingen, B.2    Papaioannou, V.E.3    Spiegelman, B.M.4
  • 64
    • 0033104956 scopus 로고    scopus 로고
    • Control of cell cycle progression by c-Jun is p53 dependent
    • Schreiber M, Kolbus A, Piu F et al (1999) Control of cell cycle progression by c-Jun is p53 dependent. Genes Dev 13(5):607-619
    • (1999) Genes Dev , vol.13 , Issue.5 , pp. 607-619
    • Schreiber, M.1    Kolbus, A.2    Piu, F.3
  • 65
    • 0027509059 scopus 로고
    • Proto-oncogenes of the fos/jun family of transcription factors are positive regulators of myeloid differentiation
    • Lord KA, Abdollahi A, Hoffman-Liebermann B, Liebermann DA (1993) Proto-oncogenes of the fos/jun family of transcription factors are positive regulators of myeloid differentiation. Mol Cell Biol 13(2):841-851
    • (1993) Mol Cell Biol , vol.13 , Issue.2 , pp. 841-851
    • Lord, K.A.1    Abdollahi, A.2    Hoffman-Liebermann, B.3    Liebermann, D.A.4
  • 66
    • 0028015668 scopus 로고
    • Constitutive cJun expression induces partial macrophage differentiation in U-937 cells
    • Szabo E, Preis LH, Birrer MJ (1994) Constitutive cJun expression induces partial macrophage differentiation in U-937 cells. Cell Growth Differ 5(4):439-446
    • (1994) Cell Growth Differ , vol.5 , Issue.4 , pp. 439-446
    • Szabo, E.1    Preis, L.H.2    Birrer, M.J.3
  • 67
    • 0032544338 scopus 로고    scopus 로고
    • AP-1 and ets transcription factors regulate the expression of the human SPRR1A keratinocyte terminal differentiation marker
    • Sark MW, Fischer DF, de Meijer E, van de Putte P, Backendorf C (1998) AP-1 and ets transcription factors regulate the expression of the human SPRR1A keratinocyte terminal differentiation marker. J Biol Chem 273(38):24683-24692
    • (1998) J Biol Chem , vol.273 , Issue.38 , pp. 24683-24692
    • Sark, M.W.1    Fischer, D.F.2    De Meijer, E.3    Van De Putte, P.4    Backendorf, C.5
  • 68
    • 0023788656 scopus 로고
    • A growth factor-repressible gene associated with protein kinase C-mediated inhibition of adipocyte differentiation
    • Navre M, Ringold GM (1988) A growth factor-repressible gene associated with protein kinase C-mediated inhibition of adipocyte differentiation. J Cell Biol 107(1):279-286
    • (1988) J Cell Biol , vol.107 , Issue.1 , pp. 279-286
    • Navre, M.1    Ringold, G.M.2
  • 69
    • 0030967305 scopus 로고    scopus 로고
    • C-Jun and JunD suppress maturation of chondrocytes
    • Kameda T,Watanabe H, Iba H (1997) C-Jun and JunD suppress maturation of chondrocytes. Cell Growth Differ 8(5):495-503
    • (1997) Cell Growth Differ , vol.8 , Issue.5 , pp. 495-503
    • Kameda, T.1    Watanabe, H.2    Iba, H.3
  • 70
    • 0026664852 scopus 로고
    • Inhibition of myogenesis by okadaic acid, an inhibitor of protein phosphatases, 1 and 2A, correlates with the induction of AP1
    • Park K, Chung M, Kim SJ (1992) Inhibition of myogenesis by okadaic acid, an inhibitor of protein phosphatases, 1 and 2A, correlates with the induction of AP1. J Biol Chem 267(15):10810-10815
    • (1992) J Biol Chem , vol.267 , Issue.15 , pp. 10810-10815
    • Park, K.1    Chung, M.2    Kim, S.J.3
  • 71
    • 0021794258 scopus 로고
    • Phorbol ester inhibits myoblast fusion and activates beta-Adrenergic receptor coupled adenylate cyclase
    • Sulakhe PV, Johnson DD, Phan NT, Wilcox R (1985) Phorbol ester inhibits myoblast fusion and activates beta-Adrenergic receptor coupled adenylate cyclase. FEBS Lett 186(2): 281-285
    • (1985) FEBS Lett , vol.186 , Issue.2 , pp. 281-285
    • Sulakhe, P.V.1    Johnson, D.D.2    Phan, N.T.3    Wilcox, R.4
  • 72
    • 85047698710 scopus 로고    scopus 로고
    • Opposing functions of ATF2 and Fos-like transcription factors in c-Jun-mediated myogenin expression and terminal differentiation of avian myoblasts
    • Daury L, Busson M, Tourkine N et al (2001) Opposing functions of ATF2 and Fos-like transcription factors in c-Jun-mediated myogenin expression and terminal differentiation of avian myoblasts. Oncogene 20(55):7998-8008
    • (2001) Oncogene , vol.20 , Issue.55 , pp. 7998-8008
    • Daury, L.1    Busson, M.2    Tourkine, N.3
  • 73
    • 0028300579 scopus 로고
    • AP-1 binds to a putative cAMP response element of the MyoD1 promoter and negatively modulates MyoD1 expression in dividing myoblasts
    • Pedraza-Alva G, Zingg JM, Jost JP (1994) AP-1 binds to a putative cAMP response element of the MyoD1 promoter and negatively modulates MyoD1 expression in dividing myoblasts. J Biol Chem 269(9):6978-6985
    • (1994) J Biol Chem , vol.269 , Issue.9 , pp. 6978-6985
    • Pedraza-Alva, G.1    Zingg, J.M.2    Jost, J.P.3
  • 74
    • 33644802545 scopus 로고    scopus 로고
    • Cloning and sequence analysis of myostatin promoter in sheep
    • Du R, Chen YF, An XR et al (2005) Cloning and sequence analysis of myostatin promoter in sheep. DNA Seq 16(6):412-417
    • (2005) DNA Seq , vol.16 , Issue.6 , pp. 412-417
    • Du, R.1    Chen, Y.F.2    An, X.R.3
  • 75
    • 0038636430 scopus 로고    scopus 로고
    • Mechanisms involved in the inhibition of myoblast proliferation and differentiation by myostatin
    • Joulia D, Bernardi H, Garandel V, Rabenoelina F, Vernus B, Cabello G (2003) Mechanisms involved in the inhibition of myoblast proliferation and differentiation by myostatin. Exp Cell Res 286(2):263-275
    • (2003) Exp Cell Res , vol.286 , Issue.2 , pp. 263-275
    • Joulia, D.1    Bernardi, H.2    Garandel, V.3    Rabenoelina, F.4    Vernus, B.5    Cabello, G.6
  • 76
    • 0026513957 scopus 로고
    • Functional antagonism between c-Jun and MyoD proteins: A direct physical association
    • Bengal E, Ransone L, Scharfmann R et al (1992) Functional antagonism between c-Jun and MyoD proteins: A direct physical association. Cell 68(3):507-519
    • (1992) Cell , vol.68 , Issue.3 , pp. 507-519
    • Bengal, E.1    Ransone, L.2    Scharfmann, R.3
  • 77
    • 0027588556 scopus 로고
    • Expression of the protooncogene c-jun is maintained during myogenic differentiation in rat L6 myoblasts
    • Thinakaran G, Bag J (1993) Expression of the protooncogene c-jun is maintained during myogenic differentiation in rat L6 myoblasts. Biochem Cell Biol 71(5-6):260-269
    • (1993) Biochem Cell Biol , vol.71 , Issue.5-6 , pp. 260-269
    • Thinakaran, G.1    Bag, J.2
  • 79
    • 0030051528 scopus 로고    scopus 로고
    • MKK3-And MKK6-regulated gene expression is mediated by the p38 mitogen-Activated protein kinase signal transduction pathway
    • Raingeaud J, Whitmarsh AJ, Barrett T, Derijard B, Davis RJ (1996) MKK3-And MKK6-regulated gene expression is mediated by the p38 mitogen-Activated protein kinase signal transduction pathway. Mol Cell Biol 16(3):1247-1255
    • (1996) Mol Cell Biol , vol.16 , Issue.3 , pp. 1247-1255
    • Raingeaud, J.1    Whitmarsh, A.J.2    Barrett, T.3    Derijard, B.4    Davis, R.J.5
  • 80
    • 0029030855 scopus 로고
    • ATF-2 is preferentially activated by stress-Activated protein kinases to mediate c-jun induction in response to genotoxic agents
    • van Dam H, Wilhelm D, Herr I, Steffen A, Herrlich P, Angel P (1995) ATF-2 is preferentially activated by stress-Activated protein kinases to mediate c-jun induction in response to genotoxic agents. Embo J 14(8):1798-1811
    • (1995) Embo J , vol.14 , Issue.8 , pp. 1798-1811
    • Van Dam, H.1    Wilhelm, D.2    Herr, I.3    Steffen, A.4    Herrlich, P.5    Angel, P.6
  • 81
    • 0033548233 scopus 로고    scopus 로고
    • Stress-Activated protein kinase-2/p38 and a rapamycin-sensitive pathway are required for C2C12 myogenesis
    • Cuenda A, Cohen P (1999) Stress-Activated protein kinase-2/p38 and a rapamycin-sensitive pathway are required for C2C12 myogenesis. J Biol Chem 274(7):4341-4346
    • (1999) J Biol Chem , vol.274 , Issue.7 , pp. 4341-4346
    • Cuenda, A.1    Cohen, P.2
  • 82
    • 0034067079 scopus 로고    scopus 로고
    • P38 and extracellular signal-regulated kinases regulate the myogenic program at multiple steps
    • Wu Z, Woodring PJ, Bhakta KS et al (2000) p38 and extracellular signal-regulated kinases regulate the myogenic program at multiple steps. Mol Cell Biol 20(11):3951-3964
    • (2000) Mol Cell Biol , vol.20 , Issue.11 , pp. 3951-3964
    • Wu, Z.1    Woodring, P.J.2    Bhakta, K.S.3
  • 83
    • 0033582459 scopus 로고    scopus 로고
    • P38 mitogen-Activated protein kinase pathway promotes skeletal muscle differentiation. Participation of the Mef2c transcription factor
    • Zetser A, Gredinger E, Bengal E (1999) p38 mitogen-Activated protein kinase pathway promotes skeletal muscle differentiation. Participation of the Mef2c transcription factor. J Biol Chem 274(8):5193-5200
    • (1999) J Biol Chem , vol.274 , Issue.8 , pp. 5193-5200
    • Zetser, A.1    Gredinger, E.2    Bengal, E.3
  • 84
    • 0033575957 scopus 로고    scopus 로고
    • Activated Raf inhibits avian myogenesis through aMAPKdependent mechanism
    • Dorman CM, Johnson SE (1999) Activated Raf inhibits avian myogenesis through aMAPKdependent mechanism. Oncogene 18(37):5167-5176
    • (1999) Oncogene , vol.18 , Issue.37 , pp. 5167-5176
    • Dorman, C.M.1    Johnson, S.E.2
  • 85
    • 0033551374 scopus 로고    scopus 로고
    • MYC oncogenes and human neoplastic disease
    • Nesbit CE, Tersak JM, Prochownik EV (1999) MYC oncogenes and human neoplastic disease. Oncogene 18(19):3004-3016
    • (1999) Oncogene , vol.18 , Issue.19 , pp. 3004-3016
    • Nesbit, C.E.1    Tersak, J.M.2    Prochownik, E.V.3
  • 86
    • 0034724389 scopus 로고    scopus 로고
    • Expression analysis with oligonucleotide microarrays reveals that MYC regulates genes involved in growth, cell cycle, signaling, and adhesion
    • Coller HA, Grandori C, Tamayo P et al (2000) Expression analysis with oligonucleotide microarrays reveals that MYC regulates genes involved in growth, cell cycle, signaling, and adhesion. Proc Natl Acad Sci U S A 97(7):3260-3265
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.7 , pp. 3260-3265
    • Coller, H.A.1    Grandori, C.2    Tamayo, P.3
  • 87
    • 0025043520 scopus 로고
    • Negative autoregulation of c-myc gene expression is inactivated in transformed cells
    • Grignani F, Lombardi L, Inghirami G, Sternas L, Cechova K, Dalla-Favera R (1990) Negative autoregulation of c-myc gene expression is inactivated in transformed cells. Embo J 9(12):3913-3922
    • (1990) Embo J , vol.9 , Issue.12 , pp. 3913-3922
    • Grignani, F.1    Lombardi, L.2    Inghirami, G.3    Sternas, L.4    Cechova, K.5    Dalla-Favera, R.6
  • 88
    • 0025317564 scopus 로고
    • Negative autoregulation of c-myc transcription
    • Penn LJ, Brooks MW, Laufer EM, Land H (1990) Negative autoregulation of c-myc transcription. Embo J 9(4):1113-1121
    • (1990) Embo J , vol.9 , Issue.4 , pp. 1113-1121
    • Penn, L.J.1    Brooks, M.W.2    Laufer, E.M.3    Land, H.4
  • 89
    • 0032535253 scopus 로고    scopus 로고
    • Transactivation-defective c-MycS retains the ability to regulate proliferation and apoptosis
    • Xiao Q, Claassen G, Shi J, Adachi S, Sedivy J, Hann SR (1998) Transactivation-defective c-MycS retains the ability to regulate proliferation and apoptosis. Genes Dev 12(24): 3803-3808
    • (1998) Genes Dev , vol.12 , Issue.24 , pp. 3803-3808
    • Xiao, Q.1    Claassen, G.2    Shi, J.3    Adachi, S.4    Sedivy, J.5    Hann, S.R.6
  • 90
    • 0033551377 scopus 로고    scopus 로고
    • Myc-mediated transformation: The repression connection
    • Claassen GF, Hann SR (1999) Myc-mediated transformation: The repression connection. Oncogene 18(19):2925-2933
    • (1999) Oncogene , vol.18 , Issue.19 , pp. 2925-2933
    • Claassen, G.F.1    Hann, S.R.2
  • 91
    • 0035089346 scopus 로고    scopus 로고
    • Function of the c-Myc oncoprotein in chromatin remodeling and transcription
    • Amati B, Frank SR, Donjerkovic D, Taubert S (2001) Function of the c-Myc oncoprotein in chromatin remodeling and transcription. Biochim Biophys Acta 1471(3):M135-145
    • (2001) Biochim Biophys Acta , vol.1471 , Issue.3
    • Amati, B.1    Frank, S.R.2    Donjerkovic, D.3    Taubert, S.4
  • 92
    • 0037084333 scopus 로고    scopus 로고
    • C-Abl is an effector of Src for growth factor-induced c-myc expression and DNA synthesis
    • Furstoss O, Dorey K, Simon V, Barila D, Superti-Furga G, Roche S (2002) c-Abl is an effector of Src for growth factor-induced c-myc expression and DNA synthesis. Embo J 21(4):514-524
    • (2002) Embo J , vol.21 , Issue.4 , pp. 514-524
    • Furstoss, O.1    Dorey, K.2    Simon, V.3    Barila, D.4    Superti-Furga, G.5    Roche, S.6
  • 93
    • 0023023281 scopus 로고
    • Modulation of c-fos and c-myc mRNA levels in normal human lymphocytes by calcium ionophore A23187 and phorbol ester
    • Grausz JD, Fradelizi D, Dautry F, Monier R, Lehn P (1986) Modulation of c-fos and c-myc mRNA levels in normal human lymphocytes by calcium ionophore A23187 and phorbol ester. Eur J Immunol 16(10):1217-1221
    • (1986) Eur J Immunol , vol.16 , Issue.10 , pp. 1217-1221
    • Grausz, J.D.1    Fradelizi, D.2    Dautry, F.3    Monier, R.4    Lehn, P.5
  • 94
    • 0034676269 scopus 로고    scopus 로고
    • The RelA NF-kappaB subunit and the aryl hydrocarbon receptor (AhR) cooperate to transactivate the c-myc promoter in mammary cells
    • Kim DW, Gazourian L, Quadri SA, Romieu-Mourez R, Sherr DH, Sonenshein GE (2000) The RelA NF-kappaB subunit and the aryl hydrocarbon receptor (AhR) cooperate to transactivate the c-myc promoter in mammary cells. Oncogene 19(48):5498-5506
    • (2000) Oncogene , vol.19 , Issue.48 , pp. 5498-5506
    • Kim, D.W.1    Gazourian, L.2    Quadri, S.A.3    Romieu-Mourez, R.4    Sherr, D.H.5    Sonenshein, G.E.6
  • 95
    • 0026812207 scopus 로고
    • Role of [Ca2+]i in induction of c-fos, c-jun, and c-myc mRNA in rat PTE after oxidative stress
    • Maki A, Berezesky IK, Fargnoli J, Holbrook NJ, Trump BF (1992) Role of [Ca2+]i in induction of c-fos, c-jun, and c-myc mRNA in rat PTE after oxidative stress. Faseb J 6(3):919-924
    • (1992) Faseb J , vol.6 , Issue.3 , pp. 919-924
    • Maki, A.1    Berezesky, I.K.2    Fargnoli, J.3    Holbrook, N.J.4    Trump, B.F.5
  • 96
    • 0025286079 scopus 로고
    • Regulation of protooncogenes c-fos and c-myc expressions by protein tyrosine kinase, protein kinase C, and cyclic AMP mitogenic pathways in dog primary thyrocytes: A positive and negative control by cyclic AMP on c-myc expression
    • Reuse S, Maenhaut C, Dumont JE (1990) Regulation of protooncogenes c-fos and c-myc expressions by protein tyrosine kinase, protein kinase C, and cyclic AMP mitogenic pathways in dog primary thyrocytes: A positive and negative control by cyclic AMP on c-myc expression. Exp Cell Res 189(1):33-40
    • (1990) Exp Cell Res , vol.189 , Issue.1 , pp. 33-40
    • Reuse, S.1    Maenhaut, C.2    Dumont, J.E.3
  • 97
    • 0023259725 scopus 로고
    • Rapid transcriptional down-regulation of c-myc expression during cyclic adenosine monophosphate-promoted differentiation of leukemic cells
    • Slungaard A, Confer DL, Schubach WH (1987) Rapid transcriptional down-regulation of c-myc expression during cyclic adenosine monophosphate- promoted differentiation of leukemic cells. J Clin Invest 79(5):1542-1547
    • (1987) J Clin Invest , vol.79 , Issue.5 , pp. 1542-1547
    • Slungaard, A.1    Confer, D.L.2    Schubach, W.H.3
  • 99
    • 0029560024 scopus 로고
    • Translational upregulation of the c-myc oncogene in Bloom's syndrome cell lines
    • West MJ, Sullivan NF, Willis AE (1995) Translational upregulation of the c-myc oncogene in Bloom's syndrome cell lines. Oncogene 11(12):2515-2524
    • (1995) Oncogene , vol.11 , Issue.12 , pp. 2515-2524
    • West, M.J.1    Sullivan, N.F.2    Willis, A.E.3
  • 100
    • 0034059667 scopus 로고    scopus 로고
    • C-Myc proteolysis by the ubiquitin-proteasome pathway: Stabilization of c-Myc in Burkitt's lymphoma cells
    • Gregory MA, Hann SR (2000) c-Myc proteolysis by the ubiquitin-proteasome pathway: Stabilization of c-Myc in Burkitt's lymphoma cells. Mol Cell Biol 20(7):2423-2435
    • (2000) Mol Cell Biol , vol.20 , Issue.7 , pp. 2423-2435
    • Gregory, M.A.1    Hann, S.R.2
  • 101
    • 0033081027 scopus 로고    scopus 로고
    • Destruction of Myc by ubiquitin-mediated proteolysis: Cancer-Associated and transforming mutations stabilize Myc
    • Salghetti SE, Kim SY, Tansey WP (1999) Destruction of Myc by ubiquitin-mediated proteolysis: Cancer-Associated and transforming mutations stabilize Myc. Embo J 18(3):717-726
    • (1999) Embo J , vol.18 , Issue.3 , pp. 717-726
    • Salghetti, S.E.1    Kim, S.Y.2    Tansey, W.P.3
  • 102
    • 2342507059 scopus 로고    scopus 로고
    • Multiple cell-Type-specific elements regulate Myc protein stability
    • Herbst A, Salghetti SE, Kim SY, Tansey WP (2004) Multiple cell-Type-specific elements regulate Myc protein stability. Oncogene 23(21):3863-3871
    • (2004) Oncogene , vol.23 , Issue.21 , pp. 3863-3871
    • Herbst, A.1    Salghetti, S.E.2    Kim, S.Y.3    Tansey, W.P.4
  • 103
    • 0029166263 scopus 로고
    • Myc inhibits CCAAT/enhancer-binding protein alpha-gene expression in HIB-1B hibernoma cells through interactions with the core promoter region
    • Antonson P, Pray MG, Jacobsson A, Xanthopoulos KG (1995) Myc inhibits CCAAT/enhancer-binding protein alpha-gene expression in HIB-1B hibernoma cells through interactions with the core promoter region. Eur J Biochem 232(2):397-403
    • (1995) Eur J Biochem , vol.232 , Issue.2 , pp. 397-403
    • Antonson, P.1    Pray, M.G.2    Jacobsson, A.3    Xanthopoulos, K.G.4
  • 104
    • 0028169192 scopus 로고
    • C-Myc represses transcription in vivo by a novel mechanism dependent on the initiator element and Myc box II
    • Li LH, Nerlov C, Prendergast G, MacGregor D, Ziff EB (1994) c-Myc represses transcription in vivo by a novel mechanism dependent on the initiator element and Myc box II. Embo J 13(17):4070-4079
    • (1994) Embo J , vol.13 , Issue.17 , pp. 4070-4079
    • Li, L.H.1    Nerlov, C.2    Prendergast, G.3    MacGregor, D.4    Ziff, E.B.5
  • 106
    • 0034662959 scopus 로고    scopus 로고
    • A role for transcriptional repression of p21CIP1 by c-Myc in overcoming transforming growth factor beta -induced cell-cycle arrest
    • Claassen GF, Hann SR (2000) A role for transcriptional repression of p21CIP1 by c-Myc in overcoming transforming growth factor beta -induced cell-cycle arrest. Proc Natl Acad Sci U S A 97(17):9498-9503
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.17 , pp. 9498-9503
    • Claassen, G.F.1    Hann, S.R.2
  • 107
    • 0037461931 scopus 로고    scopus 로고
    • Myc represses differentiation-induced p21CIP1 expression via Miz-1-dependent interaction with the p21 core promoter
    • Wu S, Cetinkaya C, Munoz-Alonso MJ, et al (2003) Myc represses differentiation-induced p21CIP1 expression via Miz-1-dependent interaction with the p21 core promoter. Oncogene 22(3):351-360
    • (2003) Oncogene , vol.22 , Issue.3 , pp. 351-360
    • Wu, S.1    Cetinkaya, C.2    Munoz-Alonso, M.J.3
  • 108
    • 0035967099 scopus 로고    scopus 로고
    • Repression of transcription of the p27(Kip1) cyclindependent kinase inhibitor gene by c-Myc
    • Yang W, Shen J, Wu M et al (2001) Repression of transcription of the p27(Kip1) cyclindependent kinase inhibitor gene by c-Myc. Oncogene 20(14):1688-1702
    • (2001) Oncogene , vol.20 , Issue.14 , pp. 1688-1702
    • Yang, W.1    Shen, J.2    Wu, M.3
  • 109
    • 0023412276 scopus 로고
    • C-myc oncogene expression inhibits the initiation of myogenic differentiation
    • Denis N, Blanc S, Leibovitch MP et al (1987) c-myc oncogene expression inhibits the initiation of myogenic differentiation. Exp Cell Res 172(1):212-217
    • (1987) Exp Cell Res , vol.172 , Issue.1 , pp. 212-217
    • Denis, N.1    Blanc, S.2    Leibovitch, M.P.3
  • 110
    • 0022373817 scopus 로고
    • Density-dependent arrest of DNA replication is accompanied by decreased levels of c-myc mRNA in myogenic but not in differentiationdefective myoblasts
    • Sejersen T, Sumegi J, Ringertz NR (1985) Density-dependent arrest of DNA replication is accompanied by decreased levels of c-myc mRNA in myogenic but not in differentiationdefective myoblasts. J Cell Physiol 125(3):465-470
    • (1985) J Cell Physiol , vol.125 , Issue.3 , pp. 465-470
    • Sejersen, T.1    Sumegi, J.2    Ringertz, N.R.3
  • 111
    • 0032546790 scopus 로고    scopus 로고
    • C-myc mRNA is downregulated during myogenic differentiation by accelerated decay that depends on translation of regulatory coding elements
    • Yeilding NM, Procopio WN, Rehman MT, Lee WM (1998) c-myc mRNA is downregulated during myogenic differentiation by accelerated decay that depends on translation of regulatory coding elements. J Biol Chem 273(25):15749-15757
    • (1998) J Biol Chem , vol.273 , Issue.25 , pp. 15749-15757
    • Yeilding, N.M.1    Procopio, W.N.2    Rehman, M.T.3    Lee, W.M.4
  • 112
    • 0028234646 scopus 로고
    • Transformation by myc prevents fusion but not biochemical differentiation of C2C12 myoblasts: Mechanisms of phenotypic correction in mixed culture with normal cells
    • Crescenzi M, Crouch DH, Tato F (1994) Transformation by myc prevents fusion but not biochemical differentiation of C2C12 myoblasts: Mechanisms of phenotypic correction in mixed culture with normal cells. J Cell Biol 125(5):1137-1145
    • (1994) J Cell Biol , vol.125 , Issue.5 , pp. 1137-1145
    • Crescenzi, M.1    Crouch, D.H.2    Tato, F.3
  • 114
    • 0242582469 scopus 로고    scopus 로고
    • Reciprocal inhibition between MyoD and STAT3 in the regulation of growth and differentiation of myoblasts
    • Kataoka Y, Matsumura I, Ezoe S et al (2003) Reciprocal inhibition between MyoD and STAT3 in the regulation of growth and differentiation of myoblasts. J Biol Chem 278(45):44178-44187
    • (2003) J Biol Chem , vol.278 , Issue.45 , pp. 44178-44187
    • Kataoka, Y.1    Matsumura, I.2    Ezoe, S.3
  • 115
    • 0026625171 scopus 로고
    • Transforming growth factor beta induces myoblast differentiation in the presence of mitogens
    • Zentella A, Massague J (1992) Transforming growth factor beta induces myoblast differentiation in the presence of mitogens. Proc Natl Acad Sci U S A 89(11):5176-5180
    • (1992) Proc Natl Acad Sci U S A , vol.89 , Issue.11 , pp. 5176-5180
    • Zentella, A.1    Massague, J.2
  • 116
    • 0031882131 scopus 로고    scopus 로고
    • Increase in p202 expression during skeletal muscle differentiation: Inhibition of MyoD protein expression and activity by p202
    • Datta B, Min W, Burma S, Lengyel P (1998) Increase in p202 expression during skeletal muscle differentiation: Inhibition of MyoD protein expression and activity by p202. Mol Cell Biol 18(2):1074-1083
    • (1998) Mol Cell Biol , vol.18 , Issue.2 , pp. 1074-1083
    • Datta, B.1    Min, W.2    Burma, S.3    Lengyel, P.4
  • 117
    • 0034282393 scopus 로고    scopus 로고
    • The interferon-And differentiation-inducible p202a protein inhibits the transcriptional activity of c-Myc by blocking its association with Max
    • Wang H, Liu C, Lu Y et al (2000) The interferon-And differentiation- inducible p202a protein inhibits the transcriptional activity of c-Myc by blocking its association with Max. J Biol Chem 275(35):27377-27285
    • (2000) J Biol Chem , vol.275 , Issue.35 , pp. 27377-27285
    • Wang, H.1    Liu, C.2    Lu, Y.3
  • 119
    • 0029779280 scopus 로고    scopus 로고
    • Cdc25 cell-cycle phosphatase as a target of c-myc
    • Galaktionov K, Chen X, Beach D (1996) Cdc25 cell-cycle phosphatase as a target of c-myc. Nature 382(6591):511-517
    • (1996) Nature , vol.382 , Issue.6591 , pp. 511-517
    • Galaktionov, K.1    Chen, X.2    Beach, D.3
  • 120
    • 0023786827 scopus 로고
    • C-myc antisense transcripts accelerate differentiation and inhibit G1 progression in murine erythroleukemia cells
    • Prochownik EV, Kukowska J, Rodgers C (1988) c-myc antisense transcripts accelerate differentiation and inhibit G1 progression in murine erythroleukemia cells. Mol Cell Biol 8(9):3683-3695
    • (1988) Mol Cell Biol , vol.8 , Issue.9 , pp. 3683-3695
    • Prochownik, E.V.1    Kukowska, J.2    Rodgers, C.3
  • 121
    • 0029094329 scopus 로고
    • Identification of a Myc-dependent step during the formation of active G1 cyclin-cdk complexes
    • Steiner P, Philipp A, Lukas J et al (1995) Identification of a Myc-dependent step during the formation of active G1 cyclin-cdk complexes. Embo J 14(19):4814-4826
    • (1995) Embo J , vol.14 , Issue.19 , pp. 4814-4826
    • Steiner, P.1    Philipp, A.2    Lukas, J.3
  • 123
    • 0034616116 scopus 로고    scopus 로고
    • Reciprocal regulation via protein-protein interaction between c-Myc and p21(cip1/waf1/sdi1) in DNA replication and transcription
    • Kitaura H, Shinshi M, Uchikoshi Y, Ono T, Iguchi-Ariga SM, Ariga H (2000) Reciprocal regulation via protein-protein interaction between c-Myc and p21(cip1/waf1/sdi1) in DNA replication and transcription. J Biol Chem 275(14):10477-10483
    • (2000) J Biol Chem , vol.275 , Issue.14 , pp. 10477-10483
    • Kitaura, H.1    Shinshi, M.2    Uchikoshi, Y.3    Ono, T.4    Iguchi-Ariga, S.M.5    Ariga, H.6
  • 124
    • 0034609818 scopus 로고    scopus 로고
    • Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins
    • Lasorella A, Noseda M, Beyna M, Yokota Y, Iavarone A (2000) Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins. Nature 407(6804): 592-598
    • (2000) Nature , vol.407 , Issue.6804 , pp. 592-598
    • Lasorella, A.1    Noseda, M.2    Beyna, M.3    Yokota, Y.4    Iavarone, A.5
  • 125
    • 0028037187 scopus 로고
    • C-Myc inhibits myogenic differentiation and myoD expression by a mechanism which can be dissociated from cell transformation
    • La Rocca SA, Crouch DH, Gillespie DA (1994). c-Myc inhibits myogenic differentiation and myoD expression by a mechanism which can be dissociated from cell transformation. Oncogene 9(12):3499-3508
    • (1994) Oncogene , vol.9 , Issue.12 , pp. 3499-3508
    • La Rocca, S.A.1    Crouch, D.H.2    Gillespie, D.A.3
  • 126
    • 0037130480 scopus 로고    scopus 로고
    • Selective repression of myoD transcription by v-Myc prevents terminal differentiation of quail embryo myoblasts transformed by the MC29 strain of avian myelocytomatosis virus
    • La Rocca SA, Vannucchi S, Pompili M et al (2002). Selective repression of myoD transcription by v-Myc prevents terminal differentiation of quail embryo myoblasts transformed by the MC29 strain of avian myelocytomatosis virus. Oncogene 21(31):4838-4842
    • (2002) Oncogene , vol.21 , Issue.31 , pp. 4838-4842
    • La Rocca, S.A.1    Vannucchi, S.2    Pompili, M.3
  • 127
    • 0029618368 scopus 로고
    • Steroid hormone receptors: Many actors in search of a plot
    • Beato M, Herrlich P, Schutz G (1995). Steroid hormone receptors: Many actors in search of a plot. Cell 83(6):851-857
    • (1995) Cell , vol.83 , Issue.6 , pp. 851-857
    • Beato, M.1    Herrlich, P.2    Schutz, G.3
  • 128
    • 0034964207 scopus 로고    scopus 로고
    • Physiological and molecular basis of thyroid hormone action
    • Yen PM (2001). Physiological and molecular basis of thyroid hormone action. Physiol Rev 81(3):1097-1142
    • (2001) Physiol Rev , vol.81 , Issue.3 , pp. 1097-1142
    • Yen, P.M.1
  • 129
    • 0031759733 scopus 로고    scopus 로고
    • Characterization of a negative thyroid hormone response element in the rat sodium, potassium-Adenosine triphosphatase alpha3 gene promoter
    • Chin S, Apriletti J, Gick G (1998) Characterization of a negative thyroid hormone response element in the rat sodium, potassium-Adenosine triphosphatase alpha3 gene promoter. Endocrinology 139(8):3423-3431
    • (1998) Endocrinology , vol.139 , Issue.8 , pp. 3423-3431
    • Chin, S.1    Apriletti, J.2    Gick, G.3
  • 130
    • 0030037216 scopus 로고    scopus 로고
    • Identification of functional positive and negative thyroid hormone-responsive elements in the rat apolipoprotein AI promoter
    • Taylor AH, Wishart P, Lawless DE, Raymond J, Wong NC (1996) Identification of functional positive and negative thyroid hormone-responsive elements in the rat apolipoprotein AI promoter. Biochemistry 35(25):8281-8288
    • (1996) Biochemistry , vol.35 , Issue.25 , pp. 8281-8288
    • Taylor, A.H.1    Wishart, P.2    Lawless, D.E.3    Raymond, J.4    Wong, N.C.5
  • 131
    • 0023664362 scopus 로고
    • Discrete positive and negative thyroid hormoneresponsive transcription regulatory elements of the rat growth hormone gene
    • Wight PA, Crew MD, Spindler SR (1987) Discrete positive and negative thyroid hormoneresponsive transcription regulatory elements of the rat growth hormone gene. J Biol Chem 262(12):5659-5663
    • (1987) J Biol Chem , vol.262 , Issue.12 , pp. 5659-5663
    • Wight, P.A.1    Crew, M.D.2    Spindler, S.R.3
  • 132
    • 0024273638 scopus 로고
    • Localization of human ERBA2 to the 3p22-3p24.1 region of chromosome 3 and variable deletion in small cell lung cancer
    • Drabkin H, Kao FT, Hartz J et al (1988) Localization of human ERBA2 to the 3p22-3p24.1 region of chromosome 3 and variable deletion in small cell lung cancer. Proc Natl Acad Sci U S A 85(23):9258-9262
    • (1988) Proc Natl Acad Sci U S A , vol.85 , Issue.23 , pp. 9258-9262
    • Drabkin, H.1    Kao, F.T.2    Hartz, J.3
  • 133
    • 0004655257 scopus 로고
    • Trans-Activation by thyroid hormone receptors: Functional parallels with steroid hormone receptors
    • Thompson CC, Evans RM (1989) Trans-Activation by thyroid hormone receptors: Functional parallels with steroid hormone receptors. Proc Natl Acad Sci U S A 86(10):3494-3498
    • (1989) Proc Natl Acad Sci U S A , vol.86 , Issue.10 , pp. 3494-3498
    • Thompson, C.C.1    Evans, R.M.2
  • 134
    • 0038407750 scopus 로고    scopus 로고
    • Thyroid hormone receptors: Lessons from knockout and knockin mutant mice
    • Flamant F, Samarut J (2003) Thyroid hormone receptors: Lessons from knockout and knockin mutant mice. Trends Endocrinol Metab 14(2):85-90
    • (2003) Trends Endocrinol Metab , vol.14 , Issue.2 , pp. 85-90
    • Flamant, F.1    Samarut, J.2
  • 135
    • 0028170232 scopus 로고
    • Vitamin D3-Thyroid hormone receptor heterodimer polarity directs ligand sensitivity of transactivation
    • Schrader M, Muller KM, Nayeri S, Kahlen JP, Carlberg C (1994) Vitamin D3-Thyroid hormone receptor heterodimer polarity directs ligand sensitivity of transactivation. Nature 370(6488):382-386
    • (1994) Nature , vol.370 , Issue.6488 , pp. 382-386
    • Schrader, M.1    Muller, K.M.2    Nayeri, S.3    Kahlen, J.P.4    Carlberg, C.5
  • 136
    • 0028307070 scopus 로고
    • A novel heterodimerization partner for thyroid hormone receptor. Peroxisome proliferator-Activated receptor
    • Bogazzi F, Hudson LD, Nikodem VM (1994) A novel heterodimerization partner for thyroid hormone receptor. Peroxisome proliferator-Activated receptor. J Biol Chem 269(16): 11683-11686
    • (1994) J Biol Chem , vol.269 , Issue.16 , pp. 11683-11686
    • Bogazzi, F.1    Hudson, L.D.2    Nikodem, V.M.3
  • 137
    • 0024457916 scopus 로고
    • A domain containing leucine-zipper-like motifs mediate novel in vivo interactions between the thyroid hormone and retinoic acid receptors
    • Forman BM, Yang CR, Au M, Casanova J, Ghysdael J, Samuels HH (1989) A domain containing leucine-zipper-like motifs mediate novel in vivo interactions between the thyroid hormone and retinoic acid receptors. Mol Endocrinol 3(10):1610-1626
    • (1989) Mol Endocrinol , vol.3 , Issue.10 , pp. 1610-1626
    • Forman, B.M.1    Yang, C.R.2    Au, M.3    Casanova, J.4    Ghysdael, J.5    Samuels, H.H.6
  • 138
    • 0024465135 scopus 로고
    • Positive and negative regulation of gene transcription by a retinoic acid-Thyroid hormone receptor heterodimer
    • Glass CK, Lipkin SM, Devary OV, Rosenfeld MG (1989) Positive and negative regulation of gene transcription by a retinoic acid-Thyroid hormone receptor heterodimer. Cell 59(4): 697-708
    • (1989) Cell , vol.59 , Issue.4 , pp. 697-708
    • Glass, C.K.1    Lipkin, S.M.2    Devary, O.V.3    Rosenfeld, M.G.4
  • 139
    • 0027248681 scopus 로고
    • Characterization and tissue expression of multiple triiodothyronine receptor-Auxiliary proteins and their relationship to the retinoid X-receptors
    • Sugawara A, Yen PM, Darling DS, ChinWW(1993) Characterization and tissue expression of multiple triiodothyronine receptor-Auxiliary proteins and their relationship to the retinoid X-receptors. Endocrinology 133(3):965-971
    • (1993) Endocrinology , vol.133 , Issue.3 , pp. 965-971
    • Sugawara, A.1    Yen, P.M.2    Darling, D.S.3    Chin, W.W.4
  • 140
    • 0025987831 scopus 로고
    • A novel mechanism of action for v-ErbA: Abrogation of the inactivation of transcription factor AP-1 by retinoic acid and thyroid hormone receptors
    • Desbois C, Aubert D, Legrand C, Pain B, Samarut J (1991) A novel mechanism of action for v-ErbA: Abrogation of the inactivation of transcription factor AP-1 by retinoic acid and thyroid hormone receptors. Cell 67(4):731-740
    • (1991) Cell , vol.67 , Issue.4 , pp. 731-740
    • Desbois, C.1    Aubert, D.2    Legrand, C.3    Pain, B.4    Samarut, J.5
  • 141
    • 0025986117 scopus 로고
    • Novel pathway for thyroid hormone receptor action through interaction with jun and fos oncogene activities
    • Zhang XK, Wills KN, Husmann M, Hermann T, Pfahl M (1991) Novel pathway for thyroid hormone receptor action through interaction with jun and fos oncogene activities. Mol Cell Biol 11(12):6016-6025
    • (1991) Mol Cell Biol , vol.11 , Issue.12 , pp. 6016-6025
    • Zhang, X.K.1    Wills, K.N.2    Husmann, M.3    Hermann, T.4    Pfahl, M.5
  • 142
    • 0027514903 scopus 로고
    • Triiodothyronine influences quail myoblast proliferation and differentiation
    • Marchal S, Cassar-Malek I, Pons F, Wrutniak C, Cabello G (1993) Triiodothyronine influences quail myoblast proliferation and differentiation. Biol Cell 78(3):191-197
    • (1993) Biol Cell , vol.78 , Issue.3 , pp. 191-197
    • Marchal, S.1    Cassar-Malek, I.2    Pons, F.3    Wrutniak, C.4    Cabello, G.5
  • 143
    • 0029935971 scopus 로고    scopus 로고
    • Induction of c-Erb A-AP-1 interactions and c-Erb A transcriptional activity in myoblasts by RXR. Consequences for muscle differentiation
    • Cassar-Malek I, Marchal S, Rochard P, et al (1996) Induction of c-Erb A-AP-1 interactions and c-Erb A transcriptional activity in myoblasts by RXR. Consequences for muscle differentiation. J Biol Chem 271(19):11392-11399
    • (1996) J Biol Chem , vol.271 , Issue.19 , pp. 11392-11399
    • Cassar-Malek, I.1    Marchal, S.2    Rochard, P.3
  • 144
    • 0027688033 scopus 로고
    • Identification of a thyroid hormone response element in the mouse myogenin gene: Characterization of the thyroid hormone and retinoid X receptor heterodimeric binding site
    • Downes M, Griggs R, Atkins A, Olson EN, Muscat GE (1993) Identification of a thyroid hormone response element in the mouse myogenin gene: Characterization of the thyroid hormone and retinoid X receptor heterodimeric binding site. Cell Growth Differ 4(11): 901-909
    • (1993) Cell Growth Differ , vol.4 , Issue.11 , pp. 901-909
    • Downes, M.1    Griggs, R.2    Atkins, A.3    Olson, E.N.4    Muscat, G.E.5
  • 145
    • 0018706325 scopus 로고
    • Studies of the effect of chloramphenicol, ethidium bromide and camptothecin on the reproduction of Rous sarcoma virus in infected chick embryo cells
    • Leblond-Larouche L, Morais R, Zollinger M (1979) Studies of the effect of chloramphenicol, ethidium bromide and camptothecin on the reproduction of Rous sarcoma virus in infected chick embryo cells. J Gen Virol 44(2):323-331
    • (1979) J Gen Virol , vol.44 , Issue.2 , pp. 323-331
    • Leblond-Larouche, L.1    Morais, R.2    Zollinger, M.3
  • 146
    • 0018862049 scopus 로고
    • Chick embryo cells rendered respiration-deficient by chloramphenicol and ethidium bromide are auxotrophic for pyrimidines
    • Morais R, Gregoire M, Jeannotte L, Gravel D (1980) Chick embryo cells rendered respiration-deficient by chloramphenicol and ethidium bromide are auxotrophic for pyrimidines. Biochem Biophys Res Commun 94(1):71-77
    • (1980) Biochem Biophys Res Commun , vol.94 , Issue.1 , pp. 71-77
    • Morais, R.1    Gregoire, M.2    Jeannotte, L.3    Gravel, D.4
  • 147
    • 0026799250 scopus 로고
    • Relationship between culture conditions and the dependency on mitochondrial function of mammalian cell proliferation
    • van den Bogert C, Spelbrink JN, Dekker HL (1992) Relationship between culture conditions and the dependency on mitochondrial function of mammalian cell proliferation. J Cell Physiol 152(3):632-638
    • (1992) J Cell Physiol , vol.152 , Issue.3 , pp. 632-638
    • Van Den Bogert, C.1    Spelbrink, J.N.2    Dekker, H.L.3
  • 148
    • 0030693962 scopus 로고    scopus 로고
    • Inhibition of mitochondrial protein synthesis impaired C2C12 myoblast differentiation
    • Hamai N, Nakamura M, Asano A (1997) Inhibition of mitochondrial protein synthesis impaired C2C12 myoblast differentiation. Cell Struct Funct 22(4):421-431
    • (1997) Cell Struct Funct , vol.22 , Issue.4 , pp. 421-431
    • Hamai, N.1    Nakamura, M.2    Asano, A.3
  • 149
    • 0023803436 scopus 로고
    • Effect of mitochondrial protein synthesis inhibitors on erythroid differentiation of mouse erythroleukemia (Friend) cells
    • Kaneko T, Watanabe T, Oishi M (1988) Effect of mitochondrial protein synthesis inhibitors on erythroid differentiation of mouse erythroleukemia (Friend) cells. Mol Cell Biol 8(8):3311-3315
    • (1988) Mol Cell Biol , vol.8 , Issue.8 , pp. 3311-3315
    • Kaneko, T.1    Watanabe, T.2    Oishi, M.3
  • 150
    • 0027351023 scopus 로고
    • Chloramphenicol, an inhibitor of mitochondrial protein syn thesis, inhibits myoblast fusion and myotube differentiation
    • Korohoda W, Pietrzkowski Z, Reiss K (1993) Chloramphenicol, an inhibitor of mitochondrial protein synthesis, inhibits myoblast fusion and myotube differentiation. Folia Histochem Cytobiol 31(1):9-13
    • (1993) Folia Histochem Cytobiol , vol.31 , Issue.1 , pp. 9-13
    • Korohoda, W.1    Pietrzkowski, Z.2    Reiss, K.3
  • 152
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • Newmeyer DD, Ferguson-Miller S (2003) Mitochondria: Releasing power for life and unleashing the machineries of death. Cell 112(4):481-490
    • (2003) Cell , vol.112 , Issue.4 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 153
    • 0031930319 scopus 로고    scopus 로고
    • Mitochondrial transcription factor A is necessary for mtDNA maintenance and embryogenesis in mice
    • Larsson NG, Wang J, Wilhelmsson H et al (1998) Mitochondrial transcription factor A is necessary for mtDNA maintenance and embryogenesis in mice. Nat Genet 18(3):231-236
    • (1998) Nat Genet , vol.18 , Issue.3 , pp. 231-236
    • Larsson, N.G.1    Wang, J.2    Wilhelmsson, H.3
  • 154
    • 0033981680 scopus 로고    scopus 로고
    • Mitochondrial defects in cardiomyopathy and neuromuscular disease
    • Wallace DC (2000) Mitochondrial defects in cardiomyopathy and neuromuscular disease. Am Heart J 139(2 Pt 3):S70-85
    • (2000) Am Heart J , vol.139 , Issue.2 PART 3
    • Wallace, D.C.1
  • 155
    • 0029736922 scopus 로고    scopus 로고
    • Changes in mitochondrial activity during avian myoblast differentiation: Influence of triiodothyronine or v-erb A expression
    • Rochard P, Cassar-Malek I,Marchal S, Wrutniak C, Cabello G (1996) Changes in mitochondrial activity during avian myoblast differentiation: Influence of triiodothyronine or v-erb A expression. J Cell Physiol 168(2):239-247
    • (1996) J Cell Physiol , vol.168 , Issue.2 , pp. 239-247
    • Rochard, P.1    Cassar-Malek, I.2    Marchal, S.3    Wrutniak, C.4    Cabello, G.5
  • 156
    • 0030920779 scopus 로고    scopus 로고
    • Mitochondrial DNA maintenance in vertebrates
    • Shadel GS, Clayton DA (1997) Mitochondrial DNA maintenance in vertebrates. Annu Rev Biochem 66:409-435
    • (1997) Annu Rev Biochem , vol.66 , pp. 409-435
    • Shadel, G.S.1    Clayton, D.A.2
  • 158
    • 0036148610 scopus 로고    scopus 로고
    • A human mitochondrial transcription factor is related to RNA adenine methyltransferases and binds S-Adenosylmethionine
    • McCulloch V, Seidel-Rogol BL, Shadel GS (2002) A human mitochondrial transcription factor is related to RNA adenine methyltransferases and binds S-Adenosylmethionine. Mol Cell Biol 22(4):1116-1125
    • (2002) Mol Cell Biol , vol.22 , Issue.4 , pp. 1116-1125
    • McCulloch, V.1    Seidel-Rogol, B.L.2    Shadel, G.S.3
  • 159
    • 0028999361 scopus 로고
    • A 43-kDa protein related to c-Erb A [IMAGE]1 is located in the mitochondrial matrix of rat liver
    • Wrutniak C, Cassar-Malek I, Marchal S et al (1995) A 43-kDa protein related to c-Erb A [IMAGE]1 is located in the mitochondrial matrix of rat liver. J Biol Chem 270(27): 16347-16354
    • (1995) J Biol Chem , vol.270 , Issue.27 , pp. 16347-16354
    • Wrutniak, C.1    Cassar-Malek, I.2    Marchal, S.3
  • 160
    • 0034725984 scopus 로고    scopus 로고
    • A 45 kDa protein related to PPARgamma2, induced by peroxisome proliferators, is located in the mitochondrial matrix
    • Casas F, Domenjoud L, Rochard P et al (2000) A 45 kDa protein related to PPARgamma2, induced by peroxisome proliferators, is located in the mitochondrial matrix. FEBS Lett 478(1-2):4-8
    • (2000) FEBS Lett , vol.478 , Issue.1-2 , pp. 4-8
    • Casas, F.1    Domenjoud, L.2    Rochard, P.3
  • 162
    • 0033506827 scopus 로고    scopus 로고
    • A variant form of the nuclear triiodothyronine receptor c-ErbAalpha1 plays a direct role in regulation of mitochondrial RNA synthesis
    • Casas F, Rochard P, Rodier A et al (1999) A variant form of the nuclear triiodothyronine receptor c-ErbAalpha1 plays a direct role in regulation of mitochondrial RNA synthesis. Mol Cell Biol 19(12):7913-7924
    • (1999) Mol Cell Biol , vol.19 , Issue.12 , pp. 7913-7924
    • Casas, F.1    Rochard, P.2    Rodier, A.3
  • 163
    • 0037334906 scopus 로고    scopus 로고
    • Endocrine regulation of mitochondrial activity: Involvement of truncated RXRalpha and c-Erb Aalpha1 proteins
    • Casas F, Daury L, Grandemange S et al (2003) Endocrine regulation of mitochondrial activity: Involvement of truncated RXRalpha and c-Erb Aalpha1 proteins. Faseb J 17(3):426-436
    • (2003) Faseb J , vol.17 , Issue.3 , pp. 426-436
    • Casas, F.1    Daury, L.2    Grandemange, S.3
  • 164
    • 45349107433 scopus 로고    scopus 로고
    • L'activité mitochondriale est un régulateur majeur de la différenciation des myoblastes et de l'expression des isoformes de myosine
    • Seyer P, Grandemange S, Pessemesse L et al (2006) L'activité mitochondriale est un régulateur majeur de la différenciation des myoblastes et de l'expression des isoformes de myosine. Prod Anim 19:279-286
    • (2006) Prod Anim , vol.19 , pp. 279-286
    • Seyer, P.1    Grandemange, S.2    Pessemesse, L.3
  • 165
    • 49249107662 scopus 로고    scopus 로고
    • Overexpression of the T3 mitochondrial receptor in mice induces changes in metabolic and contractile features of muscle fibers
    • Casas F, Pessemesse L, Grandemange S et al (2008) Overexpression of the T3 mitochondrial receptor in mice induces changes in metabolic and contractile features of muscle fibers. PLoS One 3:e2501
    • (2008) PLoS One , vol.3
    • Casas, F.1    Pessemesse, L.2    Grandemange, S.3
  • 166
    • 0028227185 scopus 로고
    • The retinoic acid and retinoid X receptors are differentially expressed during myoblast differentiation
    • Downes M, Mynett-Johnson L, Muscat GE (1994) The retinoic acid and retinoid X receptors are differentially expressed during myoblast differentiation. Endocrinology 134(6): 2658-2661
    • (1994) Endocrinology , vol.134 , Issue.6 , pp. 2658-2661
    • Downes, M.1    Mynett-Johnson, L.2    Muscat, G.E.3
  • 167
    • 33745185772 scopus 로고    scopus 로고
    • Avian MyoD and c-Jun coordinately induce transcriptional activity of the 3,5,3'-Triiodothyronine nuclear receptor c-ErbAalpha1 in proliferating myoblasts
    • Busson M, Daury L, Seyer P et al (2006) Avian MyoD and c-Jun coordinately induce transcriptional activity of the 3,5,3'-Triiodothyronine nuclear receptor c-ErbAalpha1 in proliferating myoblasts. Endocrinology 147(7):3408-3418
    • (2006) Endocrinology , vol.147 , Issue.7 , pp. 3408-3418
    • Busson, M.1    Daury, L.2    Seyer, P.3
  • 169
    • 0035900344 scopus 로고    scopus 로고
    • The triiodothyronine nuclear receptor c-ErbAalpha1 inhibits avian MyoD transcriptional activity in myoblasts
    • Daury L, Busson M, Casas F, Cassar-Malek I, Wrutniak-Cabello C, Cabello G (2001) The triiodothyronine nuclear receptor c-ErbAalpha1 inhibits avian MyoD transcriptional activity in myoblasts. FEBS Lett 508(2):236-240
    • (2001) FEBS Lett , vol.508 , Issue.2 , pp. 236-240
    • Daury, L.1    Busson, M.2    Casas, F.3    Cassar-Malek, I.4    Wrutniak-Cabello, C.5    Cabello, G.6
  • 170
    • 33645396466 scopus 로고    scopus 로고
    • Characterization of a novel thyroid hormone receptor alpha variant involved in the regulation of myoblast differentiation
    • Casas F, BussonM, Grandemange S et al (2006) Characterization of a novel thyroid hormone receptor alpha variant involved in the regulation of myoblast differentiation. Mol Endocrinol 20(4):749-763
    • (2006) Mol Endocrinol , vol.20 , Issue.4 , pp. 749-763
    • Casas, F.1    Busson, M.2    Grandemange, S.3
  • 171
    • 0029655486 scopus 로고    scopus 로고
    • A shift in the ligand responsiveness of thyroid hormone receptor alpha induced by heterodimerization with retinoid X receptor alpha
    • Claret FX, Antakly T, Karin M, Saatcioglu F (1996) A shift in the ligand responsiveness of thyroid hormone receptor alpha induced by heterodimerization with retinoid X receptor alpha. Mol Cell Biol 16(1):219-227
    • (1996) Mol Cell Biol , vol.16 , Issue.1 , pp. 219-227
    • Claret, F.X.1    Antakly, T.2    Karin, M.3    Saatcioglu, F.4
  • 172
    • 0032080350 scopus 로고    scopus 로고
    • Involvement of thyroid hormone and its alpha receptor in avian neurulation
    • Flamant F, Samarut J (1998) Involvement of thyroid hormone and its alpha receptor in avian neurulation. Dev Biol 197(1):1-11
    • (1998) Dev Biol , vol.197 , Issue.1 , pp. 1-11
    • Flamant, F.1    Samarut, J.2
  • 173
    • 0026606084 scopus 로고
    • Fos and Jun repress transcriptional activation by myogenin and MyoD: The amino terminus of Jun can mediate repression
    • Li L, Chambard JC, Karin M, Olson EN (1992) Fos and Jun repress transcriptional activation by myogenin and MyoD: The amino terminus of Jun can mediate repression. Genes Dev 6(4):676-689
    • (1992) Genes Dev , vol.6 , Issue.4 , pp. 676-689
    • Li, L.1    Chambard, J.C.2    Karin, M.3    Olson, E.N.4
  • 174
    • 0025756795 scopus 로고
    • A chromosome 12 coding region is juxtaposed to the MYC protooncogene locus in a t(812)(q24q22) translocation in a case of B-cell chronic lymphocytic leukemia
    • Rimokh R, Rouault JP, Wahbi K et al (1991) A chromosome 12 coding region is juxtaposed to the MYC protooncogene locus in a t(812)(q24q22) translocation in a case of B-cell chronic lymphocytic leukemia. Genes Chromosomes Cancer 3(1):24-36
    • (1991) Genes Chromosomes Cancer , vol.3 , Issue.1 , pp. 24-36
    • Rimokh, R.1    Rouault, J.P.2    Wahbi, K.3
  • 175
    • 0035947157 scopus 로고    scopus 로고
    • In search of a function for the TIS21/PC3/BTG1/TOB family
    • Matsuda S, Rouault J, Magaud J, Berthet C (2001) In search of a function for the TIS21/PC3/BTG1/TOB family. FEBS Lett 497(2-3):67-72
    • (2001) FEBS Lett , vol.497 , Issue.2-3 , pp. 67-72
    • Matsuda, S.1    Rouault, J.2    Magaud, J.3    Berthet, C.4
  • 176
    • 0026514995 scopus 로고
    • BTG1, a member of a new family of antiproliferative genes
    • Rouault JP, Rimokh R, Tessa C et al (1992) BTG1, a member of a new family of antiproliferative genes. Embo J 11(4):1663-1670
    • (1992) Embo J , vol.11 , Issue.4 , pp. 1663-1670
    • Rouault, J.P.1    Rimokh, R.2    Tessa, C.3
  • 177
    • 0029118588 scopus 로고
    • A novel heart derived inhibitor of vascular cell proliferation. Purification and biological activity
    • Westernacher D, Schaper W (1995) A novel heart derived inhibitor of vascular cell proliferation. Purification and biological activity. J Mol Cell Cardiol 27(8):1535-1543
    • (1995) J Mol Cell Cardiol , vol.27 , Issue.8 , pp. 1535-1543
    • Westernacher, D.1    Schaper, W.2
  • 178
    • 0035837244 scopus 로고    scopus 로고
    • Identification of functional domains involved in BTG1 cell localization
    • Rodier A, Rochard P, Berthet C et al (2001) Identification of functional domains involved in BTG1 cell localization. Oncogene 20(21):2691-2703
    • (2001) Oncogene , vol.20 , Issue.21 , pp. 2691-2703
    • Rodier, A.1    Rochard, P.2    Berthet, C.3
  • 179
    • 20144382385 scopus 로고    scopus 로고
    • Stimulation of mitochondrial activity by p43 overexpression induces human dermal fibroblast transformation
    • Grandemange S, Seyer P, Carazo A et al (2005) Stimulation of mitochondrial activity by p43 overexpression induces human dermal fibroblast transformation. Cancer Res 65(10): 4282-4291
    • (2005) Cancer Res , vol.65 , Issue.10 , pp. 4282-4291
    • Grandemange, S.1    Seyer, P.2    Carazo, A.3
  • 180
    • 0033838874 scopus 로고    scopus 로고
    • A calcineurin-NFATc3-dependent pathway regulates skeletal muscle differentiation and slow myosin heavy-chain expression
    • Delling U, Tureckova J, Lim HW, De Windt LJ, Rotwein P, Molkentin JD (2000) A calcineurin-NFATc3-dependent pathway regulates skeletal muscle differentiation and slow myosin heavy-chain expression. Mol Cell Biol 20(17):6600-6611
    • (2000) Mol Cell Biol , vol.20 , Issue.17 , pp. 6600-6611
    • Delling, U.1    Tureckova, J.2    Lim, H.W.3    De Windt, L.J.4    Rotwein, P.5    Molkentin, J.D.6
  • 181
    • 0034193421 scopus 로고    scopus 로고
    • Calcineurin activity is required for the initiation of skeletal muscle differentiation
    • Friday BB, Horsley V, Pavlath GK (2000) Calcineurin activity is required for the initiation of skeletal muscle differentiation. J Cell Biol 149(3):657-666
    • (2000) J Cell Biol , vol.149 , Issue.3 , pp. 657-666
    • Friday, B.B.1    Horsley, V.2    Pavlath, G.K.3
  • 182
    • 0035985178 scopus 로고    scopus 로고
    • P38 Mitogen-Activated protein kinase-, calcium-calmodulindependent protein kinase-, and calcineurin-mediated signaling pathways transcriptionally regulate myogenin expression
    • Xu Q, Yu L, Liu L et al (2002) p38 Mitogen-Activated protein kinase-, calcium-calmodulindependent protein kinase-, and calcineurin-mediated signaling pathways transcriptionally regulate myogenin expression. Mol Biol Cell 13(6):1940-1952
    • (2002) Mol Biol Cell , vol.13 , Issue.6 , pp. 1940-1952
    • Xu, Q.1    Yu, L.2    Liu, L.3
  • 183
    • 0032529188 scopus 로고    scopus 로고
    • A calcineurin-dependent transcriptional pathway controls skeletal muscle fiber type
    • Chin ER, Olson EN, Richardson JA et al (1998) A calcineurin-dependent transcriptional pathway controls skeletal muscle fiber type. Genes Dev 12(16):2499-2509
    • (1998) Genes Dev , vol.12 , Issue.16 , pp. 2499-2509
    • Chin, E.R.1    Olson, E.N.2    Richardson, J.A.3
  • 184
    • 33847616140 scopus 로고    scopus 로고
    • Activation of the beta myosin heavy chain promoter by MEF-2D, MyoD, p300, and the calcineurin/NFATc1 pathway
    • Meissner JD, Umeda PK, Chang KC, Gros G, Scheibe RJ (2007) Activation of the beta myosin heavy chain promoter by MEF-2D, MyoD, p300, and the calcineurin/NFATc1 pathway. J Cell Physiol 211(1):138-148
    • (2007) J Cell Physiol , vol.211 , Issue.1 , pp. 138-148
    • Meissner, J.D.1    Umeda, P.K.2    Chang, K.C.3    Gros, G.4    Scheibe, R.J.5
  • 185
    • 34047092316 scopus 로고    scopus 로고
    • Uncoupling proteins 2 and 3 are fundamental for mitochondrial Ca2+ uniport
    • Trenker M, Malli R, Fertschai I, Levak-Frank S, Graier WF (2007) Uncoupling proteins 2 and 3 are fundamental for mitochondrial Ca2+ uniport. Nat Cell Biol 9(4):445-452
    • (2007) Nat Cell Biol , vol.9 , Issue.4 , pp. 445-452
    • Trenker, M.1    Malli, R.2    Fertschai, I.3    Levak-Frank, S.4    Graier, W.F.5
  • 187
    • 0032511112 scopus 로고    scopus 로고
    • Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses
    • Rizzuto R, Pinton P, Carrington W et al (1998) Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses. Science 280(5370): 1763-1766
    • (1998) Science , vol.280 , Issue.5370 , pp. 1763-1766
    • Rizzuto, R.1    Pinton, P.2    Carrington, W.3
  • 188
    • 0021832143 scopus 로고
    • Regulation of c-myc mRNA levels in normal human lymphocytes by modulators of cell proliferation
    • Reed JC, Nowell PC, Hoover RG (1985) Regulation of c-myc mRNA levels in normal human lymphocytes by modulators of cell proliferation. Proc Natl Acad Sci U S A 82(12): 4221-4224
    • (1985) Proc Natl Acad Sci U S A , vol.82 , Issue.12 , pp. 4221-4224
    • Reed, J.C.1    Nowell, P.C.2    Hoover, R.G.3
  • 189
    • 0022271491 scopus 로고
    • Involvement of Ca2+ in platelet-derived growth factor-induced expression of c-myc oncogene in Swiss 3T3 fibroblasts
    • Tsuda T, Kaibuchi K, West B, Takai Y (1985) Involvement of Ca2+ in platelet-derived growth factor-induced expression of c-myc oncogene in Swiss 3T3 fibroblasts. FEBS Lett 187(1):43-46
    • (1985) FEBS Lett , vol.187 , Issue.1 , pp. 43-46
    • Tsuda, T.1    Kaibuchi, K.2    West, B.3    Takai, Y.4
  • 190
    • 33750471197 scopus 로고    scopus 로고
    • Mutual cross-Talk between reactive oxygen species and nuclear factor-kappa B: Molecular basis and biological significance
    • Bubici C, Papa S, Dean K, Franzoso G (2006) Mutual cross-Talk between reactive oxygen species and nuclear factor-kappa B: Molecular basis and biological significance. Oncogene 25(51):6731-6748
    • (2006) Oncogene , vol.25 , Issue.51 , pp. 6731-6748
    • Bubici, C.1    Papa, S.2    Dean, K.3    Franzoso, G.4
  • 191
    • 0036260697 scopus 로고    scopus 로고
    • Cellular response to oxidative stress: Signaling for suicide and survival
    • Martindale JL, Holbrook NJ (2002) Cellular response to oxidative stress: Signaling for suicide and survival. J Cell Physiol 192(1):1-15
    • (2002) J Cell Physiol , vol.192 , Issue.1 , pp. 1-15
    • Martindale, J.L.1    Holbrook, N.J.2
  • 193
    • 10344266986 scopus 로고    scopus 로고
    • Nontranscriptional modulation of intracellular Ca2+ signaling by ligand stimulated thyroid hormone receptor
    • Saelim N, John LM, Wu J et al (2004) Nontranscriptional modulation of intracellular Ca2+ signaling by ligand stimulated thyroid hormone receptor. J Cell Biol 167(5):915-924
    • (2004) J Cell Biol , vol.167 , Issue.5 , pp. 915-924
    • Saelim, N.1    John, L.M.2    Wu, J.3
  • 194
    • 0033081478 scopus 로고    scopus 로고
    • Retrograde Ca2+ signaling in C2C12 skeletal myocytes in response to mitochondrial genetic and metabolic stress: A novel mode of inter-organelle crosstalk
    • Biswas G, Adebanjo OA, Freedman BD et al (1999) Retrograde Ca2+ signaling in C2C12 skeletal myocytes in response to mitochondrial genetic and metabolic stress: A novel mode of inter-organelle crosstalk. Embo J 18(3):522-533
    • (1999) Embo J , vol.18 , Issue.3 , pp. 522-533
    • Biswas, G.1    Adebanjo, O.A.2    Freedman, B.D.3
  • 195
    • 0030886976 scopus 로고    scopus 로고
    • Compromised mitochondrial function leads to increased cytosolic calcium and to activation of MAP kinases
    • Luo Y, Bond JD, Ingram VM (1997) Compromised mitochondrial function leads to increased cytosolic calcium and to activation of MAP kinases. Proc Natl Acad Sci U S A 94(18):9705-9710
    • (1997) Proc Natl Acad Sci U S A , vol.94 , Issue.18 , pp. 9705-9710
    • Luo, Y.1    Bond, J.D.2    Ingram, V.M.3


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