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Volumn 1839, Issue 7, 2014, Pages 579-591

The transcriptional repression activity of STAF65γ is facilitated by promoter tethering and nuclear import of class IIa histone deacetylases

Author keywords

Histone deacetylases; Lung adenocarcinoma; STAF65 ; Transcriptional regulation; YY1

Indexed keywords

COREPRESSOR PROTEIN; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 2A; STAF 65 GAMMA PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR YY1; UNCLASSIFIED DRUG;

EID: 84901595749     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2014.05.007     Document Type: Article
Times cited : (5)

References (58)
  • 2
    • 84876884110 scopus 로고    scopus 로고
    • Dysregulation of the basal RNA polymerase transcription apparatus in cancer
    • Bywater M.J., Pearson R.B., McArthur G.A., Hannan R.D. Dysregulation of the basal RNA polymerase transcription apparatus in cancer. Nat. Rev. Cancer 2013, 13:299-314.
    • (2013) Nat. Rev. Cancer , vol.13 , pp. 299-314
    • Bywater, M.J.1    Pearson, R.B.2    McArthur, G.A.3    Hannan, R.D.4
  • 3
    • 0034283011 scopus 로고    scopus 로고
    • A new tumor-rejection antigen recognized by cytotoxic T lymphocytes infiltrating into a lung adenocarcinoma
    • Nishizaka S., Gomi S., Harada K., Oizumi K., Itoh K., Shichijo S. A new tumor-rejection antigen recognized by cytotoxic T lymphocytes infiltrating into a lung adenocarcinoma. Cancer Res. 2000, 60:4830-4837.
    • (2000) Cancer Res. , vol.60 , pp. 4830-4837
    • Nishizaka, S.1    Gomi, S.2    Harada, K.3    Oizumi, K.4    Itoh, K.5    Shichijo, S.6
  • 4
    • 0034812915 scopus 로고    scopus 로고
    • Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo
    • Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M., Kundu T.K., Chait B.T., Roeder R.G. Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo. Mol. Cell. Biol. 2001, 21:6782-6795.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6782-6795
    • Martinez, E.1    Palhan, V.B.2    Tjernberg, A.3    Lymar, E.S.4    Gamper, A.M.5    Kundu, T.K.6    Chait, B.T.7    Roeder, R.G.8
  • 5
    • 84858329099 scopus 로고    scopus 로고
    • ATAC-king the complexity of SAGA during evolution
    • Spedale G., Timmers H.T., Pijnappel W.W. ATAC-king the complexity of SAGA during evolution. Genes Dev. 2012, 26:527-541.
    • (2012) Genes Dev. , vol.26 , pp. 527-541
    • Spedale, G.1    Timmers, H.T.2    Pijnappel, W.W.3
  • 6
    • 0036311179 scopus 로고    scopus 로고
    • Analysis of Spt7 function in the Saccharomyces cerevisiae SAGA coactivator complex
    • Wu P.Y., Winston F. Analysis of Spt7 function in the Saccharomyces cerevisiae SAGA coactivator complex. Mol. Cell. Biol. 2002, 22:5367-5379.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5367-5379
    • Wu, P.Y.1    Winston, F.2
  • 7
    • 37549044715 scopus 로고    scopus 로고
    • STAGA recruits mediator to the MYC oncoprotein to stimulate transcription and cell proliferation
    • Liu X., Vorontchikhina M., Wang Y.L., Faiola F., Martinez E. STAGA recruits mediator to the MYC oncoprotein to stimulate transcription and cell proliferation. Mol. Cell. Biol. 2008, 28:108-121.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 108-121
    • Liu, X.1    Vorontchikhina, M.2    Wang, Y.L.3    Faiola, F.4    Martinez, E.5
  • 8
    • 42149161137 scopus 로고    scopus 로고
    • Multivalent binding of p53 to the STAGA complex mediates coactivator recruitment after UV damage
    • Gamper A.M., Roeder R.G. Multivalent binding of p53 to the STAGA complex mediates coactivator recruitment after UV damage. Mol. Cell. Biol. 2008, 28:2517-2527.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 2517-2527
    • Gamper, A.M.1    Roeder, R.G.2
  • 9
    • 33845766238 scopus 로고    scopus 로고
    • Transcriptional and subcellular regulation of the TRIP-Br family
    • Lai I.L., Wang S.Y., Yao Y.L., Yang W.M. Transcriptional and subcellular regulation of the TRIP-Br family. Gene 2007, 388:102-109.
    • (2007) Gene , vol.388 , pp. 102-109
    • Lai, I.L.1    Wang, S.Y.2    Yao, Y.L.3    Yang, W.M.4
  • 10
    • 18144399308 scopus 로고    scopus 로고
    • The nuclear import of TAF10 is regulated by one of its three histone fold domain-containing interaction partners
    • Soutoglou E., Demeny M.A., Scheer E., Fienga G., Sassone-Corsi P., Tora L. The nuclear import of TAF10 is regulated by one of its three histone fold domain-containing interaction partners. Mol. Cell. Biol. 2005, 25:4092-4104.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4092-4104
    • Soutoglou, E.1    Demeny, M.A.2    Scheer, E.3    Fienga, G.4    Sassone-Corsi, P.5    Tora, L.6
  • 12
    • 0142211208 scopus 로고    scopus 로고
    • The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity
    • Yao Y.L., Yang W.M. The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity. J. Biol. Chem. 2003, 278:42560-42568.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42560-42568
    • Yao, Y.L.1    Yang, W.M.2
  • 13
    • 0035976904 scopus 로고    scopus 로고
    • Tetracycline-regulated gene expression mediated by a novel chimeric repressor that recruits histone deacetylases in mammalian cells
    • Jiang W., Zhou L., Breyer B., Feng T., Cheng H., Haydon R., Ishikawa A., He T.C. Tetracycline-regulated gene expression mediated by a novel chimeric repressor that recruits histone deacetylases in mammalian cells. J. Biol. Chem. 2001, 276:45168-45174.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45168-45174
    • Jiang, W.1    Zhou, L.2    Breyer, B.3    Feng, T.4    Cheng, H.5    Haydon, R.6    Ishikawa, A.7    He, T.C.8
  • 14
    • 0033964223 scopus 로고    scopus 로고
    • Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression
    • Kao H.Y., Downes M., Ordentlich P., Evans R.M. Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. Genes Dev. 2000, 14:55-66.
    • (2000) Genes Dev. , vol.14 , pp. 55-66
    • Kao, H.Y.1    Downes, M.2    Ordentlich, P.3    Evans, R.M.4
  • 16
    • 1342306395 scopus 로고    scopus 로고
    • Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription
    • Ling Y., Sankpal U.T., Robertson A.K., McNally J.G., Karpova T., Robertson K.D. Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription. Nucleic Acids Res. 2004, 32:598-610.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 598-610
    • Ling, Y.1    Sankpal, U.T.2    Robertson, A.K.3    McNally, J.G.4    Karpova, T.5    Robertson, K.D.6
  • 17
    • 0029850458 scopus 로고    scopus 로고
    • Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3
    • Yang W.M., Inouye C., Zeng Y., Bearss D., Seto E. Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:12845-12850.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 12845-12850
    • Yang, W.M.1    Inouye, C.2    Zeng, Y.3    Bearss, D.4    Seto, E.5
  • 19
    • 77951249270 scopus 로고    scopus 로고
    • Histone deacetylase 10 relieves repression on the melanogenic program by maintaining the deacetylation status of repressors
    • Lai I.L., Lin T.P., Yao Y.L., Lin C.Y., Hsieh M.J., Yang W.M. Histone deacetylase 10 relieves repression on the melanogenic program by maintaining the deacetylation status of repressors. J. Biol. Chem. 2010, 285:7187-7196.
    • (2010) J. Biol. Chem. , vol.285 , pp. 7187-7196
    • Lai, I.L.1    Lin, T.P.2    Yao, Y.L.3    Lin, C.Y.4    Hsieh, M.J.5    Yang, W.M.6
  • 20
    • 0034905085 scopus 로고    scopus 로고
    • Regulation of transcription factor YY1 by acetylation and deacetylation
    • Yao Y.L., Yang W.M., Seto E. Regulation of transcription factor YY1 by acetylation and deacetylation. Mol. Cell. Biol. 2001, 21:5979-5991.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5979-5991
    • Yao, Y.L.1    Yang, W.M.2    Seto, E.3
  • 21
    • 0032529295 scopus 로고    scopus 로고
    • Cloning, chromosomal localization and promoter analysis of the human transcription factor YY1
    • Yao Y.L., Dupont B.R., Ghosh S., Fang Y., Leach R.J., Seto E. Cloning, chromosomal localization and promoter analysis of the human transcription factor YY1. Nucleic Acids Res. 1998, 26:3776-3783.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3776-3783
    • Yao, Y.L.1    Dupont, B.R.2    Ghosh, S.3    Fang, Y.4    Leach, R.J.5    Seto, E.6
  • 23
    • 0030474869 scopus 로고    scopus 로고
    • Cloning, characterization, and expression of the transforming growth factor-beta type I receptor promoter in fetal rat bone cells
    • Ji C., Casinghino S., McCarthy T.L., Centrella M. Cloning, characterization, and expression of the transforming growth factor-beta type I receptor promoter in fetal rat bone cells. J. Cell. Biochem. 1996, 63:478-490.
    • (1996) J. Cell. Biochem. , vol.63 , pp. 478-490
    • Ji, C.1    Casinghino, S.2    McCarthy, T.L.3    Centrella, M.4
  • 24
    • 84873097376 scopus 로고    scopus 로고
    • PARP-2 regulates cell cycle-related genes through histone deacetylation and methylation independently of poly(ADP-ribosyl)ation
    • Liang Y.C., Hsu C.Y., Yao Y.L., Yang W.M. PARP-2 regulates cell cycle-related genes through histone deacetylation and methylation independently of poly(ADP-ribosyl)ation. Biochem. Biophys. Res. Commun. 2013, 431:58-64.
    • (2013) Biochem. Biophys. Res. Commun. , vol.431 , pp. 58-64
    • Liang, Y.C.1    Hsu, C.Y.2    Yao, Y.L.3    Yang, W.M.4
  • 25
    • 33748413896 scopus 로고    scopus 로고
    • Transcriptional repression activity of PAX3 is modulated by competition between corepressor KAP1 and heterochromatin protein 1
    • Hsieh M.J., Yao Y.L., Lai I.L., Yang W.M. Transcriptional repression activity of PAX3 is modulated by competition between corepressor KAP1 and heterochromatin protein 1. Biochem. Biophys. Res. Commun. 2006, 349:573-581.
    • (2006) Biochem. Biophys. Res. Commun. , vol.349 , pp. 573-581
    • Hsieh, M.J.1    Yao, Y.L.2    Lai, I.L.3    Yang, W.M.4
  • 26
    • 0035801704 scopus 로고    scopus 로고
    • The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1
    • Yang W.M., Yao Y.L., Seto E. The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1. EMBO J. 2001, 20:4814-4825.
    • (2001) EMBO J. , vol.20 , pp. 4814-4825
    • Yang, W.M.1    Yao, Y.L.2    Seto, E.3
  • 28
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative C(T) method
    • Schmittgen T.D., Livak K.J. Analyzing real-time PCR data by the comparative C(T) method. Nat. Protoc. 2008, 3:1101-1108.
    • (2008) Nat. Protoc. , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2
  • 29
    • 77954818058 scopus 로고    scopus 로고
    • The American Joint Committee on Cancer: the 7th edition of the AJCC cancer staging manual and the future of TNM
    • Edge S.B., Compton C.C. The American Joint Committee on Cancer: the 7th edition of the AJCC cancer staging manual and the future of TNM. Ann. Surg. Oncol. 2010, 17:1471-1474.
    • (2010) Ann. Surg. Oncol. , vol.17 , pp. 1471-1474
    • Edge, S.B.1    Compton, C.C.2
  • 31
    • 0032568323 scopus 로고    scopus 로고
    • Regulation of the cdk inhibitor p21 gene during cell cycle progression is under the control of the transcription factor E2F
    • Hiyama H., Iavarone A., Reeves S.A. Regulation of the cdk inhibitor p21 gene during cell cycle progression is under the control of the transcription factor E2F. Oncogene 1998, 16:1513-1523.
    • (1998) Oncogene , vol.16 , pp. 1513-1523
    • Hiyama, H.1    Iavarone, A.2    Reeves, S.A.3
  • 32
    • 0023705623 scopus 로고
    • Regulation of CAD gene expression in mouse fibroblasts during the transition from the resting to the growing state
    • Rao G.N., Church R.L. Regulation of CAD gene expression in mouse fibroblasts during the transition from the resting to the growing state. Exp. Cell Res. 1988, 178:449-456.
    • (1988) Exp. Cell Res. , vol.178 , pp. 449-456
    • Rao, G.N.1    Church, R.L.2
  • 33
    • 0033786378 scopus 로고    scopus 로고
    • Rb function in cell-cycle regulation and apoptosis
    • Harbour J.W., Dean D.C. Rb function in cell-cycle regulation and apoptosis. Nat. Cell Biol. 2000, 2:E65-E67.
    • (2000) Nat. Cell Biol. , vol.2
    • Harbour, J.W.1    Dean, D.C.2
  • 34
    • 79952831840 scopus 로고    scopus 로고
    • Myc: the beauty and the beast
    • Wasylishen A.R., Penn L.Z. Myc: the beauty and the beast. Genes Cancer 2010, 1:532-541.
    • (2010) Genes Cancer , vol.1 , pp. 532-541
    • Wasylishen, A.R.1    Penn, L.Z.2
  • 35
    • 84900373378 scopus 로고    scopus 로고
    • The expression of c-myc, bcl-2 and p53 proteins in adenocarcinomas of lung
    • Yoo J., Jung J.H., Choi H.J., Kang S.J., Kang C.S. The expression of c-myc, bcl-2 and p53 proteins in adenocarcinomas of lung. Cancer Res. Treat. 2004, 36:146-150.
    • (2004) Cancer Res. Treat. , vol.36 , pp. 146-150
    • Yoo, J.1    Jung, J.H.2    Choi, H.J.3    Kang, S.J.4    Kang, C.S.5
  • 36
    • 77955686258 scopus 로고    scopus 로고
    • Regulatory signal transduction pathways for class IIa histone deacetylases
    • Parra M., Verdin E. Regulatory signal transduction pathways for class IIa histone deacetylases. Curr. Opin. Pharmacol. 2010, 10:454-460.
    • (2010) Curr. Opin. Pharmacol. , vol.10 , pp. 454-460
    • Parra, M.1    Verdin, E.2
  • 37
    • 0033568028 scopus 로고    scopus 로고
    • HDAC4 deacetylase associates with and represses the MEF2 transcription factor
    • Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J., Kouzarides T. HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EMBO J. 1999, 18:5099-5107.
    • (1999) EMBO J. , vol.18 , pp. 5099-5107
    • Miska, E.A.1    Karlsson, C.2    Langley, E.3    Nielsen, S.J.4    Pines, J.5    Kouzarides, T.6
  • 42
    • 14244249406 scopus 로고    scopus 로고
    • Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates
    • Gocke C.B., Yu H., Kang J. Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates. J. Biol. Chem. 2005, 280:5004-5012.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5004-5012
    • Gocke, C.B.1    Yu, H.2    Kang, J.3
  • 43
    • 67650720512 scopus 로고    scopus 로고
    • Systematic study of protein sumoylation: development of a site-specific predictor of SUMOsp 2.0
    • Ren J., Gao X., Jin C., Zhu M., Wang X., Shaw A., Wen L., Yao X., Xue Y. Systematic study of protein sumoylation: development of a site-specific predictor of SUMOsp 2.0. Proteomics 2009, 9:3409-3412.
    • (2009) Proteomics , vol.9 , pp. 3409-3412
    • Ren, J.1    Gao, X.2    Jin, C.3    Zhu, M.4    Wang, X.5    Shaw, A.6    Wen, L.7    Yao, X.8    Xue, Y.9
  • 44
    • 0033967220 scopus 로고    scopus 로고
    • The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells
    • Giorgino F., de Robertis O., Laviola L., Montrone C., Perrini S., McCowen K.C., Smith R.J. The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:1125-1130.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1125-1130
    • Giorgino, F.1    de Robertis, O.2    Laviola, L.3    Montrone, C.4    Perrini, S.5    McCowen, K.C.6    Smith, R.J.7
  • 45
    • 75649135910 scopus 로고    scopus 로고
    • Deconstructing repression: evolving models of co-repressor action
    • Perissi V., Jepsen K., Glass C.K., Rosenfeld M.G. Deconstructing repression: evolving models of co-repressor action. Nat. Rev. Genet. 2010, 11:109-123.
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 109-123
    • Perissi, V.1    Jepsen, K.2    Glass, C.K.3    Rosenfeld, M.G.4
  • 46
    • 32244435093 scopus 로고    scopus 로고
    • Reconstitution of chromatin transcription with purified components reveals a chromatin-specific repressive activity of p300
    • Santoso B., Kadonaga J.T. Reconstitution of chromatin transcription with purified components reveals a chromatin-specific repressive activity of p300. Nat. Struct. Mol. Biol. 2006, 13:131-139.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 131-139
    • Santoso, B.1    Kadonaga, J.T.2
  • 47
    • 0032189630 scopus 로고    scopus 로고
    • Drosophila CBP represses the transcription factor TCF to antagonize Wingless signalling
    • Waltzer L., Bienz M. Drosophila CBP represses the transcription factor TCF to antagonize Wingless signalling. Nature 1998, 395:521-525.
    • (1998) Nature , vol.395 , pp. 521-525
    • Waltzer, L.1    Bienz, M.2
  • 48
    • 0034916613 scopus 로고    scopus 로고
    • P300/CBP proteins: HAT for transcriptional bridges and scaffolds
    • Chen H.M., La Thangue N.B. p300/CBP proteins: HAT for transcriptional bridges and scaffolds. J. Cell Sci. 2001, 114:2363-2373.
    • (2001) J. Cell Sci. , vol.114 , pp. 2363-2373
    • Chen, H.M.1    La Thangue, N.B.2
  • 49
  • 51
    • 0036554867 scopus 로고    scopus 로고
    • Differential gene expression in human lung adenocarcinomas and squamous cell carcinomas
    • McDoniels-Silvers A.L., Nimri C.F., Stoner G.D., Lubet R.A., You M. Differential gene expression in human lung adenocarcinomas and squamous cell carcinomas. Clin. Cancer Res. 2002, 8:1127-1138.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 1127-1138
    • McDoniels-Silvers, A.L.1    Nimri, C.F.2    Stoner, G.D.3    Lubet, R.A.4    You, M.5
  • 52
    • 64749093273 scopus 로고    scopus 로고
    • Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex
    • Ouyang J., Shi Y., Valin A., Xuan Y., Gill G. Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex. Mol. Cell 2009, 34:145-154.
    • (2009) Mol. Cell , vol.34 , pp. 145-154
    • Ouyang, J.1    Shi, Y.2    Valin, A.3    Xuan, Y.4    Gill, G.5
  • 53
    • 0037593411 scopus 로고    scopus 로고
    • Functional characterization of an amino-terminal region of HDAC4 that possesses MEF2 binding and transcriptional repressive activity
    • Chan J.K., Sun L., Yang X.J., Zhu G., Wu Z. Functional characterization of an amino-terminal region of HDAC4 that possesses MEF2 binding and transcriptional repressive activity. J. Biol. Chem. 2003, 278:23515-23521.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23515-23521
    • Chan, J.K.1    Sun, L.2    Yang, X.J.3    Zhu, G.4    Wu, Z.5
  • 54
    • 80052180405 scopus 로고    scopus 로고
    • Class IIa HDACs: from important roles in differentiation to possible implications in tumourigenesis
    • Clocchiatti A., Florean C., Brancolini C. Class IIa HDACs: from important roles in differentiation to possible implications in tumourigenesis. J. Cell. Mol. Med. 2011, 15:1833-1846.
    • (2011) J. Cell. Mol. Med. , vol.15 , pp. 1833-1846
    • Clocchiatti, A.1    Florean, C.2    Brancolini, C.3
  • 57
    • 34347402459 scopus 로고    scopus 로고
    • Deficiency in glutamine but not glucose induces MYC-dependent apoptosis in human cells
    • Yuneva M., Zamboni N., Oefner P., Sachidanandam R., Lazebnik Y. Deficiency in glutamine but not glucose induces MYC-dependent apoptosis in human cells. J. Cell Biol. 2007, 178:93-105.
    • (2007) J. Cell Biol. , vol.178 , pp. 93-105
    • Yuneva, M.1    Zamboni, N.2    Oefner, P.3    Sachidanandam, R.4    Lazebnik, Y.5
  • 58
    • 0033958518 scopus 로고    scopus 로고
    • C-Myc suppresses the tumorigenicity of lung cancer cells and down-regulates vascular endothelial growth factor expression
    • Barr L.F., Campbell S.E., Diette G.B., Gabrielson E.W., Kim S., Shim H., Dang C.V. c-Myc suppresses the tumorigenicity of lung cancer cells and down-regulates vascular endothelial growth factor expression. Cancer Res. 2000, 60:143-149.
    • (2000) Cancer Res. , vol.60 , pp. 143-149
    • Barr, L.F.1    Campbell, S.E.2    Diette, G.B.3    Gabrielson, E.W.4    Kim, S.5    Shim, H.6    Dang, C.V.7


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