메뉴 건너뛰기




Volumn 22, Issue 3, 2008, Pages 511-520

Re-expression of DNA methylation-silenced CD44 gene in a resistant NB4 cell line: Rescue of CD44-dependent cell death by cAMP

Author keywords

[No Author keywords available]

Indexed keywords

5 AZA 2' DEOXYCYTIDINE; CYCLIC AMP; HERMES ANTIGEN; HISTONE H3; PROTEIN C JUN; RNA POLYMERASE II;

EID: 40749125706     PISSN: 08876924     EISSN: 14765551     Source Type: Journal    
DOI: 10.1038/sj.leu.2405071     Document Type: Article
Times cited : (15)

References (52)
  • 1
    • 0027065573 scopus 로고
    • Genomic structure of DNA encoding the lymphocyte homing receptor CD44 reveals at least 12 alternatively spliced exons
    • Screaton GR, Bell MV, Jackson DG, Cornelis FB, Gerth U, Bell JI. Genomic structure of DNA encoding the lymphocyte homing receptor CD44 reveals at least 12 alternatively spliced exons. Proc Natl Acad Sci USA 1992; 89: 12160-12164.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 12160-12164
    • Screaton, G.R.1    Bell, M.V.2    Jackson, D.G.3    Cornelis, F.B.4    Gerth, U.5    Bell, J.I.6
  • 3
    • 0027491845 scopus 로고
    • CD44 and its interaction with extracellular matrix
    • Lesley J, Hyman R, Kincade PW. CD44 and its interaction with extracellular matrix. Adv Immunol 1993; 54: 271-335.
    • (1993) Adv Immunol , vol.54 , pp. 271-335
    • Lesley, J.1    Hyman, R.2    Kincade, P.W.3
  • 4
    • 0033941950 scopus 로고    scopus 로고
    • CD44 acts both as a growth- and invasiveness-promoting molecule and as a tumor-suppressing cofactor
    • discussion 118-120
    • Herrlich P, Morrison H, Sleeman J, Orian-Rousseau V, Konig H, Weg-Remers S et al. CD44 acts both as a growth- and invasiveness-promoting molecule and as a tumor-suppressing cofactor. Ann NY Acad Sci 2000; 910: 106-118; discussion 118-120.
    • (2000) Ann NY Acad Sci , vol.910 , pp. 106-118
    • Herrlich, P.1    Morrison, H.2    Sleeman, J.3    Orian-Rousseau, V.4    Konig, H.5    Weg-Remers, S.6
  • 6
    • 0037227965 scopus 로고    scopus 로고
    • Ponta H, Sherman L. Herrlich PA. CD44: From adhesion molecules to signalling regulators. Nat Rev Mol Cell Biol 2003; 4: 33-45.
    • Ponta H, Sherman L. Herrlich PA. CD44: From adhesion molecules to signalling regulators. Nat Rev Mol Cell Biol 2003; 4: 33-45.
  • 7
    • 0033067551 scopus 로고    scopus 로고
    • Ligation of the CD44 adhesion molecule reverses blockage of differentiation in human acute myeloid leukemia
    • Charrad RS, Li Y, Delpech B, Balitrand N, Clay D, Jasmin C et al. Ligation of the CD44 adhesion molecule reverses blockage of differentiation in human acute myeloid leukemia. Nat Med 1999; 5: 669-676.
    • (1999) Nat Med , vol.5 , pp. 669-676
    • Charrad, R.S.1    Li, Y.2    Delpech, B.3    Balitrand, N.4    Clay, D.5    Jasmin, C.6
  • 8
    • 0036095957 scopus 로고    scopus 로고
    • Effects of anti-CD44 monoclonal antibodies on differentiation and apoptosis of human myeloid leukemia cell lines
    • Charrad RS, Gadhoum Z, Qi J, Glachant A, Allouche M, Jasmin C et al Effects of anti-CD44 monoclonal antibodies on differentiation and apoptosis of human myeloid leukemia cell lines. Blood 2002; 99 290-299.
    • (2002) Blood , vol.99 , pp. 290-299
    • Charrad, R.S.1    Gadhoum, Z.2    Qi, J.3    Glachant, A.4    Allouche, M.5    Jasmin, C.6
  • 9
    • 0026013478 scopus 로고
    • NB4, a maturation inducible cell line with t(15;17) marker isolated from a human acute promyelocytic leukemia (M3)
    • Lanotte M, Martin-Thouvenin V, Najman S, Balerini P, Valensi F, Berger R. NB4, a maturation inducible cell line with t(15;17) marker isolated from a human acute promyelocytic leukemia (M3). Blood 1991; 77 1080-1086.
    • (1991) Blood , vol.77 , pp. 1080-1086
    • Lanotte, M.1    Martin-Thouvenin, V.2    Najman, S.3    Balerini, P.4    Valensi, F.5    Berger, R.6
  • 10
    • 0034254777 scopus 로고    scopus 로고
    • Ligation of the CD44 adhesion molecule inhibits drug-induced apoptosis in human myeloid leukemia cells
    • Allouche M, Charrad RS, Bettaieb A, Greenland C, Grignon C, Smadja-Joffe F. Ligation of the CD44 adhesion molecule inhibits drug-induced apoptosis in human myeloid leukemia cells. Blood 2000; 96: 1187-1190.
    • (2000) Blood , vol.96 , pp. 1187-1190
    • Allouche, M.1    Charrad, R.S.2    Bettaieb, A.3    Greenland, C.4    Grignon, C.5    Smadja-Joffe, F.6
  • 11
    • 1642541151 scopus 로고    scopus 로고
    • CD44: A new means to inhibit acute myeloid leukemia cell proliferation via p27Kipl
    • Gadhoum Z, Leibovitch MP, Qi J, Dumenil D, Durand L, Leibovitch S et al. CD44: A new means to inhibit acute myeloid leukemia cell proliferation via p27Kipl. Blood 2004; 103: 1059-1068.
    • (2004) Blood , vol.103 , pp. 1059-1068
    • Gadhoum, Z.1    Leibovitch, M.P.2    Qi, J.3    Dumenil, D.4    Durand, L.5    Leibovitch, S.6
  • 12
    • 0036796742 scopus 로고    scopus 로고
    • Retinoic acid resistance in acute promyelocytic leukemia
    • Gallagher RE. Retinoic acid resistance in acute promyelocytic leukemia. Leukemia 2002; 16: 1940-1958.
    • (2002) Leukemia , vol.16 , pp. 1940-1958
    • Gallagher, R.E.1
  • 13
    • 0033561797 scopus 로고    scopus 로고
    • Deconstructing a disease: RARalpha, its fusion partners, and their roles in the parnogenesis of acute promyelocytic leukemia
    • Melnick A, Licht JD. Deconstructing a disease: RARalpha, its fusion partners, and their roles in the parnogenesis of acute promyelocytic leukemia. Blood 1999; 93: 3167-3215.
    • (1999) Blood , vol.93 , pp. 3167-3215
    • Melnick, A.1    Licht, J.D.2
  • 14
    • 0035969099 scopus 로고    scopus 로고
    • Orchestration of multiple arrays of signal cross-talk and combinatorial interactions for maturation and cell death: Another vision of t(15;17) preleukemic blast and APL-cell maturation
    • Benoit G, Roussel M, Pendino F, Segal-Bendirdjian E, Lanotte M. Orchestration of multiple arrays of signal cross-talk and combinatorial interactions for maturation and cell death: Another vision of t(15;17) preleukemic blast and APL-cell maturation. Oncogene 2001; 20 7161-7177.
    • (2001) Oncogene , vol.20 , pp. 7161-7177
    • Benoit, G.1    Roussel, M.2    Pendino, F.3    Segal-Bendirdjian, E.4    Lanotte, M.5
  • 15
    • 0028023155 scopus 로고
    • Two distinctly regulated events, priming and triggering, during retinoid-induced maturation and resistance of NB4 promyelocytic leukemia cell line
    • Ruchaud S, Duprez E, Gendron MC, Houge G, Genieser HG, Jastorff B et al. Two distinctly regulated events, priming and triggering, during retinoid-induced maturation and resistance of NB4 promyelocytic leukemia cell line. Proc Natl Acad Sci USA 1994; 91: 8428-8432.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8428-8432
    • Ruchaud, S.1    Duprez, E.2    Gendron, M.C.3    Houge, G.4    Genieser, H.G.5    Jastorff, B.6
  • 16
    • 0035969116 scopus 로고    scopus 로고
    • Maturation sensitive and resistant t(15; 17) NB4 cell lines as tools for APL physiopathology: Nomenclature of cells and repertory of their known genetic alterations and phenotypes
    • Roussel MJ, Lanotte M. Maturation sensitive and resistant t(15; 17) NB4 cell lines as tools for APL physiopathology: Nomenclature of cells and repertory of their known genetic alterations and phenotypes. Oncogene 2001; 20: 7287-7291.
    • (2001) Oncogene , vol.20 , pp. 7287-7291
    • Roussel, M.J.1    Lanotte, M.2
  • 17
    • 0029955187 scopus 로고    scopus 로고
    • cAMP signalling is decisive for recovery of nuclear bodies (PODs) during maturation of RA-resistant t(15;17) promyelocytic leukemia NB4 cells expressing PML-RAR alpha
    • Duprez E, Lillehaug JR, Naoe T, Lanotte M. cAMP signalling is decisive for recovery of nuclear bodies (PODs) during maturation of RA-resistant t(15;17) promyelocytic leukemia NB4 cells expressing PML-RAR alpha. Oncogene 1996; 12: 2451-2459.
    • (1996) Oncogene , vol.12 , pp. 2451-2459
    • Duprez, E.1    Lillehaug, J.R.2    Naoe, T.3    Lanotte, M.4
  • 18
    • 0036464602 scopus 로고    scopus 로고
    • Synergic effects of arsenic trioxide and cAMP during acute promyelocytic leukemia cell maturation subtends a novel signaling cross-talk
    • Zhu Q, Zhang JW, Zhu HQ, Shen YL, Flexor M. Jia PM et al. Synergic effects of arsenic trioxide and cAMP during acute promyelocytic leukemia cell maturation subtends a novel signaling cross-talk. Blood 2002; 99: 1014-1022.
    • (2002) Blood , vol.99 , pp. 1014-1022
    • Zhu, Q.1    Zhang, J.W.2    Zhu, H.Q.3    Shen, Y.L.4    Flexor, M.5    Jia, P.M.6
  • 19
    • 0035809924 scopus 로고    scopus 로고
    • The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear, body
    • Boisvert FM, Kruhlak MJ, Box AK, Hendzel MJ, Bazett-Jones DP. The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear, body. J Cell Biol 2001; 152: 1099-1106.
    • (2001) J Cell Biol , vol.152 , pp. 1099-1106
    • Boisvert, F.M.1    Kruhlak, M.J.2    Box, A.K.3    Hendzel, M.J.4    Bazett-Jones, D.P.5
  • 20
    • 4744351446 scopus 로고    scopus 로고
    • Phosphodiesterase IV inhibition by piclamilast potentiates the cytodifferentiating action of retinoids in myeloid leukemia cells. Cross-talk between the cAMP and the retinoic acid signaling pathways. i
    • Parrella E, Gianni M, Cecconi V. Nigro E, Barzago MM, Rambaldi A et al. Phosphodiesterase IV inhibition by piclamilast potentiates the cytodifferentiating action of retinoids in myeloid leukemia cells. Cross-talk between the cAMP and the retinoic acid signaling pathways. i J Biol Chem 2004; 279: 42026-42040.
    • (2004) J Biol Chem , vol.279 , pp. 42026-42040
    • Parrella, E.1    Gianni, M.2    Cecconi, V.3    Nigro, E.4    Barzago, M.M.5    Rambaldi, A.6
  • 21
    • 2442478144 scopus 로고    scopus 로고
    • PML-RARA-RXR oligomers mediate retinoid and rexinoid/cAMP cross-talk in acute promyelocytic leukemia cell differentiation
    • Kamashev D, Vitoux D, De The H. PML-RARA-RXR oligomers mediate retinoid and rexinoid/cAMP cross-talk in acute promyelocytic leukemia cell differentiation. J Exp Med 2004; 199: 1163-1174.
    • (2004) J Exp Med , vol.199 , pp. 1163-1174
    • Kamashev, D.1    Vitoux, D.2    De The, H.3
  • 22
    • 0032168678 scopus 로고    scopus 로고
    • CpG methylation, chromatin structure and gene silencing-a three-way connection
    • Razin A. CpG methylation, chromatin structure and gene silencing-a three-way connection. EMBO J 1998; 17: 4905-4908.
    • (1998) EMBO J , vol.17 , pp. 4905-4908
    • Razin, A.1
  • 23
    • 0142089873 scopus 로고    scopus 로고
    • The rise of DNA methylation and the importance of chromatin on multidrug resistance in cancer
    • Baker EK, El-Osta A. The rise of DNA methylation and the importance of chromatin on multidrug resistance in cancer. Exp Cell Res 2003; 290: 177-194.
    • (2003) Exp Cell Res , vol.290 , pp. 177-194
    • Baker, E.K.1    El-Osta, A.2
  • 24
    • 1242296842 scopus 로고    scopus 로고
    • A comprehensive analysis of allelic methylation status of CpG islands on human chromosome 21q
    • Yamada Y, Watanabe H, Miura F, Soejima H, Uchiyama M, Iwasaka T et al A comprehensive analysis of allelic methylation status of CpG islands on human chromosome 21q. Genome Res 2004; 14: 247-266.
    • (2004) Genome Res , vol.14 , pp. 247-266
    • Yamada, Y.1    Watanabe, H.2    Miura, F.3    Soejima, H.4    Uchiyama, M.5    Iwasaka, T.6
  • 25
    • 28544441040 scopus 로고    scopus 로고
    • CD44 ligation induces apoptosis via caspase-and serine protease-dependent pathways in acute promyelocytic leukemia cells
    • Maquarre E, Artus C, Gadhoum Z, Jasmin C, Smadja-Joffe F, Robert-Lezenes J. CD44 ligation induces apoptosis via caspase-and serine protease-dependent pathways in acute promyelocytic leukemia cells. Leukemia 2005; 19: 2296-2303.
    • (2005) Leukemia , vol.19 , pp. 2296-2303
    • Maquarre, E.1    Artus, C.2    Gadhoum, Z.3    Jasmin, C.4    Smadja-Joffe, F.5    Robert-Lezenes, J.6
  • 26
    • 0026005834 scopus 로고
    • Expression of CD44 is repressed in neuroblastoma cells
    • Shtivelman E, Bishop. JM. Expression of CD44 is repressed in neuroblastoma cells. Mol Cell Biol 1991; 11: 5446-5453.
    • (1991) Mol Cell Biol , vol.11 , pp. 5446-5453
    • Shtivelman, E.1    Bishop, J.M.2
  • 27
    • 0023216891 scopus 로고
    • CpG islands in vertebrate genomes
    • Gardiner-Garden M, Frommer M. CpG islands in vertebrate genomes. J Mol Biol 1987; 196: 261-282.
    • (1987) J Mol Biol , vol.196 , pp. 261-282
    • Gardiner-Garden, M.1    Frommer, M.2
  • 28
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • Berger SL. Histone modifications in transcriptional regulation. Curr Opin Genet Dev 2002; 12: 142-148.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 142-148
    • Berger, S.L.1
  • 29
    • 0036211013 scopus 로고    scopus 로고
    • Histone acetylation: A switch between repressive and permissive chromatin. Second in review series on chromatin dynamics
    • Eberharter A, Becker PB. Histone acetylation: A switch between repressive and permissive chromatin. Second in review series on chromatin dynamics. EMBO Rep 2002; 3: 224-229.
    • (2002) EMBO Rep , vol.3 , pp. 224-229
    • Eberharter, A.1    Becker, P.B.2
  • 30
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein M. Histone acetylation in chromatin structure and transcription. Nature 1997; 389: 349-352.
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 33
    • 6044256118 scopus 로고    scopus 로고
    • Histones and histone modifications
    • Peterson CL, Laniel MA. Histones and histone modifications. Curr Biol 2004; 14: R546-R551.
    • (2004) Curr Biol , vol.14
    • Peterson, C.L.1    Laniel, M.A.2
  • 34
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. The language of covalent histone modifications. Nature 2000; 403: 41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 35
    • 0033636595 scopus 로고    scopus 로고
    • Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation
    • Cheung P, Tanner KG, Cheung WL, Sassone-Corsi P, Denu JM, Allis CD. Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol Cell 2000; 5: 905-915.
    • (2000) Mol Cell , vol.5 , pp. 905-915
    • Cheung, P.1    Tanner, K.G.2    Cheung, W.L.3    Sassone-Corsi, P.4    Denu, J.M.5    Allis, C.D.6
  • 36
    • 0033638105 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14
    • Lo WS, Trievel RC, Rojas JR, Duggan L, Hsu JY, Allis CD et al. Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. Mol Cell 2000; 5: 917-926.
    • (2000) Mol Cell , vol.5 , pp. 917-926
    • Lo, W.S.1    Trievel, R.C.2    Rojas, J.R.3    Duggan, L.4    Hsu, J.Y.5    Allis, C.D.6
  • 37
    • 0033639243 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 correlates with transcriptionally active loci
    • Nowak SJ, Corces VG. Phosphorylation of histone H3 correlates with transcriptionally active loci. Genes Dev 2000; 14: 3003-3013.
    • (2000) Genes Dev , vol.14 , pp. 3003-3013
    • Nowak, S.J.1    Corces, V.G.2
  • 38
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 2001; 410: 116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 39
    • 0035815360 scopus 로고    scopus 로고
    • Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly
    • Nakayama J, Rice JC, Strahl BD, Allis CD, Grewal SI. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 2001; 292: 110-113.
    • (2001) Science , vol.292 , pp. 110-113
    • Nakayama, J.1    Rice, J.C.2    Strahl, B.D.3    Allis, C.D.4    Grewal, S.I.5
  • 40
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails
    • Zhang Y, Reinberg D. Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev 2001; 15: 2343-2360.
    • (2001) Genes Dev , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2
  • 41
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • Kouzarides T. Histone methylation in transcriptional control. Curr Opin Genet Dev 2002; 12: 198-209.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 42
    • 20844453092 scopus 로고    scopus 로고
    • Gene expression patterns define key transcriptional events in cell-cycle regulatioh by cAMP and protein kinase A
    • Zambon AC, Zhang L, Minovitsky S, Kanter JR, Prabhakar S, Salomonis N et al. Gene expression patterns define key transcriptional events in cell-cycle regulatioh by cAMP and protein kinase A. Proc Natl Acad Sci USA 2005; 102: 8561-8566.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8561-8566
    • Zambon, A.C.1    Zhang, L.2    Minovitsky, S.3    Kanter, J.R.4    Prabhakar, S.5    Salomonis, N.6
  • 43
    • 4444382918 scopus 로고    scopus 로고
    • Dopamine D2-like antagonists induce chromatin remodeling in striatal neurons through cyclic AMP-protein kinase A and NMDA receptor signaling
    • Li J, Guo Y, Schroeder FA, Youngs RM, Schmidt TW, Ferris C et al. Dopamine D2-like antagonists induce chromatin remodeling in striatal neurons through cyclic AMP-protein kinase A and NMDA receptor signaling. J Neurochem 2004; 90: 1117-1131.
    • (2004) J Neurochem , vol.90 , pp. 1117-1131
    • Li, J.1    Guo, Y.2    Schroeder, F.A.3    Youngs, R.M.4    Schmidt, T.W.5    Ferris, C.6
  • 44
    • 0035955717 scopus 로고    scopus 로고
    • Follicle-stimulating hormone stimulates protein kinase A-mediated histone H3 phosphorylation and acetylation leading to select gene activation in ovarian granulosa cells
    • Salvador LM, Park Y, Cottom J, Maizels ET, Jones JC, Schillace RV et al. Follicle-stimulating hormone stimulates protein kinase A-mediated histone H3 phosphorylation and acetylation leading to select gene activation in ovarian granulosa cells. J Biol Chem 2001; 276 40146-40155.
    • (2001) J Biol Chem , vol.276 , pp. 40146-40155
    • Salvador, L.M.1    Park, Y.2    Cottom, J.3    Maizels, E.T.4    Jones, J.C.5    Schillace, R.V.6
  • 45
    • 0036200058 scopus 로고    scopus 로고
    • Lack of a consistent relationship between demethylation of the CD44 promoter and CD44 expression
    • Hyman R. Lack of a consistent relationship between demethylation of the CD44 promoter and CD44 expression. Immunogenetics 2002; 53: 914-924.
    • (2002) Immunogenetics , vol.53 , pp. 914-924
    • Hyman, R.1
  • 46
    • 18144362099 scopus 로고    scopus 로고
    • SWI/SNF chromatin-remodelling factors induce changes in DNA methylation to promote transcriptional activation
    • Banine F, Bartlett C, Gunawardena R, Muchardt C, Yaniv M, Knudsen ES et al. SWI/SNF chromatin-remodelling factors induce changes in DNA methylation to promote transcriptional activation. Cancer Res 2005; 65: 3542-3547.
    • (2005) Cancer Res , vol.65 , pp. 3542-3547
    • Banine, F.1    Bartlett, C.2    Gunawardena, R.3    Muchardt, C.4    Yaniv, M.5    Knudsen, E.S.6
  • 47
    • 30044441988 scopus 로고    scopus 로고
    • The human SWI/SNF subunit Brm is a regulator of alternative splicing
    • Batsché E, Yaniv M, Muchardt C. The human SWI/SNF subunit Brm is a regulator of alternative splicing. Nat Struct Mol Biol 2006; 13 22-29.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 22-29
    • Batsché, E.1    Yaniv, M.2    Muchardt, C.3
  • 48
    • 0030796519 scopus 로고    scopus 로고
    • CD44 regulates hematopoietic progenitor distribution, granuloma formation, and tumorigenicity
    • Schmits R, Filmus J, Gerwin N, Senaldi G, Kiefer F, Kundig T et al CD44 regulates hematopoietic progenitor distribution, granuloma formation, and tumorigenicity. Blood 1997; 90: 2217-2233.
    • (1997) Blood , vol.90 , pp. 2217-2233
    • Schmits, R.1    Filmus, J.2    Gerwin, N.3    Senaldi, G.4    Kiefer, F.5    Kundig, T.6
  • 49
    • 25444455856 scopus 로고    scopus 로고
    • Dynamic combinatorial networks in nuclear receptor-mediated transcription
    • Rochette-Egly C. Dynamic combinatorial networks in nuclear receptor-mediated transcription. J Biol Chem 2005; 280: 32565-32568.
    • (2005) J Biol Chem , vol.280 , pp. 32565-32568
    • Rochette-Egly, C.1
  • 50
    • 0029055605 scopus 로고
    • All-trans retinoic acid and cyclic adenosine monophosphate cooperate in the expression of leukocyte alkaline phosphatase in acute promyelocytic leukemia cells
    • Gianni M, Terao M, Norio P, Barbui T, Rambaldi A, Garattini E. All-trans retinoic acid and cyclic adenosine monophosphate cooperate in the expression of leukocyte alkaline phosphatase in acute promyelocytic leukemia cells. Blood 1995; 85: 3619-3635.
    • (1995) Blood , vol.85 , pp. 3619-3635
    • Gianni, M.1    Terao, M.2    Norio, P.3    Barbui, T.4    Rambaldi, A.5    Garattini, E.6
  • 51
    • 14544300650 scopus 로고    scopus 로고
    • The role of protein kinase A pathway and cAMP responsive element-binding protein in androgen receptor-mediated transcription at the prostate-specific antigen locus
    • Kim J, Jia L, Stallcup MR, Coetzee GA. The role of protein kinase A pathway and cAMP responsive element-binding protein in androgen receptor-mediated transcription at the prostate-specific antigen locus. J Mol Endocrinol 2005; 34: 107-118.
    • (2005) J Mol Endocrinol , vol.34 , pp. 107-118
    • Kim, J.1    Jia, L.2    Stallcup, M.R.3    Coetzee, G.A.4
  • 52
    • 0033053037 scopus 로고    scopus 로고
    • Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling
    • Doucas V, Tini M, Egan DA, Evans RM. Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling. Proc Natl Acad Sci USA 1999; 96: 2627-2632.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2627-2632
    • Doucas, V.1    Tini, M.2    Egan, D.A.3    Evans, R.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.