메뉴 건너뛰기




Volumn 442, Issue 1-2, 2009, Pages 55-62

Activation of the brain-specific neurogranin gene in murine T-cell lymphomas by proviral insertional mutagenesis

Author keywords

Brain; Insertional mutagenesis; Murine leukemia virus; Neurogranin; T cell lymphoma

Indexed keywords

CALMODULIN; DNA; NEUROGRANIN; RNA;

EID: 67349214630     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2009.04.003     Document Type: Article
Times cited : (14)

References (54)
  • 2
    • 0025961398 scopus 로고
    • Purification and characterization of a brain-specific protein kinase C substrate, neurogranin (p17). Identification of a consensus amino acid sequence between neurogranin and neuromodulin (GAP43) that corresponds to the protein kinase C phosphorylation site and the calmodulin-binding domain
    • Baudier J., Deloulme J.C., Van Dorsselaer A., Black D., and Matthes H.W. Purification and characterization of a brain-specific protein kinase C substrate, neurogranin (p17). Identification of a consensus amino acid sequence between neurogranin and neuromodulin (GAP43) that corresponds to the protein kinase C phosphorylation site and the calmodulin-binding domain. J. Biol. Chem. 266 (1991) 229-237
    • (1991) J. Biol. Chem. , vol.266 , pp. 229-237
    • Baudier, J.1    Deloulme, J.C.2    Van Dorsselaer, A.3    Black, D.4    Matthes, H.W.5
  • 3
    • 0032588515 scopus 로고    scopus 로고
    • Ca2+-calmodulin and protein kinase Cs: a hypothetical synthesis of their conflicting convergences on shared substrate domains
    • Chakravarthy B., Morley P., and Whitfield J. Ca2+-calmodulin and protein kinase Cs: a hypothetical synthesis of their conflicting convergences on shared substrate domains. Trends Neurosci. 22 (1999) 12-16
    • (1999) Trends Neurosci. , vol.22 , pp. 12-16
    • Chakravarthy, B.1    Morley, P.2    Whitfield, J.3
  • 4
    • 0036570131 scopus 로고    scopus 로고
    • Tumor vaccine for ovarian carcinoma targeting sperm protein 17
    • Chiriva-Internati M., Wang Z., Salati E., Timmins P., and Lim S.H. Tumor vaccine for ovarian carcinoma targeting sperm protein 17. Cancer 94 (2002) 2447-2453
    • (2002) Cancer , vol.94 , pp. 2447-2453
    • Chiriva-Internati, M.1    Wang, Z.2    Salati, E.3    Timmins, P.4    Lim, S.H.5
  • 5
    • 0031796798 scopus 로고    scopus 로고
    • CTX, a Xenopus thymocyte receptor, defines a molecular family conserved throughout vertebrates
    • Chretien I., et al. CTX, a Xenopus thymocyte receptor, defines a molecular family conserved throughout vertebrates. Eur. J. Immunol. 28 (1998) 4094-4104
    • (1998) Eur. J. Immunol. , vol.28 , pp. 4094-4104
    • Chretien, I.1
  • 6
    • 0033604582 scopus 로고    scopus 로고
    • Function of the c-Myc oncogenic transcription factor
    • Dang C.V., et al. Function of the c-Myc oncogenic transcription factor. Exp. Cell Res. 253 (1999) 63-77
    • (1999) Exp. Cell Res. , vol.253 , pp. 63-77
    • Dang, C.V.1
  • 7
    • 0036587571 scopus 로고    scopus 로고
    • Transforming growth factor beta signal transduction
    • Dennler S., Goumans M.J., and Ten Dijke P. Transforming growth factor beta signal transduction. J. Leukoc. Biol. 71 (2002) 731-740
    • (2002) J. Leukoc. Biol. , vol.71 , pp. 731-740
    • Dennler, S.1    Goumans, M.J.2    Ten Dijke, P.3
  • 8
    • 0038383027 scopus 로고    scopus 로고
    • Transcriptional program of apoptosis induction following interleukin 2 deprivation: identification of RC3, a calcium/calmodulin binding protein, as a novel proapoptotic factor
    • Devireddy L.R., and Green M.R. Transcriptional program of apoptosis induction following interleukin 2 deprivation: identification of RC3, a calcium/calmodulin binding protein, as a novel proapoptotic factor. Mol. Cell. Biol. 23 (2003) 4532-4541
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4532-4541
    • Devireddy, L.R.1    Green, M.R.2
  • 10
    • 58149396888 scopus 로고    scopus 로고
    • Control of pathogenicity and disease specificity of a T-lymphomagenic gammaretrovirus by E-box motifs but not by an overlapping glucocorticoid response element
    • Ejegod D., Sorensen K.D., Mossbrugger I., Quintanilla-Martinez L., Schmidt J., and Pedersen F.S. Control of pathogenicity and disease specificity of a T-lymphomagenic gammaretrovirus by E-box motifs but not by an overlapping glucocorticoid response element. J. Virol. 83 (2009) 336-346
    • (2009) J. Virol. , vol.83 , pp. 336-346
    • Ejegod, D.1    Sorensen, K.D.2    Mossbrugger, I.3    Quintanilla-Martinez, L.4    Schmidt, J.5    Pedersen, F.S.6
  • 11
    • 0031026432 scopus 로고    scopus 로고
    • Second-site proviral enhancer alterations in lymphomas induced by enhancer mutants of SL3-3 murine leukemia virus: negative effect of nuclear factor 1 binding site
    • Ethelberg S., et al. Second-site proviral enhancer alterations in lymphomas induced by enhancer mutants of SL3-3 murine leukemia virus: negative effect of nuclear factor 1 binding site. J. Virol. 71 (1997) 1196-1206
    • (1997) J. Virol. , vol.71 , pp. 1196-1206
    • Ethelberg, S.1
  • 12
    • 0030780591 scopus 로고    scopus 로고
    • An SL3-3 murine leukemia virus enhancer variant more pathogenic than the wild type obtained by assisted molecular evolution in vivo
    • Ethelberg S., Sørensen A.B., Schmidt J., Luz A., and Pedersen F.S. An SL3-3 murine leukemia virus enhancer variant more pathogenic than the wild type obtained by assisted molecular evolution in vivo. J. Virol. 71 (1997) 9796-9799
    • (1997) J. Virol. , vol.71 , pp. 9796-9799
    • Ethelberg, S.1    Sørensen, A.B.2    Schmidt, J.3    Luz, A.4    Pedersen, F.S.5
  • 13
    • 0036948557 scopus 로고    scopus 로고
    • A re-evaluation of sperm protein 17 (Sp17) indicates a regulatory role in an A-kinase anchoring protein complex, rather than a unique role in sperm-zona pellucida binding
    • Frayne J., and Hall L. A re-evaluation of sperm protein 17 (Sp17) indicates a regulatory role in an A-kinase anchoring protein complex, rather than a unique role in sperm-zona pellucida binding. Reproduction 124 (2002) 767-774
    • (2002) Reproduction , vol.124 , pp. 767-774
    • Frayne, J.1    Hall, L.2
  • 14
    • 0033201453 scopus 로고    scopus 로고
    • Homeostatic tuning of Ca2+ signal transduction by members of the calpacitin protein family
    • Gerendasy D. Homeostatic tuning of Ca2+ signal transduction by members of the calpacitin protein family. J. Neurosci. Res. 58 (1999) 107-119
    • (1999) J. Neurosci. Res. , vol.58 , pp. 107-119
    • Gerendasy, D.1
  • 15
    • 27744591989 scopus 로고    scopus 로고
    • A tumor-suppressor function for NFATc3 in T-cell lymphomagenesis by murine leukemia virus
    • Glud S.Z., et al. A tumor-suppressor function for NFATc3 in T-cell lymphomagenesis by murine leukemia virus. Blood 106 (2005) 3546-3552
    • (2005) Blood , vol.106 , pp. 3546-3552
    • Glud, S.Z.1
  • 16
    • 33644582580 scopus 로고    scopus 로고
    • Sperm protein 17 is expressed in human nervous system tumours
    • Grizzi F., et al. Sperm protein 17 is expressed in human nervous system tumours. BMC Cancer 6 (2006) 23
    • (2006) BMC Cancer , vol.6 , pp. 23
    • Grizzi, F.1
  • 17
    • 33847339300 scopus 로고    scopus 로고
    • Characterization of transcriptional regulation of neurogranin by nitric oxide and the role of neurogranin in SNP-induced cell death: implication of neurogranin in an increased neuronal susceptibility to oxidative stress
    • Gui J., Song Y., Han N.L., and Sheu F.S. Characterization of transcriptional regulation of neurogranin by nitric oxide and the role of neurogranin in SNP-induced cell death: implication of neurogranin in an increased neuronal susceptibility to oxidative stress. Int. J. Biol. Sci. 3 (2007) 212-224
    • (2007) Int. J. Biol. Sci. , vol.3 , pp. 212-224
    • Gui, J.1    Song, Y.2    Han, N.L.3    Sheu, F.S.4
  • 18
    • 0035844164 scopus 로고    scopus 로고
    • Cloning of an immunoglobulin family adhesion molecule selectively expressed by endothelial cells
    • Hirata K., et al. Cloning of an immunoglobulin family adhesion molecule selectively expressed by endothelial cells. J. Biol. Chem. 276 (2001) 16223-16231
    • (2001) J. Biol. Chem. , vol.276 , pp. 16223-16231
    • Hirata, K.1
  • 19
    • 33745635089 scopus 로고    scopus 로고
    • Environmental enrichment enhances neurogranin expression and hippocampal learning and memory but fails to rescue the impairments of neurogranin null mutant mice
    • Huang F.L., Huang K.P., Wu J., and Boucheron C. Environmental enrichment enhances neurogranin expression and hippocampal learning and memory but fails to rescue the impairments of neurogranin null mutant mice. J. Neurosci. 26 (2006) 6230-6237
    • (2006) J. Neurosci. , vol.26 , pp. 6230-6237
    • Huang, F.L.1    Huang, K.P.2    Wu, J.3    Boucheron, C.4
  • 20
    • 9344271526 scopus 로고    scopus 로고
    • Neurogranin/RC3 enhances long-term potentiation and learning by promoting calcium-mediated signaling
    • Huang K.P., Huang F.L., Jager T., Li J., Reymann K.G., and Balschun D. Neurogranin/RC3 enhances long-term potentiation and learning by promoting calcium-mediated signaling. J. Neurosci. 24 (2004) 10660-10669
    • (2004) J. Neurosci. , vol.24 , pp. 10660-10669
    • Huang, K.P.1    Huang, F.L.2    Jager, T.3    Li, J.4    Reymann, K.G.5    Balschun, D.6
  • 21
    • 0141594945 scopus 로고    scopus 로고
    • Targeted disruption of endothelial cell-selective adhesion molecule inhibits angiogenic processes in vitro and in vivo
    • Ishida T., Kundu R.K., Yang E., Hirata K., Ho Y.D., and Quertermous T. Targeted disruption of endothelial cell-selective adhesion molecule inhibits angiogenic processes in vitro and in vivo. J. Biol. Chem. 278 (2003) 34598-34604
    • (2003) J. Biol. Chem. , vol.278 , pp. 34598-34604
    • Ishida, T.1    Kundu, R.K.2    Yang, E.3    Hirata, K.4    Ho, Y.D.5    Quertermous, T.6
  • 22
    • 0029097352 scopus 로고
    • Sequence and localization of the mouse sperm autoantigenic protein, Sp17
    • Kong M., Richardson R.T., Widgren E.E., and O'Rand M.G. Sequence and localization of the mouse sperm autoantigenic protein, Sp17. Biol. Reprod. 53 (1995) 579-590
    • (1995) Biol. Reprod. , vol.53 , pp. 579-590
    • Kong, M.1    Richardson, R.T.2    Widgren, E.E.3    O'Rand, M.G.4
  • 23
    • 0026659651 scopus 로고
    • Silencing the type II sodium channel gene: a model for neural-specific gene regulation
    • Kraner S.D., Chong J.A., Tsay H.J., and Mandel G. Silencing the type II sodium channel gene: a model for neural-specific gene regulation. Neuron 9 (1992) 37-44
    • (1992) Neuron , vol.9 , pp. 37-44
    • Kraner, S.D.1    Chong, J.A.2    Tsay, H.J.3    Mandel, G.4
  • 24
    • 0025021488 scopus 로고
    • Long-distance activation of the Myc protooncogene by provirus insertion in Mlvi-1 or Mlvi-4 in rat T-cell lymphomas
    • Lazo P., Lee J., and Tsichlis P. Long-distance activation of the Myc protooncogene by provirus insertion in Mlvi-1 or Mlvi-4 in rat T-cell lymphomas. PNAS 87 (1990) 170-173
    • (1990) PNAS , vol.87 , pp. 170-173
    • Lazo, P.1    Lee, J.2    Tsichlis, P.3
  • 25
    • 0041031707 scopus 로고    scopus 로고
    • N-methyl-D-aspartate induces neurogranin/RC3 oxidation in rat brain slices
    • Li J., Pak J.H., Huang F.L., and Huang K.P. N-methyl-D-aspartate induces neurogranin/RC3 oxidation in rat brain slices. J. Biol. Chem. 274 (1999) 1294-1300
    • (1999) J. Biol. Chem. , vol.274 , pp. 1294-1300
    • Li, J.1    Pak, J.H.2    Huang, F.L.3    Huang, K.P.4
  • 26
    • 0027405703 scopus 로고
    • Identification of a functional silencer element involved in neuron-specific expression of the synapsin I gene
    • Li L., Suzuki T., Mori N., and Greengard P. Identification of a functional silencer element involved in neuron-specific expression of the synapsin I gene. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 1460-1464
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 1460-1464
    • Li, L.1    Suzuki, T.2    Mori, N.3    Greengard, P.4
  • 27
    • 0035712310 scopus 로고    scopus 로고
    • MAGE-C1 (CT7) gene expression in multiple myeloma: relationship to sperm protein 17
    • Lim S.H., Bumm K., Chiriva-Internati M., Xue Y., and Wang Z. MAGE-C1 (CT7) gene expression in multiple myeloma: relationship to sperm protein 17. Eur. J. Haematol. 67 (2001) 332-334
    • (2001) Eur. J. Haematol. , vol.67 , pp. 332-334
    • Lim, S.H.1    Bumm, K.2    Chiriva-Internati, M.3    Xue, Y.4    Wang, Z.5
  • 28
    • 0035282736 scopus 로고    scopus 로고
    • Sperm protein 17 is a novel cancer-testis antigen in multiple myeloma
    • Lim S.H., Wang Z., Chiriva-Internati M., and Xue Y. Sperm protein 17 is a novel cancer-testis antigen in multiple myeloma. Blood 97 (2001) 1508-1510
    • (2001) Blood , vol.97 , pp. 1508-1510
    • Lim, S.H.1    Wang, Z.2    Chiriva-Internati, M.3    Xue, Y.4
  • 29
    • 10544241196 scopus 로고    scopus 로고
    • Nitric oxide modification of rat brain neurogranin. Identification of the cysteine residues involved in intramolecular disulfide bridge formation using site-directed mutagenesis
    • Mahoney C.W., Pak J.H., and Huang K.P. Nitric oxide modification of rat brain neurogranin. Identification of the cysteine residues involved in intramolecular disulfide bridge formation using site-directed mutagenesis. J. Biol. Chem. 271 (1996) 28798-28804
    • (1996) J. Biol. Chem. , vol.271 , pp. 28798-28804
    • Mahoney, C.W.1    Pak, J.H.2    Huang, K.P.3
  • 30
    • 0031569831 scopus 로고    scopus 로고
    • Structure, organization, and chromosomal mapping of the human neurogranin gene (NRGN)
    • Martinez de Arrieta C., Perez Jurado L., Bernal J., and Coloma A. Structure, organization, and chromosomal mapping of the human neurogranin gene (NRGN). Genomics 41 (1997) 243-249
    • (1997) Genomics , vol.41 , pp. 243-249
    • Martinez de Arrieta, C.1    Perez Jurado, L.2    Bernal, J.3    Coloma, A.4
  • 31
    • 0034118789 scopus 로고    scopus 로고
    • Oxidative modification of neurogranin by nitric oxide: an amperometric study
    • Miao H.H., Ye J.S., Wong S.L., Wang B.X., Li X.Y., and Sheu F.S. Oxidative modification of neurogranin by nitric oxide: an amperometric study. Bioelectrochemistry 51 (2000) 163-173
    • (2000) Bioelectrochemistry , vol.51 , pp. 163-173
    • Miao, H.H.1    Ye, J.S.2    Wong, S.L.3    Wang, B.X.4    Li, X.Y.5    Sheu, F.S.6
  • 32
    • 0037179893 scopus 로고    scopus 로고
    • Proviral activation of the tumor suppressor E2a contributes to T cell lymphomagenesis in EmuMyc transgenic mice
    • Mikkers H., Allen J., and Berns A. Proviral activation of the tumor suppressor E2a contributes to T cell lymphomagenesis in EmuMyc transgenic mice. Oncogene 21 (2002) 6559-6566
    • (2002) Oncogene , vol.21 , pp. 6559-6566
    • Mikkers, H.1    Allen, J.2    Berns, A.3
  • 33
    • 0037235453 scopus 로고    scopus 로고
    • Retroviral insertional mutagenesis: tagging cancer pathways
    • Mikkers H., and Berns A. Retroviral insertional mutagenesis: tagging cancer pathways. Adv. Cancer Res. 88 (2003) 53-99
    • (2003) Adv. Cancer Res. , vol.88 , pp. 53-99
    • Mikkers, H.1    Berns, A.2
  • 35
    • 10644278704 scopus 로고    scopus 로고
    • Analysis of wild-type and mutant SL3-3 murine leukemia virus insertions in the c-myc promoter during lymphomagenesis reveals target site hot spots, virus-dependent patterns, and frequent error-prone gap repair
    • Nielsen A.A., Sørensen A.B., Schmidt J., and Pedersen F.S. Analysis of wild-type and mutant SL3-3 murine leukemia virus insertions in the c-myc promoter during lymphomagenesis reveals target site hot spots, virus-dependent patterns, and frequent error-prone gap repair. J. Virol. 79 (2005) 67-78
    • (2005) J. Virol. , vol.79 , pp. 67-78
    • Nielsen, A.A.1    Sørensen, A.B.2    Schmidt, J.3    Pedersen, F.S.4
  • 36
    • 0034633680 scopus 로고    scopus 로고
    • Involvement of neurogranin in the modulation of calcium/calmodulin-dependent protein kinase II, synaptic plasticity, and spatial learning: a study with knockout mice
    • Pak J.H., et al. Involvement of neurogranin in the modulation of calcium/calmodulin-dependent protein kinase II, synaptic plasticity, and spatial learning: a study with knockout mice. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 11232-11237
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 11232-11237
    • Pak, J.H.1
  • 37
    • 0033583238 scopus 로고    scopus 로고
    • Interactions between neurogranin and calmodulin in vivo
    • Prichard L., Deloulme J.C., and Storm D.R. Interactions between neurogranin and calmodulin in vivo. J. Biol. Chem. 274 (1999) 7689-7694
    • (1999) J. Biol. Chem. , vol.274 , pp. 7689-7694
    • Prichard, L.1    Deloulme, J.C.2    Storm, D.R.3
  • 39
    • 20444410406 scopus 로고    scopus 로고
    • Tumor model-specific proviral insertional mutagenesis of the Fos/Jdp2/Batf locus
    • Rasmussen M.H., et al. Tumor model-specific proviral insertional mutagenesis of the Fos/Jdp2/Batf locus. Virology 337 (2005) 353-364
    • (2005) Virology , vol.337 , pp. 353-364
    • Rasmussen, M.H.1
  • 40
    • 0025624890 scopus 로고
    • Neurogranin: immunocytochemical localization of a brain-specific protein kinase C substrate
    • Represa A., Deloulme J.C., Sensenbrenner M., Ben-Ari Y., and Baudier J. Neurogranin: immunocytochemical localization of a brain-specific protein kinase C substrate. J. Neurosci. 10 (1990) 3782-3792
    • (1990) J. Neurosci. , vol.10 , pp. 3782-3792
    • Represa, A.1    Deloulme, J.C.2    Sensenbrenner, M.3    Ben-Ari, Y.4    Baudier, J.5
  • 41
    • 0042307513 scopus 로고    scopus 로고
    • The two faces of transforming growth factor beta in carcinogenesis
    • Roberts A.B., and Wakefield L.M. The two faces of transforming growth factor beta in carcinogenesis. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 8621-8623
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 8621-8623
    • Roberts, A.B.1    Wakefield, L.M.2
  • 42
    • 0028918947 scopus 로고
    • Structure and regulation of the gene encoding the neuron-specific protein kinase C substrate neurogranin (RC3 protein)
    • Sato T., Xiao D.M., Li H., Huang F.L., and Huang K.P. Structure and regulation of the gene encoding the neuron-specific protein kinase C substrate neurogranin (RC3 protein). J. Biol. Chem. 270 (1995) 10314-10322
    • (1995) J. Biol. Chem. , vol.270 , pp. 10314-10322
    • Sato, T.1    Xiao, D.M.2    Li, H.3    Huang, F.L.4    Huang, K.P.5
  • 43
    • 0028859138 scopus 로고
    • Differential responses of protein kinase C substrates (MARCKS, neuromodulin, and neurogranin) phosphorylation to calmodulin and S100
    • Sheu F.S., Huang F.L., and Huang K.P. Differential responses of protein kinase C substrates (MARCKS, neuromodulin, and neurogranin) phosphorylation to calmodulin and S100. Arch. Biochem. Biophys. 316 (1995) 335-342
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 335-342
    • Sheu, F.S.1    Huang, F.L.2    Huang, K.P.3
  • 44
    • 0029787497 scopus 로고    scopus 로고
    • Nitric oxide modification of rat brain neurogranin affects its phosphorylation by protein kinase C and affinity for calmodulin
    • Sheu F.S., Mahoney C.W., Seki K., and Huang K.P. Nitric oxide modification of rat brain neurogranin affects its phosphorylation by protein kinase C and affinity for calmodulin. J. Biol. Chem. 271 (1996) 22407-22413
    • (1996) J. Biol. Chem. , vol.271 , pp. 22407-22413
    • Sheu, F.S.1    Mahoney, C.W.2    Seki, K.3    Huang, K.P.4
  • 45
    • 0027524491 scopus 로고
    • Amplification and sequence analysis of DNA flanking integrated proviruses by a simple two-step polymerase chain reaction method
    • Sørensen A.B., Duch M., Jørgensen P., and Pedersen F.S. Amplification and sequence analysis of DNA flanking integrated proviruses by a simple two-step polymerase chain reaction method. J. Virol. 67 (1993) 7118-7124
    • (1993) J. Virol. , vol.67 , pp. 7118-7124
    • Sørensen, A.B.1    Duch, M.2    Jørgensen, P.3    Pedersen, F.S.4
  • 46
    • 0033973818 scopus 로고    scopus 로고
    • Sint1, a common integration site in SL3-3-induced T-cell lymphomas, harbors a putative proto-oncogene with homology to the septin gene family [In Process Citation]
    • Sørensen A.B., Lund A.H., Ethelberg S., Copeland N.G., Jenkins N.A., and Pedersen F.S. Sint1, a common integration site in SL3-3-induced T-cell lymphomas, harbors a putative proto-oncogene with homology to the septin gene family [In Process Citation]. J. Virol. 74 (2000) 2161-2168
    • (2000) J. Virol. , vol.74 , pp. 2161-2168
    • Sørensen, A.B.1    Lund, A.H.2    Ethelberg, S.3    Copeland, N.G.4    Jenkins, N.A.5    Pedersen, F.S.6
  • 47
    • 8644268080 scopus 로고    scopus 로고
    • Mutation of all Runx (AML1/core) sites in the enhancer of T-lymphomagenic SL3-3 murine leukemia virus unmasks a significant potential for myeloid leukemia induction and favors enhancer evolution toward induction of other disease patterns
    • Sørensen K.D., Quintanilla-Martinez L., Kunder S., Schmidt J., and Pedersen F.S. Mutation of all Runx (AML1/core) sites in the enhancer of T-lymphomagenic SL3-3 murine leukemia virus unmasks a significant potential for myeloid leukemia induction and favors enhancer evolution toward induction of other disease patterns. J. Virol. 78 (2004) 13216-13231
    • (2004) J. Virol. , vol.78 , pp. 13216-13231
    • Sørensen, K.D.1    Quintanilla-Martinez, L.2    Kunder, S.3    Schmidt, J.4    Pedersen, F.S.5
  • 48
    • 0033520481 scopus 로고    scopus 로고
    • Lysosomal and cytosolic sialic acid 9-O-acetylesterase activities can Be encoded by one gene via differential usage of a signal peptide-encoding exon at the N terminus
    • Takematsu H., Diaz S., Stoddart A., Zhang Y., and Varki A. Lysosomal and cytosolic sialic acid 9-O-acetylesterase activities can Be encoded by one gene via differential usage of a signal peptide-encoding exon at the N terminus. J. Biol. Chem. 274 (1999) 25623-25631
    • (1999) J. Biol. Chem. , vol.274 , pp. 25623-25631
    • Takematsu, H.1    Diaz, S.2    Stoddart, A.3    Zhang, Y.4    Varki, A.5
  • 49
    • 33845989934 scopus 로고    scopus 로고
    • Retroviral insertion mutagenesis in mice as a comparative oncogenomics tool to identify disease genes in human leukemia
    • Touw I.P., and Erkeland S.J. Retroviral insertion mutagenesis in mice as a comparative oncogenomics tool to identify disease genes in human leukemia. Mol. Ther. 15 (2007) 13-19
    • (2007) Mol. Ther. , vol.15 , pp. 13-19
    • Touw, I.P.1    Erkeland, S.J.2
  • 50
    • 27944496521 scopus 로고    scopus 로고
    • Retroviral insertional mutagenesis: past, present and future
    • Uren A.G., Kool J., Berns A., and van Lohuizen M. Retroviral insertional mutagenesis: past, present and future. Oncogene 24 (2005) 7656-7672
    • (2005) Oncogene , vol.24 , pp. 7656-7672
    • Uren, A.G.1    Kool, J.2    Berns, A.3    van Lohuizen, M.4
  • 51
  • 52
    • 33845508785 scopus 로고    scopus 로고
    • Activation of an oncogenic microRNA cistron by provirus integration
    • Wang C.L., et al. Activation of an oncogenic microRNA cistron by provirus integration. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 18680-18684
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 18680-18684
    • Wang, C.L.1
  • 53
    • 0025151092 scopus 로고
    • Subtractive cDNA cloning of RC3, a rodent cortex-enriched mRNA encoding a novel 78 residue protein
    • Watson J.B., Battenberg E.F., Wong K.K., Bloom F.E., and Sutcliffe J.G. Subtractive cDNA cloning of RC3, a rodent cortex-enriched mRNA encoding a novel 78 residue protein. J. Neurosci. Res. 26 (1990) 397-408
    • (1990) J. Neurosci. Res. , vol.26 , pp. 397-408
    • Watson, J.B.1    Battenberg, E.F.2    Wong, K.K.3    Bloom, F.E.4    Sutcliffe, J.G.5
  • 54
    • 29544435300 scopus 로고    scopus 로고
    • Identification of histological markers for malignant glioma by genome-wide expression analysis: dynein, alpha-PIX and sorcin
    • Yokota T., et al. Identification of histological markers for malignant glioma by genome-wide expression analysis: dynein, alpha-PIX and sorcin. Acta Neuropathol. 111 (2006) 29-38
    • (2006) Acta Neuropathol. , vol.111 , pp. 29-38
    • Yokota, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.