메뉴 건너뛰기




Volumn 1801, Issue 4, 2010, Pages 537-546

Specific interaction between E2F1 and Sp1 regulates the expression of murine CTP:phosphocholine cytidylyltransferase alpha during the S phase

Author keywords

Cytidylyltransferase; E2F1; Pcyt1a gene promoter; Phosphatidylcholine; S phase; Sp1

Indexed keywords

CHOLINE PHOSPHATE CYTIDYLYLTRANSFERASE; CHOLINE PHOSPHATE CYTIDYLYLTRANSFERASE ALPHA; TRANSCRIPTION FACTOR E2F1; TRANSCRIPTION FACTOR SP1; UNCLASSIFIED DRUG;

EID: 76749118541     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2010.01.005     Document Type: Article
Times cited : (8)

References (64)
  • 2
    • 0033994181 scopus 로고    scopus 로고
    • Transcriptional control elements and complex initiation pattern of the TATA-less bidirectional human thymidylate synthase promoter
    • Dong S., Lester L., and Johnson L.F. Transcriptional control elements and complex initiation pattern of the TATA-less bidirectional human thymidylate synthase promoter. J. Cell Biochem. 77 (2000) 50-64
    • (2000) J. Cell Biochem. , vol.77 , pp. 50-64
    • Dong, S.1    Lester, L.2    Johnson, L.F.3
  • 3
    • 0028054863 scopus 로고
    • G1/S-regulated E2F-containing protein complexes bind to the mouse thymidine kinase gene promoter
    • Dou Q.P., Zhao S., Levin A.H., Wang J., Helin K., and Pardee A.B. G1/S-regulated E2F-containing protein complexes bind to the mouse thymidine kinase gene promoter. J. Biol. Chem. 269 (1994) 1306-1313
    • (1994) J. Biol. Chem. , vol.269 , pp. 1306-1313
    • Dou, Q.P.1    Zhao, S.2    Levin, A.H.3    Wang, J.4    Helin, K.5    Pardee, A.B.6
  • 4
    • 15844389625 scopus 로고    scopus 로고
    • A genetic defect in phosphatidylcholine biosynthesis triggers apoptosis in Chinese hamster ovary cells
    • Cui Z., Houweling M., Chen M.H., Record M., Chap H., Vance D.E., and Terce F. A genetic defect in phosphatidylcholine biosynthesis triggers apoptosis in Chinese hamster ovary cells. J. Biol. Chem. 271 (1996) 14668-14671
    • (1996) J. Biol. Chem. , vol.271 , pp. 14668-14671
    • Cui, Z.1    Houweling, M.2    Chen, M.H.3    Record, M.4    Chap, H.5    Vance, D.E.6    Terce, F.7
  • 5
    • 0017692045 scopus 로고
    • Lipid requirement for cell cycling. The effect of selective inhibition of lipid synthesis
    • Cornell R., Grove G.L., Rothblat G.H., and Horwitz A.F. Lipid requirement for cell cycling. The effect of selective inhibition of lipid synthesis. Exp. Cell Res. 109 (1977) 299-307
    • (1977) Exp. Cell Res. , vol.109 , pp. 299-307
    • Cornell, R.1    Grove, G.L.2    Rothblat, G.H.3    Horwitz, A.F.4
  • 6
    • 0021996442 scopus 로고
    • Cell cycle-dependent changes in arachidonic acid and glycerol metabolism in Swiss 3T3 cells stimulated by platelet-derived growth factor
    • Habenicht A.J., Glomset J.A., Goerig M., Gronwald R., Grulich J., Loth U., and Schettler G. Cell cycle-dependent changes in arachidonic acid and glycerol metabolism in Swiss 3T3 cells stimulated by platelet-derived growth factor. J. Biol. Chem. 260 (1985) 1370-1373
    • (1985) J. Biol. Chem. , vol.260 , pp. 1370-1373
    • Habenicht, A.J.1    Glomset, J.A.2    Goerig, M.3    Gronwald, R.4    Grulich, J.5    Loth, U.6    Schettler, G.7
  • 7
    • 0028146621 scopus 로고
    • Coordination of membrane phospholipid synthesis with the cell cycle
    • Jackowski S. Coordination of membrane phospholipid synthesis with the cell cycle. J. Biol. Chem. 269 (1994) 3858-3867
    • (1994) J. Biol. Chem. , vol.269 , pp. 3858-3867
    • Jackowski, S.1
  • 8
    • 0028584213 scopus 로고
    • Requirement of phosphatidylcholine for normal progression through the cell cycle in C3H/10T1/2 fibroblasts
    • Terce F., Brun H., and Vance D.E. Requirement of phosphatidylcholine for normal progression through the cell cycle in C3H/10T1/2 fibroblasts. J. Lipid Res. 35 (1994) 2130-2142
    • (1994) J. Lipid Res. , vol.35 , pp. 2130-2142
    • Terce, F.1    Brun, H.2    Vance, D.E.3
  • 9
    • 2342572271 scopus 로고    scopus 로고
    • Phospholipid biosynthesis in mammalian cells
    • Vance J.E., and Vance D.E. Phospholipid biosynthesis in mammalian cells. Biochem. Cell Biol. 82 (2004) 113-128
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 113-128
    • Vance, J.E.1    Vance, D.E.2
  • 10
    • 0037783979 scopus 로고    scopus 로고
    • Gene structure, expression and identification of a new CTP:phosphocholine cytidylyltransferase beta isoform
    • Karim M., Jackson P., and Jackowski S. Gene structure, expression and identification of a new CTP:phosphocholine cytidylyltransferase beta isoform. Biochim. Biophys. Acta 1633 (2003) 1-12
    • (2003) Biochim. Biophys. Acta , vol.1633 , pp. 1-12
    • Karim, M.1    Jackson, P.2    Jackowski, S.3
  • 11
    • 0032577585 scopus 로고    scopus 로고
    • Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase
    • Lykidis A., Murti K.G., and Jackowski S. Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 273 (1998) 14022-14029
    • (1998) J. Biol. Chem. , vol.273 , pp. 14022-14029
    • Lykidis, A.1    Murti, K.G.2    Jackowski, S.3
  • 12
    • 0033578749 scopus 로고    scopus 로고
    • Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant
    • Lykidis A., Baburina I., and Jackowski S. Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant. J. Biol. Chem. 274 (1999) 26992-27001
    • (1999) J. Biol. Chem. , vol.274 , pp. 26992-27001
    • Lykidis, A.1    Baburina, I.2    Jackowski, S.3
  • 13
    • 0030983294 scopus 로고    scopus 로고
    • The structure of the gene for murine CTP:phosphocholine cytidylyltransferase, Ctpct. Relationship of exon structure to functional domains and identification of transcriptional start sites and potential upstream regulatory elements
    • Tang W., Keesler G.A., and Tabas I. The structure of the gene for murine CTP:phosphocholine cytidylyltransferase, Ctpct. Relationship of exon structure to functional domains and identification of transcriptional start sites and potential upstream regulatory elements. J. Biol. Chem. 272 (1997) 13146-13151
    • (1997) J. Biol. Chem. , vol.272 , pp. 13146-13151
    • Tang, W.1    Keesler, G.A.2    Tabas, I.3
  • 14
    • 0025030678 scopus 로고
    • Cloning and expression of rat liver CTP: phosphocholine cytidylyltransferase: an amphipathic protein that controls phosphatidylcholine synthesis
    • Kalmar G.B., Kay R.J., Lachance A., Aebersold R., and Cornell R.B. Cloning and expression of rat liver CTP: phosphocholine cytidylyltransferase: an amphipathic protein that controls phosphatidylcholine synthesis. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 6029-6033
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 6029-6033
    • Kalmar, G.B.1    Kay, R.J.2    Lachance, A.3    Aebersold, R.4    Cornell, R.B.5
  • 15
    • 0023645095 scopus 로고
    • CTP:phosphorylcholine cytidylyltransferase from rat liver. Isolation and characterization of the catalytic subunit
    • Feldman D.A., and Weinhold P.A. CTP:phosphorylcholine cytidylyltransferase from rat liver. Isolation and characterization of the catalytic subunit. J. Biol. Chem. 262 (1987) 9075-9081
    • (1987) J. Biol. Chem. , vol.262 , pp. 9075-9081
    • Feldman, D.A.1    Weinhold, P.A.2
  • 16
    • 0027415175 scopus 로고
    • Nuclear localization of soluble CTP:phosphocholine cytidylyltransferase
    • Wang Y., Sweitzer T.D., Weinhold P.A., and Kent C. Nuclear localization of soluble CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 268 (1993) 5899-5904
    • (1993) J. Biol. Chem. , vol.268 , pp. 5899-5904
    • Wang, Y.1    Sweitzer, T.D.2    Weinhold, P.A.3    Kent, C.4
  • 17
    • 0028816963 scopus 로고
    • Identification of the nuclear localization signal of rat liver CTP:phosphocholine cytidylyltransferase
    • Wang Y., MacDonald J.I., and Kent C. Identification of the nuclear localization signal of rat liver CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 270 (1995) 354-360
    • (1995) J. Biol. Chem. , vol.270 , pp. 354-360
    • Wang, Y.1    MacDonald, J.I.2    Kent, C.3
  • 18
    • 0035941277 scopus 로고    scopus 로고
    • Transcription of the CTP:phosphocholine cytidylyltransferase alpha gene is enhanced during the S phase of the cell cycle
    • Golfman L.S., Bakovic M., and Vance D.E. Transcription of the CTP:phosphocholine cytidylyltransferase alpha gene is enhanced during the S phase of the cell cycle. J. Biol. Chem. 276 (2001) 43688-43692
    • (2001) J. Biol. Chem. , vol.276 , pp. 43688-43692
    • Golfman, L.S.1    Bakovic, M.2    Vance, D.E.3
  • 20
    • 0031553042 scopus 로고    scopus 로고
    • CTP:phosphocholine cytidylyltransferase
    • Kent C. CTP:phosphocholine cytidylyltransferase. Biochim. Biophys. Acta 1348 (1997) 79-90
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 79-90
    • Kent, C.1
  • 21
    • 0001191635 scopus 로고
    • Intracellular distribution of some enzymes catalyzing reactions in the biosynthesis of complex lipids
    • Wilgram G.F., and Kennedy E.P. Intracellular distribution of some enzymes catalyzing reactions in the biosynthesis of complex lipids. J. Biol. Chem. 238 (1963) 2615-2619
    • (1963) J. Biol. Chem. , vol.238 , pp. 2615-2619
    • Wilgram, G.F.1    Kennedy, E.P.2
  • 22
    • 0023834871 scopus 로고
    • Intracellular processing of cytidylyltransferase in Krebs II cells during stimulation of phosphatidylcholine synthesis. Evidence that a plasma membrane modification promotes enzyme translocation specifically to the endoplasmic reticulum
    • Terce F., Record M., Ribbes G., Chap H., and Douste-Blazy L. Intracellular processing of cytidylyltransferase in Krebs II cells during stimulation of phosphatidylcholine synthesis. Evidence that a plasma membrane modification promotes enzyme translocation specifically to the endoplasmic reticulum. J. Biol. Chem. 263 (1988) 3142-3149
    • (1988) J. Biol. Chem. , vol.263 , pp. 3142-3149
    • Terce, F.1    Record, M.2    Ribbes, G.3    Chap, H.4    Douste-Blazy, L.5
  • 23
    • 0023122479 scopus 로고
    • Phosphatidylcholine synthesis for incorporation into membranes or for secretion as plasma lipoproteins by Golgi membranes of rat liver
    • Higgins J.A., and Fieldsend J.K. Phosphatidylcholine synthesis for incorporation into membranes or for secretion as plasma lipoproteins by Golgi membranes of rat liver. J. Lipid Res. 28 (1987) 268-278
    • (1987) J. Lipid Res. , vol.28 , pp. 268-278
    • Higgins, J.A.1    Fieldsend, J.K.2
  • 24
    • 4544305468 scopus 로고    scopus 로고
    • Phosphorylation of Sp1 by cyclin-dependent kinase 2 modulates the role of Sp1 in CTP:phosphocholine cytidylyltransferase alpha regulation during the S phase of the cell cycle
    • Banchio C., Schang L.M., and Vance D.E. Phosphorylation of Sp1 by cyclin-dependent kinase 2 modulates the role of Sp1 in CTP:phosphocholine cytidylyltransferase alpha regulation during the S phase of the cell cycle. J. Biol. Chem. 279 (2004) 40220-40226
    • (2004) J. Biol. Chem. , vol.279 , pp. 40220-40226
    • Banchio, C.1    Schang, L.M.2    Vance, D.E.3
  • 25
    • 0041355204 scopus 로고    scopus 로고
    • Activation of CTP:phosphocholine cytidylyltransferase alpha expression during the S phase of the cell cycle is mediated by the transcription factor Sp1
    • Banchio C., Schang L.M., and Vance D.E. Activation of CTP:phosphocholine cytidylyltransferase alpha expression during the S phase of the cell cycle is mediated by the transcription factor Sp1. J. Biol. Chem. 278 (2003) 32457-32464
    • (2003) J. Biol. Chem. , vol.278 , pp. 32457-32464
    • Banchio, C.1    Schang, L.M.2    Vance, D.E.3
  • 26
    • 33744535033 scopus 로고    scopus 로고
    • Role of histone deacetylase in the expression of CTP:phosphocholine cytidylyltransferase alpha
    • Banchio C., Lingrell S., and Vance D.E. Role of histone deacetylase in the expression of CTP:phosphocholine cytidylyltransferase alpha. J. Biol. Chem. 281 (2006) 10010-10015
    • (2006) J. Biol. Chem. , vol.281 , pp. 10010-10015
    • Banchio, C.1    Lingrell, S.2    Vance, D.E.3
  • 27
    • 34447560155 scopus 로고    scopus 로고
    • Sp-1 binds promoter elements that are regulated by retinoblastoma and regulate CTP:phosphocholine cytidylyltransferase-alpha transcription
    • Banchio C., Lingrell S., and Vance D.E. Sp-1 binds promoter elements that are regulated by retinoblastoma and regulate CTP:phosphocholine cytidylyltransferase-alpha transcription. J. Biol. Chem. 282 (2007) 14827-14835
    • (2007) J. Biol. Chem. , vol.282 , pp. 14827-14835
    • Banchio, C.1    Lingrell, S.2    Vance, D.E.3
  • 28
    • 0031815596 scopus 로고    scopus 로고
    • Toward an understanding of the functional complexity of the E2F and retinoblastoma families
    • Nevins J.R. Toward an understanding of the functional complexity of the E2F and retinoblastoma families. Cell Growth Differ. 9 (1998) 585-593
    • (1998) Cell Growth Differ. , vol.9 , pp. 585-593
    • Nevins, J.R.1
  • 29
    • 0032146274 scopus 로고    scopus 로고
    • The regulation of E2F by pRB-family proteins
    • Dyson N. The regulation of E2F by pRB-family proteins. Genes Dev. 12 (1998) 2245-2262
    • (1998) Genes Dev. , vol.12 , pp. 2245-2262
    • Dyson, N.1
  • 30
    • 0029786402 scopus 로고    scopus 로고
    • Cell cycle regulation of membrane phospholipid metabolism
    • Jackowski S. Cell cycle regulation of membrane phospholipid metabolism. J. Biol. Chem. 271 (1996) 20219-20222
    • (1996) J. Biol. Chem. , vol.271 , pp. 20219-20222
    • Jackowski, S.1
  • 31
    • 67649684294 scopus 로고    scopus 로고
    • Nuclear export of the rate-limiting enzyme in phosphatidylcholine synthesis is mediated by its membrane binding domain
    • Gehrig K., Morton C.C., and Ridgway N.D. Nuclear export of the rate-limiting enzyme in phosphatidylcholine synthesis is mediated by its membrane binding domain. J. Lipid Res. 50 (2009) 966-976
    • (2009) J. Lipid Res. , vol.50 , pp. 966-976
    • Gehrig, K.1    Morton, C.C.2    Ridgway, N.D.3
  • 32
    • 38749103064 scopus 로고    scopus 로고
    • Expansion of the nucleoplasmic reticulum requires the coordinated activity of lamins and CTP:phosphocholine cytidylyltransferase alpha
    • Gehrig K., Cornell R.B., and Ridgway N.D. Expansion of the nucleoplasmic reticulum requires the coordinated activity of lamins and CTP:phosphocholine cytidylyltransferase alpha. Mol. Biol. Cell 19 (2008) 237-247
    • (2008) Mol. Biol. Cell , vol.19 , pp. 237-247
    • Gehrig, K.1    Cornell, R.B.2    Ridgway, N.D.3
  • 33
    • 18344393150 scopus 로고    scopus 로고
    • The E2F transcriptional network: old acquaintances with new faces
    • Dimova D.K., and Dyson N.J. The E2F transcriptional network: old acquaintances with new faces. Oncogene 24 (2005) 2810-2826
    • (2005) Oncogene , vol.24 , pp. 2810-2826
    • Dimova, D.K.1    Dyson, N.J.2
  • 35
    • 0030028934 scopus 로고    scopus 로고
    • Transcriptional regulation of the dihydrofolate reductase gene
    • Slansky J.E., and Farnham P.J. Transcriptional regulation of the dihydrofolate reductase gene. Bioessays 18 (1996) 55-62
    • (1996) Bioessays , vol.18 , pp. 55-62
    • Slansky, J.E.1    Farnham, P.J.2
  • 36
    • 0033583584 scopus 로고    scopus 로고
    • Transcriptional activation of the murine CTP:phosphocholine cytidylyltransferase gene (Ctpct): combined action of upstream stimulatory and inhibitory cis-acting elements
    • Bakovic M., Waite K., Tang W., Tabas I., and Vance D.E. Transcriptional activation of the murine CTP:phosphocholine cytidylyltransferase gene (Ctpct): combined action of upstream stimulatory and inhibitory cis-acting elements. Biochim. Biophys. Acta 1438 (1999) 147-165
    • (1999) Biochim. Biophys. Acta , vol.1438 , pp. 147-165
    • Bakovic, M.1    Waite, K.2    Tang, W.3    Tabas, I.4    Vance, D.E.5
  • 37
    • 0035425499 scopus 로고    scopus 로고
    • Structures of lipid-DNA complexes: supramolecular assembly and gene delivery
    • Safinya C.R. Structures of lipid-DNA complexes: supramolecular assembly and gene delivery. Curr. Opin. Struct. Biol. 11 (2001) 440-448
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 440-448
    • Safinya, C.R.1
  • 38
    • 0025730640 scopus 로고
    • A rapid micropreparation technique for extraction of DNA-binding proteins from limiting numbers of mammalian cells
    • Andrews N.C., and Faller D.V. A rapid micropreparation technique for extraction of DNA-binding proteins from limiting numbers of mammalian cells. Nucleic Acids Res. 19 (1991) 2499
    • (1991) Nucleic Acids Res. , vol.19 , pp. 2499
    • Andrews, N.C.1    Faller, D.V.2
  • 39
    • 0017390556 scopus 로고
    • A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250
    • Sedmak J.J., and Grossberg S.E. A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250. Anal. Biochem. 79 (1977) 544-552
    • (1977) Anal. Biochem. , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 40
    • 0032895139 scopus 로고    scopus 로고
    • Chinese hamster ovary cells overexpressing the oxysterol binding protein (OSBP) display enhanced synthesis of sphingomyelin in response to 25-hydroxycholesterol
    • Lagace T.A., Byers D.M., Cook H.W., and Ridgway N.D. Chinese hamster ovary cells overexpressing the oxysterol binding protein (OSBP) display enhanced synthesis of sphingomyelin in response to 25-hydroxycholesterol. J. Lipid Res. 40 (1999) 109-116
    • (1999) J. Lipid Res. , vol.40 , pp. 109-116
    • Lagace, T.A.1    Byers, D.M.2    Cook, H.W.3    Ridgway, N.D.4
  • 41
    • 0034644651 scopus 로고    scopus 로고
    • Nuclear localization of enzymatically active green fluorescent protein-CTP:phosphocholine cytidylyltransferase alpha fusion protein is independent of cell cycle conditions and cell types
    • DeLong C.J., Qin L., and Cui Z. Nuclear localization of enzymatically active green fluorescent protein-CTP:phosphocholine cytidylyltransferase alpha fusion protein is independent of cell cycle conditions and cell types. J. Biol. Chem. 275 (2000) 32325-32330
    • (2000) J. Biol. Chem. , vol.275 , pp. 32325-32330
    • DeLong, C.J.1    Qin, L.2    Cui, Z.3
  • 42
    • 14844301707 scopus 로고    scopus 로고
    • The rate-limiting enzyme in phosphatidylcholine synthesis regulates proliferation of the nucleoplasmic reticulum
    • Lagace T.A., and Ridgway N.D. The rate-limiting enzyme in phosphatidylcholine synthesis regulates proliferation of the nucleoplasmic reticulum. Mol. Biol. Cell 16 (2005) 1120-1130
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1120-1130
    • Lagace, T.A.1    Ridgway, N.D.2
  • 44
    • 0033550316 scopus 로고    scopus 로고
    • Transcription factors of the Sp1 family: interaction with E2F and regulation of the murine thymidine kinase promoter
    • Rotheneder H., Geymayer S., and Haidweger E. Transcription factors of the Sp1 family: interaction with E2F and regulation of the murine thymidine kinase promoter. J. Mol. Biol. 293 (1999) 1005-1015
    • (1999) J. Mol. Biol. , vol.293 , pp. 1005-1015
    • Rotheneder, H.1    Geymayer, S.2    Haidweger, E.3
  • 45
    • 0035394395 scopus 로고    scopus 로고
    • E2F mediates induction of the Sp1-controlled promoter of the human DNA polymerase epsilon B-subunit gene POLE2
    • Huang D., Jokela M., Tuusa J., Skog S., Poikonen K., and Syvaoja J.E. E2F mediates induction of the Sp1-controlled promoter of the human DNA polymerase epsilon B-subunit gene POLE2. Nucleic Acids Res. 29 (2001) 2810-2821
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2810-2821
    • Huang, D.1    Jokela, M.2    Tuusa, J.3    Skog, S.4    Poikonen, K.5    Syvaoja, J.E.6
  • 46
    • 0024318029 scopus 로고
    • Transcription factor E2F is required for efficient expression of the hamster dihydrofolate reductase gene in vitro and in vivo
    • Blake M.C., and Azizkhan J.C. Transcription factor E2F is required for efficient expression of the hamster dihydrofolate reductase gene in vitro and in vivo. Mol. Cell. Biol. 9 (1989) 4994-5002
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4994-5002
    • Blake, M.C.1    Azizkhan, J.C.2
  • 47
    • 0028960161 scopus 로고
    • An inverted repeat motif stabilizes binding of E2F and enhances transcription of the dihydrofolate reductase gene
    • Wade M., Blake M.C., Jambou R.C., Helin K., Harlow E., and Azizkhan J.C. An inverted repeat motif stabilizes binding of E2F and enhances transcription of the dihydrofolate reductase gene. J. Biol. Chem. 270 (1995) 9783-9791
    • (1995) J. Biol. Chem. , vol.270 , pp. 9783-9791
    • Wade, M.1    Blake, M.C.2    Jambou, R.C.3    Helin, K.4    Harlow, E.5    Azizkhan, J.C.6
  • 48
    • 0029981560 scopus 로고    scopus 로고
    • Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction
    • Lin S.Y., Black A.R., Kostic D., Pajovic S., Hoover C.N., and Azizkhan J.C. Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction. Mol. Cell. Biol. 16 (1996) 1668-1675
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1668-1675
    • Lin, S.Y.1    Black, A.R.2    Kostic, D.3    Pajovic, S.4    Hoover, C.N.5    Azizkhan, J.C.6
  • 49
    • 0029926303 scopus 로고    scopus 로고
    • Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F
    • Karlseder J., Rotheneder H., and Wintersberger E. Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F. Mol. Cell. Biol. 16 (1996) 1659-1667
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1659-1667
    • Karlseder, J.1    Rotheneder, H.2    Wintersberger, E.3
  • 50
    • 0033543697 scopus 로고    scopus 로고
    • Shuttling of CTP:phosphocholine cytidylyltransferase between the nucleus and endoplasmic reticulum accompanies the wave of phosphatidylcholine synthesis during the G(0) -> G(1) transition
    • Northwood I.C., Tong A.H., Crawford B., Drobnies A.E., and Cornell R.B. Shuttling of CTP:phosphocholine cytidylyltransferase between the nucleus and endoplasmic reticulum accompanies the wave of phosphatidylcholine synthesis during the G(0) -> G(1) transition. J. Biol. Chem. 274 (1999) 26240-26248
    • (1999) J. Biol. Chem. , vol.274 , pp. 26240-26248
    • Northwood, I.C.1    Tong, A.H.2    Crawford, B.3    Drobnies, A.E.4    Cornell, R.B.5
  • 51
    • 0029671241 scopus 로고    scopus 로고
    • CTP: phosphocholine cytidylyltransferase is both a nuclear and cytoplasmic protein in primary hepatocytes
    • Houweling M., Cui Z., Anfuso C.D., Bussiere M., Chen M.H., and Vance D.E. CTP: phosphocholine cytidylyltransferase is both a nuclear and cytoplasmic protein in primary hepatocytes. Eur. J. Cell Biol. 69 (1996) 55-63
    • (1996) Eur. J. Cell Biol. , vol.69 , pp. 55-63
    • Houweling, M.1    Cui, Z.2    Anfuso, C.D.3    Bussiere, M.4    Chen, M.H.5    Vance, D.E.6
  • 52
    • 0035966013 scopus 로고    scopus 로고
    • CTP:phosphocholine cytidylyltransferase alpha is a cytosolic protein in pulmonary epithelial cells and tissues
    • Ridsdale R., Tseu I., Wang J., and Post M. CTP:phosphocholine cytidylyltransferase alpha is a cytosolic protein in pulmonary epithelial cells and tissues. J. Biol. Chem. 276 (2001) 49148-49155
    • (2001) J. Biol. Chem. , vol.276 , pp. 49148-49155
    • Ridsdale, R.1    Tseu, I.2    Wang, J.3    Post, M.4
  • 54
    • 1542315585 scopus 로고    scopus 로고
    • Structure and function of choline kinase isoforms in mammalian cells
    • Aoyama C., Liao H., and Ishidate K. Structure and function of choline kinase isoforms in mammalian cells. Prog. Lipid Res. 43 (2004) 266-281
    • (2004) Prog. Lipid Res. , vol.43 , pp. 266-281
    • Aoyama, C.1    Liao, H.2    Ishidate, K.3
  • 55
    • 0027450135 scopus 로고
    • CDPcholine:1, 2-diacylglycerol cholinephosphotransferase from rat liver microsomes. I. Solubilization and characterization of the partially purified enzyme and the possible existence of an endogenous inhibitor
    • Ishidate K., Matsuo R., and Nakazawa Y. CDPcholine:1, 2-diacylglycerol cholinephosphotransferase from rat liver microsomes. I. Solubilization and characterization of the partially purified enzyme and the possible existence of an endogenous inhibitor. Lipids 28 (1993) 89-96
    • (1993) Lipids , vol.28 , pp. 89-96
    • Ishidate, K.1    Matsuo, R.2    Nakazawa, Y.3
  • 56
    • 33144478270 scopus 로고    scopus 로고
    • Hutchinson-Gilford progeria mutant lamin A primarily targets human vascular cells as detected by an anti-Lamin A G608G antibody
    • McClintock D., Gordon L.B., and Djabali K. Hutchinson-Gilford progeria mutant lamin A primarily targets human vascular cells as detected by an anti-Lamin A G608G antibody. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 2154-2159
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 2154-2159
    • McClintock, D.1    Gordon, L.B.2    Djabali, K.3
  • 58
    • 0031816342 scopus 로고    scopus 로고
    • Inhibition of cyclin D1 kinase activity is associated with E2F-mediated inhibition of cyclin D1 promoter activity through E2F and Sp1
    • Watanabe G., Albanese C., Lee R.J., Reutens A., Vairo G., Henglein B., and Pestell R.G. Inhibition of cyclin D1 kinase activity is associated with E2F-mediated inhibition of cyclin D1 promoter activity through E2F and Sp1. Mol. Cell. Biol. 18 (1998) 3212-3222
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3212-3222
    • Watanabe, G.1    Albanese, C.2    Lee, R.J.3    Reutens, A.4    Vairo, G.5    Henglein, B.6    Pestell, R.G.7
  • 59
    • 0035144362 scopus 로고    scopus 로고
    • Cooperation of E2F-p130 and Sp1-pRb complexes in repression of the Chinese hamster dhfr gene
    • Chang Y.C., Illenye S., and Heintz N.H. Cooperation of E2F-p130 and Sp1-pRb complexes in repression of the Chinese hamster dhfr gene. Mol. Cell. Biol. 21 (2001) 1121-1131
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1121-1131
    • Chang, Y.C.1    Illenye, S.2    Heintz, N.H.3
  • 61
    • 0028036190 scopus 로고
    • A glutamine-rich hydrophobic patch in transcription factor Sp1 contacts the dTAFII110 component of the Drosophila TFIID complex and mediates transcriptional activation
    • Gill G., Pascal E., Tseng Z.H., and Tjian R. A glutamine-rich hydrophobic patch in transcription factor Sp1 contacts the dTAFII110 component of the Drosophila TFIID complex and mediates transcriptional activation. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 192-196
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 192-196
    • Gill, G.1    Pascal, E.2    Tseng, Z.H.3    Tjian, R.4
  • 64
    • 0001510491 scopus 로고    scopus 로고
    • The RB and p53 pathways in cancer
    • Sherr C.J., and McCormick F. The RB and p53 pathways in cancer. Cancer Cell 2 (2002) 103-112
    • (2002) Cancer Cell , vol.2 , pp. 103-112
    • Sherr, C.J.1    McCormick, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.