메뉴 건너뛰기




Volumn 290, Issue 15, 2015, Pages 9812-9822

Transcriptional activity of the islet β cell factor Pdx1 Is augmented by lysine methylation catalyzed by the methyltransferase Set7/9

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATION; AMINO ACIDS; CATALYSIS; CYTOLOGY; GENE ENCODING; GENE EXPRESSION; GENES; GLUCOSE; MAMMALS; MASS SPECTROMETRY; METHYLATION; SPECTROMETRY; TRANSCRIPTION;

EID: 84927145879     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.616219     Document Type: Article
Times cited : (42)

References (55)
  • 1
    • 12244299450 scopus 로고    scopus 로고
    • β-Cell function in subjects spanning the range from normal glucose tolerance to overt diabetes: A new analysis
    • Ferrannini, E., Gastaldelli, A., Miyazaki, Y., Matsuda, M., Mari, A., and DeFronzo, R. A. (2005) β-Cell function in subjects spanning the range from normal glucose tolerance to overt diabetes: a new analysis. J. Clin. Endocrinol. Metab. 90, 493-500
    • (2005) J. Clin. Endocrinol. Metab. , vol.90 , pp. 493-500
    • Ferrannini, E.1    Gastaldelli, A.2    Miyazaki, Y.3    Matsuda, M.4    Mari, A.5    DeFronzo, R.A.6
  • 2
    • 0028149890 scopus 로고
    • Insulin-pro-moter-factor 1 is required for pancreas development in mice
    • Jonsson, J., Carlsson, L., Edlund, T., and Edlund, H. (1994) Insulin-pro-moter-factor 1 is required for pancreas development in mice. Nature 371, 606-609
    • (1994) Nature , vol.371 , pp. 606-609
    • Jonsson, J.1    Carlsson, L.2    Edlund, T.3    Edlund, H.4
  • 4
    • 0031031571 scopus 로고    scopus 로고
    • Pancreatic agenesis attributable to a single nucleotide deletion in the human IPF1 gene coding sequence
    • Stoffers, D. A., Zinkin, N. T., Stanojevic, V., Clarke, W. L., and Habener, J. F. (1997) Pancreatic agenesis attributable to a single nucleotide deletion in the human IPF1 gene coding sequence. Nat. Genet. 15, 106-110
    • (1997) Nat. Genet. , vol.15 , pp. 106-110
    • Stoffers, D.A.1    Zinkin, N.T.2    Stanojevic, V.3    Clarke, W.L.4    Habener, J.F.5
  • 5
    • 34548418914 scopus 로고    scopus 로고
    • A feat of metabolic proportions: Pdx1 orchestrates islet development and function in the maintenance of glucose homeostasis
    • Babu, D. A., Deering, T. G., and Mirmira, R. G. (2007) A feat of metabolic proportions: Pdx1 orchestrates islet development and function in the maintenance of glucose homeostasis. Mol. Genet. Metab. 92, 43-55
    • (2007) Mol. Genet. Metab. , vol.92 , pp. 43-55
    • Babu, D.A.1    Deering, T.G.2    Mirmira, R.G.3
  • 7
    • 43749099640 scopus 로고    scopus 로고
    • Pdx1 and BETA2/neuroD1 participate in a transcriptional complex that mediates short-range DNA looping at the insulin gene
    • Babu, D. A., Chakrabarti, S. K., Garmey, J. C., and Mirmira, R. G. (2008) Pdx1 and BETA2/neuroD1 participate in a transcriptional complex that mediates short-range DNA looping at the insulin gene. J. Biol. Chem. 283, 8164-8172
    • (2008) J. Biol. Chem. , vol.283 , pp. 8164-8172
    • Babu, D.A.1    Chakrabarti, S.K.2    Garmey, J.C.3    Mirmira, R.G.4
  • 8
    • 0033962883 scopus 로고    scopus 로고
    • The homeodomain of PDX-1 mediates multiple protein-protein interactions in the formation of a transcriptional activation complex on the insulin promoter
    • Ohneda, K., Mirmira, R. G., Wang, J., Johnson, J. D., and German, M. S. (2000) The homeodomain of PDX-1 mediates multiple protein-protein interactions in the formation of a transcriptional activation complex on the insulin promoter. Mol. Cell. Biol. 20, 900-911
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 900-911
    • Ohneda, K.1    Mirmira, R.G.2    Wang, J.3    Johnson, J.D.4    German, M.S.5
  • 9
    • 77957825438 scopus 로고    scopus 로고
    • Pcif1 modulates Pdx1 protein stability and pancreatic β cell function and survival in mice
    • Claiborn, K. C., Sachdeva, M. M., Cannon, C. E., Groff, D. N., Singer, J. D., and Stoffers, D. A. (2010) Pcif1 modulates Pdx1 protein stability and pancreatic β cell function and survival in mice. J. Clin. Invest. 120, 3713-3721
    • (2010) J. Clin. Invest. , vol.120 , pp. 3713-3721
    • Claiborn, K.C.1    Sachdeva, M.M.2    Cannon, C.E.3    Groff, D.N.4    Singer, J.D.5    Stoffers, D.A.6
  • 10
    • 27744606538 scopus 로고    scopus 로고
    • Pdx-1 links histone H3-Lys-4 methylation to RNA polymerase II elongation during activation of insulin transcription
    • Francis, J., Chakrabarti, S. K., Garmey, J. C., and Mirmira, R. G. (2005) Pdx-1 links histone H3-Lys-4 methylation to RNA polymerase II elongation during activation of insulin transcription. J. Biol. Chem. 280, 36244-36253
    • (2005) J. Biol. Chem. , vol.280 , pp. 36244-36253
    • Francis, J.1    Chakrabarti, S.K.2    Garmey, J.C.3    Mirmira, R.G.4
  • 12
    • 73149099403 scopus 로고    scopus 로고
    • Regulation of NF-κB activity through lysine monomethylation of p65
    • Ea, C.-K., and Baltimore, D. (2009) Regulation of NF-κB activity through lysine monomethylation of p65. Proc. Natl. Acad. Sci. U.S.A. 106, 18972-18977
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 18972-18977
    • Ea, C.-K.1    Baltimore, D.2
  • 14
    • 67349285384 scopus 로고    scopus 로고
    • Negative regulation of NF-κB action by Set9-mediated lysine methylation of the RelA subunit
    • Yang, X.-D., Huang, B., Li, M., Lamb, A., Kelleher, N. L., and Chen, L.-F. (2009) Negative regulation of NF-κB action by Set9-mediated lysine methylation of the RelA subunit. EMBO J. 28, 1055-1066
    • (2009) EMBO J , vol.28 , pp. 1055-1066
    • Yang, X.-D.1    Huang, B.2    Li, M.3    Lamb, A.4    Kelleher, N.L.5    Chen, L.-F.6
  • 16
    • 17044392996 scopus 로고    scopus 로고
    • Role of protein methylation in regulation of transcription
    • Lee, D. Y., Teyssier, C., Strahl, B. D., and Stallcup, M. R. (2005) Role of protein methylation in regulation of transcription. Endocr. Rev. 26, 147-170
    • (2005) Endocr. Rev. , vol.26 , pp. 147-170
    • Lee, D.Y.1    Teyssier, C.2    Strahl, B.D.3    Stallcup, M.R.4
  • 18
    • 0034640429 scopus 로고    scopus 로고
    • β-Cell differentiation factor Nkx6.1 contains distinct DNA Binding interference and transcriptional repression domains
    • Mirmira, R. G., Watada, H., and German, M. S. (2000) β-Cell differentiation factor Nkx6.1 contains distinct DNA Binding interference and transcriptional repression domains. J. Biol. Chem. 275, 14743-14751
    • (2000) J. Biol. Chem. , vol.275 , pp. 14743-14751
    • Mirmira, R.G.1    Watada, H.2    German, M.S.3
  • 19
    • 0038607422 scopus 로고    scopus 로고
    • Covalent histone modifications underlie the developmental regulation of insulin gene transcription in pancreatic β cells
    • Chakrabarti, S. K., Francis, J., Ziesmann, S. M., Garmey, J. C., and Mirmira, R. G. (2003) Covalent histone modifications underlie the developmental regulation of insulin gene transcription in pancreatic β cells. J. Biol. Chem. 278, 23617-23623
    • (2003) J. Biol. Chem. , vol.278 , pp. 23617-23623
    • Chakrabarti, S.K.1    Francis, J.2    Ziesmann, S.M.3    Garmey, J.C.4    Mirmira, R.G.5
  • 20
    • 84901953809 scopus 로고    scopus 로고
    • Characterization of mice expressing Ins1 gene promoter driven CreERT recombinase for conditional gene deletion in pancreatic β-cells
    • Tamarina, N. A., Roe, M. W., and Philipson, L. (2014) Characterization of mice expressing Ins1 gene promoter driven CreERT recombinase for conditional gene deletion in pancreatic β-cells. Islets 6, e27685
    • (2014) Islets , vol.6 , pp. e27685
    • Tamarina, N.A.1    Roe, M.W.2    Philipson, L.3
  • 22
    • 84868295285 scopus 로고    scopus 로고
    • Mouse islet of Langerhans isolation using a combination of purified collagenase and neutral protease
    • Stull, N. D., Breite, A., McCarthy, R. C., Tersey, S. A., and Mirmira, R. G. (2012) Mouse islet of Langerhans isolation using a combination of purified collagenase and neutral protease. J. Vis. Exp. 67, e4137
    • (2012) J. Vis. Exp. , vol.67 , pp. e4137
    • Stull, N.D.1    Breite, A.2    McCarthy, R.C.3    Tersey, S.A.4    Mirmira, R.G.5
  • 23
    • 23944494573 scopus 로고    scopus 로고
    • The C-terminal domain of the β cell homeodomain factor Nkx6.1 enhances sequence-selective DNA binding at the insulin promoter
    • Taylor, D. G., Babu, D., and Mirmira, R. G. (2005) The C-terminal domain of the β cell homeodomain factor Nkx6.1 enhances sequence-selective DNA binding at the insulin promoter. Biochemistry 44, 11269-11278
    • (2005) Biochemistry , vol.44 , pp. 11269-11278
    • Taylor, D.G.1    Babu, D.2    Mirmira, R.G.3
  • 24
    • 0037083757 scopus 로고    scopus 로고
    • Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation
    • Nishioka, K., Chuikov, S., Sarma, K., Erdjument-Bromage, H., Allis, C. D., Tempst, P., and Reinberg, D. (2002) Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16, 479-489
    • (2002) Genes Dev. , vol.16 , pp. 479-489
    • Nishioka, K.1    Chuikov, S.2    Sarma, K.3    Erdjument-Bromage, H.4    Allis, C.D.5    Tempst, P.6    Reinberg, D.7
  • 25
    • 63249112026 scopus 로고    scopus 로고
    • Methyltransferase Set7/9 maintains transcription and euchromatin structure at islet-enriched genes
    • Deering, T. G., Ogihara, T., Trace, A. P., Maier, B., and Mirmira, R. G. (2009) Methyltransferase Set7/9 maintains transcription and euchromatin structure at islet-enriched genes. Diabetes 58, 185-193
    • (2009) Diabetes , vol.58 , pp. 185-193
    • Deering, T.G.1    Ogihara, T.2    Trace, A.P.3    Maier, B.4    Mirmira, R.G.5
  • 26
    • 77954691054 scopus 로고    scopus 로고
    • (Bis)urea and (bis)thiourea inhibitors of lysine-specific demethylase 1 as epigenetic modulators
    • Sharma, S. K., Wu, Y., Steinbergs, N., Crowley, M. L., Hanson, A. S., Casero, R. A., and Woster, P. M. (2010) (Bis)urea and (bis)thiourea inhibitors of lysine-specific demethylase 1 as epigenetic modulators. J. Med. Chem. 53, 5197-5212
    • (2010) J. Med. Chem. , vol.53 , pp. 5197-5212
    • Sharma, S.K.1    Wu, Y.2    Steinbergs, N.3    Crowley, M.L.4    Hanson, A.S.5    Casero, R.A.6    Woster, P.M.7
  • 27
    • 80053898129 scopus 로고    scopus 로고
    • Discovery of novel alkylated (bis)urea and (bis)thiourea polyamine analogues with potent antimalarial activities
    • Verlinden, B. K., Niemand, J., Snyman, J., Sharma, S. K., Beattie, R. J., Woster, P. M., and Birkholtz, L.-M. (2011) Discovery of novel alkylated (bis)urea and (bis)thiourea polyamine analogues with potent antimalarial activities. J. Med. Chem. 54, 6624-6633
    • (2011) J. Med. Chem. , vol.54 , pp. 6624-6633
    • Verlinden, B.K.1    Niemand, J.2    Snyman, J.3    Sharma, S.K.4    Beattie, R.J.5    Woster, P.M.6    Birkholtz, L.-M.7
  • 28
    • 78650053328 scopus 로고    scopus 로고
    • Inhibition of deoxyhypusine synthase enhances islet β cell function and survival in the setting of endoplasmic reticulum stress and type 2 diabetes
    • Robbins, R. D., Tersey, S. A., Ogihara, T., Gupta, D., Farb, T. B., Ficorilli, J., Bokvist, K., Maier, B., and Mirmira, R. G. (2010) Inhibition of deoxyhypusine synthase enhances islet β cell function and survival in the setting of endoplasmic reticulum stress and type 2 diabetes. J. Biol. Chem. 285, 39943-39952
    • (2010) J. Biol. Chem. , vol.285 , pp. 39943-39952
    • Robbins, R.D.1    Tersey, S.A.2    Ogihara, T.3    Gupta, D.4    Farb, T.B.5    Ficorilli, J.6    Bokvist, K.7    Maier, B.8    Mirmira, R.G.9
  • 29
    • 0037261918 scopus 로고    scopus 로고
    • Adenoviral gene transfer into β-cell lines
    • Mosley, A. L., and Ozcan, S. (2003) Adenoviral gene transfer into β-cell lines. Methods Mol. Med. 83, 73-79
    • (2003) Methods Mol. Med. , vol.83 , pp. 73-79
    • Mosley, A.L.1    Ozcan, S.2
  • 30
    • 4544233448 scopus 로고    scopus 로고
    • Glucose regulation of insulin gene expression requires the recruitment of p300 by the β-cellspecific transcription factor Pdx-1
    • Mosley, A. L., Corbett, J. A., and Ozcan, S. (2004) Glucose regulation of insulin gene expression requires the recruitment of p300 by the β-cellspecific transcription factor Pdx-1. Mol. Endocrinol. 18, 2279-2290
    • (2004) Mol. Endocrinol. , vol.18 , pp. 2279-2290
    • Mosley, A.L.1    Corbett, J.A.2    Ozcan, S.3
  • 31
    • 0026602931 scopus 로고
    • The insulin and islet amyloid polypeptide genes contain similar cell-specific promoter elements that bind identical β-cell nuclear complexes
    • German, M. S., Moss, L. G., Wang, J., and Rutter, W. J. (1992) The insulin and islet amyloid polypeptide genes contain similar cell-specific promoter elements that bind identical β-cell nuclear complexes. Mol. Cell. Biol. 12, 1777-1788
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1777-1788
    • German, M.S.1    Moss, L.G.2    Wang, J.3    Rutter, W.J.4
  • 33
    • 79251590753 scopus 로고    scopus 로고
    • Specificity analysis-based identification of new methylation targets of the SET7/9 protein lysine methyltransferase
    • Dhayalan, A., Kudithipudi, S., Rathert, P., and Jeltsch, A. (2011) Specificity analysis-based identification of new methylation targets of the SET7/9 protein lysine methyltransferase. Chem. Biol. 18, 111-120
    • (2011) Chem. Biol. , vol.18 , pp. 111-120
    • Dhayalan, A.1    Kudithipudi, S.2    Rathert, P.3    Jeltsch, A.4
  • 34
    • 84888132934 scopus 로고    scopus 로고
    • SET for life: Biochemical activities and biological functions of SET domain-containing proteins
    • Herz, H.-M., Garruss, A., and Shilatifard, A. (2013) SET for life: biochemical activities and biological functions of SET domain-containing proteins. Trends Biochem. Sci. 38, 621-639
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 621-639
    • Herz, H.-M.1    Garruss, A.2    Shilatifard, A.3
  • 35
    • 0037066694 scopus 로고    scopus 로고
    • Quantitative assessment of gene targeting in vitro and in vivo by the pancreatic transcription factor, Pdx1: Importance of chromatin structure in directing promoter binding
    • Chakrabarti, S. K., James, J. C., and Mirmira, R. G. (2002) Quantitative assessment of gene targeting in vitro and in vivo by the pancreatic transcription factor, Pdx1: importance of chromatin structure in directing promoter binding. J. Biol. Chem. 277, 13286-13293
    • (2002) J. Biol. Chem. , vol.277 , pp. 13286-13293
    • Chakrabarti, S.K.1    James, J.C.2    Mirmira, R.G.3
  • 39
    • 33646549635 scopus 로고    scopus 로고
    • Phosphorylation marks IPF1/PDX1 protein for degradation by glycogen synthase kinase 3-dependent mechanisms
    • Boucher, M.-J., Selander, L., Carlsson, L., and Edlund, H. (2006) Phosphorylation marks IPF1/PDX1 protein for degradation by glycogen synthase kinase 3-dependent mechanisms. J. Biol. Chem. 281, 6395-6403
    • (2006) J. Biol. Chem. , vol.281 , pp. 6395-6403
    • Boucher, M.-J.1    Selander, L.2    Carlsson, L.3    Edlund, H.4
  • 40
    • 84859589878 scopus 로고    scopus 로고
    • Pdx1 is post-translationally modified in vivo and serine 61 is the principal site of phosphorylation
    • Frogne, T., Sylvestersen, K. B., Kubicek, S., Nielsen, M. L., and Hecksher-Sørensen, J. (2012) Pdx1 is post-translationally modified in vivo and serine 61 is the principal site of phosphorylation. PLoS ONE 7, e35233
    • (2012) PLoS ONE , vol.7 , pp. e35233
    • Frogne, T.1    Sylvestersen, K.B.2    Kubicek, S.3    Nielsen, M.L.4    Hecksher-Sørensen, J.5
  • 41
    • 77449116389 scopus 로고    scopus 로고
    • Glucose regulates steady-state levels of PDX1 via the reciprocal actions of GSK3 and AKT kinases
    • Humphrey, R. K., Yu, S.-M., Flores, L. E., and Jhala, U. S. (2010) Glucose regulates steady-state levels of PDX1 via the reciprocal actions of GSK3 and AKT kinases. J. Biol. Chem. 285, 3406-3416
    • (2010) J. Biol. Chem. , vol.285 , pp. 3406-3416
    • Humphrey, R.K.1    Yu, S.-M.2    Flores, L.E.3    Jhala, U.S.4
  • 42
    • 84883191685 scopus 로고    scopus 로고
    • Per-Arnt-Sim kinase regulates pancreatic duodenal homeobox-1 protein stability via phosphorylation of glycogen synthase kinase 3β in pancreatic β-cells
    • Semache, M., Zarrouki, B., Fontés, G., Fogarty, S., Kikani, C., Chawki, M. B., Rutter, J., and Poitout, V. (2013) Per-Arnt-Sim kinase regulates pancreatic duodenal homeobox-1 protein stability via phosphorylation of glycogen synthase kinase 3β in pancreatic β-cells. J. Biol. Chem. 288, 24825-24833
    • (2013) J. Biol. Chem. , vol.288 , pp. 24825-24833
    • Semache, M.1    Zarrouki, B.2    Fontés, G.3    Fogarty, S.4    Kikani, C.5    Chawki, M.B.6    Rutter, J.7    Poitout, V.8
  • 43
    • 84857126831 scopus 로고    scopus 로고
    • Glucose activates free fatty acid receptor 1 gene transcription via phosphatidylinositol-3-kinase-dependent O-GlcNAcylation of pancreas-duodenum homeobox-1
    • Kebede, M., Ferdaoussi, M., Mancini, A., Alquier, T., Kulkarni, R. N., Walker, M. D., and Poitout, V. (2012) Glucose activates free fatty acid receptor 1 gene transcription via phosphatidylinositol-3-kinase-dependent O-GlcNAcylation of pancreas-duodenum homeobox-1. Proc. Natl. Acad. Sci. U.S.A. 109, 2376-2381
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 2376-2381
    • Kebede, M.1    Ferdaoussi, M.2    Mancini, A.3    Alquier, T.4    Kulkarni, R.N.5    Walker, M.D.6    Poitout, V.7
  • 44
    • 0037376447 scopus 로고    scopus 로고
    • Sumoylation of Pdx1 is associated with its nuclear localization and insulin gene activation
    • Kishi, A., Nakamura, T., Nishio, Y., Maegawa, H., and Kashiwagi, A. (2003) Sumoylation of Pdx1 is associated with its nuclear localization and insulin gene activation. Am. J. Physiol. Endocrinol. Metab. 284, E830-E840
    • (2003) Am. J. Physiol. Endocrinol. Metab. , vol.284 , pp. E830-E840
    • Kishi, A.1    Nakamura, T.2    Nishio, Y.3    Maegawa, H.4    Kashiwagi, A.5
  • 45
    • 55549140173 scopus 로고    scopus 로고
    • Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-κB-dependent inflammatory genes: Relevance to diabetes and inflammation
    • Li, Y., Reddy, M. A., Miao, F., Shanmugam, N., Yee, J. K., Hawkins, D., Ren, B., and Natarajan, R. (2008) Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-κB-dependent inflammatory genes: relevance to diabetes and inflammation. J. Biol. Chem. 283, 26771-26781
    • (2008) J. Biol. Chem. , vol.283 , pp. 26771-26781
    • Li, Y.1    Reddy, M.A.2    Miao, F.3    Shanmugam, N.4    Yee, J.K.5    Hawkins, D.6    Ren, B.7    Natarajan, R.8
  • 46
    • 1942534675 scopus 로고    scopus 로고
    • Gene-specific modulation of TAF10 function by SET9-mediated methylation
    • Kouskouti, A., Scheer, E., Staub, A., Tora, L., and Talianidis, I. (2004) Gene-specific modulation of TAF10 function by SET9-mediated methylation. Mol. Cell 14, 175-182
    • (2004) Mol. Cell. , vol.14 , pp. 175-182
    • Kouskouti, A.1    Scheer, E.2    Staub, A.3    Tora, L.4    Talianidis, I.5
  • 47
    • 32244444118 scopus 로고    scopus 로고
    • Structural basis for the methylation site specificity of SET7/9
    • Couture, J. F., Collazo, E., Hauk, G., and Trievel, R. C. (2006) Structural basis for the methylation site specificity of SET7/9. Nat. Struct. Mol. Biol. 13, 140-146
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 140-146
    • Couture, J.F.1    Collazo, E.2    Hauk, G.3    Trievel, R.C.4
  • 49
    • 77954274181 scopus 로고    scopus 로고
    • Lysine methylation regulates E2F1-induced cell death
    • Kontaki, H., and Talianidis, I. (2010) Lysine methylation regulates E2F1-induced cell death. Mol. Cell 39, 152-160
    • (2010) Mol. Cell. , vol.39 , pp. 152-160
    • Kontaki, H.1    Talianidis, I.2
  • 52
    • 0037439085 scopus 로고    scopus 로고
    • Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet
    • Kwon, T., Chang, J. H., Kwak, E., Lee, C. W., Joachimiak, A., Kim, Y. C., Lee, J., and Cho, Y. (2003) Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet. EMBO J. 22, 292-303
    • (2003) EMBO J , vol.22 , pp. 292-303
    • Kwon, T.1    Chang, J.H.2    Kwak, E.3    Lee, C.W.4    Joachimiak, A.5    Kim, Y.C.6    Lee, J.7    Cho, Y.8
  • 55
    • 20444482821 scopus 로고    scopus 로고
    • Mechanism of insulin gene regulation by the pancreatic transcription factor Pdx-1: Application of pre-mRNA analysis and chromatin immunoprecipitation to assess formation of functional transcriptional complexes
    • Iype, T., Francis, J., Garmey, J. C., Schisler, J. C., Nesher, R., Weir, G. C., Becker, T. C., Newgard, C. B., Griffen, S. C., and Mirmira, R. G. (2005) Mechanism of insulin gene regulation by the pancreatic transcription factor Pdx-1: application of pre-mRNA analysis and chromatin immunoprecipitation to assess formation of functional transcriptional complexes. J. Biol. Chem. 280, 16798-16807
    • (2005) J. Biol. Chem. , vol.280 , pp. 16798-16807
    • Iype, T.1    Francis, J.2    Garmey, J.C.3    Schisler, J.C.4    Nesher, R.5    Weir, G.C.6    Becker, T.C.7    Newgard, C.B.8    Griffen, S.C.9    Mirmira, R.G.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.