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Volumn 53, Issue 1, 2009, Pages 2-9

Transcriptional regulation of peptidylarginine deiminase expression in human keratinocytes

Author keywords

Epidermis; Keratinocytes; Peptidylarginine deiminase; Transcription factors; Transcriptional regulation

Indexed keywords

CALCIUM; CCAAT BINDING FACTOR; PROTEIN ARGININE DEIMINASE; TATA BINDING PROTEIN; TRANSCRIPTION FACTOR SP1;

EID: 57549083621     PISSN: 09231811     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jdermsci.2008.09.009     Document Type: Review
Times cited : (44)

References (50)
  • 1
    • 0017351552 scopus 로고
    • The enzymic derivation of citrulline residues from arginine residues in situ during the biosynthesis of hair proteins that are cross-linked by isopeptide bonds
    • Rogers G., and Taylor L. The enzymic derivation of citrulline residues from arginine residues in situ during the biosynthesis of hair proteins that are cross-linked by isopeptide bonds. Adv Exp Med Biol 86A (1977) 283-294
    • (1977) Adv Exp Med Biol , vol.86 A , pp. 283-294
    • Rogers, G.1    Taylor, L.2
  • 2
    • 0024473081 scopus 로고
    • 2+-dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain
    • 2+-dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain. J Biol Chem 264 (1989) 18119-18127
    • (1989) J Biol Chem , vol.264 , pp. 18119-18127
    • Inagaki, M.1    Takahara, H.2    Nishi, Y.3    Sugawara, K.4    Sato, C.5
  • 3
    • 0027317616 scopus 로고
    • Deimination of human myelin basic protein by a peptidylarginine deiminase from bovine brain
    • Lamensa J.W., and Moscarello M.A. Deimination of human myelin basic protein by a peptidylarginine deiminase from bovine brain. J Neurochem 61 (1993) 987-996
    • (1993) J Neurochem , vol.61 , pp. 987-996
    • Lamensa, J.W.1    Moscarello, M.A.2
  • 4
    • 24344505085 scopus 로고    scopus 로고
    • The peptidylarginine deiminases expressed in human epidermis differ by their substrate specificities and subcellular locations
    • Méchin M.C., Enji M., Nachat R., Chavanas S., Charveron M., Ishida-Yamamoto A., et al. The peptidylarginine deiminases expressed in human epidermis differ by their substrate specificities and subcellular locations. Cell Mol Life Sci 62 (2005) 1984-1995
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1984-1995
    • Méchin, M.C.1    Enji, M.2    Nachat, R.3    Chavanas, S.4    Charveron, M.5    Ishida-Yamamoto, A.6
  • 6
    • 22144467342 scopus 로고    scopus 로고
    • Peptidylarginine deiminase isoforms are differentially expressed in the anagen hair follicles and other human skin appendages
    • Nachat R., Mechin M.C., Charveron M., Serre G., Constans J., and Simon M. Peptidylarginine deiminase isoforms are differentially expressed in the anagen hair follicles and other human skin appendages. J Invest Dermatol 125 (2005) 34-41
    • (2005) J Invest Dermatol , vol.125 , pp. 34-41
    • Nachat, R.1    Mechin, M.C.2    Charveron, M.3    Serre, G.4    Constans, J.5    Simon, M.6
  • 7
    • 12944329841 scopus 로고    scopus 로고
    • Peptidylarginine deiminase isoforms 1-3 are expressed in the epidermis and involved in the deimination of K1 and filaggrin
    • Nachat R., Méchin M.C., Takahara H., Chavanas S., Charveron M., Serre G., et al. Peptidylarginine deiminase isoforms 1-3 are expressed in the epidermis and involved in the deimination of K1 and filaggrin. J Invest Dermatol 124 (2005) 384-393
    • (2005) J Invest Dermatol , vol.124 , pp. 384-393
    • Nachat, R.1    Méchin, M.C.2    Takahara, H.3    Chavanas, S.4    Charveron, M.5    Serre, G.6
  • 8
    • 1842829046 scopus 로고    scopus 로고
    • Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6
    • Chavanas S., Méchin M.C., Takahara H., Kawada A., Nachat R., Serre G., et al. Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6. Gene 330 (2004) 19-27
    • (2004) Gene , vol.330 , pp. 19-27
    • Chavanas, S.1    Méchin, M.C.2    Takahara, H.3    Kawada, A.4    Nachat, R.5    Serre, G.6
  • 9
    • 0242720407 scopus 로고    scopus 로고
    • PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease
    • Vossenaar E.R., Zendman A.J., van Venrooij W.J., and Pruijn G.J. PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. Bioessays 25 (2003) 1106-1118
    • (2003) Bioessays , vol.25 , pp. 1106-1118
    • Vossenaar, E.R.1    Zendman, A.J.2    van Venrooij, W.J.3    Pruijn, G.J.4
  • 10
    • 27844536541 scopus 로고    scopus 로고
    • A rigorous method for multigenic families' functional annotation: the peptidyl arginine deiminase (PADs) proteins family example
    • Balandraud N., Gouret P., Danchin E.G., Blanc M., Zinn D., Roudier J., et al. A rigorous method for multigenic families' functional annotation: the peptidyl arginine deiminase (PADs) proteins family example. BMC Genomics 6 (2005) 153
    • (2005) BMC Genomics , vol.6 , pp. 153
    • Balandraud, N.1    Gouret, P.2    Danchin, E.G.3    Blanc, M.4    Zinn, D.5    Roudier, J.6
  • 11
    • 0037442843 scopus 로고    scopus 로고
    • cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I
    • Guerrin M., Ishigami A., Mechin M.C., Nachat R., Valmary S., et al. cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I. Biochem J 370 (2003) 167-174
    • (2003) Biochem J , vol.370 , pp. 167-174
    • Guerrin, M.1    Ishigami, A.2    Mechin, M.C.3    Nachat, R.4    Valmary, S.5
  • 12
    • 0036406870 scopus 로고    scopus 로고
    • Human peptidylarginine deiminase type II: molecular cloning, gene organization, and expression in human skin
    • Ishigami A., Ohsawa T., Asaga H., Akiyama K., Kuramoto M., and Maruyama N. Human peptidylarginine deiminase type II: molecular cloning, gene organization, and expression in human skin. Arch Biochem Biophys 407 (2002) 25-31
    • (2002) Arch Biochem Biophys , vol.407 , pp. 25-31
    • Ishigami, A.1    Ohsawa, T.2    Asaga, H.3    Akiyama, K.4    Kuramoto, M.5    Maruyama, N.6
  • 13
    • 0033749775 scopus 로고    scopus 로고
    • Human peptidylarginine deiminase type III: molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin
    • Kanno T., Kawada A., Yamanouchi J., Yosida-Noro C., Yoshiki A., Shiraiwa M., et al. Human peptidylarginine deiminase type III: molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin. J Invest Dermatol 115 (2000) 813-823
    • (2000) J Invest Dermatol , vol.115 , pp. 813-823
    • Kanno, T.1    Kawada, A.2    Yamanouchi, J.3    Yosida-Noro, C.4    Yoshiki, A.5    Shiraiwa, M.6
  • 14
    • 0026035925 scopus 로고
    • Epidermal type I transglutaminase (TGM1) is assigned to human chromosome 14
    • Polakowska R.R., Eddy R.L., Shows T.B., and Goldsmith L.A. Epidermal type I transglutaminase (TGM1) is assigned to human chromosome 14. Cytogenet Cell Genet 56 (1991) 105-107
    • (1991) Cytogenet Cell Genet , vol.56 , pp. 105-107
    • Polakowska, R.R.1    Eddy, R.L.2    Shows, T.B.3    Goldsmith, L.A.4
  • 15
    • 0021027476 scopus 로고
    • Histidine-rich proteins (filaggrins): structural and functional heterogeneity during epidermal differentiation
    • Harding C.R., and Scott I.R. Histidine-rich proteins (filaggrins): structural and functional heterogeneity during epidermal differentiation. J Mol Biol 170 (1983) 651-673
    • (1983) J Mol Biol , vol.170 , pp. 651-673
    • Harding, C.R.1    Scott, I.R.2
  • 16
    • 0029103435 scopus 로고
    • Detection of deiminated proteins in rat skin: probing with a monospecific antibody after modification of citrulline residues
    • Senshu T., Akiyama K., Kan S., Asaga H., Ishigami A., and Manabe M. Detection of deiminated proteins in rat skin: probing with a monospecific antibody after modification of citrulline residues. J Invest Dermatol 105 (1995) 163-169
    • (1995) J Invest Dermatol , vol.105 , pp. 163-169
    • Senshu, T.1    Akiyama, K.2    Kan, S.3    Asaga, H.4    Ishigami, A.5    Manabe, M.6
  • 17
    • 0000301523 scopus 로고    scopus 로고
    • Preferential deimination of keratin K1 and filaggrin during the terminal differentiation of human epidermis
    • Senshu T., Kan S., Ogawa H., Manabe M., and Asaga H. Preferential deimination of keratin K1 and filaggrin during the terminal differentiation of human epidermis. Biochem Biophys Res Commun 225 (1996) 712-719
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 712-719
    • Senshu, T.1    Kan, S.2    Ogawa, H.3    Manabe, M.4    Asaga, H.5
  • 18
    • 0030784777 scopus 로고    scopus 로고
    • The fate of trichohyalin. Sequential post-translational modifications by peptidyl-arginine deiminase and transglutaminases
    • Tarcsa E., Marekov L.N., Andreoli J., Idler W.W., Candi E., Chung S.I., et al. The fate of trichohyalin. Sequential post-translational modifications by peptidyl-arginine deiminase and transglutaminases. J Biol Chem 272 (1997) 27893-27901
    • (1997) J Biol Chem , vol.272 , pp. 27893-27901
    • Tarcsa, E.1    Marekov, L.N.2    Andreoli, J.3    Idler, W.W.4    Candi, E.5    Chung, S.I.6
  • 19
    • 0029824853 scopus 로고    scopus 로고
    • Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin
    • Tarcsa E., Marekov L.N., Mei G., Melino G., Lee S.C., and Steinert P.M. Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin. J Biol Chem 271 (1996) 30709-30716
    • (1996) J Biol Chem , vol.271 , pp. 30709-30716
    • Tarcsa, E.1    Marekov, L.N.2    Mei, G.3    Melino, G.4    Lee, S.C.5    Steinert, P.M.6
  • 21
    • 0033028238 scopus 로고    scopus 로고
    • Dynamic aspects of protein deimination in developing mouse epidermis
    • Akiyama K., and Senshu T. Dynamic aspects of protein deimination in developing mouse epidermis. Exp Dermatol 8 (1999) 177-186
    • (1999) Exp Dermatol , vol.8 , pp. 177-186
    • Akiyama, K.1    Senshu, T.2
  • 22
    • 0038297515 scopus 로고    scopus 로고
    • Changing pattern of deiminated proteins in developing human epidermis
    • Tsuji Y., Akiyama M., Arita K., Senshu T., and Shimizu H. Changing pattern of deiminated proteins in developing human epidermis. J Invest Dermatol 120 (2003) 817-822
    • (2003) J Invest Dermatol , vol.120 , pp. 817-822
    • Tsuji, Y.1    Akiyama, M.2    Arita, K.3    Senshu, T.4    Shimizu, H.5
  • 23
    • 33749327922 scopus 로고    scopus 로고
    • Peptidylarginine deiminases and deimination in biology and pathology: Relevance to skin homeostasis
    • Chavanas S., Méchin M.C., Nachat R., Adoue V., Coudane F., Serre G., et al. Peptidylarginine deiminases and deimination in biology and pathology: Relevance to skin homeostasis. J Dermatol Sci 44 (2006) 63-72
    • (2006) J Dermatol Sci , vol.44 , pp. 63-72
    • Chavanas, S.1    Méchin, M.C.2    Nachat, R.3    Adoue, V.4    Coudane, F.5    Serre, G.6
  • 24
    • 39149089293 scopus 로고    scopus 로고
    • Crucial Roles of MZF1 and Sp1 in the Transcriptional Regulation of the Peptidylarginine Deiminase Type I Gene (PADI1) in Human Keratinocytes
    • Dong S., Ying S., Kojima T., Shiraiwa M., Kawada A., Mechin M.C., et al. Crucial Roles of MZF1 and Sp1 in the Transcriptional Regulation of the Peptidylarginine Deiminase Type I Gene (PADI1) in Human Keratinocytes. J Invest Dermatol 13 (2008) 549-557
    • (2008) J Invest Dermatol , vol.13 , pp. 549-557
    • Dong, S.1    Ying, S.2    Kojima, T.3    Shiraiwa, M.4    Kawada, A.5    Mechin, M.C.6
  • 25
    • 33746881392 scopus 로고    scopus 로고
    • NF-Y and Sp1/Sp3 are involved in the transcriptional regulation of the peptidylarginine deiminase type III gene (PADI3) in human keratinocytes
    • Dong S., Kanno T., Yamaki A., Kojima T., Shiraiwa M., Kawada A., et al. NF-Y and Sp1/Sp3 are involved in the transcriptional regulation of the peptidylarginine deiminase type III gene (PADI3) in human keratinocytes. Biochem J 397 (2006) 449-459
    • (2006) Biochem J , vol.397 , pp. 449-459
    • Dong, S.1    Kanno, T.2    Yamaki, A.3    Kojima, T.4    Shiraiwa, M.5    Kawada, A.6
  • 26
    • 18244363581 scopus 로고    scopus 로고
    • Regulation of the expression of peptidylarginine deiminase type II gene (PADI2) in human keratinocytes involves Sp1 and Sp3 transcription factors
    • Dong S., Kojima T., Shiraiwa M., Méchin M.C., Chavanas S., Serre G., et al. Regulation of the expression of peptidylarginine deiminase type II gene (PADI2) in human keratinocytes involves Sp1 and Sp3 transcription factors. J Invest Dermatol 24 (2005) 1026-1033
    • (2005) J Invest Dermatol , vol.24 , pp. 1026-1033
    • Dong, S.1    Kojima, T.2    Shiraiwa, M.3    Méchin, M.C.4    Chavanas, S.5    Serre, G.6
  • 27
    • 34447334574 scopus 로고    scopus 로고
    • Peptidyl argininedeiminase 2 CpG island in multiple sclerosis white matter is hypomethylated
    • Mastronardi F.G., Noor A., Wood D.D., Paton T., and Moscarello M.A. Peptidyl argininedeiminase 2 CpG island in multiple sclerosis white matter is hypomethylated. J Neurosci Res. 85 (2007) 2006-2016
    • (2007) J Neurosci Res. , vol.85 , pp. 2006-2016
    • Mastronardi, F.G.1    Noor, A.2    Wood, D.D.3    Paton, T.4    Moscarello, M.A.5
  • 28
    • 0032479079 scopus 로고    scopus 로고
    • Going the distance: a current view of enhancer action
    • Blackwood E.M., and Kadonaga J.T. Going the distance: a current view of enhancer action. Science 281 (1998) 60-63
    • (1998) Science , vol.281 , pp. 60-63
    • Blackwood, E.M.1    Kadonaga, J.T.2
  • 29
    • 0033527656 scopus 로고    scopus 로고
    • Sp1 and NF-Y synergistically mediate the effect of vitamin D3 in the p27Kip1 gene promoter that lacks vitamin D response elements
    • Inoue T., Kamiyama J., and Sakai T. Sp1 and NF-Y synergistically mediate the effect of vitamin D3 in the p27Kip1 gene promoter that lacks vitamin D response elements. J Biol Chem 274 (1999) 32309-32317
    • (1999) J Biol Chem , vol.274 , pp. 32309-32317
    • Inoue, T.1    Kamiyama, J.2    Sakai, T.3
  • 30
    • 0034723353 scopus 로고    scopus 로고
    • Transcriptional activation of the MDR1 gene by UV irradiation: role of NF-Y and Sp1
    • Hu Z., Jin S., and Scotto K.W. Transcriptional activation of the MDR1 gene by UV irradiation: role of NF-Y and Sp1. J Biol Chem 275 (2000) 2979-2985
    • (2000) J Biol Chem , vol.275 , pp. 2979-2985
    • Hu, Z.1    Jin, S.2    Scotto, K.W.3
  • 31
    • 0034636014 scopus 로고    scopus 로고
    • Sterol regulation of human fatty acid synthase promoter I requires nuclear factor-Y- and Sp-1-binding sites
    • Xiong S., Chirala S.S., and Wakil S.J. Sterol regulation of human fatty acid synthase promoter I requires nuclear factor-Y- and Sp-1-binding sites. Proc Natl Acad Sci USA 97 (2000) 3948-3953
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3948-3953
    • Xiong, S.1    Chirala, S.S.2    Wakil, S.J.3
  • 32
    • 0035947564 scopus 로고    scopus 로고
    • Cholesterol biosynthesis from lanosterol: a concerted role for Sp1 and NF-Y-binding sites for sterol-mediated regulation of rat 7-dehydrocholesterol reductase gene expression
    • Kim J.H., Lee J.N., and Paik Y.K. Cholesterol biosynthesis from lanosterol: a concerted role for Sp1 and NF-Y-binding sites for sterol-mediated regulation of rat 7-dehydrocholesterol reductase gene expression. J Biol Chem 276 (2001) 18153-18160
    • (2001) J Biol Chem , vol.276 , pp. 18153-18160
    • Kim, J.H.1    Lee, J.N.2    Paik, Y.K.3
  • 33
    • 0141456100 scopus 로고    scopus 로고
    • Modulation of DNA topoisomerase II α promoter activity by members of the Sp (specificity protein) and NF-Y (nuclear factor Y) families of transcription factors
    • Magan N., Szremska A.P., Isaacs R.J., and Stowell K.M. Modulation of DNA topoisomerase II α promoter activity by members of the Sp (specificity protein) and NF-Y (nuclear factor Y) families of transcription factors. Biochem J 374 (2003) 723-729
    • (2003) Biochem J , vol.374 , pp. 723-729
    • Magan, N.1    Szremska, A.P.2    Isaacs, R.J.3    Stowell, K.M.4
  • 34
    • 0344872679 scopus 로고    scopus 로고
    • Characterization of the role of Sp1 and NF-Y in differential regulation of PTTG/securin expression in tumor cells
    • Clem A.L., Hamid T., and Kakar S.S. Characterization of the role of Sp1 and NF-Y in differential regulation of PTTG/securin expression in tumor cells. Gene 322 (2003) 113-121
    • (2003) Gene , vol.322 , pp. 113-121
    • Clem, A.L.1    Hamid, T.2    Kakar, S.S.3
  • 35
    • 0032966918 scopus 로고    scopus 로고
    • Interaction between the two ubiquitously expressed transcription factors NF-Y and Sp1
    • Roder K., Wolf S.S., Larkin K.J., and Schweizer M. Interaction between the two ubiquitously expressed transcription factors NF-Y and Sp1. Gene 234 (1999) 61-69
    • (1999) Gene , vol.234 , pp. 61-69
    • Roder, K.1    Wolf, S.S.2    Larkin, K.J.3    Schweizer, M.4
  • 36
    • 0034674552 scopus 로고    scopus 로고
    • Sp family members and nuclear factor-Y cooperatively stimulate transcription from the rat pyruvate kinase M gene distal promoter region via their direct interactions
    • Yamada K., Tanaka T., Miyamoto K., and Noguchi T. Sp family members and nuclear factor-Y cooperatively stimulate transcription from the rat pyruvate kinase M gene distal promoter region via their direct interactions. J Biol Chem 275 (2000) 18129-18137
    • (2000) J Biol Chem , vol.275 , pp. 18129-18137
    • Yamada, K.1    Tanaka, T.2    Miyamoto, K.3    Noguchi, T.4
  • 37
    • 0030013203 scopus 로고    scopus 로고
    • Biochemistry and structural biology of transcription factor IID (TFIID)
    • Burley S.K., and Roeder R.G. Biochemistry and structural biology of transcription factor IID (TFIID). Annu Rev Biochem 65 (1996) 769-799
    • (1996) Annu Rev Biochem , vol.65 , pp. 769-799
    • Burley, S.K.1    Roeder, R.G.2
  • 38
    • 0029804314 scopus 로고    scopus 로고
    • Subunit association and DNA binding activity of the heterotrimeric transcription factor NF-Y is regulated by cellular redox
    • Nakshatri H., Bhat-Nakshatri P., and Currie R.A. Subunit association and DNA binding activity of the heterotrimeric transcription factor NF-Y is regulated by cellular redox. J Biol Chem 271 (1996) 28784-28791
    • (1996) J Biol Chem , vol.271 , pp. 28784-28791
    • Nakshatri, H.1    Bhat-Nakshatri, P.2    Currie, R.A.3
  • 39
    • 0028967755 scopus 로고
    • Transduction of calcium stress through interaction of the human transcription factor CBF with the proximal CCAAT regulatory element of the grp78/BiP promoter
    • Roy B., and Lee A.S. Transduction of calcium stress through interaction of the human transcription factor CBF with the proximal CCAAT regulatory element of the grp78/BiP promoter. Mol Cell Biol 15 (1995) 2263-2274
    • (1995) Mol Cell Biol , vol.15 , pp. 2263-2274
    • Roy, B.1    Lee, A.S.2
  • 41
    • 34347241381 scopus 로고    scopus 로고
    • Estrogen-enhanced peptidylarginine deiminase type IV gene (PADI4) expression in MCF-7 cells is mediated by estrogen receptor-alpha-promoted transfactors activator protein-1, nuclear factor-Y, and Sp1
    • Dong S., Zhang Z., and Takahara H. Estrogen-enhanced peptidylarginine deiminase type IV gene (PADI4) expression in MCF-7 cells is mediated by estrogen receptor-alpha-promoted transfactors activator protein-1, nuclear factor-Y, and Sp1. Mol Endocrinol 21 (2007) 1617-1629
    • (2007) Mol Endocrinol , vol.21 , pp. 1617-1629
    • Dong, S.1    Zhang, Z.2    Takahara, H.3
  • 42
    • 0032866999 scopus 로고    scopus 로고
    • The Sp-family of transcription factors
    • Suske G. The Sp-family of transcription factors. Gene 238 (2007) 291-300
    • (2007) Gene , vol.238 , pp. 291-300
    • Suske, G.1
  • 43
    • 33845968465 scopus 로고    scopus 로고
    • The combination of ubiquitous transcription factors AP-1 and Sp1 directs keratinocyte-specific and differentiation-specific gene expression in vitro
    • Nakamura Y., Kawachi Y., Xu X., Sakurai H., Ishii Y., Takahashi T., et al. The combination of ubiquitous transcription factors AP-1 and Sp1 directs keratinocyte-specific and differentiation-specific gene expression in vitro. Exp Dermatol 16 (2007) 143-150
    • (2007) Exp Dermatol , vol.16 , pp. 143-150
    • Nakamura, Y.1    Kawachi, Y.2    Xu, X.3    Sakurai, H.4    Ishii, Y.5    Takahashi, T.6
  • 44
    • 27544439766 scopus 로고    scopus 로고
    • Sp transcription factor family and its role in cancer
    • Safe S., and Abdelrahim M. Sp transcription factor family and its role in cancer. Eur J Cancer 41 (2005) 2438-2448
    • (2005) Eur J Cancer , vol.41 , pp. 2438-2448
    • Safe, S.1    Abdelrahim, M.2
  • 45
    • 0033960283 scopus 로고    scopus 로고
    • Differential role for Sp1/Sp3 transcription factors in the regulation of the promoter activity of multiple cyclin-dependent kinase inhibitor genes
    • Pagliuca A., Gallo P., and Lania L. Differential role for Sp1/Sp3 transcription factors in the regulation of the promoter activity of multiple cyclin-dependent kinase inhibitor genes. J Cell Biochem 76 (2000) 360-367
    • (2000) J Cell Biochem , vol.76 , pp. 360-367
    • Pagliuca, A.1    Gallo, P.2    Lania, L.3
  • 46
    • 0035793564 scopus 로고    scopus 로고
    • Sp3 is a transcriptional repressor of transforming growth factor-beta receptors
    • Ammanamanchi S., and Brattain M.G. Sp3 is a transcriptional repressor of transforming growth factor-beta receptors. J Biol Chem 276 (2001) 3348-3352
    • (2001) J Biol Chem , vol.276 , pp. 3348-3352
    • Ammanamanchi, S.1    Brattain, M.G.2
  • 47
    • 0042316806 scopus 로고    scopus 로고
    • Acetylated Sp3 is a transcriptional activator
    • Ammanamanchi S., Freeman J.W., and Brattain M.G. Acetylated Sp3 is a transcriptional activator. J Biol Chem 278 (2003) 35775-35780
    • (2003) J Biol Chem , vol.278 , pp. 35775-35780
    • Ammanamanchi, S.1    Freeman, J.W.2    Brattain, M.G.3
  • 48
    • 0018865014 scopus 로고
    • Calcium regulation of growth and differentiation of mouse epidermal cells in culture
    • Hennings H., Michael D., Cheng C., Steinert P., Holbrook K., and Yuspa S.H. Calcium regulation of growth and differentiation of mouse epidermal cells in culture. Cell 19 (1980) 245-254
    • (1980) Cell , vol.19 , pp. 245-254
    • Hennings, H.1    Michael, D.2    Cheng, C.3    Steinert, P.4    Holbrook, K.5    Yuspa, S.H.6
  • 49
    • 0028801328 scopus 로고
    • Overexpression of the zinc finger protein MZF1 inhibits hematopoietic development from embryonic stem cells: correlation with negative regulation of CD34 and c-myb promoter activity
    • Perrotti D., Melotti P., Skorski T., Casella I., Peschle C., and Calabretta B. Overexpression of the zinc finger protein MZF1 inhibits hematopoietic development from embryonic stem cells: correlation with negative regulation of CD34 and c-myb promoter activity. Mol Cell Biol 15 (1995) 6075-6087
    • (1995) Mol Cell Biol , vol.15 , pp. 6075-6087
    • Perrotti, D.1    Melotti, P.2    Skorski, T.3    Casella, I.4    Peschle, C.5    Calabretta, B.6
  • 50
    • 0026316545 scopus 로고
    • A retinoic acid-responsive human zinc finger gene, MZF-1, preferentially expressed in myeloid cells
    • Hromas R., Collins S.J., Hickstein D., Raskind W., Deaven L.L., O'Hara P., et al. A retinoic acid-responsive human zinc finger gene, MZF-1, preferentially expressed in myeloid cells. J Biol Chem 266 (1991) 14183-14187
    • (1991) J Biol Chem , vol.266 , pp. 14183-14187
    • Hromas, R.1    Collins, S.J.2    Hickstein, D.3    Raskind, W.4    Deaven, L.L.5    O'Hara, P.6


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