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Volumn 11, Issue 2, 2006, Pages 183-196

Overexpression of peptidylarginine deiminase IV features in apoptosis of haematopoietic cells

Author keywords

Apoptosis; Bax; Bcl 2; p21; p53; PADI4; PADIs

Indexed keywords

CASPASE 3; CASPASE 9; CYCLIN D; CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE 1; CYCLIN DEPENDENT KINASE 2; CYTOCHROME C; DNA FRAGMENT; MITOCHONDRIAL ENZYME; PROTEIN ARGININE DEIMINASE; PROTEIN ARGININE DEIMINASE 4; PROTEIN BAX; PROTEIN BCL 2; PROTEIN KINASE; PROTEIN P21; PROTEIN P53; UNCLASSIFIED DRUG;

EID: 33344477322     PISSN: 13608185     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10495-006-3715-4     Document Type: Article
Times cited : (70)

References (55)
  • 1
    • 0037442843 scopus 로고    scopus 로고
    • cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I
    • Guerrin M, Ishigami A, Mechin MC, et al. cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I. Biochem J 2003; 370: 167-174
    • (2003) Biochem J , vol.370 , pp. 167-174
    • Guerrin, M.1    Ishigami, A.2    Mechin, M.C.3
  • 2
    • 0036406870 scopus 로고    scopus 로고
    • Human peptidylarginme deiminase type II: Molecular cloning, gene organization, and expression in human skin
    • Ishigami A, Ohsawa T, Asaga H, Akiyama K, Kuramoto M, Maruyama N. Human peptidylarginme deiminase type II: Molecular cloning, gene organization, and expression in human skin. Arch Biochem Biophys 2002; 407: 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
  • 3
    • 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, 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 2000; 115: 813-823.
    • (2000) J Invest Dermatol , vol.115 , pp. 813-823
    • Kanno, T.1    Kawada, A.2    Yamanouchi, J.3
  • 4
    • 0033600723 scopus 로고    scopus 로고
    • Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha, 25-dihydroxyvitamin D(3)
    • Nakashima K, Hagiwara T, Ishigami A, et al. Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha, 25-dihydroxyvitamin D(3). J Biol Chem 1999; 274: 27786-27792.
    • (1999) J Biol Chem , vol.274 , pp. 27786-27792
    • Nakashima, K.1    Hagiwara, T.2    Ishigami, A.3
  • 5
    • 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, Mechin MC, Takahara H, 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 2004; 330: 19-27.
    • (2004) Gene , vol.330 , pp. 19-27
    • Chavanas, S.1    Mechin, M.C.2    Takahara, H.3
  • 6
    • 7644238939 scopus 로고    scopus 로고
    • Autoantibodies to citrullinated proteins in rheumatoid arthritis: Clinical performance and biochemical aspects of an RA-specific marker
    • Nijenhuis S, Zendman AJ, Vossenaar ER, Pruijn GJ, van Venrooij WJ. Autoantibodies to citrullinated proteins in rheumatoid arthritis: clinical performance and biochemical aspects of an RA-specific marker. Clin Chim Acta 2004; 350:17-34.
    • (2004) Clin Chim Acta , vol.350 , pp. 17-34
    • Nijenhuis, S.1    Zendman, A.J.2    Vossenaar, E.R.3    Pruijn, G.J.4    Van Venrooij, W.J.5
  • 7
    • 12344327644 scopus 로고    scopus 로고
    • Localization of peptidylarginine deiminase 4 (PADI4) and citrullinated protein in synovial tissue of rheumatoid arthritis
    • Chang X, Yamada R, Suzuki A, et al. Localization of peptidylarginine deiminase 4 (PADI4) and citrullinated protein in synovial tissue of rheumatoid arthritis. Rheumatology (Oxford) 2005; 44: 40-50.
    • (2005) Rheumatology (Oxford) , vol.44 , pp. 40-50
    • Chang, X.1    Yamada, R.2    Suzuki, A.3
  • 8
    • 0032789345 scopus 로고    scopus 로고
    • Studies on specificity of peptidylarginine deiminase reactions using an immunochemical probe that recognizes an enzymatically deiminated partial sequence of mouse keratin K1
    • Senshu T, Akiyama K, Ishigami A, Nomura K. Studies on specificity of peptidylarginine deiminase reactions using an immunochemical probe that recognizes an enzymatically deiminated partial sequence of mouse keratin K1. J Dermatol Sci 1999; 21: 113-126.
    • (1999) J Dermatol Sci , vol.21 , pp. 113-126
    • Senshu, T.1    Akiyama, K.2    Ishigami, A.3    Nomura, K.4
  • 9
    • 0036181752 scopus 로고    scopus 로고
    • Sequential reorganization of cornified cell keratin filaments involving filaggrin-mediated compaction and keratin 1 deimination
    • Ishida-Yamamoto A, Senshu T, Eady RA, et al. Sequential reorganization of cornified cell keratin filaments involving filaggrin-mediated compaction and keratin 1 deimination. J Invest Dermatol 2002; 118: 282-287.
    • (2002) J Invest Dermatol , vol.118 , pp. 282-287
    • Ishida-Yamamoto, A.1    Senshu, T.2    Eady, R.A.3
  • 10
    • 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 LN, Mei G, Melino G, Lee SC, Steinert PM. Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin. J Biol Chem 1996; 271: 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
  • 11
    • 1842619397 scopus 로고    scopus 로고
    • Rheumatoid arthritis specific anti-Sa antibodies target citrullinated vimentin
    • Vossenaar ER, Despres N, Lapointe E, et al. Rheumatoid arthritis specific anti-Sa antibodies target citrullinated vimentin. Arthritis Res Ther 2004; 6: R142-R150.
    • (2004) Arthritis Res Ther , vol.6
    • Vossenaar, E.R.1    Despres, N.2    Lapointe, E.3
  • 13
    • 5044228483 scopus 로고    scopus 로고
    • Human PAD4 regulates histone arginine methylation levels via demethylimination
    • Wang Y, Wysocka J, Sayegh J, et al. Human PAD4 regulates histone arginine methylation levels via demethylimination. Science 2004; 306: 279-283.
    • (2004) Science , vol.306 , pp. 279-283
    • Wang, Y.1    Wysocka, J.2    Sayegh, J.3
  • 14
    • 4444372638 scopus 로고    scopus 로고
    • Histone deimination antagonizes arginine methylation
    • Cuthbert GL, Daujat S, Snowden AW, et al. Histone deimination antagonizes arginine methylation. Cell 2004; 118:545-553.
    • (2004) Cell , vol.118 , pp. 545-553
    • Cuthbert, G.L.1    Daujat, S.2    Snowden, A.W.3
  • 15
    • 0141564989 scopus 로고    scopus 로고
    • Citrullination of synovial proteins in murine models of rheumatoid arthritis
    • Vossenaar ER, Nijenhuis S, Helsen MM, et al. Citrullination of synovial proteins in murine models of rheumatoid arthritis. Arthritis Rheum 2003; 48: 2489-2500.
    • (2003) Arthritis Rheum , vol.48 , pp. 2489-2500
    • Vossenaar, E.R.1    Nijenhuis, S.2    Helsen, M.M.3
  • 16
    • 20144388805 scopus 로고    scopus 로고
    • A family based study shows no association between rheumatoid arthritis and the PADI4 gene in a white French population
    • Caponi L, Petit-Teixeira E, Sebbag M, et al. A family based study shows no association between rheumatoid arthritis and the PADI4 gene in a white French population. Ann Rheum Dis 2005; 64: 587-593.
    • (2005) Ann Rheum Dis , vol.64 , pp. 587-593
    • Caponi, L.1    Petit-Teixeira, E.2    Sebbag, M.3
  • 17
    • 0035869593 scopus 로고    scopus 로고
    • The major synovial targets of the rheumatoid arthritis-specific antifilaggrin autoantibodies are deiminated forms of the alpha- and beta-chains of fibrin
    • Masson-Bessiere C, Sebbag M, Girbal-Neuhauser E, et al. The major synovial targets of the rheumatoid arthritis-specific antifilaggrin autoantibodies are deiminated forms of the alpha- and beta-chains of fibrin. J Immunol 2001; 166: 4177-4184.
    • (2001) J Immunol , vol.166 , pp. 4177-4184
    • Masson-Bessiere, C.1    Sebbag, M.2    Girbal-Neuhauser, E.3
  • 19
    • 0029927069 scopus 로고    scopus 로고
    • Acute multiple sclerosis (Marburg type) is associated with developmentally immature myelin basic protein
    • Wood DD, Bilbao JM, O'Connors P, Moscarello MA. Acute multiple sclerosis (Marburg type) is associated with developmentally immature myelin basic protein. Ann Neurol 1996; 40: 18-24.
    • (1996) Ann Neurol , vol.40 , pp. 18-24
    • Wood, D.D.1    Bilbao, J.M.2    O'Connors, P.3    Moscarello, M.A.4
  • 20
    • 0037376592 scopus 로고    scopus 로고
    • ePAD, an oocyte and early embryo-abundant peptidylarginine deiminase-like protein that localizes to egg cytoplasmic sheets
    • Wright PW, Bolling LC, Calvert ME, et al. ePAD, an oocyte and early embryo-abundant peptidylarginine deiminase-like protein that localizes to egg cytoplasmic sheets. Dev Biol 2003; 256: 73-88.
    • (2003) Dev Biol , vol.256 , pp. 73-88
    • Wright, P.W.1    Bolling, L.C.2    Calvert, M.E.3
  • 21
    • 0032562113 scopus 로고    scopus 로고
    • Selective deimination of vimentin in calcium ionophore-induced apoptosis of mouse peritoneal macrophages
    • Asaga H, Yamada M, Senshu T. Selective deimination of vimentin in calcium ionophore-induced apoptosis of mouse peritoneal macrophages. Biochem Biophys Res Commun 1998; 243: 641-646.
    • (1998) Biochem Biophys Res Commun , vol.243 , pp. 641-646
    • Asaga, H.1    Yamada, M.2    Senshu, T.3
  • 22
    • 15144354407 scopus 로고    scopus 로고
    • Deimination of 70-kD nuclear protein during epidermal apoptotic events in vitro
    • Mizoguchi M, Manabe M, Kawamura Y, et al. Deimination of 70-kD nuclear protein during epidermal apoptotic events in vitro. J Histochem Cytochem 1998; 46: 1303-1309.
    • (1998) J Histochem Cytochem , vol.46 , pp. 1303-1309
    • Mizoguchi, M.1    Manabe, M.2    Kawamura, Y.3
  • 23
    • 0024384763 scopus 로고
    • Peptidylargmine deiminase in rat pituitary: Sex difference, estrous cycle-related changes, and estrogen dependence
    • Senshu T, Akiyama K, Nagata S, Watanabe K, Hikichi K. Peptidylargmine deiminase in rat pituitary: Sex difference, estrous cycle-related changes, and estrogen dependence. Endocrinology 1989; 124: 2666-2670.
    • (1989) Endocrinology , vol.124 , pp. 2666-2670
    • Senshu, T.1    Akiyama, K.2    Nagata, S.3    Watanabe, K.4    Hikichi, K.5
  • 24
    • 0037048278 scopus 로고    scopus 로고
    • The role of nucleophosmin in centrosome duplication
    • Okuda M. The role of nucleophosmin in centrosome duplication. Oncogene 2002; 21: 6170-6174.
    • (2002) Oncogene , vol.21 , pp. 6170-6174
    • Okuda, M.1
  • 25
    • 0034637578 scopus 로고    scopus 로고
    • Mapping the functional domains of nucleolar protein B23
    • Hingorani K, Szebeni A, Olson MO. Mapping the functional domains of nucleolar protein B23. J Biol Chem 2000; 275: 24451-24457.
    • (2000) J Biol Chem , vol.275 , pp. 24451-24457
    • Hingorani, K.1    Szebeni, A.2    Olson, M.O.3
  • 26
    • 18544364163 scopus 로고    scopus 로고
    • Phosphorylation-dependent migration of retinoblastoma protein into the nucleolus triggered by binding to nucleophosmin/B23
    • Takemura M, Ohoka F, Perpelescu M, et al. Phosphorylation-dependent migration of retinoblastoma protein into the nucleolus triggered by binding to nucleophosmin/B23. Exp Cell Res 2002; 276: 233-241.
    • (2002) Exp Cell Res , vol.276 , pp. 233-241
    • Takemura, M.1    Ohoka, F.2    Perpelescu, M.3
  • 27
    • 0036295234 scopus 로고    scopus 로고
    • Deimination of arginine residues in nucleophosmin/B23 and histones in HL-60 granulocytes
    • Hagiwara T, Nakashima K, Hirano H, Senshu T, Yamada M. Deimination of arginine residues in nucleophosmin/B23 and histones in HL-60 granulocytes. Biochem Biophys Res Commun 2002; 290: 979-983.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 979-983
    • Hagiwara, T.1    Nakashima, K.2    Hirano, H.3    Senshu, T.4    Yamada, M.5
  • 28
    • 17144363594 scopus 로고    scopus 로고
    • Deimination of histone H2A and H4 at argmine 3 in HL-60 granulocytes
    • Hagiwara T, Hidaka Y, Yamada M. Deimination of histone H2A and H4 at argmine 3 in HL-60 granulocytes. Biochemistry 2005; 44: 5827-5834.
    • (2005) Biochemistry , vol.44 , pp. 5827-5834
    • Hagiwara, T.1    Hidaka, Y.2    Yamada, M.3
  • 29
    • 21244479016 scopus 로고    scopus 로고
    • Ornithine decarboxylase prevents tumor necrosis factor alpha-induced apoptosis by decreasing intracellular reactive oxygen species
    • Liu GY, Hung YC, Hsu PC, et al. Ornithine decarboxylase prevents tumor necrosis factor alpha-induced apoptosis by decreasing intracellular reactive oxygen species. Apoptosis 2005; 10: 569-581.
    • (2005) Apoptosis , vol.10 , pp. 569-581
    • Liu, G.Y.1    Hung, Y.C.2    Hsu, P.C.3
  • 30
    • 0019170507 scopus 로고
    • Optimization of conditions for the colorimetric determination of citrulline, using diacetyl monoxime
    • Boyde TR, Rahmatullah M. Optimization of conditions for the colorimetric determination of citrulline, using diacetyl monoxime. Anal. Biochem. 1980; 107: 424-431.
    • (1980) Anal. Biochem. , vol.107 , pp. 424-431
    • Boyde, T.R.1    Rahmatullah, M.2
  • 31
    • 23944520426 scopus 로고    scopus 로고
    • Ornithine decarboxylase prevents methotrexate-induced apoptosis by reducing intracellular reactive oxygen species production
    • Huang HH, Hsu PC, Hung YC et al. Ornithine decarboxylase prevents methotrexate-induced apoptosis by reducing intracellular reactive oxygen species production. Apoptosis 2005; 10: 895-907.
    • (2005) Apoptosis , vol.10 , pp. 895-907
    • Huang, H.H.1    Hsu, P.C.2    Hung, Y.C.3
  • 32
    • 12944303650 scopus 로고    scopus 로고
    • Growth factor regulation of autophagy and cell survival in the absence of apoptosis
    • Lum JJ, Bauer DE, Kong M, et al. Growth factor regulation of autophagy and cell survival in the absence of apoptosis. Cell 2005; 120: 237-248.
    • (2005) Cell , vol.120 , pp. 237-248
    • Lum, J.J.1    Bauer, D.E.2    Kong, M.3
  • 33
    • 12944308330 scopus 로고    scopus 로고
    • Eating oneself and uninvited guests: Autophagy-related pathways in cellular defense
    • Levine B. Eating oneself and uninvited guests: Autophagy-related pathways in cellular defense. Cell 2005; 120: 159-162.
    • (2005) Cell , vol.120 , pp. 159-162
    • Levine, B.1
  • 34
    • 1842453329 scopus 로고    scopus 로고
    • Expression and activity of citrullinating peptidylarginine deiminase enzymes in monocytes and macrophages
    • Vossenaar ER, Radstake TR, van der Heijden A, et al. Expression and activity of citrullinating peptidylarginine deiminase enzymes in monocytes and macrophages. Ann Rheum Dis 2004; 63: 373-381.
    • (2004) Ann Rheum Dis , vol.63 , pp. 373-381
    • Vossenaar, E.R.1    Radstake, T.R.2    Van Der Heijden, A.3
  • 35
    • 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 1989; 264: 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
  • 37
    • 0037147140 scopus 로고    scopus 로고
    • Nuclear localization of peptidylarginine deiminase V and histone deimination in granulocytes
    • Nakashima K, Hagiwara T, Yamada M. Nuclear localization of peptidylarginine deiminase V and histone deimination in granulocytes. J Biol Chem 2002; 277: 49562-49568.
    • (2002) J Biol Chem , vol.277 , pp. 49562-49568
    • Nakashima, K.1    Hagiwara, T.2    Yamada, M.3
  • 38
    • 0026496885 scopus 로고
    • A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia
    • Kastan MB, Zhan Q, el-Deiry WS, et al. A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia. Cell 1992; 71: 587-597.
    • (1992) Cell , vol.71 , pp. 587-597
    • Kastan, M.B.1    Zhan, Q.2    El-Deiry, W.S.3
  • 39
    • 0027319521 scopus 로고
    • p53 is required for radiation-induced apoptosis in mouse thymocytes
    • Lowe SW, Schmitt EM, Smith SW, Osborne BA, Jacks T. p53 is required for radiation-induced apoptosis in mouse thymocytes. Nature 1993; 362: 847-849.
    • (1993) Nature , vol.362 , pp. 847-849
    • Lowe, S.W.1    Schmitt, E.M.2    Smith, S.W.3    Osborne, B.A.4    Jacks, T.5
  • 40
    • 0027602954 scopus 로고
    • Overexpression of wild-type p53 alters growth and differentiation of normal human keratinocytes but not human papillomavirus-expressing cell lines
    • Woodworth CD, Wang H, Simpson S, Alvarez-Salas LM, Notario V. Overexpression of wild-type p53 alters growth and differentiation of normal human keratinocytes but not human papillomavirus-expressing cell lines. Cell Growth Differ 1993; 4: 367-376.
    • (1993) Cell Growth Differ , vol.4 , pp. 367-376
    • Woodworth, C.D.1    Wang, H.2    Simpson, S.3    Alvarez-Salas, L.M.4    Notario, V.5
  • 41
    • 0029057464 scopus 로고
    • p53-mediated transcriptional activity increases in differentiating epidermal keratinocytes in association with decreased p53 protein
    • Weinberg WC, Azzoli CG, Chapman K, Levine AJ, Yuspa SH. p53-mediated transcriptional activity increases in differentiating epidermal keratinocytes in association with decreased p53 protein. Oncogene 1995; 10: 2271-2279.
    • (1995) Oncogene , vol.10 , pp. 2271-2279
    • Weinberg, W.C.1    Azzoli, C.G.2    Chapman, K.3    Levine, A.J.4    Yuspa, S.H.5
  • 42
    • 0027528673 scopus 로고
    • High levels of p53 protein in UV-irradiated normal human skin
    • Hall PA, McKee PH, Menage HD, Dover R, Lane DP. High levels of p53 protein in UV-irradiated normal human skin. Oncogene 1993; 8: 203-207.
    • (1993) Oncogene , vol.8 , pp. 203-207
    • Hall, P.A.1    McKee, P.H.2    Menage, H.D.3    Dover, R.4    Lane, D.P.5
  • 43
    • 0030031401 scopus 로고    scopus 로고
    • Early p53 alterations in mouse skin carcinogenesis by UVB radiation: Immunohistochemical detection of mutant p53 protein in clusters of preneoplastic epidermal cells
    • Berg RJ, van Kranen HJ, Rebel HG, et al. Early p53 alterations in mouse skin carcinogenesis by UVB radiation: immunohistochemical detection of mutant p53 protein in clusters of preneoplastic epidermal cells. Proc Natl Acad Sci USA 1996; 93: 274-278.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 274-278
    • Berg, R.J.1    Van Kranen, H.J.2    Rebel, H.G.3
  • 44
    • 0029922051 scopus 로고    scopus 로고
    • Decreased DNA repair but normal apoptosis in ultraviolet-irradiated skin of p53-transgenic mice
    • Li G, Mitchell DL, Ho VC, Reed JC, Tron VA. Decreased DNA repair but normal apoptosis in ultraviolet-irradiated skin of p53-transgenic mice. Am J Pathol 1996; 148: 1113-1123.
    • (1996) Am J Pathol , vol.148 , pp. 1113-1123
    • Li, G.1    Mitchell, D.L.2    Ho, V.C.3    Reed, J.C.4    Tron, V.A.5
  • 45
    • 0034031250 scopus 로고    scopus 로고
    • Signaling to p53: Breaking the post-translational modification code
    • Appella E, Anderson CW. Signaling to p53: Breaking the post-translational modification code. Pathol Biol (Paris) 2000; 48: 227-245.
    • (2000) Pathol Biol (Paris) , vol.48 , pp. 227-245
    • Appella, E.1    Anderson, C.W.2
  • 46
    • 23044456914 scopus 로고    scopus 로고
    • p21Cip1 and p27Kip1 induce distinct cell cycle effects and differentiation programs in myeloid leukemia cells
    • Munoz-Alonso MJ, Acosta JC, Richard C, Delgado MD, Sedivy J, Leon J. p21Cip1 and p27Kip1 induce distinct cell cycle effects and differentiation programs in myeloid leukemia cells. J Biol Chem 2005; 280: 18120-18129.
    • (2005) J Biol Chem , vol.280 , pp. 18120-18129
    • Munoz-Alonso, M.J.1    Acosta, J.C.2    Richard, C.3    Delgado, M.D.4    Sedivy, J.5    Leon, J.6
  • 47
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: Positive and negative regulators of G1-phase progression
    • Sherr CJ, Roberts JM. CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev 1999; 13: 1501-1512.
    • (1999) Genes Dev , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 48
    • 0032716227 scopus 로고    scopus 로고
    • Effect of elevated levels of ornithine decarboxylase on cell cycle progression in skin
    • Gilmour SK, Birchler M, Smith MK, Rayca K, Mostochuk J. Effect of elevated levels of ornithine decarboxylase on cell cycle progression in skin. Cell Growth Differ 1999; 10: 739-748.
    • (1999) Cell Growth Differ , vol.10 , pp. 739-748
    • Gilmour, S.K.1    Birchler, M.2    Smith, M.K.3    Rayca, K.4    Mostochuk, J.5
  • 49
    • 2342459790 scopus 로고    scopus 로고
    • DNA damage-induced apoptosis
    • Norbury CJ, Zhivotovsky B. DNA damage-induced apoptosis. Oncogene 2004; 23: 2797-2808.
    • (2004) Oncogene , vol.23 , pp. 2797-2808
    • Norbury, C.J.1    Zhivotovsky, B.2
  • 50
    • 0031918223 scopus 로고    scopus 로고
    • BCL-2 family: Regulators of cell death
    • Chao DT, Korsmeyer SJ. BCL-2 family: Regulators of cell death. Annu. Rev Immunol 1998; 16: 395-419.
    • (1998) Annu. Rev Immunol , vol.16 , pp. 395-419
    • Chao, D.T.1    Korsmeyer, S.J.2
  • 51
    • 13944257800 scopus 로고    scopus 로고
    • Transcription, apoptosis and p53: Catch-22
    • Schuler M, Green DR. Transcription, apoptosis and p53: catch-22. Trends Genet 2005; 21: 182-187.
    • (2005) Trends Genet , vol.21 , pp. 182-187
    • Schuler, M.1    Green, D.R.2
  • 52
    • 0842278331 scopus 로고    scopus 로고
    • Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis
    • Chipuk JE, Kuwana T, Bouchier-Hayes L, et al. Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis. Science 2004; 303: 1010-1014.
    • (2004) Science , vol.303 , pp. 1010-1014
    • Chipuk, J.E.1    Kuwana, T.2    Bouchier-Hayes, L.3
  • 53
    • 0035020420 scopus 로고    scopus 로고
    • Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis
    • Byun Y, Chen F, Chang R, Trivedi M, Green KJ, Cryns VL. Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis. Cell Death Differ 2001; 8: 443-450.
    • (2001) Cell Death Differ , vol.8 , pp. 443-450
    • Byun, Y.1    Chen, F.2    Chang, R.3    Trivedi, M.4    Green, K.J.5    Cryns, V.L.6
  • 54
    • 0034697022 scopus 로고    scopus 로고
    • Ubiquitination of free cyclin D1 is independent of phosphorylation on threonine 286
    • Germain D, Russell A, Thompson A, Hendley J. Ubiquitination of free cyclin D1 is independent of phosphorylation on threonine 286. J Biol Chem 2000; 275: 12074-12079.
    • (2000) J Biol Chem , vol.275 , pp. 12074-12079
    • Germain, D.1    Russell, A.2    Thompson, A.3    Hendley, J.4
  • 55
    • 4744339875 scopus 로고    scopus 로고
    • Antizyme targets cyclin D1 for degradation. A novel mechanism for cell growth repression
    • Newman RM, Mobascher A, Mangold U, et al. Antizyme targets cyclin D1 for degradation. A novel mechanism for cell growth repression. J Biol Chem 2004; 279: 41504-41511.
    • (2004) J Biol Chem , vol.279 , pp. 41504-41511
    • Newman, R.M.1    Mobascher, A.2    Mangold, U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.