메뉴 건너뛰기




Volumn 12, Issue 3, 2007, Pages 475-487

The functional haplotype of peptidylarginine deiminase IV (S55G, A82V and A112G) associated with susceptibility to rheumatoid arthritis dominates apoptosis of acute T leukemia Jurkat cells

Author keywords

Apoptosis; Bax; Bcl xL; Cytochrome c; PADIs; SNP PADI4

Indexed keywords

CYTOCHROME C; IONOMYCIN; PEPTIDYLARGININE DEIMINASE IV; PROTEIN ARGININE DEIMINASE; PROTEIN BAX; PROTEIN BCL XL; TETRACYCLINE; UNCLASSIFIED DRUG;

EID: 33847297986     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-006-0005-0     Document Type: Article
Times cited : (24)

References (60)
  • 1
    • 0242720407 scopus 로고    scopus 로고
    • PAD, a growing family of citrullinating enzymes: Genes, features and involvement in disease
    • Vossenaar ER, Zendman AJ, van Venrooij WJ, Pruijn GJ (2003) PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. Bioessays 25:1106-1118
    • (2003) Bioessays , vol.25 , pp. 1106-1118
    • Vossenaar, E.R.1    Zendman, A.J.2    van Venrooij, W.J.3    Pruijn, G.J.4
  • 2
    • 0042667153 scopus 로고    scopus 로고
    • Functional haplotypes of PADI4, encoding citrullinating enzyme peptidylarginine deiminase 4, are associated with rheumatoid arthritis
    • Suzuki A, Yamada R, Chang X et al. (2003) Functional haplotypes of PADI4, encoding citrullinating enzyme peptidylarginine deiminase 4, are associated with rheumatoid arthritis. Nat Genet 34:395-402
    • (2003) Nat Genet , vol.34 , pp. 395-402
    • Suzuki, A.1    Yamada, R.2    Chang, X.3
  • 3
    • 33746321292 scopus 로고    scopus 로고
    • PADI4 gene in multiple sclerosis: A family-based association study
    • Tommasi C, Petit-Teixeira E, Cournu-Rebeix I et al. (2006) PADI4 gene in multiple sclerosis: a family-based association study. J Neuroimmunol 177:142-145
    • (2006) J Neuroimmunol , vol.177 , pp. 142-145
    • Tommasi, C.1    Petit-Teixeira, E.2    Cournu-Rebeix, I.3
  • 5
    • 27544492153 scopus 로고    scopus 로고
    • Pathophysiological significances of citrullinated proteins in geriatric diseases
    • Maruyama N, Ishigami A (2005) Pathophysiological significances of citrullinated proteins in geriatric diseases. Nippon Ronen Igakkai Zasshi 42:519-522
    • (2005) Nippon Ronen Igakkai Zasshi , vol.42 , pp. 519-522
    • Maruyama, N.1    Ishigami, A.2
  • 6
    • 20244368810 scopus 로고    scopus 로고
    • Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease
    • Ishigami A, Ohsawa T, Hiratsuka M et al. (2005) Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease. J Neurosci Res 80:120-128
    • (2005) J Neurosci Res , vol.80 , pp. 120-128
    • Ishigami, A.1    Ohsawa, T.2    Hiratsuka, M.3
  • 7
    • 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. (2003) cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I. Biochem J 370:167-174
    • (2003) Biochem J , vol.370 , pp. 167-174
    • Guerrin, M.1    Ishigami, A.2    Mechin, M.C.3
  • 8
    • 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, Maruyama N (2002) Human peptidylarginine deiminase type II: molecular cloning, gene organization, and expression in human skin. Arch Biochem Biophys 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
  • 9
    • 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. (2000) 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 115:813-823
    • (2000) J Invest Dermatol , vol.115 , pp. 813-823
    • Kanno, T.1    Kawada, A.2    Yamanouchi, J.3
  • 10
    • 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. (1999) Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D(3). J Biol Chem 274:27786-27792
    • (1999) J Biol Chem , vol.274 , pp. 27786-27792
    • Nakashima, K.1    Hagiwara, T.2    Ishigami, A.3
  • 11
    • 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. (2004) Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6. Gene 330:19-27
    • (2004) Gene , vol.330 , pp. 19-27
    • Chavanas, S.1    Mechin, M.C.2    Takahara, H.3
  • 12
    • 33344477322 scopus 로고    scopus 로고
    • Overexpression of peptidylarginine deiminase IV features in apoptosis of haematopoietic cells
    • Liu GY, Liao YF, Chang WH et al. (2006) Overexpression of peptidylarginine deiminase IV features in apoptosis of haematopoietic cells. Apoptosis 11:183-196
    • (2006) Apoptosis , vol.11 , pp. 183-196
    • Liu, G.Y.1    Liao, Y.F.2    Chang, W.H.3
  • 13
    • 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, vanVenrooij WJ (2004) Autoantibodies to citrullinated proteins in rheumatoid arthritis: clinical performance and biochemical aspects of an RA-specific marker. Clin Chim Acta 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    vanVenrooij, W.J.5
  • 14
    • 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. (2005) Localization of peptidylarginine deiminase 4 (PADI4) and citrullinated protein in synovial tissue of rheumatoid arthritis. Rheumatology (Oxford) 44:40-50
    • (2005) Rheumatology (Oxford) , vol.44 , pp. 40-50
    • Chang, X.1    Yamada, R.2    Suzuki, A.3
  • 15
    • 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 (1999) 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 21:113-126
    • (1999) J Dermatol Sci , vol.21 , pp. 113-126
    • Senshu, T.1    Akiyama, K.2    Ishigami, A.3    Nomura, K.4
  • 16
    • 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. (2002) Sequential reorganization of cornified cell keratin filaments involving filaggrin-mediated compaction and keratin 1 deimination. J Invest Dermatol 118:282-287
    • (2002) J Invest Dermatol , vol.118 , pp. 282-287
    • Ishida-Yamamoto, A.1    Senshu, T.2    Eady, R.A.3
  • 17
    • 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 (1996) Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin. J Biol Chem 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
  • 18
    • 1842453329 scopus 로고    scopus 로고
    • Expression and activity of citrullinating peptidylarginine deiminase enzymes inmonocytes andmacrophages
    • Vossenaar ER, Radstake TR, Van Der Heijden A et al. (2004) Expression and activity of citrullinating peptidylarginine deiminase enzymes inmonocytes andmacrophages. Ann Rheum Dis 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
  • 20
    • 5044228483 scopus 로고    scopus 로고
    • Human PAD4 regulates histone arginine methylation levels via demethylimination
    • Wang Y, Wysocka J, Sayegh J et al. (2004) Human PAD4 regulates histone arginine methylation levels via demethylimination. Science 306:279-283
    • (2004) Science , vol.306 , pp. 279-283
    • Wang, Y.1    Wysocka, J.2    Sayegh, J.3
  • 21
    • 4444372638 scopus 로고    scopus 로고
    • Histone deimination antagonizes arginine methylation
    • Cuthbert GL, Daujat S, Snowden A et al. (2004) Histone deimination antagonizes arginine methylation. Cell 118:545-553
    • (2004) Cell , vol.118 , pp. 545-553
    • Cuthbert, G.L.1    Daujat, S.2    Snowden, A.3
  • 22
    • 0141564989 scopus 로고    scopus 로고
    • Citrullination of synovial proteins in murine models of rheumatoid arthritis
    • Vossenaar ER, Nijenhuis S, Helsen M M et al. (2003) Citrullination of synovial proteins in murine models of rheumatoid arthritis. Arthritis Rheum 48:2489-2500
    • (2003) Arthritis Rheum , vol.48 , pp. 2489-2500
    • Vossenaar, E.R.1    Nijenhuis, S.2    Helsen, M.M.3
  • 23
    • 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. (2001) The major synovial targets of the rheumatoid arthritis-specific antifilaggrin autoantibodies are deiminated forms of the alpha-and beta-chains of fibrin. J Immunol 166:4177-4184
    • (2001) J Immunol , vol.166 , pp. 4177-4184
    • Masson-Bessiere, C.1    Sebbag, M.2    Girbal-Neuhauser, E.3
  • 25
    • 33644667809 scopus 로고    scopus 로고
    • Identification of citrullinated alpha-enolase as a candidate autoantigen in rheumatoid arthritis
    • Kinloch A, Tatzer V, Wait R et al. (2005) Identification of citrullinated alpha-enolase as a candidate autoantigen in rheumatoid arthritis. Arthritis Res Ther 7:1421-1429
    • (2005) Arthritis Res Ther , vol.7 , pp. 1421-1429
    • Kinloch, A.1    Tatzer, V.2    Wait, R.3
  • 26
    • 14944379544 scopus 로고    scopus 로고
    • The inhibition of antithrombin by peptidylarginine deiminase 4 may contribute to pathogenesis of rheumatoid arthritis
    • Chang X, Yamada R, Sawada T, Suzuki A, Kochi Y, Yamamoto K (2005) The inhibition of antithrombin by peptidylarginine deiminase 4 may contribute to pathogenesis of rheumatoid arthritis. Rheumatology (Oxford) 44:293-298
    • (2005) Rheumatology (Oxford) , vol.44 , pp. 293-298
    • Chang, X.1    Yamada, R.2    Sawada, T.3    Suzuki, A.4    Kochi, Y.5    Yamamoto, K.6
  • 27
    • 30944445960 scopus 로고    scopus 로고
    • Identification of citrullinated eukaryotic translation initiation factor 4G1 as novel autoantigen in rheumatoid arthritis
    • Okazaki Y, Suzuki A, Sawada T et al. (2006) Identification of citrullinated eukaryotic translation initiation factor 4G1 as novel autoantigen in rheumatoid arthritis. Biochem Biophys Res Commun 341:94-100
    • (2006) Biochem Biophys Res Commun , vol.341 , pp. 94-100
    • Okazaki, Y.1    Suzuki, A.2    Sawada, T.3
  • 28
    • 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 (1996) Acute multiple sclerosis (Marburg type) is associated with developmentally immature myelin basic protein. Ann Neurol 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
  • 29
    • 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. (2003) ePAD, an oocyte and early embryo-abundant peptidylarginine deiminase-like protein that localizes to egg cytoplasmic sheets. Dev Biol 256:73-88
    • (2003) Dev Biol , vol.256 , pp. 73-88
    • Wright, P.W.1    Bolling, L.C.2    Calvert, M.E.3
  • 30
    • 0032562113 scopus 로고    scopus 로고
    • Selective deimination of vimentin in calcium ionophore-induced apoptosis of mouse peritoneal macrophages
    • Asaga H, Yamada M, Senshu T (1998) Selective deimination of vimentin in calcium ionophore-induced apoptosis of mouse peritoneal macrophages. Biochem Biophys Res Commun 243:641-646
    • (1998) Biochem Biophys Res Commun , vol.243 , pp. 641-646
    • Asaga, H.1    Yamada, M.2    Senshu, T.3
  • 31
    • 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. (1998) Deimination of 70-kD nuclear protein during epidermal apoptotic events in vitro. J Histochem Cytochem 46:1303-1309
    • (1998) J Histochem Cytochem , vol.46 , pp. 1303-1309
    • Mizoguchi, M.1    Manabe, M.2    Kawamura, Y.3
  • 32
    • 0024384763 scopus 로고
    • Peptidylarginine deiminase in rat pituitary: Sex difference, estrous cycle-related changes, and estrogen dependence
    • Senshu T, Akiyama K, Nagata S, Watanabe K, Hikichi K (1989) Peptidylarginine deiminase in rat pituitary: sex difference, estrous cycle-related changes, and estrogen dependence. Endocrinology 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
  • 33
    • 0037048278 scopus 로고    scopus 로고
    • The role of nucleophosmin in centrosome duplication
    • Okuda M (2002) The role of nucleophosmin in centrosome duplication. Oncogene 21:6170-6174
    • (2002) Oncogene , vol.21 , pp. 6170-6174
    • Okuda, M.1
  • 34
    • 0034637578 scopus 로고    scopus 로고
    • Mapping the functional domains of nucleolar protein B23
    • Hingorani K, Szebeni A, Olson MO (2000) Mapping the functional domains of nucleolar protein B23. J Biol Chem 275:24451-24457
    • (2000) J Biol Chem , vol.275 , pp. 24451-24457
    • Hingorani, K.1    Szebeni, A.2    Olson, M.O.3
  • 35
    • 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. (2002) Phosphorylation-dependent migration of retinoblastoma protein into the nucleolus triggered by binding to nucleophosmin/B23. Exp Cell Res 276:233-241
    • (2002) Exp Cell Res , vol.276 , pp. 233-241
    • Takemura, M.1    Ohoka, F.2    Perpelescu, M.3
  • 36
    • 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 (2002) Deimination of arginine residues in nucleophosmin/B23 and histones in HL-60 granulocytes. Biochem Biophys Res Commun 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
  • 37
    • 17144363594 scopus 로고    scopus 로고
    • Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes
    • Hagiwara T, Hidaka Y, Yamada M (2005) Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes. Biochemistry 44:5827-5834
    • (2005) Biochemistry , vol.44 , pp. 5827-5834
    • Hagiwara, T.1    Hidaka, Y.2    Yamada, M.3
  • 38
    • 0037840263 scopus 로고    scopus 로고
    • The role of apoptosis in rheumatoid arthritis
    • Liu H, Pope RM (2003) The role of apoptosis in rheumatoid arthritis. Curr Opin Pharmacol 3:317-322
    • (2003) Curr Opin Pharmacol , vol.3 , pp. 317-322
    • Liu, H.1    Pope, R.M.2
  • 39
    • 31044440425 scopus 로고    scopus 로고
    • A functional haplotype of the PADI4 gene associated with increased rheumatoid arthritis susceptibility in Koreans
    • Kang CP, Lee HS, Ju H, Cho H, Kang C, Bae SC (2006) A functional haplotype of the PADI4 gene associated with increased rheumatoid arthritis susceptibility in Koreans. Arthritis Rheum 54:90-96
    • (2006) Arthritis Rheum , vol.54 , pp. 90-96
    • Kang, C.P.1    Lee, H.S.2    Ju, H.3    Cho, H.4    Kang, C.5    Bae, S.C.6
  • 40
    • 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. (2005) Ornithine decarboxylase prevents tumor necrosis factor alpha-induced apoptosis by decreasing intracellular reactive oxygen species. Apoptosis 10:569-581
    • (2005) Apoptosis , vol.10 , pp. 569-581
    • Liu, G.Y.1    Hung, Y.C.2    Hsu, P.C.3
  • 41
    • 23944520426 scopus 로고    scopus 로고
    • Ornithine decarboxylase prevents methotrexate-induced apoptosis by reducing intracellular reactive oxygen species production
    • Huang CC, Hsu PC, Hung YC et al. (2005) Ornithine decarboxylase prevents methotrexate-induced apoptosis by reducing intracellular reactive oxygen species production. Apoptosis 10:895-907
    • (2005) Apoptosis , vol.10 , pp. 895-907
    • Huang, C.C.1    Hsu, P.C.2    Hung, Y.C.3
  • 42
    • 27944438816 scopus 로고    scopus 로고
    • A continuous spectrophotometric assay method for peptidylarginine deiminase type 4 activity
    • Liao YF, Hsieh HC, Liu GY, Hung HC (2005) A continuous spectrophotometric assay method for peptidylarginine deiminase type 4 activity. Anal Biochem 347:176-181
    • (2005) Anal Biochem , vol.347 , pp. 176-181
    • Liao, Y.F.1    Hsieh, H.C.2    Liu, G.Y.3    Hung, H.C.4
  • 43
    • 0019170507 scopus 로고
    • Optimization of conditions for the colorimetric determination of citrulline, using diacetyl monoxime
    • Boyde TR, Rahmatullah M (1980) Optimization of conditions for the colorimetric determination of citrulline, using diacetyl monoxime. Anal Biochem 107:424-431
    • (1980) Anal Biochem , vol.107 , pp. 424-431
    • Boyde, T.R.1    Rahmatullah, M.2
  • 44
    • 0037376349 scopus 로고    scopus 로고
    • Impacts of glutathione peroxidase-1 knockout on the protection by injected selenium against the pro-oxidant-induced liver aponecrosis and signaling in selenium-deficient mice
    • Cheng WH, Quimby FW, Lei XG (2003) Impacts of glutathione peroxidase-1 knockout on the protection by injected selenium against the pro-oxidant-induced liver aponecrosis and signaling in selenium-deficient mice. Free Radic Biol Med 34:918-927
    • (2003) Free Radic Biol Med , vol.34 , pp. 918-927
    • Cheng, W.H.1    Quimby, F.W.2    Lei, X.G.3
  • 46
    • 33646389796 scopus 로고    scopus 로고
    • Bioenergetic aspects of apoptosis, necrosis and mitoptosis
    • Skulachev VP (2006) Bioenergetic aspects of apoptosis, necrosis and mitoptosis. Apoptosis 11:473-485
    • (2006) Apoptosis , vol.11 , pp. 473-485
    • Skulachev, V.P.1
  • 47
    • 0036016923 scopus 로고    scopus 로고
    • Molecular mechanisms of "detachment-induced apoptosis-Anoikis
    • Grossmann J (2002) Molecular mechanisms of "detachment-induced apoptosis-Anoikis". Apoptosis 7:247-260
    • (2002) Apoptosis , vol.7 , pp. 247-260
    • Grossmann, J.1
  • 48
    • 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. (2005) Growth factor regulation of autophagy and cell survival in the absence of apoptosis. Cell 120:237-248
    • (2005) Cell , vol.120 , pp. 237-248
    • Lum, J.J.1    Bauer, D.E.2    Kong, M.3
  • 49
    • 12944308330 scopus 로고    scopus 로고
    • Eating oneself and uninvited guests: Autophagy-related pathways in cellular defense
    • Levine B (2005) Eating oneself and uninvited guests: autophagy-related pathways in cellular defense. Cell 120:159-162
    • (2005) Cell , vol.120 , pp. 159-162
    • Levine, B.1
  • 51
    • 0024473081 scopus 로고
    • Ca2+-dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain
    • Inagaki M, Takahara H, Nishi Y, Sugawara K, Sato C (1989). Ca2+-dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain. J Biol Chem 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
  • 52
    • 0037147140 scopus 로고    scopus 로고
    • Nuclear localization of peptidylarginine deiminase V and histone deimination in granulocytes
    • Nakashima K, Hagiwara T, Yamada M (2002) Nuclear localization of peptidylarginine deiminase V and histone deimination in granulocytes. J Biol Chem 277:49562-49568
    • (2002) J Biol Chem , vol.277 , pp. 49562-49568
    • Nakashima, K.1    Hagiwara, T.2    Yamada, M.3
  • 53
    • 0034031250 scopus 로고    scopus 로고
    • Signaling to p53: Breaking the posttranslational modification code
    • Appella E, Anderson CW (2000) Signaling to p53: breaking the posttranslational modification code. Pathol Biol (Paris) 48:227-245
    • (2000) Pathol Biol (Paris) , vol.48 , pp. 227-245
    • Appella, E.1    Anderson, C.W.2
  • 54
    • 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 (2005) p21Cip1 and p27Kip1 induce distinct cell cycle effects and differentiation programs in myeloid leukemia cells. J Biol Chem 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
  • 55
    • 2342459790 scopus 로고    scopus 로고
    • DNA damage-induced apoptosis
    • Norbury CJ, Zhivotovsky B (2004) DNA damage-induced apoptosis. Oncogene 23:2797-2808
    • (2004) Oncogene , vol.23 , pp. 2797-2808
    • Norbury, C.J.1    Zhivotovsky, B.2
  • 56
    • 1542359516 scopus 로고    scopus 로고
    • Central role of mitochondria and p53 in Fas-mediated apoptosis of rheumatoid synovial fibroblasts
    • Itoh K, Hase H, Kojima H, Saotome K, Nishioka K, Kobata T (2004) Central role of mitochondria and p53 in Fas-mediated apoptosis of rheumatoid synovial fibroblasts. Rheumatology (Oxford) 43:277-285
    • (2004) Rheumatology (Oxford) , vol.43 , pp. 277-285
    • Itoh, K.1    Hase, H.2    Kojima, H.3    Saotome, K.4    Nishioka, K.5    Kobata, T.6
  • 57
    • 13944257800 scopus 로고    scopus 로고
    • Transcription, apoptosis and p53: Catch-22
    • Schuler M, Green DR (2005) Transcription, apoptosis and p53: catch-22. Trends Genet 21:182-187
    • (2005) Trends Genet , vol.21 , pp. 182-187
    • Schuler, M.1    Green, D.R.2
  • 58
    • 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. (2004) Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis. Science 303:1010-1014
    • (2004) Science , vol.303 , pp. 1010-1014
    • Chipuk, J.E.1    Kuwana, T.2    Bouchier-Hayes, L.3
  • 59
    • 0030777295 scopus 로고    scopus 로고
    • Inhibition of T cell apoptosis in the rheumatoid synovium
    • Salmon M, Scheel-Toellner D, Huissoon AP et al. (1997) Inhibition of T cell apoptosis in the rheumatoid synovium. J Clin Invest 99:439-446
    • (1997) J Clin Invest , vol.99 , pp. 439-446
    • Salmon, M.1    Scheel-Toellner, D.2    Huissoon, A.P.3
  • 60
    • 32044451586 scopus 로고    scopus 로고
    • Accelerated macrophage apoptosis induces autoantibody formation and organ damage in systemic lupus erythematosus
    • Denny MF, Chandaroy P, Killen PD et al. (2006) Accelerated macrophage apoptosis induces autoantibody formation and organ damage in systemic lupus erythematosus. J Immunol 176:2095-2104
    • (2006) J Immunol , vol.176 , pp. 2095-2104
    • Denny, M.F.1    Chandaroy, P.2    Killen, P.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.