메뉴 건너뛰기




Volumn 27, Issue 5, 2008, Pages 223-228

The functions of deoxyribonuclease II in immunity and development

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBONUCLEASE I; DEOXYRIBONUCLEASE II;

EID: 43249122205     PISSN: 10445498     EISSN: None     Source Type: Journal    
DOI: 10.1089/dna.2007.0691     Document Type: Review
Times cited : (20)

References (79)
  • 1
    • 0043142441 scopus 로고    scopus 로고
    • L-DNase II activation by the 24 kDa apoptotic protease (AP24) in TNF alpha-induced apoptosis
    • Altairac, S.S., Zeggai, S., Perani, P., Courtois, Y., and Torriglia, A. (2003). L-DNase II activation by the 24 kDa apoptotic protease (AP24) in TNF alpha-induced apoptosis. Cell Death Differ 10, 1109-1111.
    • (2003) Cell Death Differ , vol.10 , pp. 1109-1111
    • Altairac, S.S.1    Zeggai, S.2    Perani, P.3    Courtois, Y.4    Torriglia, A.5
  • 2
    • 2942733373 scopus 로고    scopus 로고
    • Tumour necrosis factor and other proinflammatory cytokines in systemic lupus erythematosus: A rationale for therapeutic intervention
    • Aringer, M., and Smolen, J.S. (2004). Tumour necrosis factor and other proinflammatory cytokines in systemic lupus erythematosus: a rationale for therapeutic intervention. Lupus 13, 344-347.
    • (2004) Lupus , vol.13 , pp. 344-347
    • Aringer, M.1    Smolen, J.S.2
  • 3
    • 0032581624 scopus 로고    scopus 로고
    • Molecular cloning and characterization of human and murine DNase II
    • Baker, K.P., Baron, W.F., Henzel, W.J., and Spencer, S.A. (1998). Molecular cloning and characterization of human and murine DNase II. Gene 215, 281-289.
    • (1998) Gene , vol.215 , pp. 281-289
    • Baker, K.P.1    Baron, W.F.2    Henzel, W.J.3    Spencer, S.A.4
  • 4
    • 0027164993 scopus 로고
    • Identification of deoxyribonuclease II as an endonuclease involved in apoptosis
    • Barry, M.A., and Eastman, A. (1993). Identification of deoxyribonuclease II as an endonuclease involved in apoptosis. Arch Biochem Biophys 300, 440-450.
    • (1993) Arch Biochem Biophys , vol.300 , pp. 440-450
    • Barry, M.A.1    Eastman, A.2
  • 5
    • 2442761730 scopus 로고    scopus 로고
    • Role of endogenous endonucleases and tissue site in transfection and CpG-mediated immune activation after naked DNA injection
    • Barry, M.E., Pinto-González, D., Orson, F.M., McKenzie, G.J., Petry, G.R., and Barry, M.A. (1999). Role of endogenous endonucleases and tissue site in transfection and CpG-mediated immune activation after naked DNA injection. Hum Gene Ther 10, 2461-2480.
    • (1999) Hum Gene Ther , vol.10 , pp. 2461-2480
    • Barry, M.E.1    Pinto-González, D.2    Orson, F.M.3    McKenzie, G.J.4    Petry, G.R.5    Barry, M.A.6
  • 6
    • 0036343618 scopus 로고    scopus 로고
    • Lens organelle degradation
    • Bassnett, S. (2002). Lens organelle degradation. Exp Eye Res 74, 1-6.
    • (2002) Exp Eye Res , vol.74 , pp. 1-6
    • Bassnett, S.1
  • 7
    • 0031002566 scopus 로고    scopus 로고
    • Chromatin degradation in differentiating fiber cells of the eye lens
    • Bassnett, S., and Mataic, D. (1997). Chromatin degradation in differentiating fiber cells of the eye lens. J Cell Biol 137, 37-49.
    • (1997) J Cell Biol , vol.137 , pp. 37-49
    • Bassnett, S.1    Mataic, D.2
  • 8
    • 0034627773 scopus 로고    scopus 로고
    • Nuclear translocation of a leukocyte elastase inhibitor/elastase complex during staurosporine-induced apoptosis: Role in the generation of nuclear L-DNase II activity
    • Belmokhtar, O.A., Torriglia, A., Counis, M.F., Courtois, Y., Jacquemin-Sablon, A., and Ségal-Bendirdjian, E. (2000). Nuclear translocation of a leukocyte elastase inhibitor/elastase complex during staurosporine-induced apoptosis: role in the generation of nuclear L-DNase II activity. Exp Cell Res 25, 99-109.
    • (2000) Exp Cell Res , vol.25 , pp. 99-109
    • Belmokhtar, O.A.1    Torriglia, A.2    Counis, M.F.3    Courtois, Y.4    Jacquemin-Sablon, A.5    Ségal-Bendirdjian, E.6
  • 9
    • 33645663793 scopus 로고    scopus 로고
    • DNase II and the Chk2 DNA damage pathway form a genetic barrier blocking replication of horizontally transferred DNA
    • Bergsmedh, A., Ehnfors, J., Kawane, K., Motoyama, N., Nagata, S., and Holmgren, L. (2006). DNase II and the Chk2 DNA damage pathway form a genetic barrier blocking replication of horizontally transferred DNA. Mol Cancer Res 4,187-195.
    • (2006) Mol Cancer Res , vol.4 , pp. 187-195
    • Bergsmedh, A.1    Ehnfors, J.2    Kawane, K.3    Motoyama, N.4    Nagata, S.5    Holmgren, L.6
  • 11
    • 77956929132 scopus 로고
    • Spleen acid deoxyribonuclease
    • P.D. Boyer, ed, Academic Press, New York, pp
    • Bernardi, G. (1971). Spleen acid deoxyribonuclease. In: Hydrolysis. P.D. Boyer, ed. (Academic Press, New York), pp. 271-287.
    • (1971) Hydrolysis , pp. 271-287
    • Bernardi, G.1
  • 12
    • 0031792776 scopus 로고    scopus 로고
    • Selective regulation of apoptosis: The cytotoxic lymphocyte serpin proteinase inhibitor 9 protects against granzyme B-mediated apoptosis without perturbing the Fas cell death pathway
    • Bird, C.H., Sutton, V.R., Sun, J., Hirst, C.E., Novak, A., Kumar, S., et al. (1998). Selective regulation of apoptosis: the cytotoxic lymphocyte serpin proteinase inhibitor 9 protects against granzyme B-mediated apoptosis without perturbing the Fas cell death pathway. Mol Cell Biol 18, 6387-6398.
    • (1998) Mol Cell Biol , vol.18 , pp. 6387-6398
    • Bird, C.H.1    Sutton, V.R.2    Sun, J.3    Hirst, C.E.4    Novak, A.5    Kumar, S.6
  • 13
    • 24044456041 scopus 로고    scopus 로고
    • Trichinella pseudospiralis infection is characterized by more continuous and diffuse myopathy than T. spiralis infection
    • Boonmars, T., Wu, Z., Nagano, I., and Takahashi, Y. (2005). Trichinella pseudospiralis infection is characterized by more continuous and diffuse myopathy than T. spiralis infection. Parasitol Res 97, 13-20.
    • (2005) Parasitol Res , vol.97 , pp. 13-20
    • Boonmars, T.1    Wu, Z.2    Nagano, I.3    Takahashi, Y.4
  • 14
    • 4344594795 scopus 로고    scopus 로고
    • The LEI/L-DNase II pathway is activated in light-induced retinal degeneration in rats
    • Chahory, S., Padron, L., Courtois, Y., and Torriglia, A. (2004). The LEI/L-DNase II pathway is activated in light-induced retinal degeneration in rats. Neurosci Lett 367, 205-209.
    • (2004) Neurosci Lett , vol.367 , pp. 205-209
    • Chahory, S.1    Padron, L.2    Courtois, Y.3    Torriglia, A.4
  • 15
    • 33748350938 scopus 로고    scopus 로고
    • Identification of three crucial histidine residues (His115, His132 and His297) in porcine deoxyribonuclease II
    • Cheng, Y.C., Hsueh, C.C., Lu, S.C., and Liao, T.H. (2006). Identification of three crucial histidine residues (His115, His132 and His297) in porcine deoxyribonuclease II. Biochem J 398, 177-185.
    • (2006) Biochem J , vol.398 , pp. 177-185
    • Cheng, Y.C.1    Hsueh, C.C.2    Lu, S.C.3    Liao, T.H.4
  • 16
    • 0031435917 scopus 로고    scopus 로고
    • On the mechanism of DNA transfection: Efficient gene transfer without viruses
    • Coonrod, A., Li, F.Q., and Horwitz, M. (1997). On the mechanism of DNA transfection: efficient gene transfer without viruses. Gene Ther 4, 1313-1321.
    • (1997) Gene Ther , vol.4 , pp. 1313-1321
    • Coonrod, A.1    Li, F.Q.2    Horwitz, M.3
  • 17
    • 33845334495 scopus 로고    scopus 로고
    • Acid DNases and their interest among apoptotic endonucleases
    • Counis, M.F., and Torriglia, A.T. (2006). Acid DNases and their interest among apoptotic endonucleases. Biochimie 88, 1851-1858.
    • (2006) Biochimie , vol.88 , pp. 1851-1858
    • Counis, M.F.1    Torriglia, A.T.2
  • 18
    • 27744583504 scopus 로고    scopus 로고
    • DNase II is a member of the phospholipase D superfamily
    • Cymerman, I.A., Meiss, G., and Bujnicki, J.M. (2005). DNase II is a member of the phospholipase D superfamily. Bioinformatics 21, 3959-3962.
    • (2005) Bioinformatics , vol.21 , pp. 3959-3962
    • Cymerman, I.A.1    Meiss, G.2    Bujnicki, J.M.3
  • 19
    • 0141750586 scopus 로고    scopus 로고
    • Non-classic characteristics define prominent DNase activities from the intestine and other tissues of Haemonchus contortus
    • Dongmi, K., and Douglas, P.J. (2003). Non-classic characteristics define prominent DNase activities from the intestine and other tissues of Haemonchus contortus. Exp Parasitol 104, 131-139.
    • (2003) Exp Parasitol , vol.104 , pp. 131-139
    • Dongmi, K.1    Douglas, P.J.2
  • 21
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNAduring apoptosis, and its inhibitor ICAD
    • Enari, M., Sakahira, H., Yokoyama, H., Okawa, K., Iwamatsu, A., and Nagata, S. (1998). A caspase-activated DNase that degrades DNAduring apoptosis, and its inhibitor ICAD. Nature 391, 43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 22
    • 0344009629 scopus 로고    scopus 로고
    • DNase II: Genes, enzymes and function
    • Evans, C.J., and Aguilera, R.J. (2003). DNase II: genes, enzymes and function. Gene 322, 1-15.
    • (2003) Gene , vol.322 , pp. 1-15
    • Evans, C.J.1    Aguilera, R.J.2
  • 23
    • 0036720235 scopus 로고    scopus 로고
    • Nucleotidase cascades are catalyzed by secreted proteins of the parasitic nematode Trichinella spiralis
    • Gounaris, K. (2002). Nucleotidase cascades are catalyzed by secreted proteins of the parasitic nematode Trichinella spiralis. Infect Immun 70, 4917-4924.
    • (2002) Infect Immun , vol.70 , pp. 4917-4924
    • Gounaris, K.1
  • 24
    • 2442665179 scopus 로고    scopus 로고
    • Autoimmune disease and impaired uptake of apoptotic cells in germinal centers of MFG-E8-deficient mice
    • Hanayama, R., Tanaka, M., Miyasaka, K., Aozasa, K., Koike, M., Uchiyama, Y., et al. (2004). Autoimmune disease and impaired uptake of apoptotic cells in germinal centers of MFG-E8-deficient mice. Science 304, 1147-1150.
    • (2004) Science , vol.304 , pp. 1147-1150
    • Hanayama, R.1    Tanaka, M.2    Miyasaka, K.3    Aozasa, K.4    Koike, M.5    Uchiyama, Y.6
  • 25
    • 0026045372 scopus 로고
    • Mechanism of action of deoxyribonuclease II from human lymphoblasts
    • Harosh, I., Binninger, D.M., Harris, P.V., Mezzina, M., and Boyd, J.B. (1991). Mechanism of action of deoxyribonuclease II from human lymphoblasts. Eur J Biochem 202, 479-484.
    • (1991) Eur J Biochem , vol.202 , pp. 479-484
    • Harosh, I.1    Binninger, D.M.2    Harris, P.V.3    Mezzina, M.4    Boyd, J.B.5
  • 26
    • 0024066438 scopus 로고
    • An endonuclease from Caenorhabditis elegans: Partial purification and characterization
    • Hevelone, J., and Hartman, P.S. (1988). An endonuclease from Caenorhabditis elegans: partial purification and characterization. Biochem Genet 26, 447-461.
    • (1988) Biochem Genet , vol.26 , pp. 447-461
    • Hevelone, J.1    Hartman, P.S.2
  • 28
    • 0038267170 scopus 로고    scopus 로고
    • Horizontal transfer of DNA by the uptake of apoptotic bodies
    • Holmgren, L., Bergsmedh, A., and Spetz, A.L. (2002). Horizontal transfer of DNA by the uptake of apoptotic bodies. Vox Sang 83 Suppl 1, 305-306.
    • (2002) Vox Sang , vol.83 , Issue.SUPPL. 1 , pp. 305-306
    • Holmgren, L.1    Bergsmedh, A.2    Spetz, A.L.3
  • 29
    • 0346025621 scopus 로고    scopus 로고
    • Deoxyribonuclease II is a lysosomal barrier to transfection
    • Howell, D.P., Krieser, R.J., Eastman, A., and Barry, M.A. (2003). Deoxyribonuclease II is a lysosomal barrier to transfection. Mol Ther 8, 957-963.
    • (2003) Mol Ther , vol.8 , pp. 957-963
    • Howell, D.P.1    Krieser, R.J.2    Eastman, A.3    Barry, M.A.4
  • 30
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson, M.D., weil, M., and Raff, M.C. (1997). Programmed cell death in animal development. Cell 88, 347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    weil, M.2    Raff, M.C.3
  • 31
    • 0027273267 scopus 로고
    • Trichinella spiralis infected skeletal muscle cells: Arrest in G2/M is associated with the loss of muscle gene expression
    • Jasmer, D.P. (1993). Trichinella spiralis infected skeletal muscle cells: arrest in G2/M is associated with the loss of muscle gene expression. J Cell Biol 121, 785-793.
    • (1993) J Cell Biol , vol.121 , pp. 785-793
    • Jasmer, D.P.1
  • 32
    • 0035947178 scopus 로고    scopus 로고
    • Requirement of DNase II for definitive erythropoiesis in the mouse fetal liver
    • Kawane, K., Fukuyama, H., Kondoh, G., Takeda, J., Ohsawa, Y., Uchiyama, Y., et al. (2001). Requirement of DNase II for definitive erythropoiesis in the mouse fetal liver. Science 292, 1546-1549.
    • (2001) Science , vol.292 , pp. 1546-1549
    • Kawane, K.1    Fukuyama, H.2    Kondoh, G.3    Takeda, J.4    Ohsawa, Y.5    Uchiyama, Y.6
  • 33
    • 0037321024 scopus 로고    scopus 로고
    • Impaired thymic development in mouse embryos deficient in apoptotic DNA degradation
    • Kawane, K., Fukuyama, H., Yoshida, H., Nagase, H., Ohsawa, Y., Uchiyama, Y., et al. (2003). Impaired thymic development in mouse embryos deficient in apoptotic DNA degradation. Nat Immunol 4, 138-144.
    • (2003) Nat Immunol , vol.4 , pp. 138-144
    • Kawane, K.1    Fukuyama, H.2    Yoshida, H.3    Nagase, H.4    Ohsawa, Y.5    Uchiyama, Y.6
  • 34
    • 33750465224 scopus 로고    scopus 로고
    • Chronic polyarthritis caused by mammalian DNA that escapes from degradation in macrophages
    • Kawane, K., Ohtani, M., Miwa, K., Kizawa, T., Kanbara, Y., Yoshioka, Y., et al. (2006). Chronic polyarthritis caused by mammalian DNA that escapes from degradation in macrophages. Nature 443, 998-1002.
    • (2006) Nature , vol.443 , pp. 998-1002
    • Kawane, K.1    Ohtani, M.2    Miwa, K.3    Kizawa, T.4    Kanbara, Y.5    Yoshioka, Y.6
  • 35
    • 0032553416 scopus 로고    scopus 로고
    • The cloning and expression of human deoxyribonuclease II: A possible role in apoptosis
    • Krieser, R.J., and Eastman, A. (1998). The cloning and expression of human deoxyribonuclease II: a possible role in apoptosis. J Biol Chem 273, 30909-30914.
    • (1998) J Biol Chem , vol.273 , pp. 30909-30914
    • Krieser, R.J.1    Eastman, A.2
  • 36
    • 0035897588 scopus 로고    scopus 로고
    • The cloning, genomic structure, localization, and expression of human deoxyribonuclease II
    • Krieser, R.J., MacLea, K.S., Park, J.P., and Eastman, A. (2001). The cloning, genomic structure, localization, and expression of human deoxyribonuclease II. Gene 269, 205-216.
    • (2001) Gene , vol.269 , pp. 205-216
    • Krieser, R.J.1    MacLea, K.S.2    Park, J.P.3    Eastman, A.4
  • 37
    • 0036707510 scopus 로고    scopus 로고
    • Deoxyribonuclease II alpha is required during the phagocytic phase of apoptosis and its loss causes perinatal lethality
    • Krieser, R.J., MacLea, K.S., Longnecker, D.S., Fields, J.L., Fiering, S., and Eastman, A. (2002). Deoxyribonuclease II alpha is required during the phagocytic phase of apoptosis and its loss causes perinatal lethality. Cell Death Differ 9, 956-962.
    • (2002) Cell Death Differ , vol.9 , pp. 956-962
    • Krieser, R.J.1    MacLea, K.S.2    Longnecker, D.S.3    Fields, J.L.4    Fiering, S.5    Eastman, A.6
  • 38
    • 0032962975 scopus 로고    scopus 로고
    • Metabolic instability of plasmid DNA in the cytosol: A potential barrier to gene transfer
    • Lechardeur, D., Sohn, K.J., Haardt, M., Joshi, P.B., Monck, M., Graham, R.W., et al. (1999). Metabolic instability of plasmid DNA in the cytosol: a potential barrier to gene transfer. Gene Ther 6, 482-497.
    • (1999) Gene Ther , vol.6 , pp. 482-497
    • Lechardeur, D.1    Sohn, K.J.2    Haardt, M.3    Joshi, P.B.4    Monck, M.5    Graham, R.W.6
  • 39
    • 0029099729 scopus 로고
    • Cancer gene therapy using plasmid DNA: Pharmacokinetic study of DNA following injection in mice
    • Lew, D., Parker, S.E., Latimer, T., Abai, A.M., Kuwahara-Rundell, A., Doh, S.G., et al. (1995). Cancer gene therapy using plasmid DNA: pharmacokinetic study of DNA following injection in mice. Hum Gene Ther 6, 553-564.
    • (1995) Hum Gene Ther , vol.6 , pp. 553-564
    • Lew, D.1    Parker, S.E.2    Latimer, T.3    Abai, A.M.4    Kuwahara-Rundell, A.5    Doh, S.G.6
  • 40
    • 0022238107 scopus 로고
    • The subunit structure and active site sequence of porcine spleen deoxyribonuclease
    • Liao, T.H. (1985). The subunit structure and active site sequence of porcine spleen deoxyribonuclease. J Biol Chem 260, 10708-10713.
    • (1985) J Biol Chem , vol.260 , pp. 10708-10713
    • Liao, T.H.1
  • 41
    • 0024576873 scopus 로고
    • Deoxyribonuclease II purified from the isolated lysosomes of porcine spleen and from porcine liver homogenates. Comparison with deoxyribonuclease II purified from porcine spleen homogenates
    • Liao, T.H. (1989). Deoxyribonuclease II purified from the isolated lysosomes of porcine spleen and from porcine liver homogenates. Comparison with deoxyribonuclease II purified from porcine spleen homogenates. Biochim Biophys Acta 1007, 15-22.
    • (1989) Biochim Biophys Acta , vol.1007 , pp. 15-22
    • Liao, T.H.1
  • 42
    • 0030848133 scopus 로고    scopus 로고
    • Purification and characterization of the immunoglobulin switch sequence-specific endonuclease (Endo-SR) from bovine spleen
    • Lyon, C.J., and Aguilera, R.J. (1997). Purification and characterization of the immunoglobulin switch sequence-specific endonuclease (Endo-SR) from bovine spleen. Mol Immunol 34, 209-219.
    • (1997) Mol Immunol , vol.34 , pp. 209-219
    • Lyon, C.J.1    Aguilera, R.J.2
  • 43
    • 0034636713 scopus 로고    scopus 로고
    • The C. elegans apoptotic nuclease NUC-1 is related in sequence and activity to mammalian DNase II
    • Lyon, C.J., Evans, C.J., Bill, B.R., Otsuka, A.J., and Aguilera, R.J. (2000). The C. elegans apoptotic nuclease NUC-1 is related in sequence and activity to mammalian DNase II. Gene 252, 147-154.
    • (2000) Gene , vol.252 , pp. 147-154
    • Lyon, C.J.1    Evans, C.J.2    Bill, B.R.3    Otsuka, A.J.4    Aguilera, R.J.5
  • 44
    • 0036296304 scopus 로고    scopus 로고
    • Revised structure of the active form of human deoxyribonuclease II alpha
    • MacLea, K.S., Krieser, R.J. and Eastman, A. (2002). Revised structure of the active form of human deoxyribonuclease II alpha. Biochem Biophys Res Commun 292, 415-421.
    • (2002) Biochem Biophys Res Commun , vol.292 , pp. 415-421
    • MacLea, K.S.1    Krieser, R.J.2    Eastman, A.3
  • 45
    • 0037434627 scopus 로고    scopus 로고
    • A family history of deoxyribonuclease II: Surprises from Trichinella spiralis and Burkholderia pseudomallei
    • MacLea, K.S., Krieser, R.J., and Eastman, A. (2003). A family history of deoxyribonuclease II: surprises from Trichinella spiralis and Burkholderia pseudomallei. Gene 305, 1-12.
    • (2003) Gene , vol.305 , pp. 1-12
    • MacLea, K.S.1    Krieser, R.J.2    Eastman, A.3
  • 46
    • 28444455308 scopus 로고    scopus 로고
    • Organelle degradation during the lens and erythroid differentiation is independent of autophagy
    • Matsui, M., Yamamoto, A., Kuma, A., Ohsumi, Y., and Mizushima, N. (2006). Organelle degradation during the lens and erythroid differentiation is independent of autophagy. Biochem Biophys Res Commun 339, 485-489.
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 485-489
    • Matsui, M.1    Yamamoto, A.2    Kuma, A.3    Ohsumi, Y.4    Mizushima, N.5
  • 47
    • 0024596636 scopus 로고
    • Parasite proteinases
    • McKerrow, J.H. (1989). Parasite proteinases. Exp Parasitol 68, 111-115.
    • (1989) Exp Parasitol , vol.68 , pp. 111-115
    • McKerrow, J.H.1
  • 48
    • 17644393549 scopus 로고    scopus 로고
    • DNA degradation in development and programmed cell death
    • Nagata, S. (2005). DNA degradation in development and programmed cell death. Annu Rev Immunol 23, 853-875.
    • (2005) Annu Rev Immunol , vol.23 , pp. 853-875
    • Nagata, S.1
  • 50
    • 34249806740 scopus 로고    scopus 로고
    • Degradation of nuclear DNA by DNase II-like acid DNase in cortical fiber cells of mouse eye lens
    • Nakahara, M., Nagasaka, A., Koike, M., Uchida, K., Kawane, K., Uchiyama, Y., et al. (2007). Degradation of nuclear DNA by DNase II-like acid DNase in cortical fiber cells of mouse eye lens. FEBS J 274, 3055-3064.
    • (2007) FEBS J , vol.274 , pp. 3055-3064
    • Nakahara, M.1    Nagasaka, A.2    Koike, M.3    Uchida, K.4    Kawane, K.5    Uchiyama, Y.6
  • 52
    • 27944453599 scopus 로고    scopus 로고
    • Toll-like receptor-independent gene induction program activated by mammalian DNA escaped from apoptotic DNA degradation
    • Okabe, Y., Kawane, K., Akira, S., Taniguchi, T., and Nagata, S. (2005). Toll-like receptor-independent gene induction program activated by mammalian DNA escaped from apoptotic DNA degradation. J Exp Med 202, 1333-1339.
    • (2005) J Exp Med , vol.202 , pp. 1333-1339
    • Okabe, Y.1    Kawane, K.2    Akira, S.3    Taniguchi, T.4    Nagata, S.5
  • 53
    • 0036607441 scopus 로고    scopus 로고
    • Toll-like receptor signal transduction and the tailoring of innate immunity: A role for Mal?
    • O'Neill, L.A. (2002). Toll-like receptor signal transduction and the tailoring of innate immunity: A role for Mal? Trends Immunol 23, 296-300.
    • (2002) Trends Immunol , vol.23 , pp. 296-300
    • O'Neill, L.A.1
  • 54
    • 0018747342 scopus 로고
    • Suppressive effect of interferon on erythroid cell proliferation
    • Ortega, J.A., Ma, A., Shore, N.A., Dukes, P.P., and Merigan, T.C. (1979). Suppressive effect of interferon on erythroid cell proliferation. Exp Hematol 7, 145-150.
    • (1979) Exp Hematol , vol.7 , pp. 145-150
    • Ortega, J.A.1    Ma, A.2    Shore, N.A.3    Dukes, P.P.4    Merigan, T.C.5
  • 55
    • 0015835339 scopus 로고
    • Alkylation of an essential histidine residue in porcine spleen deoxyribonuclease
    • Oshima, R.G., and Price, P.A. (1973). Alkylation of an essential histidine residue in porcine spleen deoxyribonuclease. J Biol Chem 248, 7522-7526.
    • (1973) J Biol Chem , vol.248 , pp. 7522-7526
    • Oshima, R.G.1    Price, P.A.2
  • 56
    • 34347355478 scopus 로고    scopus 로고
    • Conformational modification of serpins transforms leukocyte elastase inhibitor into an endonuclease involved in apoptosis
    • Padron-Barthe, L., Leprêtre, C., Martin, E., Counis, M.F., and Torriglia, A. (2007). Conformational modification of serpins transforms leukocyte elastase inhibitor into an endonuclease involved in apoptosis. Mol Cell Biol 27, 4028-4036.
    • (2007) Mol Cell Biol , vol.27 , pp. 4028-4036
    • Padron-Barthe, L.1    Leprêtre, C.2    Martin, E.3    Counis, M.F.4    Torriglia, A.5
  • 58
    • 0025284721 scopus 로고
    • Endogenous circulating DNA in systemic lupus erythematosus. Occurrence as multimeric complexes bound to histone
    • Rumore, P.M., and Steinman, C.R. (1990). Endogenous circulating DNA in systemic lupus erythematosus. Occurrence as multimeric complexes bound to histone. J Clin Invest 86, 69-74.
    • (1990) J Clin Invest , vol.86 , pp. 69-74
    • Rumore, P.M.1    Steinman, C.R.2
  • 59
    • 33845952655 scopus 로고    scopus 로고
    • Human lysosomal DNase IIa contains two requisite PLD-signature (HxK) motifs: Evidence for a pseudodimeric structure of the active enzyme species
    • Schäfer, P., Cymerman, I.A., Bujnicki, J.M., and Meiss, G. (2007). Human lysosomal DNase IIa contains two requisite PLD-signature (HxK) motifs: evidence for a pseudodimeric structure of the active enzyme species. Protein Sci 16, 82-91.
    • (2007) Protein Sci , vol.16 , pp. 82-91
    • Schäfer, P.1    Cymerman, I.A.2    Bujnicki, J.M.3    Meiss, G.4
  • 60
    • 43249116750 scopus 로고    scopus 로고
    • DNase II deficiency impairs innate immune function in Drosophila
    • Seong, C.S., Varela-Ramirez, A., and Aguilera, R.J. (2006). DNase II deficiency impairs innate immune function in Drosophila. Cell Immunol 7, 1-8.
    • (2006) Cell Immunol , vol.7 , pp. 1-8
    • Seong, C.S.1    Varela-Ramirez, A.2    Aguilera, R.J.3
  • 61
    • 0033570074 scopus 로고    scopus 로고
    • DLAD, a novel mammalian divalent cation-independent endonuclease with homology to DNase II
    • Shiokawa, D., and Tanuma, S. (1999). DLAD, a novel mammalian divalent cation-independent endonuclease with homology to DNase II. Nucleic Acids Res 27, 4083-4089.
    • (1999) Nucleic Acids Res , vol.27 , pp. 4083-4089
    • Shiokawa, D.1    Tanuma, S.2
  • 62
    • 4644345149 scopus 로고    scopus 로고
    • Plancitoxins, lethal factors from the crown-of-thorns starfish Acanthaster planci, are deoxyribonucleases II
    • Shiomi, K., Midorikawa, S., Ishida, M., Nagashima, Y., and Nagai, H. (2004). Plancitoxins, lethal factors from the crown-of-thorns starfish Acanthaster planci, are deoxyribonucleases II. Toxicon 44, 499-506.
    • (2004) Toxicon , vol.44 , pp. 499-506
    • Shiomi, K.1    Midorikawa, S.2    Ishida, M.3    Nagashima, Y.4    Nagai, H.5
  • 63
    • 0033566003 scopus 로고    scopus 로고
    • Functional gene transfer of HIV DNA by an HIV receptor-independent mechanism
    • Spetz, A.L., Patterson, B.K., Lore, K., Andersson, J., and Holmgren, L. (1999). Functional gene transfer of HIV DNA by an HIV receptor-independent mechanism. J Immunol 163, 736-742.
    • (1999) J Immunol , vol.163 , pp. 736-742
    • Spetz, A.L.1    Patterson, B.K.2    Lore, K.3    Andersson, J.4    Holmgren, L.5
  • 64
    • 0028929328 scopus 로고
    • Mechanisms and genes of cellular suicide
    • Steller, H. (1995). Mechanisms and genes of cellular suicide. Science 267, 1445-1449.
    • (1995) Science , vol.267 , pp. 1445-1449
    • Steller, H.1
  • 66
    • 4344632609 scopus 로고    scopus 로고
    • Molecular basis of the transformation of LEI into LDNase II during apoptosis
    • Torriglia, A. (2003). Molecular basis of the transformation of LEI into LDNase II during apoptosis. Recent Res Dev Mol Cell Biol 4, 23-38.
    • (2003) Recent Res Dev Mol Cell Biol , vol.4 , pp. 23-38
    • Torriglia, A.1
  • 68
    • 0031813791 scopus 로고    scopus 로고
    • L-DNase II, a molecule that links proteases and endonucleases in apoptosis, derives from the ubiquitous serpin leukocyte elastase inhibitor
    • Torriglia, A., Perani, P., Brossas, J.Y., Chaudun, E., Treton, J., Courtois, Y., et al. (1998). L-DNase II, a molecule that links proteases and endonucleases in apoptosis, derives from the ubiquitous serpin leukocyte elastase inhibitor. Mol Cell Biol 18, 3612-3619.
    • (1998) Mol Cell Biol , vol.18 , pp. 3612-3619
    • Torriglia, A.1    Perani, P.2    Brossas, J.Y.3    Chaudun, E.4    Treton, J.5    Courtois, Y.6
  • 69
    • 0032563812 scopus 로고    scopus 로고
    • A function for lipoxygenase in programmed organelle degradation
    • Van Leyen, K., Duvoisin, R.M., Engelhardt, H., and Wiedmann, M. (1998). A function for lipoxygenase in programmed organelle degradation. Nature 395, 392-395.
    • (1998) Nature , vol.395 , pp. 392-395
    • Van Leyen, K.1    Duvoisin, R.M.2    Engelhardt, H.3    Wiedmann, M.4
  • 70
    • 0026754442 scopus 로고
    • Analysis of a 43-kDa glycoprotein from the intracellular parasitic nematode Trichinella spiralis
    • Vassilatis, D.K., Despommier, D., Misek, D.E., Polvere, R.I., Gold, A.M., and Van der Ploeg, L.H. (1992). Analysis of a 43-kDa glycoprotein from the intracellular parasitic nematode Trichinella spiralis. J Biol Chem 267, 18459-18465.
    • (1992) J Biol Chem , vol.267 , pp. 18459-18465
    • Vassilatis, D.K.1    Despommier, D.2    Misek, D.E.3    Polvere, R.I.4    Gold, A.M.5    Van der Ploeg, L.H.6
  • 71
    • 0033593572 scopus 로고    scopus 로고
    • Cell death in development
    • Vaux, D.L., and Korsmeyer, S.J. (1999). Cell death in development. Cell 96, 245-254.
    • (1999) Cell , vol.96 , pp. 245-254
    • Vaux, D.L.1    Korsmeyer, S.J.2
  • 72
    • 0025876317 scopus 로고
    • Nuclear breakdown during terminal differentiation of primary lens fibres in mice: A transmission electron microscopic study
    • Vrensen, G.F., Graw, J., and De Wolf, A. (1991). Nuclear breakdown during terminal differentiation of primary lens fibres in mice: a transmission electron microscopic study. Exp Eye Res 52, 647-659.
    • (1991) Exp Eye Res , vol.52 , pp. 647-659
    • Vrensen, G.F.1    Graw, J.2    De Wolf, A.3
  • 73
    • 0021209279 scopus 로고
    • Sequential structural response of lens epithelium to retina-conditioned medium
    • Walton, J., and McAvoy, J. (1984). Sequential structural response of lens epithelium to retina-conditioned medium. Exp Eye Res 39, 217-229.
    • (1984) Exp Eye Res , vol.39 , pp. 217-229
    • Walton, J.1    McAvoy, J.2
  • 74
    • 14444274100 scopus 로고    scopus 로고
    • Porcine spleen deoxyribonuclease, covalent structure, cDNA sequence, molecular cloning, and gene expression
    • Wang, C.C., Lu, S.C., Chen, H.L., and Liao, T.H. (1998). Porcine spleen deoxyribonuclease, covalent structure, cDNA sequence, molecular cloning, and gene expression. J Biol Chem 273, 17192-17198.
    • (1998) J Biol Chem , vol.273 , pp. 17192-17198
    • Wang, C.C.1    Lu, S.C.2    Chen, H.L.3    Liao, T.H.4
  • 75
    • 0018830636 scopus 로고
    • Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation
    • Wyllie, A.H. (1980). Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation. Nature 284, 555-556.
    • (1980) Nature , vol.284 , pp. 555-556
    • Wyllie, A.H.1
  • 77
    • 12344290452 scopus 로고    scopus 로고
    • Lethal anemia caused by interferon-beta produced in mouse embryos carrying undigested DNA
    • Yoshida, H., Okabe, Y., Kawane, K., Fukuyama, H., and Nagata, S. (2004). Lethal anemia caused by interferon-beta produced in mouse embryos carrying undigested DNA. Nat Immunol 6, 49-56.
    • (2004) Nat Immunol , vol.6 , pp. 49-56
    • Yoshida, H.1    Okabe, Y.2    Kawane, K.3    Fukuyama, H.4    Nagata, S.5
  • 78
    • 26944463126 scopus 로고    scopus 로고
    • Phospha-tidylserine-dependent engulfment by macrophages of nuclei from erythroid precursor cells
    • Yoshida H., Kawane, K., Koike, M., Mori, Y., Uchiyama, Y., and Nagata, S. (2005). Phospha-tidylserine-dependent engulfment by macrophages of nuclei from erythroid precursor cells. Nature 437, 754-758.
    • (2005) Nature , vol.437 , pp. 754-758
    • Yoshida, H.1    Kawane, K.2    Koike, M.3    Mori, Y.4    Uchiyama, Y.5    Nagata, S.6
  • 79
    • 0037124051 scopus 로고    scopus 로고
    • Lipoplex-mediated transfection of mammalian cells occurs through the cholesterol-dependent clathrin-mediated pathway of endocytosis
    • Zuhorn, I.S., Kalicharan, R., and Hoekstra, D. (2002). Lipoplex-mediated transfection of mammalian cells occurs through the cholesterol-dependent clathrin-mediated pathway of endocytosis. J Biol Chem 277, 18021-18028.
    • (2002) J Biol Chem , vol.277 , pp. 18021-18028
    • Zuhorn, I.S.1    Kalicharan, R.2    Hoekstra, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.