메뉴 건너뛰기




Volumn 216, Issue 2, 2008, Pages 498-506

DNA damage, RAD9 and fertility/infertility of Echinococcus granulosus hydatid cysts

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; NITROGEN; PROTEIN RAD9; REACTIVE OXYGEN METABOLITE;

EID: 46049091575     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcp.21418     Document Type: Article
Times cited : (30)

References (75)
  • 1
    • 0034712743 scopus 로고    scopus 로고
    • Adoutte A, Balavoine G, Lartillot N, Lespinet O, Prud'homme B, de RR. 2000. The new animal phylogeny: Reliability and implications. Proc Natl Acad Sci USA 97:4453-4456.
    • Adoutte A, Balavoine G, Lartillot N, Lespinet O, Prud'homme B, de RR. 2000. The new animal phylogeny: Reliability and implications. Proc Natl Acad Sci USA 97:4453-4456.
  • 2
    • 0036526766 scopus 로고    scopus 로고
    • Effectiveness of free radicals in hydatid cysts
    • Amanvermez R, Celik C. 2002. Effectiveness of free radicals in hydatid cysts. J Egypt Soc Parasitol 32:259-269.
    • (2002) J Egypt Soc Parasitol , vol.32 , pp. 259-269
    • Amanvermez, R.1    Celik, C.2
  • 3
    • 0018252058 scopus 로고
    • Ultrastructural aspects of fertile and sterile cysts of Echinococcus granulosus developed in hosts of different species
    • Bortoletti G, Ferretti G. 1978. Ultrastructural aspects of fertile and sterile cysts of Echinococcus granulosus developed in hosts of different species. Int J Parasitol 8:421-431.
    • (1978) Int J Parasitol , vol.8 , pp. 421-431
    • Bortoletti, G.1    Ferretti, G.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 33644531287 scopus 로고    scopus 로고
    • Global socioeconomic impact of cystic echinococcosis
    • Budke CM. 2006. Global socioeconomic impact of cystic echinococcosis. Emerg Infect Dis 12:296-303.
    • (2006) Emerg Infect Dis , vol.12 , pp. 296-303
    • Budke, C.M.1
  • 6
    • 0023741521 scopus 로고
    • Helminth anti-oxidant enzymes: A protective mechanism against host oxidants?
    • Callahan HL, Crouch RK, James ER. 1988. Helminth anti-oxidant enzymes: A protective mechanism against host oxidants? Parasitol Today 4:218-225.
    • (1988) Parasitol Today , vol.4 , pp. 218-225
    • Callahan, H.L.1    Crouch, R.K.2    James, E.R.3
  • 7
    • 12844264108 scopus 로고    scopus 로고
    • Interaction of checkpoint proteins Hus1/Rad1/Rad9 with DNA base excision repair enzyme MutY homolog in fission yeast, Schizosaccharomyces pombe
    • Chang DY, Lu AL. 2005. Interaction of checkpoint proteins Hus1/Rad1/Rad9 with DNA base excision repair enzyme MutY homolog in fission yeast, Schizosaccharomyces pombe. J Biol Chem 280:408-417.
    • (2005) J Biol Chem , vol.280 , pp. 408-417
    • Chang, D.Y.1    Lu, A.L.2
  • 8
    • 0035844130 scopus 로고    scopus 로고
    • ATM-dependent phosphorylation of human Rad9 is required for ionizing radiation-induced checkpoint activation
    • Chen MJ, Lin YT, Lieberman HB, Chen G, Lee EY. 2001. ATM-dependent phosphorylation of human Rad9 is required for ionizing radiation-induced checkpoint activation. J Biol Chem 276:16580-16586.
    • (2001) J Biol Chem , vol.276 , pp. 16580-16586
    • Chen, M.J.1    Lin, Y.T.2    Lieberman, H.B.3    Chen, G.4    Lee, E.Y.5
  • 10
    • 0026686203 scopus 로고
    • Identification of the major soluble cuticular glycoprotein of lymphatic filarial nematode parasites (gp29) as a secretory homolog of glutathione peroxidase
    • Cookson E, Blaxter ML, Selkirk ME. 1992. Identification of the major soluble cuticular glycoprotein of lymphatic filarial nematode parasites (gp29) as a secretory homolog of glutathione peroxidase. Proc Natl Acad Sci USA 89:5837-5841.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5837-5841
    • Cookson, E.1    Blaxter, M.L.2    Selkirk, M.E.3
  • 12
    • 15944424299 scopus 로고    scopus 로고
    • Human Rad9 is required for the activation of S-phase checkpoint and the maintenance of chromosomal stability
    • Dang T, Bao S, Wang XF. 2005. Human Rad9 is required for the activation of S-phase checkpoint and the maintenance of chromosomal stability. Genes Cells 10:287-295.
    • (2005) Genes Cells , vol.10 , pp. 287-295
    • Dang, T.1    Bao, S.2    Wang, X.F.3
  • 13
    • 0029166133 scopus 로고
    • The nucleotide sequence, structure, and preliminary studies on the transcriptional regulation of the bovine alpha skeletal actin gene
    • Davey HW, Kelly JK, Wildeman AG. 1995. The nucleotide sequence, structure, and preliminary studies on the transcriptional regulation of the bovine alpha skeletal actin gene. DNA Cell Biol 14:609-618.
    • (1995) DNA Cell Biol , vol.14 , pp. 609-618
    • Davey, H.W.1    Kelly, J.K.2    Wildeman, A.G.3
  • 14
    • 0032535726 scopus 로고    scopus 로고
    • cDNA cloning and gene mapping of human homologs for Schizosaccharomyces pombe rad17, rad1, and hus1 and cloning of homologs from mouse, Caenorhabditis elegans, and Drosophila melanogaster
    • Dean FB, Lian L, O'Donnell M. 1998. cDNA cloning and gene mapping of human homologs for Schizosaccharomyces pombe rad17, rad1, and hus1 and cloning of homologs from mouse, Caenorhabditis elegans, and Drosophila melanogaster. Genomics 54:424-436.
    • (1998) Genomics , vol.54 , pp. 424-436
    • Dean, F.B.1    Lian, L.2    O'Donnell, M.3
  • 15
    • 33645233623 scopus 로고    scopus 로고
    • Molecules released by helminth parasites involved in host colonization
    • Dzik JM. 2006. Molecules released by helminth parasites involved in host colonization. Acta Biochim Pol 53:33-64.
    • (2006) Acta Biochim Pol , vol.53 , pp. 33-64
    • Dzik, J.M.1
  • 16
    • 1642556706 scopus 로고    scopus 로고
    • Biological, epidemiological, and clinical aspects of echinococcosis, a zoonosis of increasing concern
    • Eckert J, Deplazes P. 2004. Biological, epidemiological, and clinical aspects of echinococcosis, a zoonosis of increasing concern. Clin Microbiol Rev 17:107-135.
    • (2004) Clin Microbiol Rev , vol.17 , pp. 107-135
    • Eckert, J.1    Deplazes, P.2
  • 17
    • 0025373259 scopus 로고
    • Oxidative damage to DNA during aging: 8-hydroxy-2′-deoxyguanosine in rat organ DNA and urine
    • Fraga CG, Shigenaga MK, Park JW, Degan P, Ames BN. 1990. Oxidative damage to DNA during aging: 8-hydroxy-2′-deoxyguanosine in rat organ DNA and urine. Proc Natl Acad Sci USA 87:4533-4537.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4533-4537
    • Fraga, C.G.1    Shigenaga, M.K.2    Park, J.W.3    Degan, P.4    Ames, B.N.5
  • 19
    • 0036438841 scopus 로고    scopus 로고
    • Echinococcus granulosus protoscolex formation in natural infections
    • Galindo M, Gonzalez MJ, Galanti N. 2002. Echinococcus granulosus protoscolex formation in natural infections. Biol Res 35:365-371.
    • (2002) Biol Res , vol.35 , pp. 365-371
    • Galindo, M.1    Gonzalez, M.J.2    Galanti, N.3
  • 20
    • 0141640822 scopus 로고    scopus 로고
    • Regionalization of DNA and protein synthesis in developing stages of the parasitic platyhelminth Echinococcus granulosus
    • Galindo M, Paredes R, Marchant C, Mino V, Galanti N. 2003. Regionalization of DNA and protein synthesis in developing stages of the parasitic platyhelminth Echinococcus granulosus. J Cell Biochem 90:294-303.
    • (2003) J Cell Biochem , vol.90 , pp. 294-303
    • Galindo, M.1    Paredes, R.2    Marchant, C.3    Mino, V.4    Galanti, N.5
  • 21
    • 34250379523 scopus 로고    scopus 로고
    • The checkpoint clamp, Rad9-Rad1-Hus1 complex, preferentially stimulates the activity of apurinic/apyrimidinic endonuclease I and DNA polymerase beta in long patch base excision repair
    • Gembka A, Toueille M, Smirnova E, Poltz R, Ferrari E, Villani G, Hubscher U. 2007. The checkpoint clamp, Rad9-Rad1-Hus1 complex, preferentially stimulates the activity of apurinic/apyrimidinic endonuclease I and DNA polymerase beta in long patch base excision repair. Nucleic Acids Res 35:2596-2608.
    • (2007) Nucleic Acids Res , vol.35 , pp. 2596-2608
    • Gembka, A.1    Toueille, M.2    Smirnova, E.3    Poltz, R.4    Ferrari, E.5    Villani, G.6    Hubscher, U.7
  • 22
    • 30044449328 scopus 로고    scopus 로고
    • Expression of serum amyloid A, in normal, dysplastic, and neoplastic human colonic mucosa: Implication for a role in colonic tumorigenesis
    • Gutfeld O, Prus D, Ackerman Z, Dishon S, Linke RP, Levin M, Urieli-Shoval S. 2006. Expression of serum amyloid A, in normal, dysplastic, and neoplastic human colonic mucosa: Implication for a role in colonic tumorigenesis. J Histochem Cytochem 54:63-73.
    • (2006) J Histochem Cytochem , vol.54 , pp. 63-73
    • Gutfeld, O.1    Prus, D.2    Ackerman, Z.3    Dishon, S.4    Linke, R.P.5    Levin, M.6    Urieli-Shoval, S.7
  • 23
    • 0031684034 scopus 로고    scopus 로고
    • Molecular cloning and tissue-specific expression of Mrad9, a murine orthologue of the Schizosaccharomyces pombe rad9+ checkpoint control gene
    • Hang H, Rauth SJ, Hopkins KM, Davey SK, Lieberman HB. 1998. Molecular cloning and tissue-specific expression of Mrad9, a murine orthologue of the Schizosaccharomyces pombe rad9+ checkpoint control gene. J Cell Physiol 177:241-247.
    • (1998) J Cell Physiol , vol.177 , pp. 241-247
    • Hang, H.1    Rauth, S.J.2    Hopkins, K.M.3    Davey, S.K.4    Lieberman, H.B.5
  • 24
    • 0034326830 scopus 로고    scopus 로고
    • Mutant alleles of Schizosaccharomyces pombe rad9(+) alter hydroxyurea resistance, radioresistance and checkpoint control
    • Hang H, Rauth SJ, Hopkins KM, Lieberman HB. 2000. Mutant alleles of Schizosaccharomyces pombe rad9(+) alter hydroxyurea resistance, radioresistance and checkpoint control. Nucleic Acids Res 28:4340-4349.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4340-4349
    • Hang, H.1    Rauth, S.J.2    Hopkins, K.M.3    Lieberman, H.B.4
  • 25
    • 0027082270 scopus 로고
    • Role of free radicals in aging and disease
    • Harman D. 1992. Role of free radicals in aging and disease. Ann NY Acad Sci 673:126-141.
    • (1992) Ann NY Acad Sci , vol.673 , pp. 126-141
    • Harman, D.1
  • 26
    • 0037067776 scopus 로고    scopus 로고
    • A role of the C-terminal region of human Rad9 (hRad9) in nuclear transport of the hRad9 checkpoint complex
    • Hirai I, Wang HG. 2002. A role of the C-terminal region of human Rad9 (hRad9) in nuclear transport of the hRad9 checkpoint complex. J Biol Chem 277:25722-25727.
    • (2002) J Biol Chem , vol.277 , pp. 25722-25727
    • Hirai, I.1    Wang, H.G.2
  • 27
    • 0032526328 scopus 로고    scopus 로고
    • Mechanisms of macrophage stimulation through C D8: Macrophage CD8alpha and CD8beta induce nitric oxide production and associated killing of the parasite Leishmania major
    • Hirji N, Lin TJ, Bissonnette E, Belosevic M, Befus AD. 1998. Mechanisms of macrophage stimulation through C D8: Macrophage CD8alpha and CD8beta induce nitric oxide production and associated killing of the parasite Leishmania major. J Immunol 160:6004-6011.
    • (1998) J Immunol , vol.160 , pp. 6004-6011
    • Hirji, N.1    Lin, T.J.2    Bissonnette, E.3    Belosevic, M.4    Befus, A.D.5
  • 28
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • Hoeijmakers JH. 2001. Genome maintenance mechanisms for preventing cancer. Nature 411:366-374.
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.1
  • 30
    • 0028113130 scopus 로고
    • Superoxide dismutase
    • James ER. 1994. Superoxide dismutase. Parasitol Today 10:481-484.
    • (1994) Parasitol Today , vol.10 , pp. 481-484
    • James, E.R.1
  • 31
    • 0024821351 scopus 로고
    • Macrophage cytotoxicity against schistosomula of Schistosoma mansoni involves arginine-dependent production of reactive nitrogen intermediates
    • James SL, Glaven J. 1989. Macrophage cytotoxicity against schistosomula of Schistosoma mansoni involves arginine-dependent production of reactive nitrogen intermediates. J Immunol 143:4208-4212.
    • (1989) J Immunol , vol.143 , pp. 4208-4212
    • James, S.L.1    Glaven, J.2
  • 32
    • 0033868739 scopus 로고    scopus 로고
    • Echinococcus granulosus: DNA extraction from germinal layers allows strain determination in fertile and nonfertile hydatid cysts
    • Kamenetzky L, Canova SG, Guarnera EA, Rosenzvit MC. 2000. Echinococcus granulosus: DNA extraction from germinal layers allows strain determination in fertile and nonfertile hydatid cysts. Exp Parasitol 95:122-127.
    • (2000) Exp Parasitol , vol.95 , pp. 122-127
    • Kamenetzky, L.1    Canova, S.G.2    Guarnera, E.A.3    Rosenzvit, M.C.4
  • 34
    • 34548798637 scopus 로고    scopus 로고
    • Protective role and regulation of Rad9 from the fission yeast Schizosaccharomyces pombe
    • Kang MH, Park EH, Lim CJ. 2007. Protective role and regulation of Rad9 from the fission yeast Schizosaccharomyces pombe. FEMS Microbiol Lett 275:270-277.
    • (2007) FEMS Microbiol Lett , vol.275 , pp. 270-277
    • Kang, M.H.1    Park, E.H.2    Lim, C.J.3
  • 36
    • 0346056673 scopus 로고    scopus 로고
    • Functional expression and characterization of Echinococcus granulosus thioredoxin peroxidase suggests a role in protection against oxidative damage
    • Li J, Zhang WB, Loukas A, Lin RY, Ito A, Zhang LH, Jones M, McManus DP. 2004. Functional expression and characterization of Echinococcus granulosus thioredoxin peroxidase suggests a role in protection against oxidative damage. Gene 326:157-165.
    • (2004) Gene , vol.326 , pp. 157-165
    • Li, J.1    Zhang, W.B.2    Loukas, A.3    Lin, R.Y.4    Ito, A.5    Zhang, L.H.6    Jones, M.7    McManus, D.P.8
  • 37
    • 33644999937 scopus 로고    scopus 로고
    • Rad9, an evolutionary conserved gene with multiple functions for preserving genomic integrity
    • Lieberman HB. 2006. Rad9, an evolutionary conserved gene with multiple functions for preserving genomic integrity. J Cell Biochem 97:690-697.
    • (2006) J Cell Biochem , vol.97 , pp. 690-697
    • Lieberman, H.B.1
  • 40
    • 0036267642 scopus 로고    scopus 로고
    • Tissular cestodiasis: Role of helper type 1 and 2 t-lymphocytes
    • Lopez-Moreno HS. 2002. Tissular cestodiasis: Role of helper type 1 and 2 t-lymphocytes. Salud Publica Mex 44:145-152.
    • (2002) Salud Publica Mex , vol.44 , pp. 145-152
    • Lopez-Moreno, H.S.1
  • 41
    • 0023737526 scopus 로고
    • Electrophoretic analysis of genetic variation in Echinococcus granulosus from domestic hosts in Australia
    • Lymbery AJ, Thompson RC. 1988. Electrophoretic analysis of genetic variation in Echinococcus granulosus from domestic hosts in Australia. Int J Parasitol 18:803-811.
    • (1988) Int J Parasitol , vol.18 , pp. 803-811
    • Lymbery, A.J.1    Thompson, R.C.2
  • 42
    • 13844269018 scopus 로고    scopus 로고
    • Immunofluorescent detection of 8-oxo-dG and PAH bulky adducts in fish liver and mussel digestive gland
    • Machella N, Regoli F, Santella RM. 2005. Immunofluorescent detection of 8-oxo-dG and PAH bulky adducts in fish liver and mussel digestive gland. Aquat Toxicol 71:335-343.
    • (2005) Aquat Toxicol , vol.71 , pp. 335-343
    • Machella, N.1    Regoli, F.2    Santella, R.M.3
  • 43
    • 18444396177 scopus 로고    scopus 로고
    • Cellular organization and appearance of differentiated structures in developing stages of the parasitic platyhelminth Echinococcus granulosus
    • Martinez C, Paredes R, Stock RP, Saralegui A, Andreu M, Cabezon C, Ehrlich R, Galanti N. 2005. Cellular organization and appearance of differentiated structures in developing stages of the parasitic platyhelminth Echinococcus granulosus. J Cell Biochem 94:327-335.
    • (2005) J Cell Biochem , vol.94 , pp. 327-335
    • Martinez, C.1    Paredes, R.2    Stock, R.P.3    Saralegui, A.4    Andreu, M.5    Cabezon, C.6    Ehrlich, R.7    Galanti, N.8
  • 45
    • 33748950227 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a 2-Cys peroxiredoxin from Taenia solium
    • Molina-Lopez J, Jimenez L, Ochoa-Sanchez A, Landa A. 2006. Molecular cloning and characterization of a 2-Cys peroxiredoxin from Taenia solium. J Parasitol 92:796-802.
    • (2006) J Parasitol , vol.92 , pp. 796-802
    • Molina-Lopez, J.1    Jimenez, L.2    Ochoa-Sanchez, A.3    Landa, A.4
  • 46
    • 0020014315 scopus 로고
    • Characterization of glutathione S-transferase activity in Echinococcus granulosus
    • Morello A, Repetto Y, Atias A. 1982. Characterization of glutathione S-transferase activity in Echinococcus granulosus. Comp Biochem Physiol B 72:449-452.
    • (1982) Comp Biochem Physiol B , vol.72 , pp. 449-452
    • Morello, A.1    Repetto, Y.2    Atias, A.3
  • 47
    • 0025784689 scopus 로고
    • Cloning and characterisation of the rad9 DNA repair gene from Schizosaccharomyces pombe
    • Murray JM, Carr AM, Lehmann AR, Watts FZ. 1991. Cloning and characterisation of the rad9 DNA repair gene from Schizosaccharomyces pombe. Nucleic Acids Res 19:3525-3531.
    • (1991) Nucleic Acids Res , vol.19 , pp. 3525-3531
    • Murray, J.M.1    Carr, A.M.2    Lehmann, A.R.3    Watts, F.Z.4
  • 48
    • 33947609344 scopus 로고    scopus 로고
    • Apoptosis as a possible mechanism of infertility in Echinococcus granulosus hydatid cysts
    • Paredes R, Jimenez V, Cabrera G, Iraguen D, Galanti N. 2007. Apoptosis as a possible mechanism of infertility in Echinococcus granulosus hydatid cysts. J Cell Biochem 100:1200-1209.
    • (2007) J Cell Biochem , vol.100 , pp. 1200-1209
    • Paredes, R.1    Jimenez, V.2    Cabrera, G.3    Iraguen, D.4    Galanti, N.5
  • 49
  • 51
    • 34147169442 scopus 로고    scopus 로고
    • Echinococcus granulosus antigen B impairs human dendritic cell differentiation and polarizes immature dendritic cell maturation towards a Th2 cell response
    • Rigano R, Buttari B, Profumo E, Ortona E, Delunardo F, Margutti P, Mattet V, Teggi A, Sorice M, Siracusano A. 2007. Echinococcus granulosus antigen B impairs human dendritic cell differentiation and polarizes immature dendritic cell maturation towards a Th2 cell response. Infect Immun 75:1667-1678.
    • (2007) Infect Immun , vol.75 , pp. 1667-1678
    • Rigano, R.1    Buttari, B.2    Profumo, E.3    Ortona, E.4    Delunardo, F.5    Margutti, P.6    Mattet, V.7    Teggi, A.8    Sorice, M.9    Siracusano, A.10
  • 52
    • 0027954494 scopus 로고
    • Free radicals in biology: Oxidative stress and the effects of ionizing radiation. lnt
    • Riley PA. 1994. Free radicals in biology: Oxidative stress and the effects of ionizing radiation. lnt J Radiat Biol 65:27-33.
    • (1994) J Radiat Biol , vol.65 , pp. 27-33
    • Riley, P.A.1
  • 53
    • 0030797529 scopus 로고    scopus 로고
    • Immunological characteristics and localization of the Trichinella spiralis glutathione S-transferase
    • Rojas J, Rodriguez-Osorio M, Gomez-Garcia V. 1997. Immunological characteristics and localization of the Trichinella spiralis glutathione S-transferase. J Parasitol 83:630-635.
    • (1997) J Parasitol , vol.83 , pp. 630-635
    • Rojas, J.1    Rodriguez-Osorio, M.2    Gomez-Garcia, V.3
  • 54
    • 0037113871 scopus 로고    scopus 로고
    • Genotoxin-induced Rad9-Hus1-Rad1 (9-1-1) chromatin association is an early checkpoint signaling event
    • Roos-Mattjus P, Vroman BT, Burtelow MA, Rauen M, Eapen AK, Karnitz LM. 2002. Genotoxin-induced Rad9-Hus1-Rad1 (9-1-1) chromatin association is an early checkpoint signaling event. J Biol Chem 277:43809-43812.
    • (2002) J Biol Chem , vol.277 , pp. 43809-43812
    • Roos-Mattjus, P.1    Vroman, B.T.2    Burtelow, M.A.3    Rauen, M.4    Eapen, A.K.5    Karnitz, L.M.6
  • 56
    • 0030561203 scopus 로고    scopus 로고
    • Preparation of biotinylated, affinity-purified antibodies for enzyme-linked immunoassays using blotting membrane as an antigen support
    • Rucklidge GJ, Milne G, Chaudhry SM, Robins SP. 1996. Preparation of biotinylated, affinity-purified antibodies for enzyme-linked immunoassays using blotting membrane as an antigen support. Anal Biochem 243:158-164.
    • (1996) Anal Biochem , vol.243 , pp. 158-164
    • Rucklidge, G.J.1    Milne, G.2    Chaudhry, S.M.3    Robins, S.P.4
  • 57
    • 0033957655 scopus 로고    scopus 로고
    • Echinococcus granulosus: Heterogeneity and differential expression of superoxide dismutases
    • Salinas G, Cardozo S. 2000. Echinococcus granulosus: Heterogeneity and differential expression of superoxide dismutases. Exp Parasitol 94:56-59.
    • (2000) Exp Parasitol , vol.94 , pp. 56-59
    • Salinas, G.1    Cardozo, S.2
  • 59
    • 0025960650 scopus 로고
    • A protein secreted in vivo by Echinococcus granulosus inhibits elastase activity and neutrophil chemotaxis
    • Shepherd JC, Aitken A, McManus DP. 1991. A protein secreted in vivo by Echinococcus granulosus inhibits elastase activity and neutrophil chemotaxis. Mol Biochem Parasitol 44:81-90.
    • (1991) Mol Biochem Parasitol , vol.44 , pp. 81-90
    • Shepherd, J.C.1    Aitken, A.2    McManus, D.P.3
  • 60
    • 0024503932 scopus 로고
    • The effect of antioxidants on the rejection of Nippostrongylus brasiliensis
    • Smith NC, Bryant C. 1989. The effect of antioxidants on the rejection of Nippostrongylus brasiliensis. Parasite Immunol 11:161-167.
    • (1989) Parasite Immunol , vol.11 , pp. 161-167
    • Smith, N.C.1    Bryant, C.2
  • 61
    • 0033018634 scopus 로고    scopus 로고
    • The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hH US1
    • St Onge RP, Udell CM, Casselman R, Davey S. 1999. The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hH US1. Mol Biol Cell 10:1985-1995.
    • (1999) Mol Biol Cell , vol.10 , pp. 1985-1995
    • St Onge, R.P.1    Udell, C.M.2    Casselman, R.3    Davey, S.4
  • 62
    • 0035834690 scopus 로고    scopus 로고
    • DNA damage-dependent and-independent phosphorylation of the hRad9 checkpoint protein
    • St Onge RP, Besley BD, Park M, Casselman R, Davey S. 2001. DNA damage-dependent and-independent phosphorylation of the hRad9 checkpoint protein. J Biol Chem 276:41898-41905.
    • (2001) J Biol Chem , vol.276 , pp. 41898-41905
    • St Onge, R.P.1    Besley, B.D.2    Park, M.3    Casselman, R.4    Davey, S.5
  • 63
    • 0037698170 scopus 로고    scopus 로고
    • A role for the phosphorylation of hRad9 in checkpoint signaling
    • St Onge RP, Besley BD, Pelley JL, Davey S. 2003. A role for the phosphorylation of hRad9 in checkpoint signaling. J Biol Chem 278:26620-26628.
    • (2003) J Biol Chem , vol.278 , pp. 26620-26628
    • St Onge, R.P.1    Besley, B.D.2    Pelley, J.L.3    Davey, S.4
  • 64
    • 0034826950 scopus 로고    scopus 로고
    • In-vitro susceptibility of hydatid cysts of Echinococcus granulosus to nitric oxide and the effect of the laminated layer on nitric oxide production
    • Steers NJ, Rogan MT, Heath S. 2001. In-vitro susceptibility of hydatid cysts of Echinococcus granulosus to nitric oxide and the effect of the laminated layer on nitric oxide production. Parasite Immunol 23:411-417.
    • (2001) Parasite Immunol , vol.23 , pp. 411-417
    • Steers, N.J.1    Rogan, M.T.2    Heath, S.3
  • 65
    • 1642514804 scopus 로고    scopus 로고
    • Death and more: DNA damage response pathways in the nematode C. elegans
    • Stergiou L, Hengartner MO. 2004. Death and more: DNA damage response pathways in the nematode C. elegans. Cell Death Differ 11:21-28.
    • (2004) Cell Death Differ , vol.11 , pp. 21-28
    • Stergiou, L.1    Hengartner, M.O.2
  • 66
    • 0033582906 scopus 로고    scopus 로고
    • A sliding clamp model for the Rad1 family of cell cycle checkpoint proteins
    • Thelen MP, Venclovas C, Fidelis K. 1999. A sliding clamp model for the Rad1 family of cell cycle checkpoint proteins. Cell 96:769-770.
    • (1999) Cell , vol.96 , pp. 769-770
    • Thelen, M.P.1    Venclovas, C.2    Fidelis, K.3
  • 67
    • 0032131512 scopus 로고    scopus 로고
    • Production of nitric oxide (NO) in human hydatidosis; Relationship between nitrite production and interferon-gamma levels
    • Touil-Boukoffa C, Bauvois B, Sanceau J, Hamrioui B, Wietzerbin J. 1998. Production of nitric oxide (NO) in human hydatidosis; Relationship between nitrite production and interferon-gamma levels. Biochimie 80:739-744.
    • (1998) Biochimie , vol.80 , pp. 739-744
    • Touil-Boukoffa, C.1    Bauvois, B.2    Sanceau, J.3    Hamrioui, B.4    Wietzerbin, J.5
  • 68
    • 0034235463 scopus 로고    scopus 로고
    • Structure-based predictions of RadI, Rad9, Hus1 and Rad17 participation in sliding clamp and clamp-loading complexes
    • Venclovas C, Thelen MP. 2000. Structure-based predictions of RadI, Rad9, Hus1 and Rad17 participation in sliding clamp and clamp-loading complexes. Nucleic Acids Res 28:2481-2493.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2481-2493
    • Venclovas, C.1    Thelen, M.P.2
  • 69
    • 0033534613 scopus 로고    scopus 로고
    • Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9 form a DNA damage-responsive protein complex
    • Volkmer E, Karnitz LM. 1999. Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9 form a DNA damage-responsive protein complex. J Biol Chem 274:567-570.
    • (1999) J Biol Chem , vol.274 , pp. 567-570
    • Volkmer, E.1    Karnitz, L.M.2
  • 70
    • 0037328435 scopus 로고    scopus 로고
    • The ambiguous role of immunity in echinococcosis: Protection of the host or of the parasite?
    • Vuitton DA. 2003. The ambiguous role of immunity in echinococcosis: Protection of the host or of the parasite? Acta Trop 85:119-132.
    • (2003) Acta Trop , vol.85 , pp. 119-132
    • Vuitton, D.A.1
  • 71
    • 0032565577 scopus 로고    scopus 로고
    • Mutagenicity and repair of oxidative DNA damage: Insights from studies using defined lesions
    • Wang D, Kreutzer DA, Essigmann JM. 1998. Mutagenicity and repair of oxidative DNA damage: insights from studies using defined lesions. Mutat Res 400:99-115.
    • (1998) Mutat Res , vol.400 , pp. 99-115
    • Wang, D.1    Kreutzer, D.A.2    Essigmann, J.M.3
  • 72
    • 0023833774 scopus 로고
    • Molecular structure of free radicals and their importance in biological reactions
    • Webster NR, Nunn JF. 1988. Molecular structure of free radicals and their importance in biological reactions. Br J Anaesth 60:98-108.
    • (1988) Br J Anaesth , vol.60 , pp. 98-108
    • Webster, N.R.1    Nunn, J.F.2
  • 73
    • 33744505197 scopus 로고    scopus 로고
    • Expression of TOLL-like receptors (TLR) by bovine antigen-presenting cells-potential role in pathogen discrimination?
    • Werling D, Piercy J, Coffey TJ. 2006. Expression of TOLL-like receptors (TLR) by bovine antigen-presenting cells-potential role in pathogen discrimination? Vet Immunol Immunopathol 112:2-11.
    • (2006) Vet Immunol Immunopathol , vol.112 , pp. 2-11
    • Werling, D.1    Piercy, J.2    Coffey, T.J.3
  • 74
    • 0038237433 scopus 로고    scopus 로고
    • Protein kinase Cdelta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9
    • Yoshida K, Wang HG, Miki Y, Kufe D. 2003. Protein kinase Cdelta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9. EMBO J 22:1431-1441.
    • (2003) EMBO J , vol.22 , pp. 1431-1441
    • Yoshida, K.1    Wang, H.G.2    Miki, Y.3    Kufe, D.4
  • 75
    • 0034707047 scopus 로고    scopus 로고
    • The DNA damage response: Putting checkpoints in perspective
    • Zhou BB, Elledge SJ. 2000. The DNA damage response: Putting checkpoints in perspective. Nature 408:433-439.
    • (2000) Nature , vol.408 , pp. 433-439
    • Zhou, B.B.1    Elledge, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.