메뉴 건너뛰기




Volumn 260, Issue 2, 1999, Pages 477-481

Characterization of endonuclease activity from excretory/secretory products of a parasitic nematode, Trichinella spiralis

Author keywords

Acid endonuclease; Double stranded endonuclease; Excretory secretory products; Nematode; Trichinella spiralis

Indexed keywords

ENDONUCLEASE;

EID: 0033106414     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00174.x     Document Type: Article
Times cited : (35)

References (32)
  • 1
    • 0001122944 scopus 로고
    • Pathophysiology of the muscle phase
    • (Campbell, W.C., ed.). Plenum Publishing Corp, New York
    • Stewart, G.L. (1983) Pathophysiology of the muscle phase. In Trichinella and Trichinosis (Campbell, W.C., ed.), pp. 241-264. Plenum Publishing Corp, New York,
    • (1983) Trichinella and Trichinosis , pp. 241-264
    • Stewart, G.L.1
  • 2
    • 0027273267 scopus 로고
    • 2/M and cease muscle gene expression
    • 2/M and cease muscle gene expression. J. Cell Biol. 121, 785-793.
    • (1993) J. Cell Biol. , vol.121 , pp. 785-793
    • Jasmer, D.P.1
  • 3
    • 0027957354 scopus 로고
    • Changes in host muscles induced by excretory/secretory products of larval Trichinella spiralis and Trichinella pseudospiralis
    • Ko, R.C., Fan, L., Lee, D.L. & Compton, H. (1994) Changes in host muscles induced by excretory/secretory products of larval Trichinella spiralis and Trichinella pseudospiralis. Parasitology 108, 195-205.
    • (1994) Parasitology , vol.108 , pp. 195-205
    • Ko, R.C.1    Fan, L.2    Lee, D.L.3    Compton, H.4
  • 4
    • 0031005648 scopus 로고    scopus 로고
    • In vitro effects of Trichinella spiralis on muscle cells
    • Leung, R.K.M. & Ko, R.C. (1997) In vitro effects of Trichinella spiralis on muscle cells. J. Helminthol. 71, 113-118.
    • (1997) J. Helminthol. , vol.71 , pp. 113-118
    • Leung, R.K.M.1    Ko, R.C.2
  • 5
    • 0030065985 scopus 로고    scopus 로고
    • Heat shock response of Trichinella spiralis and T. Pseudospiralis
    • Ko, R.C. & Fan, L. (1996) Heat shock response of Trichinella spiralis and T. pseudospiralis. Parasitology 112, 89-95.
    • (1996) Parasitology , vol.112 , pp. 89-95
    • Ko, R.C.1    Fan, L.2
  • 6
    • 0020567110 scopus 로고
    • Trichinella spiralis: Identification and purification of superoxide dismutase
    • Rhoads, M.L. (1983) Trichinella spiralis: identification and purification of superoxide dismutase. Exp. Parasitol. 56, 41-54.
    • (1983) Exp. Parasitol. , vol.56 , pp. 41-54
    • Rhoads, M.L.1
  • 9
    • 0031469951 scopus 로고    scopus 로고
    • Identification of serine/threonine protein kinases secreted by Trichinella spiralis infective larvae
    • Arden, S.R., Smith, A.M., Booth, M.J., Tweedie, S., Gounaris, K. & Selkirk, M.E. (1997) Identification of serine/threonine protein kinases secreted by Trichinella spiralis infective larvae. Mol. Biochem. Parasitol. 90, 111-119.
    • (1997) Mol. Biochem. Parasitol. , vol.90 , pp. 111-119
    • Arden, S.R.1    Smith, A.M.2    Booth, M.J.3    Tweedie, S.4    Gounaris, K.5    Selkirk, M.E.6
  • 10
    • 0025969554 scopus 로고
    • Trichinella spiralis: Antigenic epitopes from the stichocytes detected in the hypertrophic nuclei and cytoplasm of the parasitized muscle fibre (nurse cell) of the host
    • Lee, D.L., Ko, R.C., Yi, X.Y. & Yeung, M.H.E (1991) Trichinella spiralis: antigenic epitopes from the stichocytes detected in the hypertrophic nuclei and cytoplasm of the parasitized muscle fibre (nurse cell) of the host. Parasitology 102, 117-123.
    • (1991) Parasitology , vol.102 , pp. 117-123
    • Lee, D.L.1    Ko, R.C.2    Yi, X.Y.3    Yeung, M.H.E.4
  • 12
  • 13
    • 0017401236 scopus 로고
    • Nuclease activity detection in polyacrylamide gels
    • Rosenthal, A.L. & Lacks, S.A. (1977) Nuclease activity detection in polyacrylamide gels. Anal. Biochem. 80, 76-90.
    • (1977) Anal. Biochem. , vol.80 , pp. 76-90
    • Rosenthal, A.L.1    Lacks, S.A.2
  • 14
    • 0025075165 scopus 로고
    • Enhanced removal of detergent and recovery of enzymatic activity following sodium dodecyl sulfate-polyacrylamide gel electrophoresis: Use of casein in gel wash buffer
    • McGrew, B.R. & Green, D.M. (1990) Enhanced removal of detergent and recovery of enzymatic activity following sodium dodecyl sulfate-polyacrylamide gel electrophoresis: use of casein in gel wash buffer. Anal. Biochem. 189, 68-74.
    • (1990) Anal. Biochem. , vol.189 , pp. 68-74
    • McGrew, B.R.1    Green, D.M.2
  • 15
    • 0027458695 scopus 로고
    • Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death)
    • Peitsch, M.C., Polzar, B., Stephan, H., Crompton, T., MacDonald, H.R., Mannherz, H.G. & Tschopp, J. (1993) Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death), EMBO J. 12, 371-377.
    • (1993) EMBO J. , vol.12 , pp. 371-377
    • Peitsch, M.C.1    Polzar, B.2    Stephan, H.3    Crompton, T.4    MacDonald, H.R.5    Mannherz, H.G.6    Tschopp, J.7
  • 16
    • 0030965491 scopus 로고    scopus 로고
    • Functional characterization of a human DNase-like protein encoded by a gene positioned in Xq28
    • Appierto, V., Bardella, L., Vijayasarathy, C., Avadhani, N., Sgaramella, V. & Biunno, I. (1997) Functional characterization of a human DNase-like protein encoded by a gene positioned in Xq28. Gene 188, 119-122.
    • (1997) Gene , vol.188 , pp. 119-122
    • Appierto, V.1    Bardella, L.2    Vijayasarathy, C.3    Avadhani, N.4    Sgaramella, V.5    Biunno, I.6
  • 17
    • 0027973581 scopus 로고
    • Identification of an endonuclease responsible for apoptosis in rat thymocytes
    • Shiokawa, D., Ohyama, H., Yamada, T., Takahashi, K. & Tanuma, S. (1994) Identification of an endonuclease responsible for apoptosis in rat thymocytes. Eur. J. Biochem. 226, 23-30.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 23-30
    • Shiokawa, D.1    Ohyama, H.2    Yamada, T.3    Takahashi, K.4    Tanuma, S.5
  • 18
    • 0028171035 scopus 로고
    • Purification and characterization of a deoxyribonuclease acting on native and UV irradiated DNA from young and aging rat brain
    • Suvarchala, E. & Subba Rao, K. (1994) Purification and characterization of a deoxyribonuclease acting on native and UV irradiated DNA from young and aging rat brain. Mol, Cell. Biochem. 137, 109-116.
    • (1994) Mol, Cell. Biochem. , vol.137 , pp. 109-116
    • Suvarchala, E.1    Subba Rao, K.2
  • 19
    • 0027164993 scopus 로고
    • Identification of deoxyribonuclease II as an endonuclease involved in apoptosis
    • Barry, M.A. & 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
  • 20
    • 0024066438 scopus 로고
    • An endonuclease from Caenorhabditis elegans: Partial purification and characterization
    • Hevelone, J. & 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
  • 21
    • 0028341657 scopus 로고
    • Isolation of active recombinant XPG protein, a human DNA repair endonuclease
    • O'Donovan, A., Scherly, D., Clarkson, S.G. & Wood, R.D. (1994) Isolation of active recombinant XPG protein, a human DNA repair endonuclease. J. Biol. Chem. 269, 15965-15968.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15965-15968
    • O'Donovan, A.1    Scherly, D.2    Clarkson, S.G.3    Wood, R.D.4
  • 23
    • 0031313187 scopus 로고    scopus 로고
    • Deoxyribonuclease secreted from an insectivorous plant dorsera adelae
    • Okabe, T., Mori, H. & Ohyama, T. (1997) Deoxyribonuclease secreted from an insectivorous plant Dorsera adelae. Nucl. Acids Symposium Ser. 37, 127-128.
    • (1997) Nucl. Acids Symposium Ser. , vol.37 , pp. 127-128
    • Okabe, T.1    Mori, H.2    Ohyama, T.3
  • 24
    • 0031004496 scopus 로고    scopus 로고
    • A persistent double-strand break destabilizes human DNA in yeast and can lead to G2 arrest and lethality
    • Bennett, C.B., Snipe, J.R. & Resnick, M.A. (1997) A persistent double-strand break destabilizes human DNA in yeast and can lead to G2 arrest and lethality. Cancer Res. 57, 1970-1980.
    • (1997) Cancer Res. , vol.57 , pp. 1970-1980
    • Bennett, C.B.1    Snipe, J.R.2    Resnick, M.A.3
  • 25
    • 0032525333 scopus 로고    scopus 로고
    • The G2: Block induced by DNA damage; A caffeine-resistant component independent of Cdc25C, MPM-2 phosphorylation, and H1 kinase activity
    • Barratt, R.A., Kao, G., McKenna, W.G., Kuang, J. & Muschel, R.J. (1998) The G2: block induced by DNA damage; a caffeine-resistant component independent of Cdc25C, MPM-2 phosphorylation, and H1 kinase activity. Cancer Res. 58, 2639-2645.
    • (1998) Cancer Res. , vol.58 , pp. 2639-2645
    • Barratt, R.A.1    Kao, G.2    McKenna, W.G.3    Kuang, J.4    Muschel, R.J.5
  • 26
    • 0029682556 scopus 로고    scopus 로고
    • Mammalian DNA repair responses and genomic instability
    • ap-Rhys. C.M. & Bohr, V.A. (1996) Mammalian DNA repair responses and genomic instability. Experientia Supplementum 77, 289-305.
    • (1996) Experientia Supplementum , vol.77 , pp. 289-305
    • Ap-Rhys, C.M.1    Bohr, V.A.2
  • 27
    • 0032493889 scopus 로고    scopus 로고
    • Saccharomyces Ku 70, mer11/rad50 and RPA proteins regulate adaptation to G2/M arrest after DNA damage
    • Lee, S.E., Moore, J.K., Holmes, A., Umezu, K., Kolodner, R.D. & Haber, J.E. (1998) Saccharomyces Ku 70, mer11/rad50 and RPA proteins regulate adaptation to G2/M arrest after DNA damage. Cell 94, 399-409.
    • (1998) Cell , vol.94 , pp. 399-409
    • Lee, S.E.1    Moore, J.K.2    Holmes, A.3    Umezu, K.4    Kolodner, R.D.5    Haber, J.E.6
  • 28
    • 0029892120 scopus 로고    scopus 로고
    • Cell cycle-dependent cytotoxicity, G2/M phase arrest, and disruption of p34cdc2/cyclin B1 activity induced by doxorubicin in synchronized P388 cells
    • Ling, Y.H., el-Naggar, A.K., Priebe, W. & Perez-Soler, R. (1996) Cell cycle-dependent cytotoxicity, G2/M phase arrest, and disruption of p34cdc2/cyclin B1 activity induced by doxorubicin in synchronized P388 cells. Mol. Pharmacol. 49, 832-841.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 832-841
    • Ling, Y.H.1    El-Naggar, A.K.2    Priebe, W.3    Perez-Soler, R.4
  • 29
    • 0020564083 scopus 로고
    • Vaccinia virus induces cellular mRNA degradation
    • Rice, A.P. & Roberts, B.E. (1983) Vaccinia virus induces cellular mRNA degradation. J. Virol. 47, 529-539.
    • (1983) J. Virol. , vol.47 , pp. 529-539
    • Rice, A.P.1    Roberts, B.E.2
  • 30
    • 0022638725 scopus 로고
    • Identification and preliminary characterization of external membrane-bound nuclease activities in Mycoplasma pulmonis
    • Minion, F.C. & Goguen, J.D. (1986) Identification and preliminary characterization of external membrane-bound nuclease activities in Mycoplasma pulmonis. Infect. Immunol. 51, 352-354.
    • (1986) Infect. Immunol. , vol.51 , pp. 352-354
    • Minion, F.C.1    Goguen, J.D.2
  • 31
    • 0026084164 scopus 로고
    • In vitro mRNA degradation system to study the virion host shutoff function of herpes simplex virus
    • Krikorian, C.R. & Read, G.S. (1991) In vitro mRNA degradation system to study the virion host shutoff function of herpes simplex virus. J. Virol. 65, 112-122.
    • (1991) J. Virol. , vol.65 , pp. 112-122
    • Krikorian, C.R.1    Read, G.S.2
  • 32
    • 0019775161 scopus 로고
    • Epstein-Barr virus-induced deoxynuclease and reutilization of host-cell DNA degradation products in viral DNA replication
    • Feighny, R.J., Henry,B.E.I.I. & Pagano, J.S. (1981) Epstein-Barr virus-induced deoxynuclease and reutilization of host-cell DNA degradation products in viral DNA replication. Virology 115, 395-400.
    • (1981) Virology , vol.115 , pp. 395-400
    • Feighny, R.J.1    Henry, B.E.I.I.2    Pagano, J.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.