메뉴 건너뛰기




Volumn 215, Issue 2, 1998, Pages 291-301

Cloning and characterization of an actin-resistant DNase I-like endonuclease secreted by macrophages

Author keywords

Apoptosis; Gene family; Homolog

Indexed keywords

ACTIN; COMPLEMENTARY DNA; DEOXYRIBONUCLEASE I; ENDONUCLEASE; RECOMBINANT ENZYME;

EID: 0032581495     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00281-9     Document Type: Article
Times cited : (40)

References (33)
  • 1
    • 0030965491 scopus 로고    scopus 로고
    • Functional characterization of 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 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
  • 2
    • 77956929132 scopus 로고
    • Boyer, P.D. (Ed.), The Enzymes. Academic Press, New York
    • Bernardi, G., 1971. Spleen acid deoxyribonuclease. In: Boyer, P.D. (Ed.), The Enzymes. Academic Press, New York, Vol. 4, pp. 271-287.
    • (1971) Spleen Acid Deoxyribonuclease , vol.4 , pp. 271-287
    • Bernardi, G.1
  • 3
    • 0019332501 scopus 로고
    • The effect of divalent cations on the mode of action of DNase I: The initial reaction products produced from covalently closed circular DNA
    • Campbell, V.W., Jackson, D.A., 1980. The effect of divalent cations on the mode of action of DNase I: The initial reaction products produced from covalently closed circular DNA. J. Biol. Chem. 255, 3726-3735.
    • (1980) J. Biol. Chem. , vol.255 , pp. 3726-3735
    • Campbell, V.W.1    Jackson, D.A.2
  • 4
    • 0344077785 scopus 로고
    • Presence of two different desoxyribonucleodepolymerases in veal kidney
    • Cunningham, L., Laskowski, M., 1953. Presence of two different desoxyribonucleodepolymerases in veal kidney. Biochim. Biophys. Acta 11, 590-591.
    • (1953) Biochim. Biophys. Acta , vol.11 , pp. 590-591
    • Cunningham, L.1    Laskowski, M.2
  • 5
    • 0029244997 scopus 로고
    • Survival factors, intracellular signal transduction, and the activation of endonucleases in apoptosis
    • Eastman, A., 1995. Survival factors, intracellular signal transduction, and the activation of endonucleases in apoptosis. Semin. Cancer Biol. 6, 45-52.
    • (1995) Semin. Cancer Biol. , vol.6 , pp. 45-52
    • Eastman, A.1
  • 6
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari, M., Sakahira, H., Yokoyama, H., Okawa, K., Iwamatsu, A., Nagata, S., 1998. A caspase-activated DNase that degrades DNA during 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
  • 7
    • 0001789834 scopus 로고
    • Transient production of proteins using an adenovirus transformed cell line
    • Gorman, C.M., Gies, D.R., McCray, G., 1990. Transient production of proteins using an adenovirus transformed cell line. DNA Prot. Eng. Tech. 2, 3-10.
    • (1990) DNA Prot. Eng. Tech. , vol.2 , pp. 3-10
    • Gorman, C.M.1    Gies, D.R.2    McCray, G.3
  • 8
    • 0029994333 scopus 로고    scopus 로고
    • Systemic Lupus Erythematosus
    • Kotzin, B.L., 1996. Systemic Lupus Erythematosus. Cell 85, 303-306.
    • (1996) Cell , vol.85 , pp. 303-306
    • Kotzin, B.L.1
  • 9
    • 0023665902 scopus 로고
    • An analysis of 5 ·-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak, M., 1987. An analysis of 5 ·-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 15, 8125-8132.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8125-8132
    • Kozak, M.1
  • 10
    • 76549250377 scopus 로고
    • Crystalline desoxyribonuclease: Isolation and general properties; a spectrophotometric method for the measurement of desoxyribonuclease activity
    • Kunitz, M., 1950. Crystalline desoxyribonuclease: Isolation and general properties; a spectrophotometric method for the measurement of desoxyribonuclease activity. J. Gen. Physiol. 33, 349-362.
    • (1950) J. Gen. Physiol. , vol.33 , pp. 349-362
    • Kunitz, M.1
  • 11
    • 0019887828 scopus 로고
    • Deoxyribonuclease I in mammalian tissues: Specificity of inhibition by actin
    • Lacks, S.A., 1981. Deoxyribonuclease I in mammalian tissues: Specificity of inhibition by actin. J. Biol. Chem. 256, 2644-2648.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2644-2648
    • Lacks, S.A.1
  • 12
    • 77956933603 scopus 로고
    • Deoxyribonuclease I
    • Boyer, P.D. (Ed.), Academic Press, New York
    • Laskowski, M., 1971. Deoxyribonuclease I. In: Boyer, P.D. (Ed.), The Enzymes. Academic Press, New York, Vol. 4, pp. 289-311.
    • (1971) The Enzymes , vol.4 , pp. 289-311
    • Laskowski, M.1
  • 13
    • 0016361516 scopus 로고
    • Actin is the naturally occurring inhibitor of deoxyribonuclease I
    • Lazarides, E., Lindberg, U., 1974. Actin is the naturally occurring inhibitor of deoxyribonuclease I. Proc. Natl. Acad. Sci. USA 71, 4742-4746.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4742-4746
    • Lazarides, E.1    Lindberg, U.2
  • 14
    • 0000459041 scopus 로고
    • An optimized protocol for in situ hybridization using PCR-generated 33P-labeled riboprobes
    • Lu, L.H., Gillett, N.A., 1994. An optimized protocol for in situ hybridization using PCR-generated 33P-labeled riboprobes. Cell Vision 1, 169-176.
    • (1994) Cell Vision , vol.1 , pp. 169-176
    • Lu, L.H.1    Gillett, N.A.2
  • 15
    • 77956944804 scopus 로고
    • Pancreatic DNase
    • Boyer, P.D. (Ed.), Academic Press, New York
    • Moore, S., 1981. Pancreatic DNase. In: Boyer, P.D. (Ed.), The Enzymes. Academic Press, New York, Vol. 4, pp.281-296.
    • (1981) The Enzymes , vol.4 , pp. 281-296
    • Moore, S.1
  • 18
    • 0022993944 scopus 로고
    • Comparison of the three primary structures of deoxyribonuclease isolated from bovine, ovine and porcine pancreas
    • Paudel, H.K., Liao, T.-H., 1986. Comparison of the three primary structures of deoxyribonuclease isolated from bovine, ovine and porcine pancreas. J. Biol. Chem. 261, 16012-16017.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16012-16017
    • Paudel, H.K.1    Liao, T.-H.2
  • 19
    • 0028057478 scopus 로고
    • The apoptosis endonuclease: Cleaning up after cell death
    • Peitsch, M.C., Mannherz, H.G., Tschopp, J., 1994. The apoptosis endonuclease: cleaning up after cell death. Trends Cell Biol. 4, 37-41.
    • (1994) Trends Cell Biol. , vol.4 , pp. 37-41
    • Peitsch, M.C.1    Mannherz, H.G.2    Tschopp, J.3
  • 21
  • 22
    • 0031570688 scopus 로고    scopus 로고
    • Identification, localization, and expression of two novel human genes similar to deoxyribonuclease I
    • Rodriguez, A.M., Rodin, D., Nomura, H., Morton, C., Weremowicz, S., Schneider, M.C., 1997. Identification, localization, and expression of two novel human genes similar to deoxyribonuclease I. Genomics 42, 507-513.
    • (1997) Genomics , vol.42 , pp. 507-513
    • Rodriguez, A.M.1    Rodin, D.2    Nomura, H.3    Morton, C.4    Weremowicz, S.5    Schneider, M.C.6
  • 25
    • 0028868212 scopus 로고
    • Aerosoloized recombinant human DNase I for the treatment of cystic fibrosis
    • Shak, S., 1995. Aerosoloized recombinant human DNase I for the treatment of cystic fibrosis. Chest (suppl.) 107, 65-70.
    • (1995) Chest (Suppl.) , vol.107 , pp. 65-70
    • Shak, S.1
  • 26
    • 0028020636 scopus 로고
    • Colorimetric determination of DNase I activity with a DNA-methyl green substrate
    • Sinicropi, D., Baker, D.L., Prince, W.S., Shiffer, K., Shak, S., 1994. Colorimetric determination of DNase I activity with a DNA-methyl green substrate. Analyt. Biochem. 222, 351-358.
    • (1994) Analyt. Biochem. , vol.222 , pp. 351-358
    • Sinicropi, D.1    Baker, D.L.2    Prince, W.S.3    Shiffer, K.4    Shak, S.5
  • 27
    • 0028446567 scopus 로고
    • DNA recognition by DNase I
    • Suck, D., 1994. DNA recognition by DNase I. J. Mol. Recognit. 7, 65-70.
    • (1994) J. Mol. Recognit. , vol.7 , pp. 65-70
    • Suck, D.1
  • 30
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • von Heijne, G., 1983. Patterns of amino acids near signal-sequence cleavage sites. Eur. J. Biochem. 133, 17-21.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 17-21
    • Von Heijne, G.1
  • 31
    • 0342962801 scopus 로고
    • Structure of human pancreatic DNase at 2.2 Å resolution
    • Wolf, E., Frenz, J., Suck, D., 1995. Structure of human pancreatic DNase at 2.2 Å resolution. Prot. Eng. 8 (suppl), 79
    • (1995) Prot. Eng. , vol.8 , Issue.SUPPL. , pp. 79
    • Wolf, E.1    Frenz, J.2    Suck, D.3
  • 32
    • 0028990297 scopus 로고
    • Localization of deoxyribonuclease I gene transcripts and in rat tissues and its correlation with apoptotic cell elimination
    • Zanotti, S., Polzar, B., Stephan, H., Doll, U., Niessing, J., Mannherz, H.G., 1995. Localization of deoxyribonuclease I gene transcripts and in rat tissues and its correlation with apoptotic cell elimination. Histochemistry 103, 369-377.
    • (1995) Histochemistry , vol.103 , pp. 369-377
    • Zanotti, S.1    Polzar, B.2    Stephan, H.3    Doll, U.4    Niessing, J.5    Mannherz, H.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.