메뉴 건너뛰기




Volumn , Issue SUPPL.93, 2011, Pages

Endonucleases

Author keywords

DNA fragmentation; DNase I; Micrococcal nuclease; MNase; Mung bean nuclease; Next generation DNA sequencing

Indexed keywords

BAL 31 PROTEIN; DEOXYRIBONUCLEASE I; ENDONUCLEASE; ESTERASE; MICROCOCCAL NUCLEASE; NUCLEASE S1; UNCLASSIFIED DRUG; BAL 31 NUCLEASE; MUNG BEAN NUCLEASE;

EID: 79953272019     PISSN: 19343639     EISSN: 19343647     Source Type: Journal    
DOI: 10.1002/0471142727.mb0312s93     Document Type: Article
Times cited : (6)

References (16)
  • 1
    • 0000721357 scopus 로고
    • The purification and properties of micrococcal nuclease
    • Alexander, M., Heppel, L.A., and Hurwitz, J. 1961. The purification and properties of micrococcal nuclease. J. Biol. Chem. 236:3014-3019.
    • (1961) J. Biol. Chem. , vol.236 , pp. 3014-3019
    • Alexander, M.1    Heppel, L.A.2    Hurwitz, J.3
  • 2
    • 0019877035 scopus 로고
    • Shotgun DNA sequencing using cloned DNase I-generated fragments
    • Anderson, S. 1981. Shotgun DNA sequencing using cloned DNase I-generated fragments. Nucleic Acids Res. 9:3015-3027.
    • (1981) Nucleic Acids Res , vol.9 , pp. 3015-3027
    • Anderson, S.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. and 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
    • 0016766372 scopus 로고
    • Extracellular nucleases of Pseudomonas Bal 31 I. Characterization of single strand-specific deoxyriboendonuclease and doublestrand deoxyriboexonuclease activites
    • Gray, H.B., Ostrander, D.A., Hodnett, J.L., Legerski, R.J., and Robberson, D.L. 1975. Extracellular nucleases of Pseudomonas Bal 31. I. Characterization of single strand-specific deoxyriboendonuclease and doublestrand deoxyriboexonuclease activites. Nucleic Acids Res. 2:1459-1492.
    • (1975) Nucleic Acids Res , vol.2 , pp. 1459-1492
    • Gray, H.B.1    Ostrander, D.A.2    Hodnett, J.L.3    Legerski, R.J.4    Robberson, D.L.5
  • 5
    • 0019733080 scopus 로고
    • The extracellular nuclease from Alteromonas espejiana: An enzyme highly specific for nonduplex structure in nominally duplex DNAs
    • Structural Analysis of Nucleic Acids (J.G. Chirikjian and T.S. Papas, eds.) Elsevier/North Holland, New York
    • Gray, H.B., Winston, T.P., Hodnett, J.L., Legerski, R.J., Nees, D.W., Wei, C.-F., and Robberson, D.L. 1981. The extracellular nuclease from Alteromonas espejiana: An enzyme highly specific for nonduplex structure in nominally duplex DNAs. In Gene Amplification and Analysis, Vol. 2: Structural Analysis of Nucleic Acids (J.G. Chirikjian and T.S. Papas, eds.) pp. 169-203. Elsevier/North Holland, New York.
    • (1981) Gene Amplification and Analysis , vol.2 , pp. 169-203
    • Gray, H.B.1    Winston, T.P.2    Hodnett, J.L.3    Legerski, R.J.4    Nees, D.W.5    Wei, C.-F.6    Robberson, D.L.7
  • 6
    • 65449154418 scopus 로고    scopus 로고
    • Method for improving sequence coverage uniformity of targeted genomic intervals amplified by LR-PCR using Illumina GA sequencing-by-synthesis technology
    • Harismendy, O. and Frazer, K.A. 2009. Method for improving sequence coverage uniformity of targeted genomic intervals amplified by LR-PCR using Illumina GA sequencing-by-synthesis technology. BioTechniques 46:229-231.
    • (2009) BioTechniques , vol.46 , pp. 229-231
    • Harismendy, O.1    Frazer, K.A.2
  • 7
    • 0017331464 scopus 로고
    • Structure of chromatin
    • Kornberg, R.D. 1977. Structure of chromatin. Ann. Rev. Biochem. 46:931-954.
    • (1977) Ann. Rev. Biochem. , vol.46 , pp. 931-954
    • Kornberg, R.D.1
  • 8
    • 0017202381 scopus 로고
    • Mung bean nuclease I. Terminally directed hydrolysis of native DNA
    • Kroeker, W.D., Kowalski, D., and Laskowski, M. 1976. Mung bean nuclease I. Terminally directed hydrolysis of native DNA. Biochemistry 15:4463-4467.
    • (1976) Biochemistry , vol.15 , pp. 4463-4467
    • Kroeker, W.D.1    Kowalski, D.2    Laskowski, M.3
  • 9
    • 0018311913 scopus 로고
    • Extracellular nucleases of Alteromonas espejiana Bal 31 IV. The single strand-specific deoxyriboendonuclease activity as a probe for regions of staltered secondary structure in negatively and positively supercoiled closed circular DNA
    • Lau, P.P. and Gray, H.B. 1979. Extracellular nucleases of Alteromonas espejiana Bal 31. IV. The single strand-specific deoxyriboendonuclease activity as a probe for regions of staltered secondary structure in negatively and positively supercoiled closed circular DNA. Nucleic Acids Res. 6:331-357.
    • (1979) Nucleic Acids Res , vol.6 , pp. 331-357
    • Lau, P.P.1    Gray, H.B.2
  • 10
    • 0017650804 scopus 로고
    • A sensitive endonuclease probe for lesions in DNA helix structure produced by carcinogenic or mutagenic agents
    • Legerski, R.J., Gray, H.B., and Robberson, D.L. 1977. A sensitive endonuclease probe for lesions in DNA helix structure produced by carcinogenic or mutagenic agents. J. Biol. Chem. 252:8740-8746.
    • (1977) J. Biol. Chem. , vol.252 , pp. 8740-8746
    • Legerski, R.J.1    Gray, H.B.2    Robberson, D.L.3
  • 11
    • 0017848516 scopus 로고
    • Extracellular nucleases of Pseudomonas Bal 31 III. Use of the double-strand deoxyriboexonuclease activity as a basis of a convenient method for the mapping of fragments of DNA produced by cleavage with restriction enzymes
    • Legerski, R.J., Hodnett, J.L., and Gray, H.B. 1978. Extracellular nucleases of Pseudomonas Bal 31. III. Use of the double-strand deoxyriboexonuclease activity as a basis of a convenient method for the mapping of fragments of DNA produced by cleavage with restriction enzymes. Nucleic Acids Res. 5:1445-1464.
    • (1978) Nucleic Acids Res , vol.5 , pp. 1445-1464
    • Legerski, R.J.1    Hodnett, J.L.2    Gray, H.B.3
  • 12
    • 77956944804 scopus 로고
    • Pancreatic DNase
    • (P.D. Boyer, ed.) Academic Press, San Diego, California
    • Moore, S. 1981. Pancreatic DNase. In The Enzymes, Vol. 14A (P.D. Boyer, ed.) pp. 281-298. Academic Press, San Diego, California.
    • (1981) The Enzymes , vol.14 A , pp. 281-298
    • Moore, S.1
  • 13
    • 0041668072 scopus 로고    scopus 로고
    • Immunoprecipitation of native chromatin: NChIP
    • O'Neill, L.P. and Turner, B.M. 2003. Immunoprecipitation of native chromatin: NChIP. Methods 31:76-82.
    • (2003) Methods , vol.31 , pp. 76-82
    • O'Neill, L.P.1    Turner, B.M.2
  • 14
    • 0017191401 scopus 로고
    • An efficient mRNA-dependent translation system from reticulocyte lysates
    • Pelham, H.R.B. and Jackson, R.J. 1976. An efficient mRNA-dependent translation system from reticulocyte lysates. Eur. J. Biochem. 67:247-256.
    • (1976) Eur. J. Biochem. , vol.67 , pp. 247-256
    • Pelham, H.R.B.1    Jackson, R.J.2
  • 15
    • 0018846634 scopus 로고
    • Purification and properties of S1 nuclease from Aspergillus
    • Vogt, V.M. 1980. Purification and properties of S1 nuclease from Aspergillus. Methods Enzymol. 65:248-254.
    • (1980) Methods Enzymol , vol.65 , pp. 248-254
    • Vogt, V.M.1
  • 16
    • 0021112801 scopus 로고
    • Isolation and comparison of two molecular species of the Bal 31 nuclease from Alteromonas espejiana with distinct kinetic properties
    • Wei, C.-F., Alianell, G.A., Bencen, G.H., and Gray, H.B. 1983. Isolation and comparison of two molecular species of the Bal 31 nuclease from Alteromonas espejiana with distinct kinetic properties. J. Biol. Chem. 258:13506-13512.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13506-13512
    • Wei, C.-F.1    Alianell, G.A.2    Bencen, G.H.3    Gray, H.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.