메뉴 건너뛰기




Volumn 26, Issue 5, 2003, Pages 457-491

Single-strand-specific nucleases

Author keywords

Applications of nucleases; Enzymology; Nuclease; Nucleic acids; Reaction mechanism; Substrate specificity

Indexed keywords

8 QUINOLINOL; CITRIC ACID; CYCLOHEXIMIDE; DACTINOMYCIN; DEOXYRIBONUCLEASE; DIMETHYL SULFOXIDE; EDETIC ACID; EGTAZIC ACID; ENDONUCLEASE; EXONUCLEASE; FORMAMIDE; GLUTAMATE SODIUM; GLUTAMIC ACID; GLYCOPROTEIN; GLYOXAL; GUANOSINE PHOSPHATE; HOMOCYSTEIC ACID; INOSINE PHOSPHATE; N,N DIMETHYLFORMAMIDE; NUCLEIC ACID; OLIGONUCLEOTIDE; PHOSPHATASE; POLYNUCLEOTIDE; POTASSIUM CHLORIDE; RIBONUCLEASE T1; SINGLE STRANDED DNA; SODIUM CHLORIDE; SPERMIDINE; SPERMINE; UNINDEXED DRUG;

EID: 0037264483     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-6445(02)00129-8     Document Type: Review
Times cited : (152)

References (381)
  • 1
    • 84933357752 scopus 로고
    • Enzymatic decomposition of nucleic acids
    • Araki T. Enzymatic decomposition of nucleic acids. Z. Physiol. Chem. 38:1903;84-92.
    • (1903) Z. Physiol. Chem. , vol.38 , pp. 84-92
    • Araki, T.1
  • 2
    • 84931940972 scopus 로고
    • Crystalline ribonuclease
    • Kunitz M. Crystalline ribonuclease. J. Gen. Physiol. 24:1940;15-30.
    • (1940) J. Gen. Physiol. , vol.24 , pp. 15-30
    • Kunitz, M.1
  • 3
    • 76549250377 scopus 로고
    • Crystalline desoxyribonuclease. I. Isolation and general properties: Spectrophotometric method for the measurement of deoxyribonuclease activity
    • Kunitz M. Crystalline desoxyribonuclease. I. Isolation and general properties: spectrophotometric method for the measurement of deoxyribonuclease activity. J. Gen. Physiol. 33:1950;349-355.
    • (1950) J. Gen. Physiol. , vol.33 , pp. 349-355
    • Kunitz, M.1
  • 5
    • 0014162145 scopus 로고
    • DNases and their use in the studies of primary structure of nucleic acids
    • Laskowski M. Sr. DNases and their use in the studies of primary structure of nucleic acids. Adv. Enzymol. 29:1967;165-220.
    • (1967) Adv. Enzymol. , vol.29 , pp. 165-220
    • Laskowski M., Sr.1
  • 7
    • 0002014146 scopus 로고
    • Nucleases: Historical perspectives
    • Linn S.M. and Roberts, R.J., Eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Laskowski, M., Sr. (1985) Nucleases: historical perspectives. In: Nucleases (Linn S.M. and Roberts, R.J., Eds.), pp1-21. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1985) Nucleases , pp. 1-21
    • Laskowski, M.Sr.1
  • 8
    • 0000656815 scopus 로고
    • The deoxyribonucleases of Escherichia coli. I. Purification and properties of a phosphodiesterase
    • Lehman I.R. The deoxyribonucleases of Escherichia coli. I. Purification and properties of a phosphodiesterase. J. Biol. Chem. 235:1960;1479-1487.
    • (1960) J. Biol. Chem. , vol.235 , pp. 1479-1487
    • Lehman, I.R.1
  • 9
    • 0002571496 scopus 로고
    • Single-strand-specific nucleases
    • Linn S.M. and Roberts, R.J., Eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Shishido, K. and Ando, T. (1985) Single-strand-specific nucleases. In: Nucleases (Linn S.M. and Roberts, R.J., Eds.), pp. 155-185. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1985) Nucleases , pp. 155-185
    • Shishido, K.1    Ando, T.2
  • 10
    • 0021724702 scopus 로고
    • Structural specificities of five commonly used DNA nucleases
    • Drew H.R. Structural specificities of five commonly used DNA nucleases. J. Mol. Biol. 176:1984;535-557.
    • (1984) J. Mol. Biol. , vol.176 , pp. 535-557
    • Drew, H.R.1
  • 11
    • 0013076585 scopus 로고
    • Role of nucleases in genetic recombination
    • Linn S.M. and Roberts, R.J., Eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sadowski, P.D. (1985) Role of nucleases in genetic recombination. In: Nucleases (Linn S.M. and Roberts, R.J., Eds.), pp. 23-40. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1985) Nucleases , pp. 23-40
    • Sadowski, P.D.1
  • 12
    • 0013076586 scopus 로고
    • Nucleases involved in DNA repair
    • Linn S.M. and Roberts, R.J., Eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Linn, S. (1985) Nucleases involved in DNA repair. In: Nucleases (Linn S.M. and Roberts, R.J., Eds.), pp. 59-83. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1985) Nucleases , pp. 59-83
    • Linn, S.1
  • 13
    • 0002001031 scopus 로고
    • Nuclease activities involved in DNA replication
    • Linn S.M. and Roberts, R.J., Eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Brown, D.R., Hurwitz, J., Reinberg, D. and Zipursky, S.L. (1985) Nuclease activities involved in DNA replication. In: Nucleases (Linn S.M. and Roberts, R.J., Eds.), pp. 187-209. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1985) Nucleases , pp. 187-209
    • Brown, D.R.1    Hurwitz, J.2    Reinberg, D.3    Zipursky, S.L.4
  • 14
    • 0013131179 scopus 로고
    • Studies on the autolysis of Aspergillus oryzae. Part V. Purification of an intracellular new nuclease
    • Uozumi T., Tamura G., Arima K. Studies on the autolysis of Aspergillus oryzae. Part V. Purification of an intracellular new nuclease. Agric. Biol. Chem. 33:1969;25-30.
    • (1969) Agric. Biol. Chem. , vol.33 , pp. 25-30
    • Uozumi, T.1    Tamura, G.2    Arima, K.3
  • 15
    • 84948628876 scopus 로고
    • Studies on 5′-phosphodiesterases in microorganisms. Part II. Properties and application of Penicillium citrinum 5′-phosphodiaesterase
    • Kuninaka A., Kibi M., Yoshino H., Sakaguchi K. Studies on 5′-phosphodiesterases in microorganisms. Part II. Properties and application of Penicillium citrinum 5′-phosphodiaesterase. Agric. Biol. Chem. 25:1961;693-701.
    • (1961) Agric. Biol. Chem. , vol.25 , pp. 693-701
    • Kuninaka, A.1    Kibi, M.2    Yoshino, H.3    Sakaguchi, K.4
  • 16
    • 0016766372 scopus 로고
    • Extracellular nucleases of Pseudomonas BAL 31. I. Characterization of single-strand-specific deoxyriboendonuclease and double-strand deoxyriboexonuclease activities
    • Gray H.B. Jr., Ostrander D.A., Hodnett J.L., Legerski R.J., Robberson D.L. Extracellular nucleases of Pseudomonas BAL 31. I. Characterization of single-strand-specific deoxyriboendonuclease and double-strand deoxyriboexonuclease activities. Nucleic Acids Res. 2:1975;1459-1492.
    • (1975) Nucleic Acids Res. , vol.2 , pp. 1459-1492
    • Gray H.B., Jr.1    Ostrander, D.A.2    Hodnett, J.L.3    Legerski, R.J.4    Robberson, D.L.5
  • 17
    • 0032145316 scopus 로고    scopus 로고
    • Serratia marcescens and its extracellular nuclease
    • Benedik M.J., Strych U. Serratia marcescens and its extracellular nuclease. FEMS Microbiol. Lett. 165:1998;1-13.
    • (1998) FEMS Microbiol. Lett. , vol.165 , pp. 1-13
    • Benedik, M.J.1    Strych, U.2
  • 18
    • 0017847689 scopus 로고
    • Purification and properties of an extracellular exonuclease from Thermus thermophilus HB8
    • Takahashi M., Uchida T. Purification and properties of an extracellular exonuclease from Thermus thermophilus HB8. J. Biochem. (Tokyo). 83:1978;1521-1532.
    • (1978) J. Biochem. (Tokyo) , vol.83 , pp. 1521-1532
    • Takahashi, M.1    Uchida, T.2
  • 19
    • 0026746322 scopus 로고
    • Identification, genetic analysis and characterization of a sugar-non-specific nuclease from the cyanobacterium Anabaena sp. PCC 7120
    • Muro-Pastor A.M., Flores E., Herrero A., Wolk C.P. Identification, genetic analysis and characterization of a sugar-non-specific nuclease from the cyanobacterium Anabaena sp. PCC 7120. Mol. Microbiol. 6:1992;3021-3030.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3021-3030
    • Muro-Pastor, A.M.1    Flores, E.2    Herrero, A.3    Wolk, C.P.4
  • 20
    • 0033877124 scopus 로고    scopus 로고
    • Purification and characterization of the single-strand-specific and guanylic-acid-preferential deoxyribonuclease activity of the extracellular nuclease from Basidiobolus haptosporus
    • Desai N.A., Shankar V. Purification and characterization of the single-strand-specific and guanylic-acid-preferential deoxyribonuclease activity of the extracellular nuclease from Basidiobolus haptosporus. Eur. J. Biochem. 267:2000;5123-5135.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5123-5135
    • Desai, N.A.1    Shankar, V.2
  • 21
    • 0013891499 scopus 로고
    • Cellular site in Bacillus subtilis of a nuclease which preferentially degrades single-stranded nucleic acids
    • Birnboim H.C. Cellular site in Bacillus subtilis of a nuclease which preferentially degrades single-stranded nucleic acids. J. Bacteriol. 91:1966;1004-1011.
    • (1966) J. Bacteriol. , vol.91 , pp. 1004-1011
    • Birnboim, H.C.1
  • 22
    • 0020641335 scopus 로고
    • Intracellular localization of Neurospora crassa endo-exonuclease and its putative precursor
    • Fraser M.J., Cohen H. Intracellular localization of Neurospora crassa endo-exonuclease and its putative precursor. J. Bacteriol. 154:1983;460-470.
    • (1983) J. Bacteriol. , vol.154 , pp. 460-470
    • Fraser, M.J.1    Cohen, H.2
  • 23
  • 26
    • 0018784235 scopus 로고
    • Purification of an alkaline nucleases from Physarum polycephalum
    • Waterborg J.H., Kuyper C.M. Purification of an alkaline nucleases from Physarum polycephalum. Biochim. Biophys. Acta. 571:1979;359-367.
    • (1979) Biochim. Biophys. Acta , vol.571 , pp. 359-367
    • Waterborg, J.H.1    Kuyper, C.M.2
  • 27
    • 0019888072 scopus 로고
    • Studies on nuclease α from Ustilago maydis
    • Holloman W.K., Rowe T.C., Rusche J.R. Studies on nuclease α from Ustilago maydis. J. Biol. Chem. 256:1981;5087-5094.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5087-5094
    • Holloman, W.K.1    Rowe, T.C.2    Rusche, J.R.3
  • 28
    • 0019321660 scopus 로고
    • Purification and characterization of nuclease β from Ustilago maydis
    • Rusche J.R., Rowe T.C., Holloman W.K. Purification and characterization of nuclease β from Ustilago maydis. J. Biol. Chem. 255:1980;9117-9123.
    • (1980) J. Biol. Chem. , vol.255 , pp. 9117-9123
    • Rusche, J.R.1    Rowe, T.C.2    Holloman, W.K.3
  • 29
    • 0021367541 scopus 로고
    • Purification and properties of nuclease γ from Ustilago maydis
    • Yarnall M., Rowe T.C., Holloman W.K. Purification and properties of nuclease γ from Ustilago maydis. J. Biol. Chem. 259:1984;3026-3032.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3026-3032
    • Yarnall, M.1    Rowe, T.C.2    Holloman, W.K.3
  • 30
    • 0013169249 scopus 로고
    • Purification and general properties of a nuclease from the fruit body of Flammulina velutipes
    • Kurosawa S., Kawai T., Akahane N., Sen K. Purification and general properties of a nuclease from the fruit body of Flammulina velutipes. Agric. Biol. Chem. 54:1990;2733-2735.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 2733-2735
    • Kurosawa, S.1    Kawai, T.2    Akahane, N.3    Sen, K.4
  • 31
    • 0023758622 scopus 로고
    • Purification and characterization of an endonuclease from fruiting caps of basidiomycete Coprinus cinereus
    • Lu B.C., Wong W., Fanning L., Sakaguchi K. Purification and characterization of an endonuclease from fruiting caps of basidiomycete Coprinus cinereus. Eur. J. Biochem. 174:1988;725-732.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 725-732
    • Lu, B.C.1    Wong, W.2    Fanning, L.3    Sakaguchi, K.4
  • 32
    • 0026003327 scopus 로고
    • Purification and characterization of a nuclease from Lentinus edodes
    • Shimada H., Inokuchi N., Koyama T., Irie M. Purification and characterization of a nuclease from Lentinus edodes. Chem. Pharm. Bull. 39:1991;2633-2637.
    • (1991) Chem. Pharm. Bull. , vol.39 , pp. 2633-2637
    • Shimada, H.1    Inokuchi, N.2    Koyama, T.3    Irie, M.4
  • 34
    • 0018864891 scopus 로고
    • Single-strand-specific nuclease from the nucleoplasm of rye germ nuclei
    • Przykorska A.N., Szarkowski J.W. Single-strand-specific nuclease from the nucleoplasm of rye germ nuclei. Eur. J. Biochem. 108:1980;285-294.
    • (1980) Eur. J. Biochem. , vol.108 , pp. 285-294
    • Przykorska, A.N.1    Szarkowski, J.W.2
  • 35
    • 38249032573 scopus 로고
    • Purification and properties of endonuclease from wheat chloroplasts, specific for single-stranded DNA
    • Kuligowska E., Klarkowska D., Szarkowski J.W. Purification and properties of endonuclease from wheat chloroplasts, specific for single-stranded DNA. Phytochemistry. 27:1988;1275-1279.
    • (1988) Phytochemistry , vol.27 , pp. 1275-1279
    • Kuligowska, E.1    Klarkowska, D.2    Szarkowski, J.W.3
  • 36
    • 0028026215 scopus 로고
    • A single-strand-specific nuclease from a fraction of wheat chloroplast stromal protein
    • Monko M., Kuligowaska E., Szarkowaski J.W. A single-strand-specific nuclease from a fraction of wheat chloroplast stromal protein. Phytochemistry. 37:1994;301-305.
    • (1994) Phytochemistry , vol.37 , pp. 301-305
    • Monko, M.1    Kuligowaska, E.2    Szarkowaski, J.W.3
  • 37
    • 0030458873 scopus 로고    scopus 로고
    • Separation and purification of both acid and neutral nucleases from germinated alfalfa seeds
    • Yupsanis T., Eleftheriou P., Kelepiri Z. Separation and purification of both acid and neutral nucleases from germinated alfalfa seeds. Plant Physiol. 149:1996;641-649.
    • (1996) Plant Physiol. , vol.149 , pp. 641-649
    • Yupsanis, T.1    Eleftheriou, P.2    Kelepiri, Z.3
  • 39
    • 38249022022 scopus 로고
    • Partial purification and properties of a chromatin-bound deoxyribonuclease from the embryo axes of germinating pea
    • Weir A.F., Bryant J.A. Partial purification and properties of a chromatin-bound deoxyribonuclease from the embryo axes of germinating pea. Phytochemistry. 28:1989;1339-1343.
    • (1989) Phytochemistry , vol.28 , pp. 1339-1343
    • Weir, A.F.1    Bryant, J.A.2
  • 40
    • 0016282398 scopus 로고
    • An extracellular nuclease from suspension culture of tobacco
    • Oleson A.E., Janski A.M., Clark E.T. An extracellular nuclease from suspension culture of tobacco. Biochim. Biophys. Acta. 366:1974;89-100.
    • (1974) Biochim. Biophys. Acta , vol.366 , pp. 89-100
    • Oleson, A.E.1    Janski, A.M.2    Clark, E.T.3
  • 41
    • 0015239311 scopus 로고
    • Isolation from avena leaf tissues of a nuclease with the same type of specificity towards RNA and DNA: Accumulation of the enzyme during leaf senescence
    • Wyen N.V., Erdei S., Farkas G.L. Isolation from avena leaf tissues of a nuclease with the same type of specificity towards RNA and DNA: accumulation of the enzyme during leaf senescence. Biochim. Biophys. Acta. 232:1971;472-483.
    • (1971) Biochim. Biophys. Acta , vol.232 , pp. 472-483
    • Wyen, N.V.1    Erdei, S.2    Farkas, G.L.3
  • 42
    • 0024297013 scopus 로고
    • Nuclease SP: A novel enzyme from spinach that incises damaged duplex DNA preferentially at site of adenine
    • Doetsch P.W., McCray W.H. Jr., Lee K., Bettler D.R., Valenzuela M.R.L. Nuclease SP: a novel enzyme from spinach that incises damaged duplex DNA preferentially at site of adenine. Nucleic Acids Res. 16:1988;6935-6952.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6935-6952
    • Doetsch, P.W.1    McCray W.H., Jr.2    Lee, K.3    Bettler, D.R.4    Valenzuela, M.R.L.5
  • 43
    • 0000848004 scopus 로고
    • Purification and characterization of nucleases from tea leaves
    • Imagawa H., Toryu H., Ozawa T., Takino Y. Purification and characterization of nucleases from tea leaves. Agric. Biol. Chem. 46:1982;1261-1269.
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 1261-1269
    • Imagawa, H.1    Toryu, H.2    Ozawa, T.3    Takino, Y.4
  • 44
    • 0001161168 scopus 로고
    • A nuclease from mung bean sprouts
    • Sung S.-C., Laskowski M. Sr. A nuclease from mung bean sprouts. J. Biol. Chem. 237:1962;506-511.
    • (1962) J. Biol. Chem. , vol.237 , pp. 506-511
    • Sung, S.-C.1    Laskowski M., Sr.2
  • 45
    • 0018501867 scopus 로고
    • Partial purification and properties of an endonuclease from germinating pea seeds, specific for single-stranded DNA
    • Wani A.A., Hadi S.M. Partial purification and properties of an endonuclease from germinating pea seeds, specific for single-stranded DNA. Arch. Biochem. Biophys. 196:1979;138-146.
    • (1979) Arch. Biochem. Biophys. , vol.196 , pp. 138-146
    • Wani, A.A.1    Hadi, S.M.2
  • 46
    • 0001879917 scopus 로고
    • Chromatin-associated nucleases of germinating barley
    • Yupsanis T., Georgatsos J.B. Chromatin-associated nucleases of germinating barley. Int. J. Biochem. 15:1983;959-963.
    • (1983) Int. J. Biochem. , vol.15 , pp. 959-963
    • Yupsanis, T.1    Georgatsos, J.B.2
  • 47
    • 0015164647 scopus 로고
    • Studies on 3′-nucleotidase-nuclease from potato tubers. I. Purification and some properties of the enzyme
    • Nomura A., Suno M., Mizuno Y. Studies on 3′-nucleotidase-nuclease from potato tubers. I. Purification and some properties of the enzyme. J. Biochem. (Tokyo). 70:1971;993-1001.
    • (1971) J. Biochem. (Tokyo) , vol.70 , pp. 993-1001
    • Nomura, A.1    Suno, M.2    Mizuno, Y.3
  • 48
    • 0002539368 scopus 로고
    • Purification and properties of extracellular nuclease from tobacco pollen
    • Matousek J., Tupy J. Purification and properties of extracellular nuclease from tobacco pollen. Biol. Plant. 26:1984;62-73.
    • (1984) Biol. Plant. , vol.26 , pp. 62-73
    • Matousek, J.1    Tupy, J.2
  • 49
    • 0000874797 scopus 로고
    • Isolation and partial characterization of an extracellular nuclease from pollen of Petunia hybrida
    • Van der Westhuizen A.J., Gliemeroth A.K., Wenzel W., Hess D. Isolation and partial characterization of an extracellular nuclease from pollen of Petunia hybrida. J. Plant. Physiol. 131:1987;373-384.
    • (1987) J. Plant. Physiol. , vol.131 , pp. 373-384
    • Van der Westhuizen, A.J.1    Gliemeroth, A.K.2    Wenzel, W.3    Hess, D.4
  • 50
    • 0021341229 scopus 로고
    • Surface membrane localization of 3′- and 5′-nucleotidase activities in Leishmania donovani promastigotes
    • Dwyer D.M., Gottlieb M. Surface membrane localization of 3′- and 5′-nucleotidase activities in Leishmania donovani promastigotes. Mol. Biochem. Parasitol. 10:1984;139-150.
    • (1984) Mol. Biochem. Parasitol. , vol.10 , pp. 139-150
    • Dwyer, D.M.1    Gottlieb, M.2
  • 51
    • 0024021390 scopus 로고
    • Crithidia luciliae: Factors affecting the expression of 3′-nucleotidase/nuclease activity
    • Gottlieb M., Mackow M.C., Neubert T.A. Crithidia luciliae: factors affecting the expression of 3′-nucleotidase/nuclease activity. Exp. Parasitol. 66:1988;108-117.
    • (1988) Exp. Parasitol. , vol.66 , pp. 108-117
    • Gottlieb, M.1    Mackow, M.C.2    Neubert, T.A.3
  • 52
    • 0022994969 scopus 로고
    • A nicking enzyme from trypanosomatids which specifically affects the topological linking of duplex DNA circles: Purification and characterization
    • Shlomai J., Linial M. A nicking enzyme from trypanosomatids which specifically affects the topological linking of duplex DNA circles: purification and characterization. J. Biol. Chem. 261:1986;16219-16225.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16219-16225
    • Shlomai, J.1    Linial, M.2
  • 53
    • 0026509755 scopus 로고
    • Purification and characterization of an endo-exonuclease from adult flies of Drosophila melanogaster
    • Shuai K., Das Gupta C.K., Hawley R.S., Chase J.W., Stone K.L., Williams K.R. Purification and characterization of an endo-exonuclease from adult flies of Drosophila melanogaster. Nucleic Acids Res. 20:1992;1379-1385.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1379-1385
    • Shuai, K.1    Das Gupta, C.K.2    Hawley, R.S.3    Chase, J.W.4    Stone, K.L.5    Williams, K.R.6
  • 54
    • 0014081271 scopus 로고
    • Sheep kidney nuclease: Hydrolysis of tRNA
    • Kasai K., Grunberg-Manago M. Sheep kidney nuclease: hydrolysis of tRNA. Eur. J. Biochem. 1:1967;152-163.
    • (1967) Eur. J. Biochem. , vol.1 , pp. 152-163
    • Kasai, K.1    Grunberg-Manago, M.2
  • 56
    • 0016703877 scopus 로고
    • Purification and characterization of a major endonuclease from rat liver nuclei
    • Cordis G.A., Goldblatt P.-J., Deutscher M. Purification and characterization of a major endonuclease from rat liver nuclei. Biochemistry. 14:1975;2596-2603.
    • (1975) Biochemistry , vol.14 , pp. 2596-2603
    • Cordis, G.A.1    Goldblatt, P.-J.2    Deutscher, M.3
  • 57
    • 0021099832 scopus 로고
    • +2-dependent/poly(ADP-ribose)-sensitive endonuclease
    • +2-dependent/poly(ADP-ribose)-sensitive endonuclease. J. Biol. Chem. 258:1983;9184-9191.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9184-9191
    • Tanigawa, Y.1    Shimoyama, M.2
  • 58
    • 0022977126 scopus 로고
    • Purification and properties of single-strand specific endonuclease from mouse cell mitochondria
    • Tomkinson A.E., Linn S. Purification and properties of single-strand specific endonuclease from mouse cell mitochondria. Nucleic Acids Res. 14:1986;9579-9593.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 9579-9593
    • Tomkinson, A.E.1    Linn, S.2
  • 59
    • 0007778422 scopus 로고
    • Rapid method for determining the activity of microorganisms on nucleic acids
    • Jefferies C.D., Holtman D.F., Guse D.G. Rapid method for determining the activity of microorganisms on nucleic acids. J. Bacteriol. 73:1957;590-591.
    • (1957) J. Bacteriol. , vol.73 , pp. 590-591
    • Jefferies, C.D.1    Holtman, D.F.2    Guse, D.G.3
  • 60
    • 0015245950 scopus 로고
    • Deoxyribonuclease: A sensitive assay using radial diffusion in agarose containing methyl green-DNA complex
    • Horney D.L., Webster D.A. Deoxyribonuclease: a sensitive assay using radial diffusion in agarose containing methyl green-DNA complex. Biochim. Biophys. Acta. 247:1971;54-61.
    • (1971) Biochim. Biophys. Acta , vol.247 , pp. 54-61
    • Horney, D.L.1    Webster, D.A.2
  • 61
    • 0002705905 scopus 로고
    • Identification of deoxyribonucleases in polyacrylamide gel following their separation by disk electrophoresis
    • Boyd J.B., Mitchell H.K. Identification of deoxyribonucleases in polyacrylamide gel following their separation by disk electrophoresis. Anal. Biochem. 13:1965;28-42.
    • (1965) Anal. Biochem. , vol.13 , pp. 28-42
    • Boyd, J.B.1    Mitchell, H.K.2
  • 62
    • 0017401236 scopus 로고
    • Nuclease detection in SDS-polyacrylamide gel electrophoresis
    • Rosenthal A.L., Lacks S.A. Nuclease detection in SDS-polyacrylamide gel electrophoresis. Anal. Biochem. 80:1977;76-90.
    • (1977) Anal. Biochem. , vol.80 , pp. 76-90
    • Rosenthal, A.L.1    Lacks, S.A.2
  • 63
    • 0022578931 scopus 로고
    • A sensitive staining technique for the detection of phosphohydrolase activities after polyacrylamide gel electrophoresis
    • Zlotnick G.W., Gottlieb M. A sensitive staining technique for the detection of phosphohydrolase activities after polyacrylamide gel electrophoresis. Anal. Biochem. 153:1986;121-125.
    • (1986) Anal. Biochem. , vol.153 , pp. 121-125
    • Zlotnick, G.W.1    Gottlieb, M.2
  • 65
    • 0014047917 scopus 로고
    • The isolation and subunit structure of Streptococcal membrane adenosine triphosphatase
    • Abrams A., Baron C. The isolation and subunit structure of Streptococcal membrane adenosine triphosphatase. Biochemistry. 6:1967;225-229.
    • (1967) Biochemistry , vol.6 , pp. 225-229
    • Abrams, A.1    Baron, C.2
  • 66
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske C.H., Subbarow Y. The colorimetric determination of phosphorus. J. Biol. Chem. 66:1925;375-400.
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 67
    • 0017288235 scopus 로고
    • The subcellular distribution and properties of Crithidia sp. hydrolases with particular reference to pyrophosphate and orthophosphate monoester phosphohydrolases
    • McLaughlin J., Injeyan H.S., Meerovitch E. The subcellular distribution and properties of Crithidia sp. hydrolases with particular reference to pyrophosphate and orthophosphate monoester phosphohydrolases. Can. J. Biochem. 54:1976;365-381.
    • (1976) Can. J. Biochem. , vol.54 , pp. 365-381
    • McLaughlin, J.1    Injeyan, H.S.2    Meerovitch, E.3
  • 68
    • 0000283876 scopus 로고
    • Viscometric determination of thymonucleodepolymerase
    • Laskowski M. Sr., Seidel M.D. Viscometric determination of thymonucleodepolymerase. Arch. Biochem. 7:1945;465-472.
    • (1945) Arch. Biochem. , vol.7 , pp. 465-472
    • Laskowski M., Sr.1    Seidel, M.D.2
  • 69
    • 0001523067 scopus 로고
    • Intracellular distribution of enzymes. X. Desoxyribonuclease and ribonuclease
    • Schneider W.C., Hogeboom G.H. Intracellular distribution of enzymes. X. Desoxyribonuclease and ribonuclease. J. Biol. Chem. 198:1952;155-163.
    • (1952) J. Biol. Chem. , vol.198 , pp. 155-163
    • Schneider, W.C.1    Hogeboom, G.H.2
  • 70
    • 0016186237 scopus 로고
    • Purification of a nuclease from Penicillium citrinum
    • Fujimoto M., Kuninaka A., Yoshino H. Purification of a nuclease from Penicillium citrinum. Agric. Biol. Chem. 38:1974;777-783.
    • (1974) Agric. Biol. Chem. , vol.38 , pp. 777-783
    • Fujimoto, M.1    Kuninaka, A.2    Yoshino, H.3
  • 71
    • 0015924086 scopus 로고
    • Purification and further properties of single-strand-specific nuclease from Aspergillus oryzae
    • Vogt V.M. Purification and further properties of single-strand-specific nuclease from Aspergillus oryzae. Eur. J. Biochem. 33:1973;192-200.
    • (1973) Eur. J. Biochem. , vol.33 , pp. 192-200
    • Vogt, V.M.1
  • 73
  • 74
    • 0001625396 scopus 로고
    • A simple assay for DNA endonucleases
    • Geiduschek E.P., Daniels A. A simple assay for DNA endonucleases. Anal. Biochem. 11:1965;133-136.
    • (1965) Anal. Biochem. , vol.11 , pp. 133-136
    • Geiduschek, E.P.1    Daniels, A.2
  • 75
    • 0030571045 scopus 로고    scopus 로고
    • A quantitative microtiter plate nuclease assay based on ethidium/DNA fluorescence
    • Friedhoff P., Matzen S.E., Meiss G., Pingoud A. A quantitative microtiter plate nuclease assay based on ethidium/DNA fluorescence. Anal. Biochem. 240:1996;283-288.
    • (1996) Anal. Biochem. , vol.240 , pp. 283-288
    • Friedhoff, P.1    Matzen, S.E.2    Meiss, G.3    Pingoud, A.4
  • 76
    • 0022501019 scopus 로고
    • Quantitation of single- and double-strand DNA breaks in vitro and in vivo
    • Kohen R., Szyf M., Chevion M. Quantitation of single- and double-strand DNA breaks in vitro and in vivo. Anal. Biochem. 154:1986;485-491.
    • (1986) Anal. Biochem. , vol.154 , pp. 485-491
    • Kohen, R.1    Szyf, M.2    Chevion, M.3
  • 78
    • 0024967726 scopus 로고
    • Partial purification and characterization of an endonuclease from spinach that cleaves ultraviolet light-damaged duplex DNA
    • Doetsch P.W., McGray W.H. Jr., Valenzuela M.R. Partial purification and characterization of an endonuclease from spinach that cleaves ultraviolet light-damaged duplex DNA. Biochim. Biophys. Acta. 1007:1989;309-317.
    • (1989) Biochim. Biophys. Acta , vol.1007 , pp. 309-317
    • Doetsch, P.W.1    McGray W.H., Jr.2    Valenzuela, M.R.3
  • 79
    • 0022871114 scopus 로고
    • Conformational analysis of hairpin oligodeoxyribonucleotides by a single-strand-specific nuclease
    • Baumann U., Frank R., Blöcker H. Conformational analysis of hairpin oligodeoxyribonucleotides by a single-strand-specific nuclease. Eur. J. Biochem. 161:1986;409-413.
    • (1986) Eur. J. Biochem. , vol.161 , pp. 409-413
    • Baumann, U.1    Frank, R.2    Blöcker, H.3
  • 80
    • 17044442114 scopus 로고    scopus 로고
    • AFM characterization of single-strand-specific endonuclease activity on linear DNA
    • Umemura K., Nagami F., Okada T., Kuroda R. AFM characterization of single-strand-specific endonuclease activity on linear DNA. Nucleic Acids Res. 28:2000;E39.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 39
    • Umemura, K.1    Nagami, F.2    Okada, T.3    Kuroda, R.4
  • 81
    • 0019227024 scopus 로고
    • S1 nuclease of Aspergillus oryzae: A glycoprotein with an associated nucleotidase activity
    • Oleson A.E., Sasakuma M. S1 nuclease of Aspergillus oryzae: a glycoprotein with an associated nucleotidase activity. Arch. Biochem. Biophys. 204:1980;361-370.
    • (1980) Arch. Biochem. Biophys. , vol.204 , pp. 361-370
    • Oleson, A.E.1    Sasakuma, M.2
  • 82
    • 0014406173 scopus 로고
    • The nucleases of yeast. II. Purification, properties and specificity of an endonuclease from yeast
    • Lee S.Y., Nakao Y., Bock R.M. The nucleases of yeast. II. Purification, properties and specificity of an endonuclease from yeast. Biochim. Biophys. Acta. 151:1968;126-136.
    • (1968) Biochim. Biophys. Acta , vol.151 , pp. 126-136
    • Lee, S.Y.1    Nakao, Y.2    Bock, R.M.3
  • 83
    • 0017841706 scopus 로고
    • Studies on sheep kidney nuclease. I. An improved purification method and some properties
    • Watanabe T., Kasai K. Studies on sheep kidney nuclease. I. An improved purification method and some properties. Biochim. Biophys. Acta. 520:1978;52-60.
    • (1978) Biochim. Biophys. Acta , vol.520 , pp. 52-60
    • Watanabe, T.1    Kasai, K.2
  • 84
    • 0015244458 scopus 로고
    • A crude nuclease preparation suitable for use in DNA reassociation experiments
    • Sutton W.D. A crude nuclease preparation suitable for use in DNA reassociation experiments. Biochim. Biophys. Acta. 240:1971;522-531.
    • (1971) Biochim. Biophys. Acta , vol.240 , pp. 522-531
    • Sutton, W.D.1
  • 85
    • 0017072588 scopus 로고
    • Elimination of double strand nuclease activity from S1 nuclease prepared from crude α amylase
    • Hahn W.E., Van Ness J. Elimination of double strand nuclease activity from S1 nuclease prepared from crude α amylase. Nucleic Acids Res. 3:1976;1419-1423.
    • (1976) Nucleic Acids Res. , vol.3 , pp. 1419-1423
    • Hahn, W.E.1    Van Ness, J.2
  • 86
    • 0014952454 scopus 로고
    • Further purification and properties of phosphodiesterase from carrot
    • Harvey C.L., Olson K.C., Wright R. Further purification and properties of phosphodiesterase from carrot. Biochemistry. 9:1970;921-925.
    • (1970) Biochemistry , vol.9 , pp. 921-925
    • Harvey, C.L.1    Olson, K.C.2    Wright, R.3
  • 87
    • 0015420598 scopus 로고
    • Purification and properties of an endonuclease from Chlamydomonas
    • Small G.D., Sparks R.B. Jr. Purification and properties of an endonuclease from Chlamydomonas. Arch. Biochem. Biophys. 153:1972;171-179.
    • (1972) Arch. Biochem. Biophys. , vol.153 , pp. 171-179
    • Small, G.D.1    Sparks R.B., Jr.2
  • 88
    • 0023359487 scopus 로고
    • Single-strand-specific nuclease of pea seeds: Glycoprotein nature and associated nucleotidase activity
    • Naseem I., Hadi S.M. Single-strand-specific nuclease of pea seeds: glycoprotein nature and associated nucleotidase activity. Arch. Biochem. Biophys. 255:1987;437-445.
    • (1987) Arch. Biochem. Biophys. , vol.255 , pp. 437-445
    • Naseem, I.1    Hadi, S.M.2
  • 90
    • 0016592665 scopus 로고
    • Purification of S1 nuclease from Takadiastase by affinity chromatography on single-stranded DNA-acrylamide columns
    • Slor H. Purification of S1 nuclease from Takadiastase by affinity chromatography on single-stranded DNA-acrylamide columns. Nucleic Acids Res. 2:1975;587-593.
    • (1975) Nucleic Acids Res. , vol.2 , pp. 587-593
    • Slor, H.1
  • 91
    • 0021100135 scopus 로고
    • Purification and properties of single strand DNA-binding endo-exonuclease of Neurospora crassa
    • Chow T.Y., Fraser M.J. Purification and properties of single strand DNA-binding endo-exonuclease of Neurospora crassa. J. Biol. Chem. 258:1983;12010-12018.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12010-12018
    • Chow, T.Y.1    Fraser, M.J.2
  • 92
    • 0020358901 scopus 로고
    • Purification and characteristics of a mitochondrial endonuclease from the yeast Saccharomyces cerevisiae
    • von Tigerstrom R.G. Purification and characteristics of a mitochondrial endonuclease from the yeast Saccharomyces cerevisiae. Biochemistry. 21:1982;6397-6403.
    • (1982) Biochemistry , vol.21 , pp. 6397-6403
    • Von Tigerstrom, R.G.1
  • 93
    • 0022534837 scopus 로고
    • Partial purification and properties of a nuclease from Schizophyllum commune with a preference toward single-stranded nucleic acid
    • Martin S.A., Ullrich R.C., Meyer W.L. Partial purification and properties of a nuclease from Schizophyllum commune with a preference toward single-stranded nucleic acid. Biochim. Biophys. Acta. 867:1986;67-75.
    • (1986) Biochim. Biophys. Acta , vol.867 , pp. 67-75
    • Martin, S.A.1    Ullrich, R.C.2    Meyer, W.L.3
  • 94
    • 0023656318 scopus 로고
    • Biochemical properties and hormonal regulation of barley nuclease
    • Brown P.H., Ho T.H. Biochemical properties and hormonal regulation of barley nuclease. Eur. J. Biochem. 168:1987;357-364.
    • (1987) Eur. J. Biochem. , vol.168 , pp. 357-364
    • Brown, P.H.1    Ho, T.H.2
  • 95
    • 0023675716 scopus 로고
    • Purification and characterization of an endonuclease (E.C. 3.1.30.1) from Streptomyces tendae
    • Engel P., Ullah A.H. Purification and characterization of an endonuclease (E.C. 3.1.30.1) from Streptomyces tendae. Prep. Biochem. 18:1988;137-152.
    • (1988) Prep. Biochem. , vol.18 , pp. 137-152
    • Engel, P.1    Ullah, A.H.2
  • 96
    • 0019733080 scopus 로고
    • The extracellular nuclease from Alteromonas espejiana: An enzyme highly specific for nonduplex structure in nominally duplex DNAs
    • Chirikijian, J.G. and Papas, T.S., Eds. Elsevier, North Holland/New York
    • Gray, H.B., Jr., 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 (Chirikijian, J.G. and Papas, T.S., Eds.), pp. 169-203. Elsevier, North Holland/New York.
    • (1981) Gene Amplification and Analysis , vol.2 , pp. 169-203
    • Gray H.B., Jr.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
  • 97
    • 0026643811 scopus 로고
    • Active-site characterization of S1 nuclease. I. Affinity purification and influence of amino-group modification
    • Gite S., Reddy G., Shankar V. Active-site characterization of S1 nuclease. I. Affinity purification and influence of amino-group modification. Biochem. J. 285:1992;489-494.
    • (1992) Biochem. J. , vol.285 , pp. 489-494
    • Gite, S.1    Reddy, G.2    Shankar, V.3
  • 98
    • 0029364786 scopus 로고
    • S1 nuclease: Immunoaffinity purification and evidence for the proximity of cysteine 25 to the substrate binding site
    • Gite S., Shankar V. S1 nuclease: immunoaffinity purification and evidence for the proximity of cysteine 25 to the substrate binding site. J. Mol. Recognit. 8:1995;281-289.
    • (1995) J. Mol. Recognit. , vol.8 , pp. 281-289
    • Gite, S.1    Shankar, V.2
  • 99
    • 0025650586 scopus 로고
    • Purification and characterization of a nuclease (3′-nucleotidase) from a Penicillium sp
    • Kazama H., Tabata N., Ohgi K., Irie M. Purification and characterization of a nuclease (3′-nucleotidase) from a Penicillium sp. Chem. Pharm. Bull. 38:1990;3081-3085.
    • (1990) Chem. Pharm. Bull. , vol.38 , pp. 3081-3085
    • Kazama, H.1    Tabata, N.2    Ohgi, K.3    Irie, M.4
  • 100
    • 0024570616 scopus 로고
    • Purification and characterization of nuclease I associated with rye germ ribosomes
    • Siwecka M.A., Rytel M., Szarkowski J.W. Purification and characterization of nuclease I associated with rye germ ribosomes. Acta Biochim. Pol. 36:1989;45-62.
    • (1989) Acta Biochim. Pol. , vol.36 , pp. 45-62
    • Siwecka, M.A.1    Rytel, M.2    Szarkowski, J.W.3
  • 101
    • 0018813278 scopus 로고
    • Purification and properties of the mung bean nuclease
    • Laskowski M. Sr. Purification and properties of the mung bean nuclease. Methods Enzymol. 65:1980;263-275.
    • (1980) Methods Enzymol. , vol.65 , pp. 263-275
    • Laskowski M., Sr.1
  • 102
    • 0028221327 scopus 로고
    • Purification and characterization of fungal nuclease composed of heterogeneous subunits
    • Ito K., Matsuura Y., Miniamura N. Purification and characterization of fungal nuclease composed of heterogeneous subunits. Arch. Biochem. Biophys. 309:1994;160-167.
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 160-167
    • Ito, K.1    Matsuura, Y.2    Miniamura, N.3
  • 103
    • 0015514399 scopus 로고
    • An exonuclease of Nurospora crassa specific for single-stranded nucleic acids
    • Rabin E.Z., Tenenhouse H., Fraser M.J. An exonuclease of Nurospora crassa specific for single-stranded nucleic acids. Biochim. Biophys. Acta. 259:1972;50-68.
    • (1972) Biochim. Biophys. Acta , vol.259 , pp. 50-68
    • Rabin, E.Z.1    Tenenhouse, H.2    Fraser, M.J.3
  • 104
    • 0017131029 scopus 로고
    • A second form of the single-strand specific endonuclease of Neurospora crassa which is associated with a double-strand exonuclease
    • Fraser M.J., Tjeerde R., Matsumoto K. A second form of the single-strand specific endonuclease of Neurospora crassa which is associated with a double-strand exonuclease. Can. J. Biochem. 54:1976;971-980.
    • (1976) Can. J. Biochem. , vol.54 , pp. 971-980
    • Fraser, M.J.1    Tjeerde, R.2    Matsumoto, K.3
  • 105
    • 0017886542 scopus 로고
    • Neurospora endoexonuclease and its inactive (precursor?) form
    • Kwong S., Fraser M.J. Neurospora endoexonuclease and its inactive (precursor?) form. Can. J. Biochem. 56:1978;370-377.
    • (1978) Can. J. Biochem. , vol.56 , pp. 370-377
    • Kwong, S.1    Fraser, M.J.2
  • 106
    • 0018289821 scopus 로고
    • The major intracellular alkaline deoxyribonuclease activity expressed in wild-type and Rec-like mutants of Neurospora crassa
    • Chow T.Y., Fraser M.J. The major intracellular alkaline deoxyribonuclease activity expressed in wild-type and Rec-like mutants of Neurospora crassa. Can. J. Biochem. 57:1979;889-901.
    • (1979) Can. J. Biochem. , vol.57 , pp. 889-901
    • Chow, T.Y.1    Fraser, M.J.2
  • 107
    • 0018312137 scopus 로고
    • Alkaline deoxyribonucleases released from Neurospora crassa mycelia: Two activities not released by mutants with multiple sensitivities to mutagens
    • Fraser M.J. Alkaline deoxyribonucleases released from Neurospora crassa mycelia: two activities not released by mutants with multiple sensitivities to mutagens. Nucleic Acids Res. 6:1979;231-246.
    • (1979) Nucleic Acids Res. , vol.6 , pp. 231-246
    • Fraser, M.J.1
  • 108
    • 0019281224 scopus 로고
    • Nucleases and their control in wild-type and nuh mutants of Neurospora
    • Fraser M.J., Chow T.Y.-K., Käfer E. Nucleases and their control in wild-type and nuh mutants of Neurospora. Basic Life Sci. 15:1980;63-74.
    • (1980) Basic Life Sci. , vol.15 , pp. 63-74
    • Fraser, M.J.1    Chow, T.Y.-K.2    Käfer, E.3
  • 109
    • 0018815074 scopus 로고
    • Purification and properties of Neurospora crassa endo-exonuclease, an enzyme which can be converted to a single-strand specific endonuclease
    • Fraser M.J. Purification and properties of Neurospora crassa endo-exonuclease, an enzyme which can be converted to a single-strand specific endonuclease. Methods Enzymol. 65:1980;255-263.
    • (1980) Methods Enzymol. , vol.65 , pp. 255-263
    • Fraser, M.J.1
  • 110
    • 0000040706 scopus 로고
    • Fungal and mitochondrial nucleases
    • Linn, S.M., Lloyd, R.S. and Roberts, R.J., Eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Fraser, M.J. and Low, R.L. (1993) Fungal and mitochondrial nucleases. In: Nucleases (Linn, S.M., Lloyd, R.S. and Roberts, R.J., Eds.), pp. 171-207. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1993) Nucleases , pp. 171-207
    • Fraser, M.J.1    Low, R.L.2
  • 111
    • 78651173353 scopus 로고
    • An endonuclease from Neurospora crassa specific for polynucleotides lacking an ordered structure. I. Purification and properties of the enzyme
    • Linn S., Lehman I.R. An endonuclease from Neurospora crassa specific for polynucleotides lacking an ordered structure. I. Purification and properties of the enzyme. J. Biol. Chem. 240:1965;1287-1293.
    • (1965) J. Biol. Chem. , vol.240 , pp. 1287-1293
    • Linn, S.1    Lehman, I.R.2
  • 112
    • 0001585295 scopus 로고
    • An endonuclease from Neurospora crassa specific for polynucleotides lacking an ordered structure. II. Studies on enzyme specificity
    • Linn S., Lehman I.R. An endonuclease from Neurospora crassa specific for polynucleotides lacking an ordered structure. II. Studies on enzyme specificity. J. Biol. Chem. 240:1965;1294-1304.
    • (1965) J. Biol. Chem. , vol.240 , pp. 1294-1304
    • Linn, S.1    Lehman, I.R.2
  • 113
    • 0021112801 scopus 로고
    • Isolation and comparison of two molecular species of BAL 31 nuclease from Alteromonas espejiana with distinct kinetic properties
    • Wei C.F., Alianell G.A., Bencen G.H., Gray H.B. Jr. Isolation and comparison of two molecular species of BAL 31 nuclease from Alteromonas espejiana with distinct kinetic properties. J. Biol. Chem. 258:1983;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., Jr.4
  • 114
    • 0016646157 scopus 로고
    • Some physical and chemical properties of nuclease P1
    • Fujimoto M., Kuninaka A., Yoshino H. Some physical and chemical properties of nuclease P1. Agric. Biol. Chem. 39:1975;1991-1997.
    • (1975) Agric. Biol. Chem. , vol.39 , pp. 1991-1997
    • Fujimoto, M.1    Kuninaka, A.2    Yoshino, H.3
  • 115
    • 0016588507 scopus 로고
    • S1 nuclease hydrolysis of single-stranded nucleic acid with partial double stranded configuration
    • Rushizky G.W., Shaternikov V.A., Mozejko J.H., Sober H.A. S1 nuclease hydrolysis of single-stranded nucleic acid with partial double stranded configuration. Biochemistry. 14:1975;4221-4226.
    • (1975) Biochemistry , vol.14 , pp. 4221-4226
    • Rushizky, G.W.1    Shaternikov, V.A.2    Mozejko, J.H.3    Sober, H.A.4
  • 116
    • 0019733039 scopus 로고
    • S1 nuclease of Aspergillus oryzae
    • Chirikjian, J.G. and Papas, T.S., Eds. Elsevier, North Holland/New York
    • Rushizky, G.W. (1981) S1 nuclease of Aspergillus oryzae. In: Gene Amplification and analysis, Vol. 2 (Chirikjian, J.G. and Papas, T.S., Eds.), pp. 205-215. Elsevier, North Holland/New York.
    • (1981) Gene Amplification and analysis , vol.2 , pp. 205-215
    • Rushizky, G.W.1
  • 117
    • 0020144513 scopus 로고
    • Nuclease I from suspension-cultured Nicotiana tabacum: Purification and properties of the extracellular enzyme
    • Oleson A.K., Janski A.M., Fahrlander P.D., Wiesner T.A. Nuclease I from suspension-cultured Nicotiana tabacum: purification and properties of the extracellular enzyme. Arch. Biochem. Biophys. 216:1982;223-233.
    • (1982) Arch. Biochem. Biophys. , vol.216 , pp. 223-233
    • Oleson, A.K.1    Janski, A.M.2    Fahrlander, P.D.3    Wiesner, T.A.4
  • 118
    • 0031705343 scopus 로고    scopus 로고
    • Similarities and differences in the properties of alfalfa endonucleases
    • Christou A., Mantrangou C., Yupsanis T. Similarities and differences in the properties of alfalfa endonucleases. J. Plant. Physiol. 153:1998;16-24.
    • (1998) J. Plant. Physiol. , vol.153 , pp. 16-24
    • Christou, A.1    Mantrangou, C.2    Yupsanis, T.3
  • 120
    • 0017698574 scopus 로고
    • The use of endo-β-N-acetylglucosaminidase H in characterizing the structure and function of glycoproteins
    • Trimble R.B., Maley F. The use of endo-β-N-acetylglucosaminidase H in characterizing the structure and function of glycoproteins. Biochem. Biophys. Res. Commun. 78:1977;935-944.
    • (1977) Biochem. Biophys. Res. Commun. , vol.78 , pp. 935-944
    • Trimble, R.B.1    Maley, F.2
  • 121
    • 0013078881 scopus 로고
    • Resistance of glycoprotein to proteolysis, ribonuclease A and B compared
    • Birkeland A.J., Christensen T.B. Resistance of glycoprotein to proteolysis, ribonuclease A and B compared. J. Carbohydr. 83:1975;2-7.
    • (1975) J. Carbohydr. , vol.83 , pp. 2-7
    • Birkeland, A.J.1    Christensen, T.B.2
  • 122
    • 0016272751 scopus 로고
    • Purification and specificity of Aspergillus sojae DNase
    • Suzuki M., Sakaguchi K. Purification and specificity of Aspergillus sojae DNase. Eur. J. Biochem. 49:1974;619-625.
    • (1974) Eur. J. Biochem. , vol.49 , pp. 619-625
    • Suzuki, M.1    Sakaguchi, K.2
  • 123
    • 0017059787 scopus 로고
    • Isolation, subunit structure and properties of the ATP-dependent deoxyribonuclease of Bacillus subtilis: State of the protein in a mutant devoid of activity
    • Doly J., Anagnostopoulos C. Isolation, subunit structure and properties of the ATP-dependent deoxyribonuclease of Bacillus subtilis: state of the protein in a mutant devoid of activity. Eur. J. Biochem. 71:1976;309-316.
    • (1976) Eur. J. Biochem. , vol.71 , pp. 309-316
    • Doly, J.1    Anagnostopoulos, C.2
  • 124
    • 0015239751 scopus 로고
    • Endonuclease I of Proteus mirabilis. Properties of the noncomplexed and transfer ribonucleic acid-complexed forms of the enzyme
    • Goebel W., Helinski D.R. Endonuclease I of Proteus mirabilis. Properties of the noncomplexed and transfer ribonucleic acid-complexed forms of the enzyme. J. Biol. Chem. 246:1971;5341-5349.
    • (1971) J. Biol. Chem. , vol.246 , pp. 5341-5349
    • Goebel, W.1    Helinski, D.R.2
  • 125
  • 126
    • 0014010720 scopus 로고
    • An endonuclease from mitochondria of Neurospora crassa
    • Linn S., Lehman I.R. An endonuclease from mitochondria of Neurospora crassa. J. Biol. Chem. 241:1966;2694-2699.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2694-2699
    • Linn, S.1    Lehman, I.R.2
  • 128
    • 0019731293 scopus 로고
    • S1 nuclease of Aspergillus oryzae: Characterization of the associated phosphomonoesterase activity
    • Oleson A.E., Hoganson E.D. S1 nuclease of Aspergillus oryzae: characterization of the associated phosphomonoesterase activity. Arch. Biochem. Biophys. 211:1981;478-484.
    • (1981) Arch. Biochem. Biophys. , vol.211 , pp. 478-484
    • Oleson, A.E.1    Hoganson, E.D.2
  • 129
    • 0035761626 scopus 로고    scopus 로고
    • Nuclease Bh1 from Basidiobolus haptosporus: Characterization of the associated-adenylic acid preferential-ribonuclease activity
    • Desai N.A., Shankar V. Nuclease Bh1 from Basidiobolus haptosporus: characterization of the associated-adenylic acid preferential-ribonuclease activity. J. Biochem. Mol. Biol. Biophys. 5:2001;169-176.
    • (2001) J. Biochem. Mol. Biol. Biophys. , vol.5 , pp. 169-176
    • Desai, N.A.1    Shankar, V.2
  • 130
    • 0035761180 scopus 로고    scopus 로고
    • Nuclease Bh1 from Basidiobolus haptosporus: Characterization of the associated-ribonucleotide specific-3′phosphomonoesterase activity
    • Desai N.A., Shankar V. Nuclease Bh1 from Basidiobolus haptosporus: characterization of the associated-ribonucleotide specific-3′phosphomonoesterase activity. J. Biochem. Mol. Biol. Biophys. 5:2001;267-275.
    • (2001) J. Biochem. Mol. Biol. Biophys. , vol.5 , pp. 267-275
    • Desai, N.A.1    Shankar, V.2
  • 131
    • 0013122436 scopus 로고
    • Purification and characterization of nucleases S1 from Aspergillus oryzae
    • Chem. Abstr. 108:90477
    • Liou, F.C., Lin, C.M. and Hsieh, W.T. (1986) Purification and characterization of nucleases S1 from Aspergillus oryzae. J. Chin. Biochem. Soc. 15, 39-49 (Chem. Abstr. 108:90477).
    • (1986) J. Chin. Biochem. Soc. , vol.15 , pp. 39-49
    • Liou, F.C.1    Lin, C.M.2    Hsieh, W.T.3
  • 132
    • 0023059050 scopus 로고
    • Purification of S1 nuclease to homogeneity and its chemical, physical and catalytic properties
    • Shishido K., Habuka N. Purification of S1 nuclease to homogeneity and its chemical, physical and catalytic properties. Biochim. Biophys. Acta. 884:1986;215-218.
    • (1986) Biochim. Biophys. Acta , vol.884 , pp. 215-218
    • Shishido, K.1    Habuka, N.2
  • 133
    • 0017202381 scopus 로고
    • Mung bean nuclease I: Terminally directed hydrolysis of native DNA
    • Kowalski D., Kroeker W.D., Laskowski M. Sr. Mung bean nuclease I: terminally directed hydrolysis of native DNA. Biochemistry. 15:1976;4463-4467.
    • (1976) Biochemistry , vol.15 , pp. 4463-4467
    • Kowalski, D.1    Kroeker, W.D.2    Laskowski M., Sr.3
  • 135
    • 0025304339 scopus 로고
    • An inducible 3′-nucleotidase/nuclease from the trypanosomatid Crithidia luciliae: Purification and characterization
    • Neubert A.T., Gottlieb M. An inducible 3′-nucleotidase/nuclease from the trypanosomatid Crithidia luciliae: purification and characterization. J. Biol. Chem. 265:1990;7236-7242.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7236-7242
    • Neubert, A.T.1    Gottlieb, M.2
  • 136
    • 0028950665 scopus 로고
    • Molecular states of fungal nuclease composed of heterogeneous subunits as estimated from the effects of urea and chelating agents
    • Ito K., Hara C., Matsuura Y., Miniamura N. Molecular states of fungal nuclease composed of heterogeneous subunits as estimated from the effects of urea and chelating agents. Arch. Biochem. Biophys. 317:1995;25-32.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 25-32
    • Ito, K.1    Hara, C.2    Matsuura, Y.3    Miniamura, N.4
  • 137
    • 0014020901 scopus 로고
    • A nuclease specific for heat-denatured DNA isolated from the product of Aspergillus oryzae
    • Ando T. A nuclease specific for heat-denatured DNA isolated from the product of Aspergillus oryzae. Biochim. Biophys. Acta. 114:1966;158-168.
    • (1966) Biochim. Biophys. Acta , vol.114 , pp. 158-168
    • Ando, T.1
  • 139
    • 0014852171 scopus 로고
    • 5′-P-forming exonuclease from Actinomyces sp. of coelicolor group, strain No. 5 (exonuclease A 5): Purification and some properties
    • Tatarskaya R.I., Lvova T.N., Abrossimova-Amelyanchik N.M., Korenyako A.I., Bayev A.A. 5′-P-forming exonuclease from Actinomyces sp. of coelicolor group, strain No. 5 (exonuclease A 5): purification and some properties. Eur. J. Biochem. 15:1970;442-449.
    • (1970) Eur. J. Biochem. , vol.15 , pp. 442-449
    • Tatarskaya, R.I.1    Lvova, T.N.2    Abrossimova-Amelyanchik, N.M.3    Korenyako, A.I.4    Bayev, A.A.5
  • 140
    • 0015959160 scopus 로고
    • Extracellular nucleases of Bacillus subtilis. I. Purification and properties
    • Kanamori N., Sakabe K., Okazaki R. Extracellular nucleases of Bacillus subtilis. I. Purification and properties. Biochim. Biophys. Acta. 335:1973;155-172.
    • (1973) Biochim. Biophys. Acta , vol.335 , pp. 155-172
    • Kanamori, N.1    Sakabe, K.2    Okazaki, R.3
  • 141
    • 0001118631 scopus 로고
    • An endonuclease from Neurospora crassa specific for polynucleotides lacking an ordered structure
    • Linn S. An endonuclease from Neurospora crassa specific for polynucleotides lacking an ordered structure. Methods Enzymol. 12A:1967;247-255.
    • (1967) Methods Enzymol. , vol.12 A , pp. 247-255
    • Linn, S.1
  • 142
    • 0015752423 scopus 로고
    • Studies on a nuclease from Ustilago maydis. I. Purification, properties, and implication in recombination of the enzyme
    • Holloman W.K., Holliday R. Studies on a nuclease from Ustilago maydis. I. Purification, properties, and implication in recombination of the enzyme. J. Biol. Chem. 248:1973;8107-8113.
    • (1973) J. Biol. Chem. , vol.248 , pp. 8107-8113
    • Holloman, W.K.1    Holliday, R.2
  • 144
    • 0025747944 scopus 로고
    • An endo-exonuclease from meiotic tissues of the basidiomycete Coprinus cinereus: Its purification and characterization
    • Lu B.C., Sakaguchi K. An endo-exonuclease from meiotic tissues of the basidiomycete Coprinus cinereus: its purification and characterization. J. Biol. Chem. 266:1991;21060-21066.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21060-21066
    • Lu, B.C.1    Sakaguchi, K.2
  • 145
    • 0020214153 scopus 로고
    • Substrate specificity and mode of action of the zinc-metallo nuclease from Physarum polycephalum
    • Waterborg J.H., Kuyper C.M.A. Substrate specificity and mode of action of the zinc-metallo nuclease from Physarum polycephalum. J. Biochem. (Tokyo). 92:1982;1655-1661.
    • (1982) J. Biochem. (Tokyo) , vol.92 , pp. 1655-1661
    • Waterborg, J.H.1    Kuyper, C.M.A.2
  • 146
    • 0015245035 scopus 로고
    • Kinetic studies of denaturation and reaction with formaldehyde on polydeoxyribonucleotides
    • Utiyama H., Doty P. Kinetic studies of denaturation and reaction with formaldehyde on polydeoxyribonucleotides. Biochemistry. 10:1971;1254-1264.
    • (1971) Biochemistry , vol.10 , pp. 1254-1264
    • Utiyama, H.1    Doty, P.2
  • 147
    • 0015246488 scopus 로고
    • The reaction of glyoxal with nucleic acid components. 3. Kinetics of the reaction with monomers
    • Broude N.E., Budowsky E.I. The reaction of glyoxal with nucleic acid components. 3. Kinetics of the reaction with monomers. Biochim. Biophys. Acta. 254:1971;380-388.
    • (1971) Biochim. Biophys. Acta , vol.254 , pp. 380-388
    • Broude, N.E.1    Budowsky, E.I.2
  • 148
    • 0014944907 scopus 로고
    • Partial denaturation of thymine- and 5-bromouracil-containing λ DNA in alkali
    • Inman R.B., Schnös M. Partial denaturation of thymine- and 5-bromouracil-containing λ DNA in alkali. J. Mol. Biol. 49:1970;93-98.
    • (1970) J. Mol. Biol. , vol.49 , pp. 93-98
    • Inman, R.B.1    Schnös, M.2
  • 149
    • 0015223571 scopus 로고
    • A study in evolution: The DNA base sequence homology between coliphages T7 and T3
    • Davis R., Hyman R. A study in evolution: the DNA base sequence homology between coliphages T7 and T3. J. Mol. Biol. 62:1971;287-301.
    • (1971) J. Mol. Biol. , vol.62 , pp. 287-301
    • Davis, R.1    Hyman, R.2
  • 150
    • 77957009991 scopus 로고
    • Electron microscope heteroduplex methods for mapping regions of base sequence homology in nucleic acids
    • Davis R.W., Simon M., Davidson N. Electron microscope heteroduplex methods for mapping regions of base sequence homology in nucleic acids. Methods Enzymol. 21D:1971;413-428.
    • (1971) Methods Enzymol. , vol.21 D , pp. 413-428
    • Davis, R.W.1    Simon, M.2    Davidson, N.3
  • 151
    • 0016594749 scopus 로고
    • Activity of endonuclease S1 in denaturing solvents: Dimethylsulfoxide, dimethylformamide, formamide and formaldehyde
    • Hutton J.R., Wetmur J.G. Activity of endonuclease S1 in denaturing solvents: dimethylsulfoxide, dimethylformamide, formamide and formaldehyde. Biochem. Biophys. Res. Commun. 66:1975;942-948.
    • (1975) Biochem. Biophys. Res. Commun. , vol.66 , pp. 942-948
    • Hutton, J.R.1    Wetmur, J.G.2
  • 152
    • 0016788564 scopus 로고
    • Investigation in to the use of Aspergillus oryzae S1 nuclease in the presence of solvents which destabilize or prevent DNA secondary structure: Formaldehyde, formamide and glyoxal
    • Case S.T., Baker R.F. Investigation in to the use of Aspergillus oryzae S1 nuclease in the presence of solvents which destabilize or prevent DNA secondary structure: formaldehyde, formamide and glyoxal. Anal. Biochem. 64:1975;477-488.
    • (1975) Anal. Biochem. , vol.64 , pp. 477-488
    • Case, S.T.1    Baker, R.F.2
  • 153
    • 0023046869 scopus 로고
    • Specific cleavage of kinetoplast minicircle DNA from Leishmania tarentolae by mung bean nuclease and identification of several additional minicircle sequence classes
    • Muhich M.L., Simpson L. Specific cleavage of kinetoplast minicircle DNA from Leishmania tarentolae by mung bean nuclease and identification of several additional minicircle sequence classes. Nucleic Acids Res. 14:1986;5531-5556.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 5531-5556
    • Muhich, M.L.1    Simpson, L.2
  • 154
    • 0026516869 scopus 로고
    • Purification and characterization of a nutritionally controlled endodeoxyribonuclease from Streptomyces glaucescens
    • Aparicio J.F., Hardisson C., Sanchez J. Purification and characterization of a nutritionally controlled endodeoxyribonuclease from Streptomyces glaucescens. Biochem. J. 281:1992;231-237.
    • (1992) Biochem. J. , vol.281 , pp. 231-237
    • Aparicio, J.F.1    Hardisson, C.2    Sanchez, J.3
  • 156
    • 0001982455 scopus 로고
    • Micrococcal nuclease as a probe of DNA conformation
    • von Hippel P.H., Felsenfeld G. Micrococcal nuclease as a probe of DNA conformation. Biochemistry. 3:1964;27-35.
    • (1964) Biochemistry , vol.3 , pp. 27-35
    • Von Hippel, P.H.1    Felsenfeld, G.2
  • 157
    • 0014421795 scopus 로고
    • The conformation dependent hydrolysis of DNA by micrococcal nuclease
    • Wingert L., von Hippel P.H. The conformation dependent hydrolysis of DNA by micrococcal nuclease. Biochim. Biophys. Acta. 157:1968;114-126.
    • (1968) Biochim. Biophys. Acta , vol.157 , pp. 114-126
    • Wingert, L.1    Von Hippel, P.H.2
  • 158
    • 0014961405 scopus 로고
    • Mung bean nuclease I. II. Resistance of double stranded deoxyribonucleic acid and susceptibility of regions rich in adenosine and thymidine to enzymatic hydrolysis
    • Johnson P.H., Laskowski M. Sr. Mung bean nuclease I. II. Resistance of double stranded deoxyribonucleic acid and susceptibility of regions rich in adenosine and thymidine to enzymatic hydrolysis. J. Biol. Chem. 245:1970;891-898.
    • (1970) J. Biol. Chem. , vol.245 , pp. 891-898
    • Johnson, P.H.1    Laskowski M., Sr.2
  • 159
    • 0017902973 scopus 로고
    • Cleavage of bacteriophage PM2 DNA by nuclease S1
    • Chem. Abstr. 89:159346
    • Gonikberg, E.M. (1978) Cleavage of bacteriophage PM2 DNA by nuclease S1. Biokhimiya (Moscow) 7, 1285-1293 (Chem. Abstr. 89:159346).
    • (1978) Biokhimiya (Moscow) , vol.7 , pp. 1285-1293
    • Gonikberg, E.M.1
  • 160
    • 0022409144 scopus 로고
    • Effect of spermine on cleavage of plasmid DNA by nuclease S1 and BAL 31
    • Shishido K. Effect of spermine on cleavage of plasmid DNA by nuclease S1 and BAL 31. Biochim. Biophys. Acta. 826:1985;147-150.
    • (1985) Biochim. Biophys. Acta , vol.826 , pp. 147-150
    • Shishido, K.1
  • 161
    • 0024278708 scopus 로고
    • Purification and properties of the major nuclease from mitochondria of Saccharomyces cerevisiae
    • Dake E., Hofmann T.J., McIntire S., Hudson A., Zassenhaus H.P. Purification and properties of the major nuclease from mitochondria of Saccharomyces cerevisiae. J. Biol. Chem. 263:1988;7691-7702.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7691-7702
    • Dake, E.1    Hofmann, T.J.2    McIntire, S.3    Hudson, A.4    Zassenhaus, H.P.5
  • 162
    • 0016612129 scopus 로고
    • Polyamine activation of Staphylococcal nuclease
    • Frank J.J., Hawk I.A., Levy C.C. Polyamine activation of Staphylococcal nuclease. Biochim. Biophys. Acta. 390:1975;117-124.
    • (1975) Biochim. Biophys. Acta , vol.390 , pp. 117-124
    • Frank, J.J.1    Hawk, I.A.2    Levy, C.C.3
  • 163
    • 0017601462 scopus 로고
    • Ionic control of biochemical reactions
    • Douzou P., Maurel P. Ionic control of biochemical reactions. Trends Biochem. Sci. 2:1977;14-17.
    • (1977) Trends Biochem. Sci. , vol.2 , pp. 14-17
    • Douzou, P.1    Maurel, P.2
  • 164
    • 0020571977 scopus 로고
    • Evidence for distinct 5′- and 3′-nucleotidase activities in the surface membrane fraction of Leishmania donovani promastigotes
    • Gottlieb M., Dwyer D.M. Evidence for distinct 5′- and 3′-nucleotidase activities in the surface membrane fraction of Leishmania donovani promastigotes. Mol. Biochem. Parasitol. 7:1983;303-317.
    • (1983) Mol. Biochem. Parasitol. , vol.7 , pp. 303-317
    • Gottlieb, M.1    Dwyer, D.M.2
  • 165
    • 0022378646 scopus 로고
    • Effect of netropsin on plasmid DNA cleavage by BAL 31 nuclease
    • Sakaguchi R., Joho K., Shishido K. Effect of netropsin on plasmid DNA cleavage by BAL 31 nuclease. FEBS Lett. 191:1985;59-62.
    • (1985) FEBS Lett. , vol.191 , pp. 59-62
    • Sakaguchi, R.1    Joho, K.2    Shishido, K.3
  • 166
    • 0021713451 scopus 로고
    • Enhancement of S1 nuclease-susceptibility of negatively superhelical DNA by netropsin
    • Shishido K., Sakaguchi R., Nosoh Y. Enhancement of S1 nuclease-susceptibility of negatively superhelical DNA by netropsin. Biochem. Biophys. Res. Commun. 124:1984;388-392.
    • (1984) Biochem. Biophys. Res. Commun. , vol.124 , pp. 388-392
    • Shishido, K.1    Sakaguchi, R.2    Nosoh, Y.3
  • 167
    • 0000266828 scopus 로고
    • Specific inhibitors of Neurospora endo-exonuclease
    • Hatahet Z., Fraser M.J. Specific inhibitors of Neurospora endo-exonuclease. Biochem. Cell Biol. 67:1989;632-641.
    • (1989) Biochem. Cell Biol. , vol.67 , pp. 632-641
    • Hatahet, Z.1    Fraser, M.J.2
  • 168
    • 0017164164 scopus 로고
    • Purification and properties of the nuclease inhibitor of Aspergillus oryzae and kinetics of its interaction with crystalline nuclease O
    • Uozumi T., Ishino K., Beppu T., Arima K. Purification and properties of the nuclease inhibitor of Aspergillus oryzae and kinetics of its interaction with crystalline nuclease O. J. Biol. Chem. 251:1976;2808-2813.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2808-2813
    • Uozumi, T.1    Ishino, K.2    Beppu, T.3    Arima, K.4
  • 169
    • 0032006766 scopus 로고    scopus 로고
    • Biochemical characterization of Anabaena sp. strain PCC 7120 non-specific nuclease NucA and its inhibitor NuiA
    • Meiss G., Franke I., Gimadutdinow O., Urbanke C., Pingoud A. Biochemical characterization of Anabaena sp. strain PCC 7120 non-specific nuclease NucA and its inhibitor NuiA. Eur. J. Biochem. 251:1998;924-934.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 924-934
    • Meiss, G.1    Franke, I.2    Gimadutdinow, O.3    Urbanke, C.4    Pingoud, A.5
  • 170
    • 0034708328 scopus 로고    scopus 로고
    • Mechanism of DNA cleavage by the DNA/RNA-non-specific Anabaena sp. PCC 7120 endonuclease NucA and its inhibition by NuiA
    • Meiss G., Gimadutdinow O., Haberland B., Pingoud A. Mechanism of DNA cleavage by the DNA/RNA-non-specific Anabaena sp. PCC 7120 endonuclease NucA and its inhibition by NuiA. J. Mol. Biol. 297:2000;521-534.
    • (2000) J. Mol. Biol. , vol.297 , pp. 521-534
    • Meiss, G.1    Gimadutdinow, O.2    Haberland, B.3    Pingoud, A.4
  • 171
    • 0015878455 scopus 로고
    • Studies on 3′-nucleotidase-nuclease from potato tubers. II. Further studies on substrate specificity and mode of action
    • Suno M., Nomura A., Mizuno Y. Studies on 3′-nucleotidase-nuclease from potato tubers. II. Further studies on substrate specificity and mode of action. J. Biochem. (Tokyo). 73:1973;1291-1297.
    • (1973) J. Biochem. (Tokyo) , vol.73 , pp. 1291-1297
    • Suno, M.1    Nomura, A.2    Mizuno, Y.3
  • 172
    • 0014940314 scopus 로고
    • Mung bean nuclease. I. III. Purification procedure and (3′)-ω-monophosphatase activity
    • Mikulski A.J., Laskowski M. Sr. Mung bean nuclease. I. III. Purification procedure and (3′)-ω-monophosphatase activity. J. Biol. Chem. 245:1970;5026-5031.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5026-5031
    • Mikulski, A.J.1    Laskowski M., Sr.2
  • 173
    • 0022497945 scopus 로고
    • A comparative study of nucleases exhibiting preference for single-stranded nucleic acid
    • Martin S.A., Ullrich R.C., Meyer W.L. A comparative study of nucleases exhibiting preference for single-stranded nucleic acid. Biochim. Biophys. Acta. 867:1986;76-80.
    • (1986) Biochim. Biophys. Acta , vol.867 , pp. 76-80
    • Martin, S.A.1    Ullrich, R.C.2    Meyer, W.L.3
  • 174
    • 0000905550 scopus 로고
    • Staphylococcal nuclease: X-ray structure
    • Boyer, P.D., Ed. Academic Press, New York
    • Cotton, F.A. and Hazen, E.E., Jr. (1971) Staphylococcal nuclease: X-ray structure. In: The Enzymes, Vol. 3 (Boyer, P.D., Ed.), pp. 153-170. Academic Press, New York.
    • (1971) The Enzymes , vol.3 , pp. 153-170
    • Cotton, F.A.1    Hazen E.E., Jr.2
  • 175
    • 0032733904 scopus 로고    scopus 로고
    • Extracellular nuclease from Rhizopus stolonifer: Purification and characteristics of - Single strand preferential - Deoxyribonuclease activity
    • Rangarajan S., Shankar V. Extracellular nuclease from Rhizopus stolonifer: purification and characteristics of - single strand preferential - deoxyribonuclease activity. Biochim. Biophys. Acta. 1473:1999;293-304.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 293-304
    • Rangarajan, S.1    Shankar, V.2
  • 176
    • 0032415387 scopus 로고    scopus 로고
    • A novel endonuclease from kinetoplastid hemoflagellated protozoan parasite Leishamania
    • Mittra B., Sadhukhan P.N., Majumder H.K. A novel endonuclease from kinetoplastid hemoflagellated protozoan parasite Leishamania. J. Biochem. (Tokyo). 124:1998;1198-1205.
    • (1998) J. Biochem. (Tokyo) , vol.124 , pp. 1198-1205
    • Mittra, B.1    Sadhukhan, P.N.2    Majumder, H.K.3
  • 177
    • 0014670050 scopus 로고
    • Enzymes of nucleic acid metabolism from wheat seedlings. I. Purification and general properties of associated deoxyribonuclease, ribonuclease, and 3′-nucleotidase activities
    • Hanson D.M., Fairely J.L. Enzymes of nucleic acid metabolism from wheat seedlings. I. Purification and general properties of associated deoxyribonuclease, ribonuclease, and 3′-nucleotidase activities. J. Biol. Chem. 244:1969;2440-2449.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2440-2449
    • Hanson, D.M.1    Fairely, J.L.2
  • 178
    • 0014670660 scopus 로고
    • An extracellular nuclease from Serratia marcescens. I. Purification and some properties of the enzyme
    • Nestle M., Roberts W.K. An extracellular nuclease from Serratia marcescens. I. Purification and some properties of the enzyme. J. Biol. Chem. 244:1969;5213-5218.
    • (1969) J. Biol. Chem. , vol.244 , pp. 5213-5218
    • Nestle, M.1    Roberts, W.K.2
  • 179
    • 0014670710 scopus 로고
    • An extracellular nuclease from Serratia marcescens. II. Specificity of the enzyme
    • Nestle M., Roberts W.K. An extracellular nuclease from Serratia marcescens. II. Specificity of the enzyme. J. Biol. Chem. 244:1969;5219-5225.
    • (1969) J. Biol. Chem. , vol.244 , pp. 5219-5225
    • Nestle, M.1    Roberts, W.K.2
  • 180
    • 0027234753 scopus 로고
    • Deoxyribonuclease of Syncephalastrum racemosum - Enzymatic properties and molecular structure
    • Chen L.Y., Ho H.C., Tsai Y.C., Liao T.H. Deoxyribonuclease of Syncephalastrum racemosum - enzymatic properties and molecular structure. Arch. Biochem. Biophys. 303:1993;51-56.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 51-56
    • Chen, L.Y.1    Ho, H.C.2    Tsai, Y.C.3    Liao, T.H.4
  • 181
    • 0028012341 scopus 로고
    • Analysis of the role of the NUC1 endo/exonuclease in yeast mitochondrial DNA recombination
    • Zassenhaus H.P., Denniger G. Analysis of the role of the NUC1 endo/exonuclease in yeast mitochondrial DNA recombination. Curr. Genet. 25:1994;142-149.
    • (1994) Curr. Genet. , vol.25 , pp. 142-149
    • Zassenhaus, H.P.1    Denniger, G.2
  • 182
    • 0015979164 scopus 로고
    • Extracellular nuclease of Bacillus subtilis. II. The nuclease as 5′-end-group reagents
    • Kanamori N., Cozzarrelli N.R., Okazaki R. Extracellular nuclease of Bacillus subtilis. II. The nuclease as 5′-end-group reagents. Biochim. Biophys. Acta. 335:1974;173-184.
    • (1974) Biochim. Biophys. Acta , vol.335 , pp. 173-184
    • Kanamori, N.1    Cozzarrelli, N.R.2    Okazaki, R.3
  • 183
    • 0016694692 scopus 로고
    • Activity of wheat seedling nuclease toward single-stranded nucleic acids
    • Kroeker W.D., Hanson D.M., Fairely J.L. Activity of wheat seedling nuclease toward single-stranded nucleic acids. J. Biol. Chem. 250:1975;3767-3772.
    • (1975) J. Biol. Chem. , vol.250 , pp. 3767-3772
    • Kroeker, W.D.1    Hanson, D.M.2    Fairely, J.L.3
  • 184
    • 0013077628 scopus 로고
    • Mode of action of a nuclease from the fruit body of Flammulina velutipes
    • Sen K., Kawai T., Kurosawa S. Mode of action of a nuclease from the fruit body of Flammulina velutipes. Agric. Biol. Chem. 55:1991;775-780.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 775-780
    • Sen, K.1    Kawai, T.2    Kurosawa, S.3
  • 186
    • 0017834117 scopus 로고
    • Ribonuclease H activity in cultured plant cells
    • Sawai Y., Sugano N., Tsukada K. Ribonuclease H activity in cultured plant cells. Biochim. Biophys. Acta. 518:1978;181-185.
    • (1978) Biochim. Biophys. Acta , vol.518 , pp. 181-185
    • Sawai, Y.1    Sugano, N.2    Tsukada, K.3
  • 187
    • 0030629874 scopus 로고    scopus 로고
    • Purification and some properties of a novel dsRNA degrading nuclease bound to rye germ ribosomes
    • Siwecka M.A. Purification and some properties of a novel dsRNA degrading nuclease bound to rye germ ribosomes. Acta Biochim. Pol. 44:1997;61-68.
    • (1997) Acta Biochim. Pol. , vol.44 , pp. 61-68
    • Siwecka, M.A.1
  • 188
    • 0000424193 scopus 로고
    • Circular DNAs
    • Cantoni, G.L. and Davis, D.R. Eds. Academic Press, New York
    • Bauer, W. and Vinograd, J. (1974) Circular DNAs. In: Basic Principles of Nucleic Acid Chemistry, Vol. 2 (Cantoni, G.L. and Davis, D.R. Eds.), pp. 265-303, Academic Press, New York.
    • (1974) Basic Principles of Nucleic Acid Chemistry , vol.2 , pp. 265-303
    • Bauer, W.1    Vinograd, J.2
  • 190
    • 0019376425 scopus 로고
    • DNA topoisomerases
    • Gellert M. DNA topoisomerases. Annu. Rev. Biochem. 50:1981;879-910.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 879-910
    • Gellert, M.1
  • 191
    • 0015698349 scopus 로고
    • Action of S1 endonuclease from Aspergillus oryzae on simian virus 40 supercoiled component I DNA
    • Méchali M., de Recondo A.M., Girard M. Action of S1 endonuclease from Aspergillus oryzae on simian virus 40 supercoiled component I DNA. Biochem. Biophys. Res. Commun. 54:1973;1306-1320.
    • (1973) Biochem. Biophys. Res. Commun. , vol.54 , pp. 1306-1320
    • Méchali, M.1    De Recondo, A.M.2    Girard, M.3
  • 192
    • 0020479260 scopus 로고
    • Action of mung bean nuclease on supercoiled PM2 DNA
    • Kowalski D., Sanford J.P. Action of mung bean nuclease on supercoiled PM2 DNA. J. Biol. Chem. 257:1982;7820-7825.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7820-7825
    • Kowalski, D.1    Sanford, J.P.2
  • 193
    • 0017660782 scopus 로고
    • An endonuclease activity of venom phosphodiesterase specific for single-stranded and superhelical DNA
    • Pritchard A.E., Kowalski D., Laskowski M. Sr. An endonuclease activity of venom phosphodiesterase specific for single-stranded and superhelical DNA. J. Biol. Chem. 252:1977;8652-8659.
    • (1977) J. Biol. Chem. , vol.252 , pp. 8652-8659
    • Pritchard, A.E.1    Kowalski, D.2    Laskowski M., Sr.3
  • 194
    • 0019832575 scopus 로고
    • Efficiency of T4 DNA ligase-catalyzed end joining after S1 endonuclease treatment on duplex DNA containing single-stranded portions
    • Shishido K., Ando T. Efficiency of T4 DNA ligase-catalyzed end joining after S1 endonuclease treatment on duplex DNA containing single-stranded portions. Biochim. Biophys. Acta. 656:1981;123-127.
    • (1981) Biochim. Biophys. Acta , vol.656 , pp. 123-127
    • Shishido, K.1    Ando, T.2
  • 195
    • 0023851012 scopus 로고
    • Circular intermediates with missing nucleotides in the conversion of supercoiled or nicked circular to linear duplex DNA catalyzed by two species of BAL 31 nuclease
    • Przykorska A.K., Hauser C.R., Gray H.B. Jr. Circular intermediates with missing nucleotides in the conversion of supercoiled or nicked circular
    • (1988) Biochim. Biophys. Acta , vol.949 , pp. 16-26
    • Przykorska, A.K.1    Hauser, C.R.2    Gray H.B., Jr.3
  • 196
    • 0001210691 scopus 로고
    • Model for DNA and protein interactions and the function of the operator
    • Gierer A. Model for DNA and protein interactions and the function of the operator. Nature (London). 212:1966;1480-1481.
    • (1966) Nature (London) , vol.212 , pp. 1480-1481
    • Gierer, A.1
  • 197
    • 0016638632 scopus 로고
    • Thermodynamic properties of superhelical DNAs
    • Hsieh T.S., Wang J.C. Thermodynamic properties of superhelical DNAs. Biochemistry. 14:1975;527-535.
    • (1975) Biochemistry , vol.14 , pp. 527-535
    • Hsieh, T.S.1    Wang, J.C.2
  • 198
    • 0021811956 scopus 로고
    • A cruciform in the direct repeats of the yeast 2 μ DNA: Selective S1 nuclease cleavage at one of the three homologous palindromes
    • Asakura Y., Kikuchi Y., Yanagida M. A cruciform in the direct repeats of the yeast 2 μ DNA: selective S1 nuclease cleavage at one of the three homologous palindromes. J. Biochem (Tokyo). 98:1985;41-47.
    • (1985) J. Biochem (Tokyo). , vol.98 , pp. 41-47
    • Asakura, Y.1    Kikuchi, Y.2    Yanagida, M.3
  • 199
    • 0019350114 scopus 로고
    • Cruciform structures in supercoiled DNA
    • Panyotatos N., Wells R.D. Cruciform structures in supercoiled DNA. Nature. 289:1981;466-470.
    • (1981) Nature , vol.289 , pp. 466-470
    • Panyotatos, N.1    Wells, R.D.2
  • 200
    • 0029894803 scopus 로고    scopus 로고
    • A supercoil-specific endonuclease from Salmonella typhimurium cleaves both negatively and positively supercoiled DNA
    • Zargar M.A., Chakravorty M. A supercoil-specific endonuclease from Salmonella typhimurium cleaves both negatively and positively supercoiled DNA. Biochem. Mol. Biol. Int. 39:1996;307-317.
    • (1996) Biochem. Mol. Biol. Int. , vol.39 , pp. 307-317
    • Zargar, M.A.1    Chakravorty, M.2
  • 201
    • 0023930795 scopus 로고
    • A unique endonuclease from Crithidia fasciculata which recognizes a bend in the DNA helix: Specificity of the cleavage reaction
    • Linial M., Shlomai J. A unique endonuclease from Crithidia fasciculata which recognizes a bend in the DNA helix: specificity of the cleavage reaction. J. Biol. Chem. 263:1988;290-297.
    • (1988) J. Biol. Chem. , vol.263 , pp. 290-297
    • Linial, M.1    Shlomai, J.2
  • 202
    • 0021770888 scopus 로고
    • Mung bean nuclease cleavage of a dA+dT-rich sequence or an inverted repeat sequence in supercoiled PM2 DNA depends on ionic environment
    • Sheflin L.G., Kowalski D. Mung bean nuclease cleavage of a dA+dT-rich sequence or an inverted repeat sequence in supercoiled PM2 DNA depends on ionic environment. Nucleic Acids Res. 12:1984;7087-7104.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 7087-7104
    • Sheflin, L.G.1    Kowalski, D.2
  • 203
    • 0022423575 scopus 로고
    • Altered DNA conformations detected by mung bean nuclease occur in promoter and terminator regions of supercoiled pBR322 DNA
    • Sheflin L.G., Kowalski D. Altered DNA conformations detected by mung bean nuclease occur in promoter and terminator regions of supercoiled pBR322 DNA. Nucleic Acids Res. 13:1985;6137-6154.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 6137-6154
    • Sheflin, L.G.1    Kowalski, D.2
  • 204
    • 0023651009 scopus 로고
    • Yeast regulatory sequences preferentially adopt a non-B conformation in supercoiled DNA
    • Umek R.M., Kowalski D. Yeast regulatory sequences preferentially adopt a non-B conformation in supercoiled DNA. Nucleic Acids Res. 15:1987;4467-4480.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 4467-4480
    • Umek, R.M.1    Kowalski, D.2
  • 205
    • 0024297539 scopus 로고
    • The ease of DNA unwinding as a determinant of initiation at yeast replication origins
    • Umek R.M., Kowalski D. The ease of DNA unwinding as a determinant of initiation at yeast replication origins. Cell. 52:1988;559-567.
    • (1988) Cell , vol.52 , pp. 559-567
    • Umek, R.M.1    Kowalski, D.2
  • 206
    • 0021770872 scopus 로고
    • Changes in site specificity of single-strand-specific endonucleases on supercoiled PM2 DNA with temperature and ionic environment
    • Kowalski D. Changes in site specificity of single-strand-specific endonucleases on supercoiled PM2 DNA with temperature and ionic environment. Nucleic Acids Res. 12:1984;7071-7086.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 7071-7086
    • Kowalski, D.1
  • 207
    • 0342927819 scopus 로고
    • Stable DNA unwinding, not 'breathing' accounts for single-strand-specific nuclease hypersensitivity of specific A+T-rich sequences
    • Kowalski D., Natale D.A., Eddy M.J. Stable DNA unwinding, not 'breathing' accounts for single-strand-specific nuclease hypersensitivity of specific A+T-rich sequences. Proc. Natl. Acad. Sci. USA. 85:1988;9464-9468.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9464-9468
    • Kowalski, D.1    Natale, D.A.2    Eddy, M.J.3
  • 208
    • 0020022917 scopus 로고
    • The three-dimensional structure of DNA
    • Zimmermann S.B. The three-dimensional structure of DNA. Annu. Rev. Biochem. 51:1982;395-427.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 395-427
    • Zimmermann, S.B.1
  • 209
    • 0019932819 scopus 로고
    • Left-handed Z-DNA is induced by supercoiling in physiological ionic conditions
    • Singleton C.K., Klysik J., Stirdivant S.M., Wells R.D. Left-handed Z-DNA is induced by supercoiling in physiological ionic conditions. Nature. 299:1982;312-316.
    • (1982) Nature , vol.299 , pp. 312-316
    • Singleton, C.K.1    Klysik, J.2    Stirdivant, S.M.3    Wells, R.D.4
  • 210
    • 0020760881 scopus 로고
    • Conformational flexibility of junctions between contiguous B- and Z-DNAs in supercoiled plasmids
    • Singleton C.K., Klysik J., Wells R.D. Conformational flexibility of junctions between contiguous B- and Z-DNAs in supercoiled plasmids. Proc. Natl. Acad. Sci. USA. 80:1983;2447-2451.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2447-2451
    • Singleton, C.K.1    Klysik, J.2    Wells, R.D.3
  • 211
    • 0021340141 scopus 로고
    • S1 nuclease recognizes DNA conformational junctions between left-handed helical (dT-dG n.dC-dA)n and contiguous right-handed sequences
    • Singleton C.K., Kilpatrick M.W., Wells R.D. S1 nuclease recognizes DNA conformational junctions between left-handed helical (dT-dG n.dC-dA)n and contiguous right-handed sequences. J. Biol. Chem. 259:1984;1963-1967.
    • (1984) J. Biol. Chem. , vol.259 , pp. 1963-1967
    • Singleton, C.K.1    Kilpatrick, M.W.2    Wells, R.D.3
  • 212
    • 0021100915 scopus 로고
    • BAL 31 nuclease as a probe in concentrated salt for the B-Z DNA junction
    • Kilpatrick M.W., Wei C.F., Gray H.B. Jr., Wells R.D. BAL 31 nuclease as a probe in concentrated salt for the B-Z DNA junction. Nucleic Acids Res. 11:1983;3811-3822.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 3811-3822
    • Kilpatrick, M.W.1    Wei, C.F.2    Gray H.B., Jr.3    Wells, R.D.4
  • 213
    • 0033532211 scopus 로고    scopus 로고
    • The DNA/RNA non-specific Serratia nuclease prefers double stranded A-form nucleic acids as substrates
    • Meiss G., Gast F.U., Pingoud A. The DNA/RNA non-specific Serratia nuclease prefers double stranded A-form nucleic acids as substrates. J. Mol. Biol. 288:1999;377-390.
    • (1999) J. Mol. Biol. , vol.288 , pp. 377-390
    • Meiss, G.1    Gast, F.U.2    Pingoud, A.3
  • 214
    • 0019457162 scopus 로고
    • Enzymatic properties of the bacteriophage φ X174 A protein on superhelical φ X174 DNA: A model for the termination of the rolling circle DNA replication
    • van der Ende A., Langeveld S.A., Teertstra R., van Arkel G.A., Weisbeek P.J. Enzymatic properties of the bacteriophage φ X174 A protein on superhelical φ X174 DNA: a model for the termination of the rolling circle DNA replication. Nucleic Acids Res. 9:1981;2037-2053.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 2037-2053
    • Van der Ende, A.1    Langeveld, S.A.2    Teertstra, R.3    Van Arkel, G.A.4    Weisbeek, P.J.5
  • 215
    • 0024529253 scopus 로고
    • Activation of the vaccinia virus nicking-joining enzyme by trypsinization
    • Reddy M.K., Bauer W.R. Activation of the vaccinia virus nicking-joining enzyme by trypsinization. J. Biol. Chem. 264:1989;443-449.
    • (1989) J. Biol. Chem. , vol.264 , pp. 443-449
    • Reddy, M.K.1    Bauer, W.R.2
  • 216
    • 0023741168 scopus 로고
    • Holliday intermediates and reaction by-products in FLP protein-promoted site-specific recombination
    • Meyer-Leon L., Huang L.-C., Umlauf S.W., Cox M.M., Inman R.B. Holliday intermediates and reaction by-products in FLP protein-promoted site-specific recombination. Mol. Cell Biol. 8:1988;3784-3796.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 3784-3796
    • Meyer-Leon, L.1    Huang, L.-C.2    Umlauf, S.W.3    Cox, M.M.4    Inman, R.B.5
  • 217
    • 0024463676 scopus 로고
    • Heteroduplex substrates for bacteriophage λ site-specific recombination: Cleavage and strand transfer products
    • Nash H.A., Robertson C.A. Heteroduplex substrates for bacteriophage λ site-specific recombination: cleavage and strand transfer products. EMBO J. 8:1989;3523-3533.
    • (1989) EMBO J. , vol.8 , pp. 3523-3533
    • Nash, H.A.1    Robertson, C.A.2
  • 218
    • 0028352363 scopus 로고
    • Intermolecular disintegration and intramolecular strand transfer activities of wild-type and mutant HIV-1 integrase
    • Mazumder A., Engelman A., Craigie R., Fesen M., Pommier Y. Intermolecular disintegration and intramolecular strand transfer activities of wild-type and mutant HIV-1 integrase. Nucleic Acids Res. 22:1994;1037-1043.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1037-1043
    • Mazumder, A.1    Engelman, A.2    Craigie, R.3    Fesen, M.4    Pommier, Y.5
  • 219
    • 0003100670 scopus 로고
    • Consequences and mechanisms of transposition in Antirrhinum majus
    • Berg, D.E. and Howe, M.M., Eds. ASM Press, Washington DC
    • Coen, E., Robbins, T.P., Almeida, J., Hudson, A. and Carpenter, R. (1989) Consequences and mechanisms of transposition in Antirrhinum majus. In: Mobile DNA (Berg, D.E. and Howe, M.M., Eds.), pp. 413-436. ASM Press, Washington DC.
    • (1989) Mobile DNA , pp. 413-436
    • Coen, E.1    Robbins, T.P.2    Almeida, J.3    Hudson, A.4    Carpenter, R.5
  • 220
    • 0026792892 scopus 로고
    • V(D)J recombination: Broken DNA molecules with covalently sealed (hairpin) coding ends in scid mouse thymocytes
    • Roth D.B., Menetski J.P., Nakajima P.B., Bosma M.J., Gillert M. V(D)J recombination: broken DNA molecules with covalently sealed (hairpin) coding ends in scid mouse thymocytes. Cell. 70:1992;983-991.
    • (1992) Cell , vol.70 , pp. 983-991
    • Roth, D.B.1    Menetski, J.P.2    Nakajima, P.B.3    Bosma, M.J.4    Gillert, M.5
  • 221
    • 0030391216 scopus 로고    scopus 로고
    • Double-strand breaks, DNA hairpins, and the mechanism of V(D)J recombination
    • Steen S.B., Zhu C., Roth D.B. Double-strand breaks, DNA hairpins, and the mechanism of V(D)J recombination. Curr. Top. Microbiol. Immunol. 217:1996;61-77.
    • (1996) Curr. Top. Microbiol. Immunol. , vol.217 , pp. 61-77
    • Steen, S.B.1    Zhu, C.2    Roth, D.B.3
  • 223
    • 0000271390 scopus 로고
    • The synthesis of polynucleotide-celluloses and their use in the fractionation of polynucleotides
    • Gilham P.T. The synthesis of polynucleotide-celluloses and their use in the fractionation of polynucleotides. J. Am. Chem. Soc. 86:1964;4982-4985.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 4982-4985
    • Gilham, P.T.1
  • 225
    • 77956899130 scopus 로고
    • Staphylococcal nuclease: Chemical properties and catalysis
    • Boyer, P.D., Ed. Academic Press, London
    • Anfinsen, C.B., Cuatrecasas, P. and Taniuchi, H. (1971) Staphylococcal nuclease: chemical properties and catalysis. In: The Enzymes, Vol. 4 (Boyer, P.D., Ed), pp. 177-204. Academic Press, London.
    • (1971) The Enzymes , vol.4 , pp. 177-204
    • Anfinsen, C.B.1    Cuatrecasas, P.2    Taniuchi, H.3
  • 226
    • 0021111959 scopus 로고
    • Structural perturbation in supercoiled DNA: Hypersensitivity to modification by a single-strand-selective chemical reagent conferred by inverted repeat sequences
    • Lilley D.M. Structural perturbation in supercoiled DNA: hypersensitivity to modification by a single-strand-selective chemical reagent conferred by inverted repeat sequences. Nucleic Acids Res. 11:1983;3097-3112.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 3097-3112
    • Lilley, D.M.1
  • 227
    • 0029760491 scopus 로고    scopus 로고
    • Interaction of the periplasmic dG-selective Streptomyces antibioticus nuclease with oligodeoxynucleotide substrates
    • Cal S., Nicieza R.G., Connolly B.A., Sanchez J. Interaction of the periplasmic dG-selective Streptomyces antibioticus nuclease with oligodeoxynucleotide substrates. Biochemistry. 35:1996;10828-10836.
    • (1996) Biochemistry , vol.35 , pp. 10828-10836
    • Cal, S.1    Nicieza, R.G.2    Connolly, B.A.3    Sanchez, J.4
  • 228
    • 0015732096 scopus 로고
    • Studies on a nuclease from Ustilago maydis. II. Substrate specificity and mode of action of the enzyme
    • Holloman W.K. Studies on a nuclease from Ustilago maydis. II. Substrate specificity and mode of action of the enzyme. J. Biol. Chem. 248:1973;8114-8119.
    • (1973) J. Biol. Chem. , vol.248 , pp. 8114-8119
    • Holloman, W.K.1
  • 229
    • 0000072580 scopus 로고
    • Preferential resistance of phosphodiester bond between deoxycytidine and 5′-adjacent bases to Chlamydomonas nuclease C
    • Ogawa K., Kuroiwa T. Preferential resistance of phosphodiester bond between deoxycytidine and 5′-adjacent bases to Chlamydomonas nuclease C. Plant Cell Physiol. 28:1987;323-332.
    • (1987) Plant Cell Physiol. , vol.28 , pp. 323-332
    • Ogawa, K.1    Kuroiwa, T.2
  • 230
    • 0009038030 scopus 로고
    • A site-specific single-strand endonuclease from the eukaryote Chlamydomonas
    • Burton W.G., Roberts R.J., Myers P.A., Sager R. A site-specific single-strand endonuclease from the eukaryote Chlamydomonas. Proc. Natl. Acad. Sci. USA. 74:1977;2687-2691.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2687-2691
    • Burton, W.G.1    Roberts, R.J.2    Myers, P.A.3    Sager, R.4
  • 231
    • 0023283902 scopus 로고
    • Endonuclease G: A (dG)n.(dC)n-specific DNase from higher eukaryotes
    • Ruiz-Carillo A., Renaud J. Endonuclease G: a (dG)n.(dC)n-specific DNase from higher eukaryotes. EMBO J. 6:1987;401-407.
    • (1987) EMBO J. , vol.6 , pp. 401-407
    • Ruiz-Carillo, A.1    Renaud, J.2
  • 232
    • 0023808723 scopus 로고
    • The preference of the mitochondrial endonuclease for a conserved sequence block in mitochondrial DNA is highly conserved during mammalian evolution
    • Low R.L., Buzan J.M., Couper C.L. The preference of the mitochondrial endonuclease for a conserved sequence block in mitochondrial DNA is highly conserved during mammalian evolution. Nucleic Acids Res. 16:1988;6427-6445.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6427-6445
    • Low, R.L.1    Buzan, J.M.2    Couper, C.L.3
  • 233
    • 0024978057 scopus 로고
    • n sequences by endonuclease G: Characterization of the calf thymus nuclease
    • n sequences by endonuclease G: characterization of the calf thymus nuclease. J. Biol. Chem. 264:1989;3301-3310.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3301-3310
    • Côtè, J.1    Renaud, J.2    Ruiz-Carillo, A.3
  • 234
    • 0027284549 scopus 로고
    • Primers for mitochondrial DNA replication generated by endonuclease G
    • Côtè J., Ruiz-Carillo A. Primers for mitochondrial DNA replication generated by endonuclease G. Science. 261:1993;765-769.
    • (1993) Science , vol.261 , pp. 765-769
    • Côtè, J.1    Ruiz-Carillo, A.2
  • 235
    • 0024297192 scopus 로고
    • A site-specific single strand endonuclease activity induced by NYs-1 virus infection of a Chlorella-like green alga
    • Xia Y.N., Morgan R., Schildkraut I., van Etten J.L. A site-specific single strand endonuclease activity induced by NYs-1 virus infection of a Chlorella-like green alga. Nucleic Acids Res. 16:1988;9477-9487.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 9477-9487
    • Xia, Y.N.1    Morgan, R.2    Schildkraut, I.3    Van Etten, J.L.4
  • 236
    • 0016286446 scopus 로고
    • Mode of action of nuclease P1 on nucleic acids and its specificity for synthetic phosphodiesters
    • Fujimoto M., Fujiyama K., Kuninaka A., Yoshino H. Mode of action of nuclease P1 on nucleic acids and its specificity for synthetic phosphodiesters. Agric. Biol. Chem. 38:1974;2141-2147.
    • (1974) Agric. Biol. Chem. , vol.38 , pp. 2141-2147
    • Fujimoto, M.1    Fujiyama, K.2    Kuninaka, A.3    Yoshino, H.4
  • 238
    • 0028834157 scopus 로고
    • Properties and specificity of a calcium dependent endonuclease from germinated lentil (Lens culinaris)
    • Kefalas P.S., Yupsanis T. Properties and specificity of a calcium dependent endonuclease from germinated lentil (Lens culinaris). J. Plant Physiol. 146:1995;1-9.
    • (1995) J. Plant Physiol. , vol.146 , pp. 1-9
    • Kefalas, P.S.1    Yupsanis, T.2
  • 239
    • 0013077909 scopus 로고
    • A site-specific endonuclease from Saccharomyces cerevisiae which plays an essential role in mating type interconversion
    • Chem. Abstr. 100:187876
    • Kostriken, R., Strathern, J., Klar. Amar J.S., Hicks, J.B., Moomaw, C. and Heffron, F. (1983) A site-specific endonuclease from Saccharomyces cerevisiae which plays an essential role in mating type interconversion. UCLA Symp. Mol. Cell. Biol., New Ser. 10, 785-795 (Chem. Abstr. 100:187876).
    • (1983) UCLA Symp. Mol. Cell. Biol., New Ser. , vol.10 , pp. 785-795
    • Kostriken, R.1    Strathern, J.2    Klar Amar, J.S.3    Hicks, J.B.4    Moomaw, C.5    Heffron, F.6
  • 240
    • 0021053220 scopus 로고
    • A site-specific endonuclease essential for mating-type switching in Saccharomyces cerevisiae
    • Kostriken R., Strathern J.N., Klar A.J., Hicks J.B., Heffron F. A site-specific endonuclease essential for mating-type switching in Saccharomyces cerevisiae. Cell. 35:1983;167-174.
    • (1983) Cell , vol.35 , pp. 167-174
    • Kostriken, R.1    Strathern, J.N.2    Klar, A.J.3    Hicks, J.B.4    Heffron, F.5
  • 241
    • 0021254552 scopus 로고
    • On the nucleotide sequence recognized by a eukaryotic site-specific endonuclease, Endo.SceI from yeast
    • Shibata T., Watabe H., Kaneko T., Iino T., Ando T. On the nucleotide sequence recognized by a eukaryotic site-specific endonuclease, Endo.SceI from yeast. J. Biol. Chem. 259:1984;10499-10506.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10499-10506
    • Shibata, T.1    Watabe, H.2    Kaneko, T.3    Iino, T.4    Ando, T.5
  • 242
    • 0024967904 scopus 로고
    • Characterization of a novel endonuclease from Crithidia fasciculata
    • Holdsworth M.L., Hines J.C., Ray D.S. Characterization of a novel endonuclease from Crithidia fasciculata. Nucleic Acids Res. 17:1989;4047-4060.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4047-4060
    • Holdsworth, M.L.1    Hines, J.C.2    Ray, D.S.3
  • 243
    • 0015852123 scopus 로고
    • Action of single-strand specific Neurospora crassa endonuclease on ultraviolet light-irradiated native DNA
    • Kato A.C., Fraser M.J. Action of single-strand specific Neurospora crassa endonuclease on ultraviolet light-irradiated native DNA. Biochim. Biophys. Acta. 312:1973;645-655.
    • (1973) Biochim. Biophys. Acta , vol.312 , pp. 645-655
    • Kato, A.C.1    Fraser, M.J.2
  • 244
    • 0016197728 scopus 로고
    • Cleavage of ultraviolet light-irradiated DNA by single strand-specific S1 endonuclease
    • Shishido K., Ando T. Cleavage of ultraviolet light-irradiated DNA by single strand-specific S1 endonuclease. Biochem. Biophys. Res. Commun. 59:1974;1380-1388.
    • (1974) Biochem. Biophys. Res. Commun. , vol.59 , pp. 1380-1388
    • Shishido, K.1    Ando, T.2
  • 245
    • 0019431394 scopus 로고
    • S1-sensitive sites in DNA after γ-irradiation
    • Martin B.H. S1-sensitive sites in DNA after γ-irradiation. Biochim. Biophys. Acta. 652:1981;261-265.
    • (1981) Biochim. Biophys. Acta , vol.652 , pp. 261-265
    • Martin, B.H.1
  • 246
    • 0021246537 scopus 로고
    • S1 nuclease-sensitive sites in yeast DNA: An assay for radiation-induced base damage
    • Chem. Abstr. 101:68499
    • Andrews, J., Martin-Bertram, H. and Hagen, U. (1984) S1 nuclease-sensitive sites in yeast DNA: an assay for radiation-induced base damage. Int. J. Radiat. Biol. Relat. Stud. Phys., Chem. Med. 45, 497-504 (Chem. Abstr. 101:68499).
    • (1984) Int. J. Radiat. Biol. Relat. Stud. Phys., Chem. Med. , vol.45 , pp. 497-504
    • Andrews, J.1    Martin-Bertram, H.2    Hagen, U.3
  • 247
    • 0019971170 scopus 로고
    • Effect of alkylation on the secondary structure of DNA
    • Rizvi R.Y., Alvi N.K., Hadi S.M. Effect of alkylation on the secondary structure of DNA. Biosci. Rep. 2:1982;315-322.
    • (1982) Biosci. Rep. , vol.2 , pp. 315-322
    • Rizvi, R.Y.1    Alvi, N.K.2    Hadi, S.M.3
  • 248
    • 0022726062 scopus 로고
    • Effect of alkylation with streptozotocin on the secondary structure of DNA
    • Rizvi R.Y., Shahabuddin R.A., Hadi S.M. Effect of alkylation with streptozotocin on the secondary structure of DNA. Biosci. Rep. 6:1986;557-564.
    • (1986) Biosci. Rep. , vol.6 , pp. 557-564
    • Rizvi, R.Y.1    Shahabuddin, R.A.2    Hadi, S.M.3
  • 249
    • 0016849392 scopus 로고
    • In vitro recognition of carcinogen-induced local denaturation sites native DNA by S1 endonuclease from Aspergillus oryzae
    • Fuchs R.P.P. In vitro recognition of carcinogen-induced local denaturation sites native DNA by S1 endonuclease from Aspergillus oryzae. Nature. 257:1975;151-152.
    • (1975) Nature , vol.257 , pp. 151-152
    • Fuchs, R.P.P.1
  • 250
    • 0025216572 scopus 로고
    • Kinetic studies of the hydrolysis of platinum-DNA complexes by nuclease S1
    • Butour J.L., Mazard A.M., Vieussens C., Johnson N.P. Kinetic studies of the hydrolysis of platinum-DNA complexes by nuclease S1. Chem.-Biol. Interact. 73:1990;195-205.
    • (1990) Chem.-Biol. Interact. , vol.73 , pp. 195-205
    • Butour, J.L.1    Mazard, A.M.2    Vieussens, C.3    Johnson, N.P.4
  • 251
    • 0024580615 scopus 로고
    • Enzymatic analysis of isomeric trithymidylates containing ultraviolet light-induced cyclobutane pyrimidine dimers. I. Nuclease P1-mediated hydrolysis of the intradimer phosphodiester linkage
    • Liuzzi M., Weinfeld M., Paterson M.C. Enzymatic analysis of isomeric trithymidylates containing ultraviolet light-induced cyclobutane pyrimidine dimers. I. Nuclease P1-mediated hydrolysis of the intradimer phosphodiester linkage. J. Biol. Chem. 264:1989;6355-6363.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6355-6363
    • Liuzzi, M.1    Weinfeld, M.2    Paterson, M.C.3
  • 252
    • 0033573829 scopus 로고    scopus 로고
    • Incision at nucleotide insertions/deletions and base pair mismatches by the SP nuclease of spinach
    • Oleykowski C.A., Bronson Mullinss C.R., Chang D.W., Yeung A.T. Incision at nucleotide insertions/deletions and base pair mismatches by the SP nuclease of spinach. Biochemistry. 38:1999;2200-2205.
    • (1999) Biochemistry , vol.38 , pp. 2200-2205
    • Oleykowski, C.A.1    Bronson Mullinss, C.R.2    Chang, D.W.3    Yeung, A.T.4
  • 253
    • 0027157443 scopus 로고
    • Endonuclease VII of phage T4 triggers mismatch correction in vitro
    • Solaro P.C., Birkenkamp K., Pfeiffer P., Kemper B. Endonuclease VII of phage T4 triggers mismatch correction in vitro. J. Mol. Biol. 230:1993;868-877.
    • (1993) J. Mol. Biol. , vol.230 , pp. 868-877
    • Solaro, P.C.1    Birkenkamp, K.2    Pfeiffer, P.3    Kemper, B.4
  • 254
    • 0028859503 scopus 로고
    • Induction of double-strand breaks by S1 nuclease, mung bean nuclease and nuclease P1 in DNA containing abasic sites and nicks
    • Chaudhry M.A., Weinfeld M. Induction of double-strand breaks by S1 nuclease, mung bean nuclease and nuclease P1 in DNA containing abasic sites and nicks. Nucleic Acids Res. 23:1995;3805-3809.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3805-3809
    • Chaudhry, M.A.1    Weinfeld, M.2
  • 255
    • 0025925214 scopus 로고
    • Characterization of conformational features of DNA heteroduplexes containing aldehydic abasic sites
    • Withka J.M., Wilde J.A., Bolton P.H., Mazumder A., Gerlt J.A. Characterization of conformational features of DNA heteroduplexes containing aldehydic abasic sites. Biochemistry. 30:1991;9931-9940.
    • (1991) Biochemistry , vol.30 , pp. 9931-9940
    • Withka, J.M.1    Wilde, J.A.2    Bolton, P.H.3    Mazumder, A.4    Gerlt, J.A.5
  • 256
    • 0026442902 scopus 로고
    • Effects of the presence of an aldehydic abasic site on the thermal stability and rates of helix opening and closing of duplex DNA
    • Goljer I., Withka J.M., Kao J.Y., Bolton P.H. Effects of the presence of an aldehydic abasic site on the thermal stability and rates of helix opening and closing of duplex DNA. Biochemistry. 31:1992;11614-11619.
    • (1992) Biochemistry , vol.31 , pp. 11614-11619
    • Goljer, I.1    Withka, J.M.2    Kao, J.Y.3    Bolton, P.H.4
  • 258
    • 0014674855 scopus 로고
    • Variation of the average rotation angle of the DNA helix and the superhelical turns of covalently closed cyclic λ DNA
    • Wang J.C. Variation of the average rotation angle of the DNA helix and the superhelical turns of covalently closed cyclic λ DNA. J. Mol. Biol. 43:1969;25-39.
    • (1969) J. Mol. Biol. , vol.43 , pp. 25-39
    • Wang, J.C.1
  • 259
    • 0015243840 scopus 로고
    • Sedimentation velocity behavior of closed circular SV40 DNA as a function of superhelix density, ionic strength, counterion and temperature
    • Upholt W.B., Gray H.B. Jr., Vinograd J. Sedimentation velocity behavior of closed circular SV40 DNA as a function of superhelix density, ionic strength, counterion and temperature. J. Mol. Biol. 62:1971;21-38.
    • (1971) J. Mol. Biol. , vol.62 , pp. 21-38
    • Upholt, W.B.1    Gray H.B., Jr.2    Vinograd, J.3
  • 260
    • 0015523755 scopus 로고
    • Conformational aspects and reactivity of DNA: Effects of manganese and magnesium ions on interaction with DNA
    • Luck G., Zimmer C. Conformational aspects and reactivity of DNA: effects of manganese and magnesium ions on interaction with DNA. Eur. J. Biochem. 29:1972;528-536.
    • (1972) Eur. J. Biochem. , vol.29 , pp. 528-536
    • Luck, G.1    Zimmer, C.2
  • 261
    • 0016229794 scopus 로고
    • Conformation and reactivity of DNA. IV. Base binding ability of transition metal ions to native DNA and effect on helix conformation with special reference to DNA-Zn(II) complex
    • Zimmer C., Luck G., Triebel H. Conformation and reactivity of DNA. IV. Base binding ability of transition metal ions to native DNA and effect on helix conformation with special reference to DNA-Zn(II) complex. Biopolymers. 13:1974;425-453.
    • (1974) Biopolymers. , vol.13 , pp. 425-453
    • Zimmer, C.1    Luck, G.2    Triebel, H.3
  • 262
    • 0024341026 scopus 로고
    • Selective hydrolysis by exo- and endonucleases of phosphodiester bonds adjacent to an apurinic site
    • Weinfeld M., Liuzzi M., Paterson M.C. Selective hydrolysis by exo- and endonucleases of phosphodiester bonds adjacent to an apurinic site. Nucleic Acids Res. 17:1989;3735-3745.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 3735-3745
    • Weinfeld, M.1    Liuzzi, M.2    Paterson, M.C.3
  • 264
    • 0027205006 scopus 로고
    • Influence of nucleic acid base aromaticity on substrate reactivity with enzymes acting on single-stranded DNA
    • Weinfeld M., Soderlind K.J.M., Buchko G.W. Influence of nucleic acid base aromaticity on substrate reactivity with enzymes acting on single-stranded DNA. Nucleic Acids Res. 21:1993;621-626.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 621-626
    • Weinfeld, M.1    Soderlind, K.J.M.2    Buchko, G.W.3
  • 265
    • 0021099187 scopus 로고
    • Stereochemical course of DNA hydrolysis by nuclease S1
    • Potter B.V., Romaniuk P.J., Eckstein F. Stereochemical course of DNA hydrolysis by nuclease S1. J. Biol. Chem. 258:1983;1758-1760.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1758-1760
    • Potter, B.V.1    Romaniuk, P.J.2    Eckstein, F.3
  • 266
    • 0020536591 scopus 로고
    • Synthesis and configurational analysis of a dinucleoside phosphate isotopically chiral at phosphorus: Stereochemical course of Penicillium citrinum nuclease P1 reaction
    • Potter B.V., Connolly B.A., Eckstein F. Synthesis and configurational analysis of a dinucleoside phosphate isotopically chiral at phosphorus: stereochemical course of Penicillium citrinum nuclease P1 reaction. Biochemistry. 22:1983;1369-1377.
    • (1983) Biochemistry , vol.22 , pp. 1369-1377
    • Potter, B.V.1    Connolly, B.A.2    Eckstein, F.3
  • 267
    • 0032167693 scopus 로고    scopus 로고
    • Structure-specific DNA cleavage by 5′ nucleases
    • Ceska T.A., Sayers J.R. Structure-specific DNA cleavage by 5′ nucleases. Trends Biochem. Sci. 23:1998;331-336.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 331-336
    • Ceska, T.A.1    Sayers, J.R.2
  • 268
    • 0015239451 scopus 로고
    • The role of exonuclease and β protein of phage λ in genetic recombination. II. Substrate specificity and the mode of action of λ exonuclease
    • Carter D.M., Radding C.M. The role of exonuclease and β protein of phage λ in genetic recombination. II. Substrate specificity and the mode of action of λ exonuclease. J. Biol. Chem. 246:1971;2502-2512.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2502-2512
    • Carter, D.M.1    Radding, C.M.2
  • 269
    • 0025114469 scopus 로고
    • Properties of overexpressed phage T5 D15 exonuclease: Similarities with Escherichia coli DNA polymerase I 5′-3′ exonuclease
    • Sayers J.R., Eckstein F. Properties of overexpressed phage T5 D15 exonuclease: similarities with Escherichia coli DNA polymerase I 5′-3′ exonuclease. J. Biol. Chem. 265:1990;18311-18317.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18311-18317
    • Sayers, J.R.1    Eckstein, F.2
  • 270
    • 0028281443 scopus 로고
    • The characterization of a mammalian DNA structure-specific endonuclease
    • Harrington J.J., Lieber M.R. The characterization of a mammalian DNA structure-specific endonuclease. EMBO J. 13:1994;1235-1246.
    • (1994) EMBO J. , vol.13 , pp. 1235-1246
    • Harrington, J.J.1    Lieber, M.R.2
  • 271
    • 0014472219 scopus 로고
    • Deoxyribonuclease IV: A new exonuclease from mammalian tissues
    • Lindahl T., Gally J.A., Edelman G.M. Deoxyribonuclease IV: a new exonuclease from mammalian tissues. Proc. Natl. Acad. Sci. USA. 62:1969;597-603.
    • (1969) Proc. Natl. Acad. Sci. USA , vol.62 , pp. 597-603
    • Lindahl, T.1    Gally, J.A.2    Edelman, G.M.3
  • 272
    • 0027215222 scopus 로고
    • Structure-specific endonucleolytic cleavage of nucleic acids by eubacterial DNA polymerases
    • Lyamichev V., Brow M.A., Dahlberg J.E. Structure-specific endonucleolytic cleavage of nucleic acids by eubacterial DNA polymerases. Science. 260:1993;778-783.
    • (1993) Science , vol.260 , pp. 778-783
    • Lyamichev, V.1    Brow, M.A.2    Dahlberg, J.E.3
  • 273
    • 0016067523 scopus 로고
    • Mung bean nuclease: Mode of action and specificity vs synthetic esters of 3′-nucleotides
    • Kole R., Sierakowska H., Szempliska H., Shugar D. Mung bean nuclease: mode of action and specificity vs synthetic esters of 3′-nucleotides. Nucleic Acids Res. 1:1974;699-706.
    • (1974) Nucleic Acids Res. , vol.1 , pp. 699-706
    • Kole, R.1    Sierakowska, H.2    Szempliska, H.3    Shugar, D.4
  • 274
    • 0025743483 scopus 로고
    • Primary structure of nuclease P1 from Penicillium citrinum
    • Maekawa K., Tsunasawa S., Dibó G., Sakiyama F. Primary structure of nuclease P1 from Penicillium citrinum. Eur. J. Biochem. 200:1991;651-661.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 651-661
    • Maekawa, K.1    Tsunasawa, S.2    Dibó, G.3    Sakiyama, F.4
  • 275
    • 0026114761 scopus 로고
    • Primary structure of a nuclease (nuclease PA3) from a Penicillium sp
    • Tabata N., Kazama H., Ohgi K., Irie M. Primary structure of a nuclease (nuclease PA3) from a Penicillium sp. Agric. Biol. Chem. 55:1991;461-469.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 461-469
    • Tabata, N.1    Kazama, H.2    Ohgi, K.3    Irie, M.4
  • 276
    • 0029850216 scopus 로고    scopus 로고
    • Isolation and characterization of the nuclease O gene (nucO) from Aspergillus oryzae
    • Sano M., Nakamura A., Masaki H., Uozomi T. Isolation and characterization of the nuclease O gene (nucO) from Aspergillus oryzae. Curr. Genet. 30:1996;312-317.
    • (1996) Curr. Genet. , vol.30 , pp. 312-317
    • Sano, M.1    Nakamura, A.2    Masaki, H.3    Uozomi, T.4
  • 277
    • 0026498017 scopus 로고
    • Cloning and differential expression during the sexual cycle of a meiotic endonuclease-encoding gene from the basidiomycete Coprinus cinereus
    • Charlton S., Boulianne R., Chow Y.-C., Lu B.C. Cloning and differential expression during the sexual cycle of a meiotic endonuclease-encoding gene from the basidiomycete Coprinus cinereus. Gene. 122:1992;163-169.
    • (1992) Gene , vol.122 , pp. 163-169
    • Charlton, S.1    Boulianne, R.2    Chow, Y.-C.3    Lu, B.C.4
  • 279
    • 0029610214 scopus 로고
    • Cloning, characterization and overproduction of nuclease S1 gene (nucS) from Aspergillus oryzae
    • Lee B.R., Kitamoto K., Yamada O., Kumagai C. Cloning, characterization and overproduction of nuclease S1 gene (nucS) from Aspergillus oryzae. Appl. Microbiol. Biotechnol. 44:1995;425-431.
    • (1995) Appl. Microbiol. Biotechnol. , vol.44 , pp. 425-431
    • Lee, B.R.1    Kitamoto, K.2    Yamada, O.3    Kumagai, C.4
  • 280
    • 0025093863 scopus 로고
    • Crystallisation and preliminary crystallographic analysis of P1 nuclease from Penicillium citrinum
    • Lahm A., Volbeda A., Suck D. Crystallisation and preliminary crystallographic analysis of P1 nuclease from Penicillium citrinum. J. Mol. Biol. 215:1990;207-210.
    • (1990) J. Mol. Biol. , vol.215 , pp. 207-210
    • Lahm, A.1    Volbeda, A.2    Suck, D.3
  • 281
    • 0025763145 scopus 로고
    • Crystal structure of Penicillium citrinum P1 nuclease at 2.8Å resolution
    • Volbeda A., Lahm A., Sakiyama F., Suck D. Crystal structure of Penicillium citrinum P1 nuclease at 2.8Å resolution. EMBO J. 10:1991;1607-1618.
    • (1991) EMBO J. , vol.10 , pp. 1607-1618
    • Volbeda, A.1    Lahm, A.2    Sakiyama, F.3    Suck, D.4
  • 283
    • 0026492496 scopus 로고
    • Characterization of S1 nuclease: Involvement of carboxylate groups in metal binding
    • Gite S., Shankar V. Characterization of S1 nuclease: involvement of carboxylate groups in metal binding. Eur. J. Biochem. 210:1992;437-441.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 437-441
    • Gite, S.1    Shankar, V.2
  • 285
    • 0003147860 scopus 로고
    • Recognition of double- and single-stranded substrates by nucleases: Structural studies of DNase I and P1 nuclease
    • Kyogozu, Y. and Nishimura, Y., Eds.. CRC Press, Boca Raton, FL
    • Suck, D. (1992) Recognition of double- and single-stranded substrates by nucleases: structural studies of DNase I and P1 nuclease. In: Molecular Structure and Life (Kyogozu, Y. and Nishimura, Y., Eds.), pp. 141-156. CRC Press, Boca Raton, FL.
    • (1992) Molecular Structure and Life , pp. 141-156
    • Suck, D.1
  • 286
    • 0033591238 scopus 로고    scopus 로고
    • The active site of Serratia endonuclease contains a conserved magnesium-water cluster
    • Miller M.D., Cai J., Krause K.L. The active site of Serratia endonuclease contains a conserved magnesium-water cluster. J. Mol. Biol. 288:1999;975-987.
    • (1999) J. Mol. Biol. , vol.288 , pp. 975-987
    • Miller, M.D.1    Cai, J.2    Krause, K.L.3
  • 287
    • 0018801720 scopus 로고
    • Staphylococcal nuclease reviewed: A prototypic study in contemporary enzymology. III. Correlation of the three-dimensional structure with the mechanisms of enzymatic action
    • Tucker P.W., Hazen E.E. Jr., Cotton F.A. Staphylococcal nuclease reviewed: a prototypic study in contemporary enzymology. III. Correlation of the three-dimensional structure with the mechanisms of enzymatic action. Mol. Cell Biochem. 23:1979;67-86.
    • (1979) Mol. Cell Biochem. , vol.23 , pp. 67-86
    • Tucker, P.W.1    Hazen E.E., Jr.2    Cotton, F.A.3
  • 288
    • 0016155198 scopus 로고
    • Identity of phosphodiesterase and phosphomonoesterase activities with nuclease P1 (a nuclease from Penicillium citrinum)
    • Fujimoto M., Kuninaka A., Yoshino H. Identity of phosphodiesterase and phosphomonoesterase activities with nuclease P1 (a nuclease from Penicillium citrinum). Agric. Biol. Chem. 38:1974;785-790.
    • (1974) Agric. Biol. Chem. , vol.38 , pp. 785-790
    • Fujimoto, M.1    Kuninaka, A.2    Yoshino, H.3
  • 289
    • 0024748187 scopus 로고
    • Influence of lectin concentration on the catalytic properties of S1 nuclease bound to concanavalin A-Sepharose
    • Reddy L.G., Shankar V. Influence of lectin concentration on the catalytic properties of S1 nuclease bound to concanavalin A-Sepharose. Appl. Biochem. Biotechnol. 22:1989;79-94.
    • (1989) Appl. Biochem. Biotechnol. , vol.22 , pp. 79-94
    • Reddy, L.G.1    Shankar, V.2
  • 290
    • 0026489354 scopus 로고
    • Active-site characterization of S1 nuclease. II. Involvement of histidine in catalysis
    • Gite S., Reddy G., Shankar V. Active-site characterization of S1 nuclease. II. Involvement of histidine in catalysis. Biochem. J. 288:1992;571-575.
    • (1992) Biochem. J. , vol.288 , pp. 571-575
    • Gite, S.1    Reddy, G.2    Shankar, V.3
  • 291
    • 0035761214 scopus 로고    scopus 로고
    • Active site characterization of nuclease Bh1 from Basidiobolus haptosporus: Involvement of lysine in substrate binding and carboxylate in catalysis
    • Desai N.A., Shankar V. Active site characterization of nuclease Bh1 from Basidiobolus haptosporus: involvement of lysine in substrate binding and carboxylate in catalysis. J. Biochem. Mol. Biol. Biophys. 5:2001;327-334.
    • (2001) J. Biochem. Mol. Biol. Biophys. , vol.5 , pp. 327-334
    • Desai, N.A.1    Shankar, V.2
  • 292
    • 0031850427 scopus 로고    scopus 로고
    • Recognition of single-stranded DNA by nuclease P1: High resolution crystal structures of complexes with substrate analogs
    • Romier C., Dominguez R., Lahm A., Dahl O., Suck D. Recognition of single-stranded DNA by nuclease P1: high resolution crystal structures of complexes with substrate analogs. Proteins Struct. Funct. Genet. 32:1998;414-424.
    • (1998) Proteins Struct. Funct. Genet. , vol.32 , pp. 414-424
    • Romier, C.1    Dominguez, R.2    Lahm, A.3    Dahl, O.4    Suck, D.5
  • 294
    • 0031090688 scopus 로고    scopus 로고
    • Common fold, common function, common origin?
    • Suck D. Common fold, common function, common origin? Nat. Struct. Biol. 4:1997;161-165.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 161-165
    • Suck, D.1
  • 295
    • 0033524487 scopus 로고    scopus 로고
    • Mutagenesis of conserved lysine residues in bacteriophage T5 5′-3′ exonuclease suggests separate mechanisms of endo- and exonucleolytic cleavage
    • Garforth S.J., Ceska T.A., Suck D., Sayers J.R. Mutagenesis of conserved lysine residues in bacteriophage T5 5′-3′ exonuclease suggests separate mechanisms of endo- and exonucleolytic cleavage. Proc. Natl. Acad. Sci. USA. 96:1999;38-43.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 38-43
    • Garforth, S.J.1    Ceska, T.A.2    Suck, D.3    Sayers, J.R.4
  • 296
    • 0025333937 scopus 로고
    • Crystal structure of the complex of carboxypeptidase A with a strongly bound phosphonate in a new crystalline form: Comparison with structures of other complexes
    • Kim H., Lipscomb W.N. Crystal structure of the complex of carboxypeptidase A with a strongly bound phosphonate in a new crystalline form: comparison with structures of other complexes. Biochemistry. 29:1990;5546-5555.
    • (1990) Biochemistry , vol.29 , pp. 5546-5555
    • Kim, H.1    Lipscomb, W.N.2
  • 297
    • 0026019625 scopus 로고
    • Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism
    • Beese L.S., Steitz T.A. Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. EMBO J. 10:1991;25-33.
    • (1991) EMBO J. , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 298
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz T.A., Steitz J.A. A general two-metal-ion mechanism for catalytic RNA. Proc. Natl. Acad. Sci. USA. 90:1993;6498-6502.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 299
    • 0025777694 scopus 로고
    • Reaction mechanism of alkaline phosphatase based on crystal structures: Two-metal ion catalysis
    • Kim E.E., Wyckoff H.W. Reaction mechanism of alkaline phosphatase based on crystal structures: two-metal ion catalysis. J. Mol. Biol. 218:1991;449-464.
    • (1991) J. Mol. Biol. , vol.218 , pp. 449-464
    • Kim, E.E.1    Wyckoff, H.W.2
  • 300
    • 0028983795 scopus 로고
    • Crystal structure of Thermus aquaticus DNA polymerase
    • Kim Y., Eom S.H., Wang J., Lee D.S., Suh S.W., Steitz T.A. Crystal structure of Thermus aquaticus DNA polymerase. Nature. 376:1995;612-616.
    • (1995) Nature , vol.376 , pp. 612-616
    • Kim, Y.1    Eom, S.H.2    Wang, J.3    Lee, D.S.4    Suh, S.W.5    Steitz, T.A.6
  • 301
    • 0030789339 scopus 로고    scopus 로고
    • Modification of an essential amino group of glutathione reductase from yeast by pyridoxal 5′-phosphate
    • Pandey A., Iyengar L., Katiyar S.S. Modification of an essential amino group of glutathione reductase from yeast by pyridoxal 5′-phosphate. J. Enzyme Inhib. 12:1997;143-154.
    • (1997) J. Enzyme Inhib. , vol.12 , pp. 143-154
    • Pandey, A.1    Iyengar, L.2    Katiyar, S.S.3
  • 302
    • 0030692045 scopus 로고    scopus 로고
    • Identification of residues of T4 RNase H required for catalysis and DNA binding
    • Bhagwat M., Meara D., Nossal N.G. Identification of residues of T4 RNase H required for catalysis and DNA binding. J. Biol. Chem. 272:1997;28531-28538.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28531-28538
    • Bhagwat, M.1    Meara, D.2    Nossal, N.G.3
  • 303
    • 0030872252 scopus 로고    scopus 로고
    • Functional analysis of point mutations in human flap endonuclease-1 active site
    • Shen B., Nolan J.P., Sklar L.A., Park M.S. Functional analysis of point mutations in human flap endonuclease-1 active site. Nucleic Acids Res. 25:1997;3332-3338.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3332-3338
    • Shen, B.1    Nolan, J.P.2    Sklar, L.A.3    Park, M.S.4
  • 304
    • 0030002197 scopus 로고    scopus 로고
    • A helical arch allowing single-stranded DNA to thread through T5 5′-exonuclease
    • Ceska T.A., Sayers J.R., Stier G., Suck D. A helical arch allowing single-stranded DNA to thread through T5 5′-exonuclease. Nature. 382:1996;90-93.
    • (1996) Nature , vol.382 , pp. 90-93
    • Ceska, T.A.1    Sayers, J.R.2    Stier, G.3    Suck, D.4
  • 305
    • 0027977143 scopus 로고
    • 2.1 Å structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA
    • Miller M.D., Tanner J., Alpaugh M., Benedik M.J., Krause K.L. 2.1 Å structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA. Nat. Struct. Biol. 1:1994;461-468.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 461-468
    • Miller, M.D.1    Tanner, J.2    Alpaugh, M.3    Benedik, M.J.4    Krause, K.L.5
  • 306
    • 0030592844 scopus 로고    scopus 로고
    • Analysis of the reaction mechanism of the non-specific endonuclease of Serratia marcescens using an artificial minimal substrate
    • Kolmes B., Franke I., Friedhoff P., Pingoud A. Analysis of the reaction mechanism of the non-specific endonuclease of Serratia marcescens using an artificial minimal substrate. FEBS Lett. 397:1996;343-346.
    • (1996) FEBS Lett. , vol.397 , pp. 343-346
    • Kolmes, B.1    Franke, I.2    Friedhoff, P.3    Pingoud, A.4
  • 308
    • 0001431264 scopus 로고    scopus 로고
    • Binuclear metallohydrolases
    • Wilcox D.E. Binuclear metallohydrolases. Chem. Rev. 96:1996;2435-2458.
    • (1996) Chem. Rev. , vol.96 , pp. 2435-2458
    • Wilcox, D.E.1
  • 309
    • 0013172970 scopus 로고
    • Correlation of endonuclease activity at meiotic prophase and cofactor-induced genetic recombination in Basidiomycete Coprinus cinerus
    • Lu B.C., Li X.-Y. Correlation of endonuclease activity at meiotic prophase and cofactor-induced genetic recombination in Basidiomycete Coprinus cinerus. Genome. 30:1988;380-386.
    • (1988) Genome , vol.30 , pp. 380-386
    • Lu, B.C.1    Li, X.-Y.2
  • 310
    • 0019983232 scopus 로고
    • Meiosis in Coprinus: Characterization and activities of two forms of DNA polymerase during meiotic stages
    • Sakaguchi K., Lu B.C. Meiosis in Coprinus: characterization and activities of two forms of DNA polymerase during meiotic stages. Mol. Cell. Biol. 2:1982;752-757.
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 752-757
    • Sakaguchi, K.1    Lu, B.C.2
  • 311
    • 0024232801 scopus 로고
    • Adsorption capability determines phage plaque size on Streptomyces antibioticus producing endodeoxyribonuclease
    • De los Reyes-Gavilan C.G., Aparicio J.F., Barbes C., Hardisson C., Sanchez J. Adsorption capability determines phage plaque size on Streptomyces antibioticus producing endodeoxyribonuclease. FEMS Microbiol. Lett. 56:1988;301-306.
    • (1988) FEMS Microbiol. Lett. , vol.56 , pp. 301-306
    • De los Reyes-Gavilan, C.G.1    Aparicio, J.F.2    Barbes, C.3    Hardisson, C.4    Sanchez, J.5
  • 312
    • 0025971585 scopus 로고
    • Nutritional regulation of differentiation and synthesis of an exocytoplasmic deoxyriboendonuclease in Streptomyces antibioticus
    • De los Reyes-Gavilan C., Cal S., Barbés C., Hardisson C., Sánchez J. Nutritional regulation of differentiation and synthesis of an exocytoplasmic deoxyriboendonuclease in Streptomyces antibioticus. J. Gen. Microbiol. 137:1991;299-305.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 299-305
    • De los Reyes-Gavilan, C.1    Cal, S.2    Barbés, C.3    Hardisson, C.4    Sánchez, J.5
  • 313
    • 0033575318 scopus 로고    scopus 로고
    • Purification, characterization, and role of nucleases and serine proteases in Streptomyces differentiation: Analogies with the biochemical processes described in late steps of eukaryotic apoptosis
    • Nicieza R.G., Huergo J., Connolly B.A., Sanchez J. Purification, characterization, and role of nucleases and serine proteases in Streptomyces differentiation: analogies with the biochemical processes described in late steps of eukaryotic apoptosis. J. Biol. Chem. 274:1999;20366-20375.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20366-20375
    • Nicieza, R.G.1    Huergo, J.2    Connolly, B.A.3    Sanchez, J.4
  • 314
    • 0023655179 scopus 로고
    • Identification of a glucocorticoid-induced nuclease in thymocytes: A potential 'lysis gene' product
    • Compton M.M., Cidlowski J.A. Identification of a glucocorticoid-induced nuclease in thymocytes: a potential 'lysis gene' product. J. Biol. Chem. 262:1987;8288-8292.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8288-8292
    • Compton, M.M.1    Cidlowski, J.A.2
  • 315
    • 0026006943 scopus 로고
    • Identification, purification, and characterization of a calcium-dependent endonuclease (NUC18) from apoptotic rat thymocytes: NUC18 is not histone H2B
    • Gaido M.L., Cidlowski J.A. Identification, purification, and characterization of a calcium-dependent endonuclease (NUC18) from apoptotic rat thymocytes: NUC18 is not histone H2B. J. Biol. Chem. 266:1991;18580-18585.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18580-18585
    • Gaido, M.L.1    Cidlowski, J.A.2
  • 316
    • 0028242351 scopus 로고
    • A calcium-dependent nuclease from apoptotic rat thymocytes is homologous with cyclophilin: Recombinant cyclophilins A, B, and C have nuclease activity
    • Montague J.W., Gaido M.L., Frye C., Cidlowski J.A. A calcium-dependent nuclease from apoptotic rat thymocytes is homologous with cyclophilin: recombinant cyclophilins A, B, and C have nuclease activity. J. Biol. Chem. 269:1994;18877-18880.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18877-18880
    • Montague, J.W.1    Gaido, M.L.2    Frye, C.3    Cidlowski, J.A.4
  • 317
    • 0030972976 scopus 로고    scopus 로고
    • Native recombinant cyclophilins A, B, and C degrade DNA independently of peptidylprolyl cis-trans-isomerase activity: Potential roles of cyclophilins in apoptosis
    • Montague J.W., Hughes F.M. Jr., Cidlowski J.A. Native recombinant cyclophilins A, B, and C degrade DNA independently of peptidylprolyl cis-trans-isomerase activity: potential roles of cyclophilins in apoptosis. J. Biol. Chem. 272:1997;6677-6684.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6677-6684
    • Montague, J.W.1    Hughes F.M., Jr.2    Cidlowski, J.A.3
  • 318
    • 0029909597 scopus 로고    scopus 로고
    • Programmed cell death: A way of life for plants
    • Greenberg J.T. Programmed cell death: a way of life for plants. Proc. Natl. Acad. Sci. USA. 93:1996;12094-12097.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12094-12097
    • Greenberg, J.T.1
  • 319
    • 0029893702 scopus 로고    scopus 로고
    • The origin of programmed cell death
    • Ameisen J.C. The origin of programmed cell death. Science. 272:1996;1278-1279.
    • (1996) Science , vol.272 , pp. 1278-1279
    • Ameisen, J.C.1
  • 320
    • 0030861751 scopus 로고    scopus 로고
    • Programmed cell death in prokaryotes
    • Hochman A. Programmed cell death in prokaryotes. Crit. Rev. Microbiol. 23:1997;207-214.
    • (1997) Crit. Rev. Microbiol. , vol.23 , pp. 207-214
    • Hochman, A.1
  • 322
    • 0030046508 scopus 로고    scopus 로고
    • Life, death, and the pursuit of apoptosis
    • Chem. Abstr. 124:107758
    • White, E. (1996) Life, death, and the pursuit of apoptosis. Genes Dev. 10, 1-15 (Chem. Abstr. 124:107758).
    • (1996) Genes Dev. , vol.10 , pp. 1-15
    • White, E.1
  • 323
    • 0030759279 scopus 로고    scopus 로고
    • Kinase cascades regulating entry into apoptosis
    • Anderson P. Kinase cascades regulating entry into apoptosis. Microbiol. Mol. Biol. Rev. 61:1997;33-46.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 33-46
    • Anderson, P.1
  • 324
    • 0030992234 scopus 로고    scopus 로고
    • Candidate nuclease responsible for genomic degradation during apoptosis
    • Chem. Abstr. 127:93039
    • Huang, S.-T., Hughes, F.M., Jr. and Cidlowski, J.A. (1997) Candidate nuclease responsible for genomic degradation during apoptosis. Comments Toxicol. 5, 555-569 (Chem. Abstr. 127:93039).
    • (1997) Comments Toxicol. , vol.5 , pp. 555-569
    • Huang, S.-T.1    Hughes F.M., Jr.2    Cidlowski, J.A.3
  • 325
    • 14044256627 scopus 로고    scopus 로고
    • Micrococcal nuclease (endonuclease) digestion causes apoptosis and mitotic catastrophe with interphase chromosome condensation in human Chang liver
    • Yin L., Sit K-H. Micrococcal nuclease (endonuclease) digestion causes apoptosis and mitotic catastrophe with interphase chromosome condensation in human Chang liver. Cell Death Differ. 4:1997;796-805.
    • (1997) Cell Death Differ. , vol.4 , pp. 796-805
    • Yin, L.1    Sit, K.-H.2
  • 326
    • 0033047287 scopus 로고    scopus 로고
    • Activation of a low pH-dependent nuclease by apoptotic agents
    • Chem. Abstr. 131:85942
    • Famulski, K.S., Macdonald, D., Paterson, M.C. and Sikora, E. (1999) Activation of a low pH-dependent nuclease by apoptotic agents. Cell Death Differ. 6, 281-289 (Chem. Abstr. 131:85942).
    • (1999) Cell Death Differ. , vol.6 , pp. 281-289
    • Famulski, K.S.1    Macdonald, D.2    Paterson, M.C.3    Sikora, E.4
  • 328
  • 329
    • 0018847066 scopus 로고
    • Measurement of Staphylcoccus aureus nuclease and antinucleases: Applicability for the assessment of mastitic milk
    • Chem. Abstr. 93:163241
    • Gudding, R. (1980) Measurement of Staphylcoccus aureus nuclease and antinucleases: applicability for the assessment of mastitic milk. Acta Vet. Scand. 21, 229-241 (Chem. Abstr. 93:163241).
    • (1980) Acta Vet. Scand. , vol.21 , pp. 229-241
    • Gudding, R.1
  • 330
    • 0018815324 scopus 로고
    • Nuclease of Staphylococcus epidermidis isolated from mastitic milk: Production and some properties
    • Chem. Abstr. 93: 110305
    • Gudding, R. (1980) Nuclease of Staphylococcus epidermidis isolated from mastitic milk: production and some properties. Acta Vet. Scand. 21, 267-277 (Chem. Abstr. 93: 110305).
    • (1980) Acta Vet. Scand. , vol.21 , pp. 267-277
    • Gudding, R.1
  • 331
    • 0020001427 scopus 로고
    • Thermostable nuclease activity of Staphylococci from clinical sources
    • Chem. Abstr. 96:177612
    • Sundaram, S.P., Kumari, S.L.S. and Murthy, K.V. (1982) Thermostable nuclease activity of Staphylococci from clinical sources. Indian J. Med. Res. 75, 19-22 (Chem. Abstr. 96:177612).
    • (1982) Indian J. Med. Res. , vol.75 , pp. 19-22
    • Sundaram, S.P.1    Kumari, S.L.S.2    Murthy, K.V.3
  • 332
    • 0001216075 scopus 로고
    • Staphylococcus aureus growth and thermostable nuclease and enterotoxin production in canned salmon and sardines
    • Chem. Abstr. 105:77691
    • Stersky, A.K., Szabo, R., Todd, E.C.D., Thacker, C., Dickie, N. and Akhtar, M. (1986) Staphylococcus aureus growth and thermostable nuclease and enterotoxin production in canned salmon and sardines. J. Food Prot. 49, 428-435 (Chem. Abstr. 105:77691).
    • (1986) J. Food Prot. , vol.49 , pp. 428-435
    • Stersky, A.K.1    Szabo, R.2    Todd, E.C.D.3    Thacker, C.4    Dickie, N.5    Akhtar, M.6
  • 333
    • 0023736880 scopus 로고
    • Staphylococcus aureus, thermostable nuclease and Staphylococcal enterotoxins in raw ewes′ milk Manchego cheese
    • Chem. Abstr. 110:6595
    • Nunez, M., Bautista, L., Medina, M., and Gaya, P. (1988) Staphylococcus aureus, thermostable nuclease and Staphylococcal enterotoxins in raw ewes′ milk Manchego cheese. J. Appl. Bacteriol. 65, 29-34 (Chem. Abstr. 110:6595).
    • (1988) J. Appl. Bacteriol. , vol.65 , pp. 29-34
    • Nunez, M.1    Bautista, L.2    Medina, M.3    Gaya, P.4
  • 334
    • 0030817752 scopus 로고    scopus 로고
    • Serratia marcescens
    • Chem. Abstr. 128:20317
    • Hejazi, A. and Falkiner, F.R. (1997) Serratia marcescens. J. Med. Microbiol. 46, 903-912 (Chem. Abstr. 128:20317).
    • (1997) J. Med. Microbiol. , vol.46 , pp. 903-912
    • Hejazi, A.1    Falkiner, F.R.2
  • 336
    • 0028913520 scopus 로고
    • Major allergen Phl p Vb in timothy grass is a novel pollen RNase
    • Bufe A., Schramm G., Keown M.B., Schlaak M., Becker W.M. Major allergen Phl p Vb in timothy grass is a novel pollen RNase. FEBS Lett. 363:1995;6-12.
    • (1995) FEBS Lett. , vol.363 , pp. 6-12
    • Bufe, A.1    Schramm, G.2    Keown, M.B.3    Schlaak, M.4    Becker, W.M.5
  • 338
    • 0032828291 scopus 로고    scopus 로고
    • A nonspecific, single-stranded nuclease activity with characteristics of a topoisomerase found in a major grass pollen allergen: Possible biological significance
    • Bufe A., Uhlig U., Scholzen T., Matousek J., Schlaak M., Weber W. A nonspecific, single-stranded nuclease activity with characteristics of a topoisomerase found in a major grass pollen allergen: possible biological significance. Biol. Chem. 380:1999;1009-1016.
    • (1999) Biol. Chem. , vol.380 , pp. 1009-1016
    • Bufe, A.1    Uhlig, U.2    Scholzen, T.3    Matousek, J.4    Schlaak, M.5    Weber, W.6
  • 339
    • 0031954117 scopus 로고    scopus 로고
    • In situ localization of a high molecular weight cross-reactive allergen in pollen and plant-derived food by immunogold electron microscopy
    • Grote M., Fischer S., Muller W.D., Valenta R. In situ localization of a high molecular weight cross-reactive allergen in pollen and plant-derived food by immunogold electron microscopy. J. Allergy Clin. Immunol. 101:1998;250-257.
    • (1998) J. Allergy Clin. Immunol. , vol.101 , pp. 250-257
    • Grote, M.1    Fischer, S.2    Muller, W.D.3    Valenta, R.4
  • 340
    • 0027431127 scopus 로고
    • Properties of tree and grass pollen allergens: Reinvestigation of the linkage between solubility and allergenicity
    • Chem. Abstr. 120:104869
    • Vrtala, S., Grote, M., Duchene, M., van Ree, R., Kraft, D., Scheiner, O. and Valenta, R. (1993) Properties of tree and grass pollen allergens: reinvestigation of the linkage between solubility and allergenicity. Int. Arch. Allergy Immunol. 102, 160-169 (Chem. Abstr. 120:104869).
    • (1993) Int. Arch. Allergy Immunol. , vol.102 , pp. 160-169
    • Vrtala, S.1    Grote, M.2    Duchene, M.3    Van Ree, R.4    Kraft, D.5    Scheiner, O.6    Valenta, R.7
  • 341
    • 0029861903 scopus 로고    scopus 로고
    • Crystallization and preliminary diffraction data of a major pollen allergen: Crystal growth separates a low molecular weight form with elevated biological activity
    • Bufe A., Betzel C., Schramm G., Petersen A., Becker W.M., Schlaak M., Perbandt M., Dauter Z., Weber W. Crystallization and preliminary diffraction data of a major pollen allergen: crystal growth separates a low molecular weight form with elevated biological activity. J. Biol. Chem. 271:1996;27193-27196.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27193-27196
    • Bufe, A.1    Betzel, C.2    Schramm, G.3    Petersen, A.4    Becker, W.M.5    Schlaak, M.6    Perbandt, M.7    Dauter, Z.8    Weber, W.9
  • 343
    • 0015520302 scopus 로고
    • Estimation of the double-helical content in various single-stranded nucleic acids by treatment with a single strand-specific nuclease
    • Shishido K., Ando T. Estimation of the double-helical content in various single-stranded nucleic acids by treatment with a single strand-specific nuclease. Biochim. Biophys. Acta. 287:1972;477-484.
    • (1972) Biochim. Biophys. Acta , vol.287 , pp. 477-484
    • Shishido, K.1    Ando, T.2
  • 344
    • 0014803154 scopus 로고
    • Some properties of the polynucleotide segments isolated from heat-denatured DNA by digestion with a nuclease specific for single stranded DNA
    • Shishido K., Ikeda Y. Some properties of the polynucleotide segments isolated from heat-denatured DNA by digestion with a nuclease specific for single stranded DNA. J. Biochem. (Tokyo). 67:1970;759-763.
    • (1970) J. Biochem. (Tokyo) , vol.67 , pp. 759-763
    • Shishido, K.1    Ikeda, Y.2
  • 345
    • 0015211118 scopus 로고
    • Isolation of double-helical regions rich in guanine-cytosine base pairing from bacteriophage fl DNA
    • Shishido K., Ikeda Y. Isolation of double-helical regions rich in guanine-cytosine base pairing from bacteriophage fl DNA. Biochem. Biophys. Res. Commun. 42:1971;482-489.
    • (1971) Biochem. Biophys. Res. Commun. , vol.42 , pp. 482-489
    • Shishido, K.1    Ikeda, Y.2
  • 346
    • 0015242818 scopus 로고
    • Isolation of double helical regions rich in adenine-thymine base pairing from bacteriophage f1 DNA
    • Shishido K., Ikeda Y. Isolation of double helical regions rich in adenine-thymine base pairing from bacteriophage f1 DNA. J. Mol. Biol. 55:1971;287-291.
    • (1971) J. Mol. Biol. , vol.55 , pp. 287-291
    • Shishido, K.1    Ikeda, Y.2
  • 347
    • 0017724552 scopus 로고
    • Sizing and mapping of early adenovirus mRNAs by gel electrophoresis of S1 endonuclease-digested hybrids
    • Berk A.J., Sharp P.A. Sizing and mapping of early adenovirus mRNAs by gel electrophoresis of S1 endonuclease-digested hybrids. Cell. 12:1977;721-732.
    • (1977) Cell , vol.12 , pp. 721-732
    • Berk, A.J.1    Sharp, P.A.2
  • 348
    • 0031616481 scopus 로고    scopus 로고
    • S1 mapping using single-stranded DNA probes
    • Viville S., Mantovani R. S1 mapping using single-stranded DNA probes. Methods Mol. Biol. 86:1998;195-200.
    • (1998) Methods Mol. Biol. , vol.86 , pp. 195-200
    • Viville, S.1    Mantovani, R.2
  • 349
    • 0018787476 scopus 로고
    • Mapping of RNA by a modification of the Berk-Sharp procedure: The 5′ termini of 15 S β-globin mRNA precursor and mature 10 s β-globin mRNA have identical map coordinates
    • Weaver R.F., Weissmann C. Mapping of RNA by a modification of the Berk-Sharp procedure: the 5′ termini of 15 S β-globin mRNA precursor and mature 10 s β-globin mRNA have identical map coordinates. Nucleic Acids Res. 7:1979;1175-1193.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1175-1193
    • Weaver, R.F.1    Weissmann, C.2
  • 350
    • 0018846450 scopus 로고
    • Transcription map of polyoma virus-specific RNA: Analysis by two-dimensional nuclease S1 gel mapping
    • Favalaro J., Treisman R., Kamen R. Transcription map of polyoma virus-specific RNA: analysis by two-dimensional nuclease S1 gel mapping. Methods Enzymol. 65:1980;718-730.
    • (1980) Methods Enzymol. , vol.65 , pp. 718-730
    • Favalaro, J.1    Treisman, R.2    Kamen, R.3
  • 352
    • 0024756969 scopus 로고
    • Rapid and sensitive detection of point mutations and DNA polymorphisms using the polymerase chain reaction
    • Orita M., Suzuki Y., Sekiya T., Hayashi K. Rapid and sensitive detection of point mutations and DNA polymorphisms using the polymerase chain reaction. Genomics. 5:1989;874-879.
    • (1989) Genomics , vol.5 , pp. 874-879
    • Orita, M.1    Suzuki, Y.2    Sekiya, T.3    Hayashi, K.4
  • 356
    • 0032520005 scopus 로고    scopus 로고
    • DNA-carrying latex particles for DNA diagnosis 2. Distinction of normal and point mutant DNA using S1 nuclease
    • Chem. Abstr. 128:279295
    • Hatakeyama, M., Nakamura, K., Iwato, S., Handa, H., Fujimoto, K. and Kawaguchi, H. (1998) DNA-carrying latex particles for DNA diagnosis 2. Distinction of normal and point mutant DNA using S1 nuclease. Colloids Surf. B. Biointerfaces 10, 171-175 (Chem. Abstr. 128:279295).
    • (1998) Colloids Surf. B. Biointerfaces , vol.10 , pp. 171-175
    • Hatakeyama, M.1    Nakamura, K.2    Iwato, S.3    Handa, H.4    Fujimoto, K.5    Kawaguchi, H.6
  • 357
    • 0017133050 scopus 로고
    • Specific excision of the inserted DNA segment from hybrid plasmids constructed by the poly(dA), poly(dT) method
    • Hofstetter H., Schamböck A., van Den Berg J., Weissmann C. Specific excision of the inserted DNA segment from hybrid plasmids constructed by the poly(dA), poly(dT) method. Biochim. Biophys. Acta. 454:1976;587-591.
    • (1976) Biochim. Biophys. Acta , vol.454 , pp. 587-591
    • Hofstetter, H.1    Schamböck, A.2    Van Den Berg, J.3    Weissmann, C.4
  • 358
    • 0018832897 scopus 로고
    • A temperature-sensitive single-stranded DNA-binding protein from Escherichia coli
    • Meyer R.R., Glassberg J., Scott J.V., Kornberg A. A temperature-sensitive single-stranded DNA-binding protein from Escherichia coli. J. Biol. Chem. 255:1980;2897-2901.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2897-2901
    • Meyer, R.R.1    Glassberg, J.2    Scott, J.V.3    Kornberg, A.4
  • 359
    • 84998371538 scopus 로고
    • Enzymatic studies on binding of mutagenic principles in tryptophan pyrolysate to DNA
    • Shishido K., Tachibana T., Ando T. Enzymatic studies on binding of mutagenic principles in tryptophan pyrolysate to DNA. Agric. Biol. Chem. 44:1980;1609-1616.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 1609-1616
    • Shishido, K.1    Tachibana, T.2    Ando, T.3
  • 362
    • 0013129204 scopus 로고    scopus 로고
    • Detection of non-β-DNA secondary structures by S1 nuclease digestion
    • Del Olmo M., Aranda A., Perez-Ortin J.E. Detection of non-β-DNA secondary structures by S1 nuclease digestion. J. Chem. Educ. 75:1998;762-765.
    • (1998) J. Chem. Educ. , vol.75 , pp. 762-765
    • Del Olmo, M.1    Aranda, A.2    Perez-Ortin, J.E.3
  • 363
    • 0024820208 scopus 로고
    • Characterization of RNA molecules by S1 nuclease analysis
    • Berk A.J. Characterization of RNA molecules by S1 nuclease analysis. Methods Enzymol. 180:1989;334-347.
    • (1989) Methods Enzymol. , vol.180 , pp. 334-347
    • Berk, A.J.1
  • 364
    • 0013167455 scopus 로고    scopus 로고
    • S1 nuclease analysis of RNA
    • Rapley, R. and Walker, J.M., Eds. Humana Press, Totowa, NJ
    • Lefebvre, L. and Viville, S. (1998) S1 nuclease analysis of RNA. In: Molecular Biomethods Handbook (Rapley, R. and Walker, J.M., Eds.), pp. 35-49. Humana Press, Totowa, NJ.
    • (1998) Molecular Biomethods Handbook , pp. 35-49
    • Lefebvre, L.1    Viville, S.2
  • 369
    • 0028922710 scopus 로고
    • Influence of modified nucleosides on tRNA structure as probed by two plant nucleases
    • Przykorska A. Influence of modified nucleosides on tRNA structure as probed by two plant nucleases. Biochimie. 77:1995;109-112.
    • (1995) Biochimie , vol.77 , pp. 109-112
    • Przykorska, A.1
  • 370
    • 0016442397 scopus 로고
    • Reovirus messenger RNA contains a methylated, blocked 5′-terminal structure: M-7G(5′)ppp(5′)G-MpCp
    • Furuichi Y., Morgan M., Muthukrishnan S., Shatkin A.J. Reovirus messenger RNA contains a methylated, blocked 5′-terminal structure: m-7G(5′)ppp(5′)G-MpCp. Proc. Natl. Acad. Sci. USA. 72:1975;362-366.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 362-366
    • Furuichi, Y.1    Morgan, M.2    Muthukrishnan, S.3    Shatkin, A.J.4
  • 371
    • 84954931371 scopus 로고
    • Estimation of DNA base composition by high performance liquid chromatography of its nuclease P1 hydrolysate
    • Katayama-Fujimura Y., Komatsu Y., Kuraishi H., Kaneko T. Estimation of DNA base composition by high performance liquid chromatography of its nuclease P1 hydrolysate. Agric. Biol. Chem. 48:1984;3169-3172.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 3169-3172
    • Katayama-Fujimura, Y.1    Komatsu, Y.2    Kuraishi, H.3    Kaneko, T.4
  • 372
    • 0024035125 scopus 로고
    • Removal of nucleic acid contaminants using nuclease enzymes during protein isolation
    • Zabriskie D.W., DiPaolo M. Removal of nucleic acid contaminants using nuclease enzymes during protein isolation. Biotechnol. Bioeng. 32:1988;100-104.
    • (1988) Biotechnol. Bioeng. , vol.32 , pp. 100-104
    • Zabriskie, D.W.1    DiPaolo, M.2
  • 373
    • 0017621467 scopus 로고
    • The use of nuclease P1 in sequence analysis of end group labeled RNA
    • Silberklang M., Gillum A.M., RajBhandary U.L. The use of nuclease P1 in sequence analysis of end group labeled RNA. Nucleic Acids Res. 4:1977;4091-4108.
    • (1977) Nucleic Acids Res. , vol.4 , pp. 4091-4108
    • Silberklang, M.1    Gillum, A.M.2    RajBhandary, U.L.3
  • 374
    • 0020149828 scopus 로고
    • Partial P1 nuclease digestion as a probe of tRNA structure
    • Aultman K.S., Chang S.H. Partial P1 nuclease digestion as a probe of tRNA structure. Eur. J. Biochem. 124:1982;471-476.
    • (1982) Eur. J. Biochem. , vol.124 , pp. 471-476
    • Aultman, K.S.1    Chang, S.H.2
  • 376
    • 0014945068 scopus 로고
    • Isolation of Escherichia coli transfer RNA-gene hybrids
    • Marks A., Spencer J.H. Isolation of Escherichia coli transfer RNA-gene hybrids. J. Mol. Biol. 51:1970;115-130.
    • (1970) J. Mol. Biol. , vol.51 , pp. 115-130
    • Marks, A.1    Spencer, J.H.2
  • 377
    • 0017256122 scopus 로고
    • Purification of sea urchin ribosomal RNA genes with a single-strand specific nuclease
    • Joseph D.R., Stafford D.W. Purification of sea urchin ribosomal RNA genes with a single-strand specific nuclease. Biochim. Biophys. Acta. 418:1976;167-174.
    • (1976) Biochim. Biophys. Acta , vol.418 , pp. 167-174
    • Joseph, D.R.1    Stafford, D.W.2
  • 378
    • 0016213896 scopus 로고
    • Detection of sequence heterology by use of Neurospora crassa nuclease
    • Bartok K., Fraser M.J., Fareed G.C. Detection of sequence heterology by use of Neurospora crassa nuclease. Biochem. Biophys. Res. Commun. 60:1974;507-514.
    • (1974) Biochem. Biophys. Res. Commun. , vol.60 , pp. 507-514
    • Bartok, K.1    Fraser, M.J.2    Fareed, G.C.3
  • 379
    • 0017848516 scopus 로고
    • Extracellular nucleases of Pseudomonas BAL 31. III. Use of the double-strand deoxyriboexonuclease activity as the basis of a convenient method for the mapping of fragments of DNA produced by cleavage with restriction enzymes
    • Legerski R.J., Hodnett J.L., Gray H.B. Jr. Extracellular nucleases of Pseudomonas BAL 31. III. Use of the double-strand deoxyriboexonuclease activity as the basis of a convenient method for the mapping of fragments of DNA produced by cleavage with restriction enzymes. Nucleic Acids Res. 5:1978;1445-1464.
    • (1978) Nucleic Acids Res. , vol.5 , pp. 1445-1464
    • Legerski, R.J.1    Hodnett, J.L.2    Gray H.B., Jr.3
  • 380
    • 0013173502 scopus 로고
    • Nucleotides as flavor enhances
    • Gutcho, S., Ed. Noyes Data Corporation, NJ
    • Gutcho, S. (1970) Nucleotides as flavor enhances. In: Nucleotides and Nucleosides (Gutcho, S., Ed.), pp. 181-195. Noyes Data Corporation, NJ.
    • (1970) Nucleotides and Nucleosides , pp. 181-195
    • Gutcho, S.1
  • 381
    • 0018225125 scopus 로고
    • Application of sheep kidney nuclease to nucleic acid research: Enzymatic preparation of deoxy dinucleotides
    • Watanabe T. Application of sheep kidney nuclease to nucleic acid research: enzymatic preparation of deoxy dinucleotides. Anal. Biochem. 88:1978;62-68.
    • (1978) Anal. Biochem. , vol.88 , pp. 62-68
    • Watanabe, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.