메뉴 건너뛰기




Volumn 216, Issue 1, 1996, Pages 102-123

Analysis of 94 kb of the Chlorella virus PBCV-1 330-kb genome: Map positions 88 to 182

Author keywords

[No Author keywords available]

Indexed keywords

ALGA; ARTICLE; CHLORELLA; DNA SEQUENCE; GENETIC ANALYSIS; NONHUMAN; OPEN READING FRAME; PLANT VIRUS; PRIORITY JOURNAL;

EID: 0029918423     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1996.0038     Document Type: Article
Times cited : (46)

References (106)
  • 5
    • 0029001791 scopus 로고
    • A mutational analysis of the yeast proliferating cell nuclear antigen indicates distinct roles in DNA replication and DNA repair
    • Ayyagari, R., Impellizzeri, K. J., Yoder, B. L., Gary, S. L., and Burgers, P. M. J. (1995). A mutational analysis of the yeast proliferating cell nuclear antigen indicates distinct roles in DNA replication and DNA repair. Mol. Cell. Biol. 15, 4420-4429.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4420-4429
    • Ayyagari, R.1    Impellizzeri, K.J.2    Yoder, B.L.3    Gary, S.L.4    Burgers, P.M.J.5
  • 6
    • 0025882349 scopus 로고
    • PROSITE: A dictionary of sites and patterns in protein
    • Bairoch, A. (1991). PROSITE: A dictionary of sites and patterns in protein. Nucleic Acids Res. 19, 2241-2245.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 2241-2245
    • Bairoch, A.1
  • 7
    • 0023463279 scopus 로고
    • Aspects of the structure, function, and applications of superoxide dismutase
    • Bannister, J. V., Bannister, W. H., and Rotilio, G. (1987). Aspects of the structure, function, and applications of superoxide dismutase. CRC Biochem. 22, 111-180.
    • (1987) CRC Biochem. , vol.22 , pp. 111-180
    • Bannister, J.V.1    Bannister, W.H.2    Rotilio, G.3
  • 8
    • 0028173675 scopus 로고
    • Identification of Fuz7, a Ustilago maydis MEK/MAPKK homolog required for a-locus-dependent and -independent steps in the fungal life cycle
    • Banuett, F., and Herskowitz, I. (1994). Identification of Fuz7, a Ustilago maydis MEK/MAPKK homolog required for a-locus-dependent and -independent steps in the fungal life cycle. Genes Dev. 8, 1367-1378.
    • (1994) Genes Dev. , vol.8 , pp. 1367-1378
    • Banuett, F.1    Herskowitz, I.2
  • 9
    • 0024043518 scopus 로고
    • The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae:Cloning, sequencing, and biological activity
    • Bermingham-McDonogh, O., Gralla, E. B., and Valentine, J. S. (1988). The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae:Cloning, sequencing, and biological activity. Proc. Natl. Acad. Sci. USA 85, 4789-4793.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4789-4793
    • Bermingham-McDonogh, O.1    Gralla, E.B.2    Valentine, J.S.3
  • 10
    • 0026761188 scopus 로고
    • Primary structure of a chitinase-encoding gene (chi1) from the filamentous fungus Aphanocladium album: Similarity to bacterial chitinases
    • Blaiseau, P., and Lafay, J. (1992). Primary structure of a chitinase-encoding gene (chi1) from the filamentous fungus Aphanocladium album: Similarity to bacterial chitinases. Gene 120, 243-248.
    • (1992) Gene , vol.120 , pp. 243-248
    • Blaiseau, P.1    Lafay, J.2
  • 11
    • 0025993126 scopus 로고
    • Sequence analysis, expression, and deletion of a vaccinia virus gene encoding a homolog of profilin, a eukaryotic actin-binding protein
    • Blasco, R., Cole, N. B., and Moss, B. (1991). Sequence analysis, expression, and deletion of a vaccinia virus gene encoding a homolog of profilin, a eukaryotic actin-binding protein. J. Virol. 65, 4598-4608.
    • (1991) J. Virol. , vol.65 , pp. 4598-4608
    • Blasco, R.1    Cole, N.B.2    Moss, B.3
  • 13
    • 0026446050 scopus 로고
    • Cloning and expression of a conjugated bile acid hydrolase gene from Lactobacillus plantarum by using a direct plate assay
    • Christiaens, H., Leer, R. J., Pouwels, P. H., and Verstraete, W. (1992). Cloning and expression of a conjugated bile acid hydrolase gene from Lactobacillus plantarum by using a direct plate assay. Appl. Environ. Microbiol. 58, 3792-3798.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3792-3798
    • Christiaens, H.1    Leer, R.J.2    Pouwels, P.H.3    Verstraete, W.4
  • 15
    • 0028106317 scopus 로고
    • Cloning, sequencing, and expression of a fibronectin/fibrinogen-binding protein from group A streptococci
    • Courtney, H. S., Li, Y., Dale, J. B., and Hasty, D. L. (1994). Cloning, sequencing, and expression of a fibronectin/fibrinogen-binding protein from group A streptococci. Infect. Immun. 62, 3937-3946.
    • (1994) Infect. Immun. , vol.62 , pp. 3937-3946
    • Courtney, H.S.1    Li, Y.2    Dale, J.B.3    Hasty, D.L.4
  • 16
    • 0023804990 scopus 로고
    • Characterization of an early gene accelerating expression of late genes of the baculovirus Autographa californica nuclear polyhedrosis virus
    • Crawford, A. M., and Miller, L. K. (1988). Characterization of an early gene accelerating expression of late genes of the baculovirus Autographa californica nuclear polyhedrosis virus. J. Virol. 62, 2773-2781.
    • (1988) J. Virol. , vol.62 , pp. 2773-2781
    • Crawford, A.M.1    Miller, L.K.2
  • 17
    • 0026695481 scopus 로고
    • Sequestered end products and enzyme regulation: The case of ornithine decarboxylase
    • Davis, R. H., Morris, D. R., and Coffino, P. (1992). Sequestered end products and enzyme regulation: The case of ornithine decarboxylase. Microbiol. Rev. 56, 280-290.
    • (1992) Microbiol. Rev. , vol.56 , pp. 280-290
    • Davis, R.H.1    Morris, D.R.2    Coffino, P.3
  • 18
    • 0021103457 scopus 로고
    • Random subcloning of sonicated DNA: Application to shotgun DNA sequence analysis
    • Deininger, P. L. (1983). Random subcloning of sonicated DNA: Application to shotgun DNA sequence analysis. Anal. Biochem. 129, 216-223.
    • (1983) Anal. Biochem. , vol.129 , pp. 216-223
    • Deininger, P.L.1
  • 19
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haeberli, P., and Smithies, O. (1984). A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12, 387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 21
    • 0027221966 scopus 로고
    • Nucleotide sequence of the heme subunit of flavocytochrome c from the purple phototrophic bacterium, Chromatium vinosum: A 2.6-kilobase pair DNA fragment contains two multiheme cytochromes, a flavoprotein, and a homolog of human ankyrin
    • Dolata, M. M., Van Beeumen, J. J., Ambler, R. P., Meyer, T. E., and Cusanovich, M. A. (1993). Nucleotide sequence of the heme subunit of flavocytochrome c from the purple phototrophic bacterium, Chromatium vinosum: A 2.6-kilobase pair DNA fragment contains two multiheme cytochromes, a flavoprotein, and a homolog of human ankyrin. J. Biol. Chem. 268, 14426-14431.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14426-14431
    • Dolata, M.M.1    Van Beeumen, J.J.2    Ambler, R.P.3    Meyer, T.E.4    Cusanovich, M.A.5
  • 22
    • 0028173073 scopus 로고
    • Ankyrin and β-spectrin accumulate independently of α-spectrin in Drosophila
    • Dubreuil, R. R., and Yu, J. Q. (1994). Ankyrin and β-spectrin accumulate independently of α-spectrin in Drosophila. Proc. Natl. Acad. Sci. USA 91, 10285-10289.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10285-10289
    • Dubreuil, R.R.1    Yu, J.Q.2
  • 23
    • 0023664659 scopus 로고
    • The gene and the primary structure of ornithine decarboxylase from Saccharomyces cerevisiae
    • Fonzi, W. A., and Sypherd, P. S. (1987). The gene and the primary structure of ornithine decarboxylase from Saccharomyces cerevisiae. J. Biol. Chem. 262, 10127-10133.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10127-10133
    • Fonzi, W.A.1    Sypherd, P.S.2
  • 25
    • 0027358729 scopus 로고
    • Nucleotide sequence of a nucleoside triphosphate phosphohydrolase gene from African swine fever virus
    • Freije, J. M. P., Lain, S., Vinuela, E., and Lopez-Otin, C. (1993). Nucleotide sequence of a nucleoside triphosphate phosphohydrolase gene from African swine fever virus. Virus Res. 30, 63-72.
    • (1993) Virus Res. , vol.30 , pp. 63-72
    • Freije, J.M.P.1    Lain, S.2    Vinuela, E.3    Lopez-Otin, C.4
  • 26
    • 0027168279 scopus 로고
    • Multiple domain structure in a chitinase gene (chiC) of Streptomyces lividans
    • Fujii, T., and Miyashita, K. (1993). Multiple domain structure in a chitinase gene (chiC) of Streptomyces lividans. J. Gen. Microbiol. 139, 677-686.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 677-686
    • Fujii, T.1    Miyashita, K.2
  • 27
    • 0023216891 scopus 로고
    • CpG islands in vertebrate genomes
    • Gardiner-Garden, M., and Frommer, M. (1987). CpG islands in vertebrate genomes. J. Mol. Biol. 196, 261-282.
    • (1987) J. Mol. Biol. , vol.196 , pp. 261-282
    • Gardiner-Garden, M.1    Frommer, M.2
  • 28
    • 0025695392 scopus 로고
    • Nucleotide sequence of bovine copper/zinc superoxide dismutase cDNA generated by the polymerase chain reaction
    • Gibbs, S., and Shaffer, J. B. (1990). Nucleotide sequence of bovine copper/zinc superoxide dismutase cDNA generated by the polymerase chain reaction. Nucleic Acids Res. 18, 717.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 717
    • Gibbs, S.1    Shaffer, J.B.2
  • 29
    • 0000843156 scopus 로고
    • Restriction site map of the Chlorella virus PBCV-1 genome
    • Girton, L. E., and Van Etten, J. L. (1987). Restriction site map of the Chlorella virus PBCV-1 genome. Plant Mol. Biol. 9, 247-257.
    • (1987) Plant Mol. Biol. , vol.9 , pp. 247-257
    • Girton, L.E.1    Van Etten, J.L.2
  • 31
    • 0002928992 scopus 로고
    • Role of chitinases in fungal growth
    • (M. Muzzarelli, C. Jeuniaux, and G. W. Gooday, Eds.), Plenum, New York
    • Gooday, G. W., Humphreys, A. M., and McIntosh, W. H. (1986). Role of chitinases in fungal growth. In "Chitin in Nature and Technology" (M. Muzzarelli, C. Jeuniaux, and G. W. Gooday, Eds.), pp. 83-91. Plenum, New York.
    • (1986) Chitin in Nature and Technology , pp. 83-91
    • Gooday, G.W.1    Humphreys, A.M.2    McIntosh, W.H.3
  • 32
    • 0024344173 scopus 로고
    • Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes
    • Gorbalenya, A. E., Koonin, E. V., Donchenko, A. P., and Blinov, V. (1989). Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 17, 4713-4730.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4713-4730
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.4
  • 33
    • 0025866063 scopus 로고
    • Regulation of capsular polysaccharide synthesis in Escherichia coli K12
    • Gottesman, S., and Stout, V. (1991). Regulation of capsular polysaccharide synthesis in Escherichia coli K12. Mol. Microbiol. 5, 1599-1606.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1599-1606
    • Gottesman, S.1    Stout, V.2
  • 34
    • 0026658938 scopus 로고
    • The DNA polymerase gene from Chlorella viruses PBCV-1 and NY-2A contains an intron with nuclear splicing sequences
    • Grabherr, R., Strasser, P., and Van Etten, J. L. (1992). The DNA polymerase gene from Chlorella viruses PBCV-1 and NY-2A contains an intron with nuclear splicing sequences. Virology 188, 721-731.
    • (1992) Virology , vol.188 , pp. 721-731
    • Grabherr, R.1    Strasser, P.2    Van Etten, J.L.3
  • 35
    • 0026691692 scopus 로고
    • Characterization of the major capsid protein and cloning of its gene from algal virus PBCV-1
    • Graves, M. V., and Meints, R. H. (1992a). Characterization of the major capsid protein and cloning of its gene from algal virus PBCV-1. Virology 188, 198-207.
    • (1992) Virology , vol.188 , pp. 198-207
    • Graves, M.V.1    Meints, R.H.2
  • 36
    • 0026534306 scopus 로고
    • Characterization of the gene encoding the most abundant in vitro translation product from virus-infected chlorella-like algae
    • Graves, M. V., and Meints, R. H. (1992b). Characterization of the gene encoding the most abundant in vitro translation product from virus-infected chlorella-like algae. Gene 113, 149-155.
    • (1992) Gene , vol.113 , pp. 149-155
    • Graves, M.V.1    Meints, R.H.2
  • 37
    • 0025787954 scopus 로고
    • Biochemical mechanisms of constitutive and regulated pre-mRNA splicing
    • Green, M. R. (1991). Biochemical mechanisms of constitutive and regulated pre-mRNA splicing. Annu. Rev. Cell Biol. 7, 559-599.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 559-599
    • Green, M.R.1
  • 38
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members
    • Hanks, S. K., and Quinn, A. M. (1991). Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members. Methods Enzymol. 200, 38-62.
    • (1991) Methods Enzymol. , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 40
    • 0028350404 scopus 로고
    • Isolation and sequence of an endochitinase-encoding gene from a cDNA library of Trichoderma harzianum
    • Hayes, C. K., Klemsdal, S., Lorito, M., Di Pietro, A., Peterbauer, C., Nakas, J. P., Tronsmo, A., and Harman, G. E. (1994). Isolation and sequence of an endochitinase-encoding gene from a cDNA library of Trichoderma harzianum. Gene 138, 143-148.
    • (1994) Gene , vol.138 , pp. 143-148
    • Hayes, C.K.1    Klemsdal, S.2    Lorito, M.3    Di Pietro, A.4    Peterbauer, C.5    Nakas, J.P.6    Tronsmo, A.7    Harman, G.E.8
  • 41
    • 0002180586 scopus 로고
    • Comparison of chitin fibril structure and assembly in three unicellular organisms
    • (R. Muzzarelli, C. Jeuniaux, and G. W. Gooday, Eds.), Plenum, New York
    • Herth, W., Mulisch, M., and Zugenmaier, P. (1986). Comparison of chitin fibril structure and assembly in three unicellular organisms. In "Chitin in Nature and Technology" (R. Muzzarelli, C. Jeuniaux, and G. W. Gooday, Eds.), pp. 107-120. Plenum, New York.
    • (1986) Chitin in Nature and Technology , pp. 107-120
    • Herth, W.1    Mulisch, M.2    Zugenmaier, P.3
  • 42
    • 0025738784 scopus 로고
    • In vivo genetic exchange of a functional domain from a type II A methylase between lactococcal plasmid pTR2030 and a virulent bacteriophage
    • Hill, C., Miller, L. A., and Klaenhammer, T. R. (1991). In vivo genetic exchange of a functional domain from a type II A methylase between lactococcal plasmid pTR2030 and a virulent bacteriophage. J. Bacteriol. 173, 4363-4370.
    • (1991) J. Bacteriol. , vol.173 , pp. 4363-4370
    • Hill, C.1    Miller, L.A.2    Klaenhammer, T.R.3
  • 43
    • 0001669533 scopus 로고
    • Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens
    • Jones, J. D. G., Grady, K. L., Suslow, T. V., and Bedbrook, J. R. (1986). Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens. EMBO J. 5, 467-473.
    • (1986) EMBO J. , vol.5 , pp. 467-473
    • Jones, J.D.G.1    Grady, K.L.2    Suslow, T.V.3    Bedbrook, J.R.4
  • 44
    • 0021867425 scopus 로고
    • Nucleotide sequence of murine ornithine decarboxylase mRNA
    • Kahana, C., and Nathans, D. (1985). Nucleotide sequence of murine ornithine decarboxylase mRNA. Proc. Natl. Acad. Sci. USA 82, 1673-1677.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1673-1677
    • Kahana, C.1    Nathans, D.2
  • 45
    • 0024382168 scopus 로고
    • Amino acid sequence of chitinase from Streptomyces erythraeus
    • Kamei, K., Yamamura, Y., Hara, S., and Ikenaka, T. (1989). Amino acid sequence of chitinase from Streptomyces erythraeus. J. Biochem. 105, 979-985.
    • (1989) J. Biochem. , vol.105 , pp. 979-985
    • Kamei, K.1    Yamamura, Y.2    Hara, S.3    Ikenaka, T.4
  • 46
    • 0024536167 scopus 로고
    • The Fokl restriction-modification system. I. Organization and nucleotide sequences of the restriction and modification genes
    • Kita, K., Kotani, H., Sugisaki, H., and Takanami, M. (1989). The Fokl restriction-modification system. I. Organization and nucleotide sequences of the restriction and modification genes. J. Biol. Chem. 264, 5751-5756.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5751-5756
    • Kita, K.1    Kotani, H.2    Sugisaki, H.3    Takanami, M.4
  • 47
    • 0026646706 scopus 로고
    • Cloning and sequence analysis of the Stsl restriction-modification genes: Presence of homology to Fokl restriction-modification enzymes
    • Kita, K., Suisha, M., Kotani, H., Yanase, H., and Kato, N. (1992). Cloning and sequence analysis of the Stsl restriction-modification genes: Presence of homology to Fokl restriction-modification enzymes. Nucleic Acids Res. 20, 4167-4172.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4167-4172
    • Kita, K.1    Suisha, M.2    Kotani, H.3    Yanase, H.4    Kato, N.5
  • 48
    • 0028985712 scopus 로고
    • G: A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of ranvier
    • G: A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of ranvier. J. Biol. Chem. 270, 2352-2359.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2352-2359
    • Kordeli, E.1    Lambert, S.2    Bennet, V.3
  • 49
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna, T. S. R., Kong, X. P., Gary, S., Burgers, P. M., and Kuriyan, J. (1994). Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell 79, 1233-1243.
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.R.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 50
    • 0028816845 scopus 로고
    • Multiple dual specificity protein tyrosine phosphatases are expressed and regulated differentially in liver cell lines
    • Kwak, S. P., and Dixon, J. E. (1995). Multiple dual specificity protein tyrosine phosphatases are expressed and regulated differentially in liver cell lines. J. Biol. Chem. 270, 1156-1160.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1156-1160
    • Kwak, S.P.1    Dixon, J.E.2
  • 51
    • 0025036332 scopus 로고
    • Cloning and characterization of two tandemly arranged DNA methyltransferase genes of Neisseria lactamica: An adenine-specific M. NlaIII and a cytosine-type methylase
    • Labbe, D., Holtke, H. J., and Lau, P. C. K. (1990). Cloning and characterization of two tandemly arranged DNA methyltransferase genes of Neisseria lactamica: An adenine-specific M. NlaIII and a cytosine-type methylase. Mol. Gen. Genet. 224, 101-110.
    • (1990) Mol. Gen. Genet. , vol.224 , pp. 101-110
    • Labbe, D.1    Holtke, H.J.2    Lau, P.C.K.3
  • 52
    • 0026742792 scopus 로고
    • CpG islands as gene markers in the human genome
    • Larsen, F., Gundersen, G., Lopez, R., and Prydz, H. (1992). CpG islands as gene markers in the human genome. Genomics 13, 1095-1107.
    • (1992) Genomics , vol.13 , pp. 1095-1107
    • Larsen, F.1    Gundersen, G.2    Lopez, R.3    Prydz, H.4
  • 53
    • 0025087142 scopus 로고
    • 1+) is important for growth polarity in Schizosaccharomyces pombe
    • 1+) is important for growth polarity in Schizosaccharomyces pombe. Proc. Natl. Acad. Sci. USA 87, 8272-8276.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8272-8276
    • Levin, D.E.1    Bishop, J.M.2
  • 55
    • 0028803831 scopus 로고
    • Analysis of 43 kb of the chlorella virus PBCV-1 330-kb genome: Map positions 45 to 88
    • Li, Y., Lu, Z., Burbank, D. E., Kutish, G. F., Rock, D. L., and Van Etten, J. L. (1995). Analysis of 43 kb of the chlorella virus PBCV-1 330-kb genome: Map positions 45 to 88. Virology 212, 134-150.
    • (1995) Virology , vol.212 , pp. 134-150
    • Li, Y.1    Lu, Z.2    Burbank, D.E.3    Kutish, G.F.4    Rock, D.L.5    Van Etten, J.L.6
  • 56
    • 0028797833 scopus 로고
    • Analysis of 45 kb of DNA located at the left end of the chlorella virus PBCV-1 genome
    • Lu, Z., Li, Y., Zhang, Y., Kutish, G. F., Rock, D. L., and Van Etten, J. L. (1995). Analysis of 45 kb of DNA located at the left end of the chlorella virus PBCV-1 genome. Virology 206, 339-352.
    • (1995) Virology , vol.206 , pp. 339-352
    • Lu, Z.1    Li, Y.2    Zhang, Y.3    Kutish, G.F.4    Rock, D.L.5    Van Etten, J.L.6
  • 58
    • 0028786960 scopus 로고
    • A new chitosanase gene from a Nocardioides sp. is a third member of glycosyl hydrolase family 46
    • Masson, J. Y., Boucher, I., Neugebauer, W. A., Ramotar, D., and Brzezinski, R. (1995). A new chitosanase gene from a Nocardioides sp. is a third member of glycosyl hydrolase family 46. Microbiology 141, 2629-2635.
    • (1995) Microbiology , vol.141 , pp. 2629-2635
    • Masson, J.Y.1    Boucher, I.2    Neugebauer, W.A.3    Ramotar, D.4    Brzezinski, R.5
  • 59
    • 0028265410 scopus 로고
    • Primary sequence of the chitosanase from Streptomyces sp. strain N174 and comparison with other endoglycosidases
    • Masson, J. Y., Denis, F., and Brzezinski, R. (1994). Primary sequence of the chitosanase from Streptomyces sp. strain N174 and comparison with other endoglycosidases. Gene 140, 103-107.
    • (1994) Gene , vol.140 , pp. 103-107
    • Masson, J.Y.1    Denis, F.2    Brzezinski, R.3
  • 60
    • 0023301988 scopus 로고
    • Molecular cloning of cDNA coding for rat proliferating cell nuclear antigen (PCNA)/cyclin
    • Matsumoto, K., Moriuchi, T., Kogi, T., and Nakane, P. K. (1987). Molecular cloning of cDNA coding for rat proliferating cell nuclear antigen (PCNA)/cyclin. EMBO J. 6, 637-642.
    • (1987) EMBO J. , vol.6 , pp. 637-642
    • Matsumoto, K.1    Moriuchi, T.2    Kogi, T.3    Nakane, P.K.4
  • 61
    • 0001818585 scopus 로고
    • The primary structure of plant pathogenesis-related glucanohydrolases and their genes
    • T. Boller and F. Meins, Eds., Springer-Verlag, Vienna
    • Meins, F., Neuhaus, J. M., Sperisen, C., and Ryals, J. (1992). The primary structure of plant pathogenesis-related glucanohydrolases and their genes. In "Genes Involved in Plant Defense" (T. Boller and F. Meins, Eds.), pp. 245-282. Springer-Verlag, Vienna.
    • (1992) Genes Involved in Plant Defense , pp. 245-282
    • Meins, F.1    Neuhaus, J.M.2    Sperisen, C.3    Ryals, J.4
  • 62
    • 0023461268 scopus 로고
    • Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction
    • Mullis, K. B., and Faloona, F. A. (1987). Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction. Methods Enzymol. 155, 335-350.
    • (1987) Methods Enzymol. , vol.155 , pp. 335-350
    • Mullis, K.B.1    Faloona, F.A.2
  • 63
    • 0027342249 scopus 로고
    • DNA methyltransferases and DNA site-specific endonucleases encoded by chlorella viruses
    • P. J. Jost and P. H. Saluz, Eds., Birkhäuser, Basel
    • Nelson, M., Zhang, Y., and Van Etten, J. L. (1993). DNA methyltransferases and DNA site-specific endonucleases encoded by chlorella viruses. In "DNA Methylation: Molecular Biology and Biological Significance" (P. J. Jost and P. H. Saluz, Eds.), pp. 186-211. Birkhäuser, Basel.
    • (1993) DNA Methylation: Molecular Biology and Biological Significance , pp. 186-211
    • Nelson, M.1    Zhang, Y.2    Van Etten, J.L.3
  • 64
    • 0023013740 scopus 로고
    • Sequencing and heterologous expression of the gene encoding penicillin V amidase from Bacillus sphaericus
    • Olsson, A., and Uhlen, M. (1986). Sequencing and heterologous expression of the gene encoding penicillin V amidase from Bacillus sphaericus. Gene 45, 175-181.
    • (1986) Gene , vol.45 , pp. 175-181
    • Olsson, A.1    Uhlen, M.2
  • 65
    • 0024972095 scopus 로고
    • Viral proliferating cell nuclear antigen
    • O'Reilly, D. R., Crawford, A. M., and Miller, L. K. (1989). Viral proliferating cell nuclear antigen. Nature 337, 606.
    • (1989) Nature , vol.337 , pp. 606
    • O'Reilly, D.R.1    Crawford, A.M.2    Miller, L.K.3
  • 66
    • 0025272240 scopus 로고
    • Rapid and sensitive sequence comparison with FASTP and FASTA
    • Pearson, W. R. (1990). Rapid and sensitive sequence comparison with FASTP and FASTA. Methods Enzymol. 183, 63-98.
    • (1990) Methods Enzymol. , vol.183 , pp. 63-98
    • Pearson, W.R.1
  • 67
    • 0023219692 scopus 로고
    • Cloning and sequencing of the ornithine decarboxylase gene from Trypanosoma brucei: Implications for enzyme turnover and selective difluoromethylornithine inhibition
    • Phillips, M. A., Coffino, P., and Wang, C. C. (1987). Cloning and sequencing of the ornithine decarboxylase gene from Trypanosoma brucei: Implications for enzyme turnover and selective difluoromethylornithine inhibition. J. Biol. Chem. 262, 8721-8727.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8721-8727
    • Phillips, M.A.1    Coffino, P.2    Wang, C.C.3
  • 68
    • 0026599430 scopus 로고
    • Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by α-difluoromethylornithine: Characterization of sequences at the inhibitor and coenzyme binding sites
    • Poulin, R., Lu, L., Ackermann, B., Bey, P., and Pegg, A. E. (1992). Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by α-difluoromethylornithine: Characterization of sequences at the inhibitor and coenzyme binding sites. J. Biol. Chem. 267, 150-158.
    • (1992) J. Biol. Chem. , vol.267 , pp. 150-158
    • Poulin, R.1    Lu, L.2    Ackermann, B.3    Bey, P.4    Pegg, A.E.5
  • 69
    • 0028965015 scopus 로고
    • Characterization of a protein kinase gene from two Chlorella viruses
    • Que, Q., and Van Etten, J. L. (1995). Characterization of a protein kinase gene from two Chlorella viruses. Virus Res. 35, 291-305.
    • (1995) Virus Res. , vol.35 , pp. 291-305
    • Que, Q.1    Van Etten, J.L.2
  • 70
    • 0027964371 scopus 로고
    • Protein glycosylation and myristylation in chlorella virus PBCV-1 and its antigenic variants
    • Que, Q., Li, Y., Wang, I. N., Lane, L. C., Chaney, W. G., and Van Etten, J. L. (1994). Protein glycosylation and myristylation in chlorella virus PBCV-1 and its antigenic variants. Virology 203, 320-327.
    • (1994) Virology , vol.203 , pp. 320-327
    • Que, Q.1    Li, Y.2    Wang, I.N.3    Lane, L.C.4    Chaney, W.G.5    Van Etten, J.L.6
  • 72
    • 0026517235 scopus 로고
    • Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus
    • Robbins, P. W., Overbye, K., Albright, C., Benfield, B., and Pero, J. (1992). Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus. Gene 111, 69-76.
    • (1992) Gene , vol.111 , pp. 69-76
    • Robbins, P.W.1    Overbye, K.2    Albright, C.3    Benfield, B.4    Pero, J.5
  • 73
    • 0024618862 scopus 로고
    • Chlorella viruses contain linear nonpermuted double-stranded DNA genomes with co-valently closed hairpin ends
    • Rohozinski, J., Girton, L., and Van Etten, J. L. (1989). Chlorella viruses contain linear nonpermuted double-stranded DNA genomes with co-valently closed hairpin ends. Virology 168, 363-369.
    • (1989) Virology , vol.168 , pp. 363-369
    • Rohozinski, J.1    Girton, L.2    Van Etten, J.L.3
  • 74
    • 0026863931 scopus 로고
    • Nucleotide sequences of two cDNA clones encoding different Cu/Zn-superoxide dismutases expressed in developing rice seed (Oryza sativa L.)
    • Sakamoto, A., Ohsuga, H., and Tanaka, K. (1992). Nucleotide sequences of two cDNA clones encoding different Cu/Zn-superoxide dismutases expressed in developing rice seed (Oryza sativa L.). Plant Mol. Biol. 19, 323-327.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 323-327
    • Sakamoto, A.1    Ohsuga, H.2    Tanaka, K.3
  • 76
    • 0021152755 scopus 로고
    • Structural proteins and lipids in a virus, PBCV-1 which replicates in a chlorella-like alga
    • Skrdla, M. P., Burbank, D. E., Xia, Y., Meints, R. H., and Van Etten, J. L. (1984). Structural proteins and lipids in a virus, PBCV-1 which replicates in a chlorella-like alga. Virology 135, 308-315.
    • (1984) Virology , vol.135 , pp. 308-315
    • Skrdla, M.P.1    Burbank, D.E.2    Xia, Y.3    Meints, R.H.4    Van Etten, J.L.5
  • 77
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith, T. F., and Waterman, M. S. (1981). Identification of common molecular subsequences. J. Mol. Biol. 147, 195-197.
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 78
    • 0020480482 scopus 로고
    • Automation of the computer handling of gel reading data produced by the shotgun method of DNA sequencing
    • Staden, R. (1982). Automation of the computer handling of gel reading data produced by the shotgun method of DNA sequencing. Nucleic Acids Res. 10, 4731-4751.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 4731-4751
    • Staden, R.1
  • 79
    • 0021760028 scopus 로고
    • Measurements of the effects that coding for a protein has on a DNA sequence and their use for finding genes
    • Staden, R. (1984). Measurements of the effects that coding for a protein has on a DNA sequence and their use for finding genes. Nucleic Acids Res. 12, 551-567.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 551-567
    • Staden, R.1
  • 80
    • 0020039567 scopus 로고
    • Codon preference and its use in identifying protein coding regions in long DNA sequences
    • Staden, R., and McLachlan, A. D. (1982). Codon preference and its use in identifying protein coding regions in long DNA sequences. Nucleic Acids Res. 10, 141-156.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 141-156
    • Staden, R.1    McLachlan, A.D.2
  • 81
    • 0027936237 scopus 로고
    • Smart machines at the DNA replication fork
    • Stillman, B. (1994). Smart machines at the DNA replication fork. Cell 78, 725-728.
    • (1994) Cell , vol.78 , pp. 725-728
    • Stillman, B.1
  • 82
    • 0026088489 scopus 로고
    • The termini of the chlorella virus PBCV-1 genome are identical 2.2-kbp inverted repeats
    • Strasser, P., Zhang, Y., Rohozinski, J., and Van Etten, J. L. (1991). The termini of the chlorella virus PBCV-1 genome are identical 2.2-kbp inverted repeats. Virology 180, 763-769.
    • (1991) Virology , vol.180 , pp. 763-769
    • Strasser, P.1    Zhang, Y.2    Rohozinski, J.3    Van Etten, J.L.4
  • 83
    • 0025280671 scopus 로고
    • Genome size of Mycoplasma genitalium
    • Su, C. J., and Baseman, J. B. (1990). Genome size of Mycoplasma genitalium. J. Bacteriol. 172, 4705-4707.
    • (1990) J. Bacteriol. , vol.172 , pp. 4705-4707
    • Su, C.J.1    Baseman, J.B.2
  • 84
    • 0000358392 scopus 로고
    • Gene for proliferating-cell nuclear antigen (DNA polymerase δ auxiliary protein) is present in both mammalian and higher plant genomes
    • Suzuka, I., Daidoji, H., Matsuoka, M., Kadowaki, K. I., Takasaki, Y., Nakane, P. K., and Moriuchi, T. (1989). Gene for proliferating-cell nuclear antigen (DNA polymerase δ auxiliary protein) is present in both mammalian and higher plant genomes. Proc. Natl. Acad. Sci. USA 86, 3189-3193.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3189-3193
    • Suzuka, I.1    Daidoji, H.2    Matsuoka, M.3    Kadowaki, K.I.4    Takasaki, Y.5    Nakane, P.K.6    Moriuchi, T.7
  • 85
    • 0026026230 scopus 로고
    • Highly conserved structure of proliferating cell nuclear antigen (DNA polymerase δ auxilary protein) gene in plants
    • Suzuka, I., Hata, S., Matsuoka, M., Kosugi, S., and Hashimoto, J. (1991). Highly conserved structure of proliferating cell nuclear antigen (DNA polymerase δ auxilary protein) gene in plants. Eur. J. Biochem. 195, 571-575.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 571-575
    • Suzuka, I.1    Hata, S.2    Matsuoka, M.3    Kosugi, S.4    Hashimoto, J.5
  • 86
    • 0025271540 scopus 로고
    • Structure of the gene of tum transplantation antigen P35B: Presence of a point mutation in the antigenic allele
    • Szikora, J. P., Van Pel, A., Brichard, V., Andre, M., Van Baren, N., Henry, P., Plaen, E. D., and Boon, T. (1990). Structure of the gene of tum transplantation antigen P35B: Presence of a point mutation in the antigenic allele. EMBO J. 9, 1041-1050.
    • (1990) EMBO J. , vol.9 , pp. 1041-1050
    • Szikora, J.P.1    Van Pel, A.2    Brichard, V.3    Andre, M.4    Van Baren, N.5    Henry, P.6    Plaen, E.D.7    Boon, T.8
  • 87
    • 0023371227 scopus 로고
    • DNA sequence analysis with a modified bacteriophage T7 DNA polymerase
    • Tabor, S., and Richardson, C. C. (1987). DNA sequence analysis with a modified bacteriophage T7 DNA polymerase. Proc. Natl. Acad. Sci. USA 84, 4767-4771.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4767-4771
    • Tabor, S.1    Richardson, C.C.2
  • 88
    • 0025914179 scopus 로고
    • A baculovirus homolog of a Cu/Zn superoxide dismutase gene
    • Tomalski, M. D., Eldridge, R., and Miller, L. K. (1991). A baculovirus homolog of a Cu/Zn superoxide dismutase gene. Virology 184, 149-161.
    • (1991) Virology , vol.184 , pp. 149-161
    • Tomalski, M.D.1    Eldridge, R.2    Miller, L.K.3
  • 89
    • 0024284507 scopus 로고
    • Genome organization of the killer plasmid pGK12 from Kluyveromyces lactis
    • Tommasino, M., Ricci, S., and Galeotti, C. L. (1988). Genome organization of the killer plasmid pGK12 from Kluyveromyces lactis. Nucleic Acids Res. 16, 5863-5878.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 5863-5878
    • Tommasino, M.1    Ricci, S.2    Galeotti, C.L.3
  • 90
    • 0029130581 scopus 로고
    • Temperature-sensitive mutants with lesions in the vaccinia virus F10 kinase undergo arrest at the earliest stage of virion morphogenesis
    • Trakman, P., Caligiuri, A., Jesty, S. A., Liu, K., and Sankar, U. (1995). Temperature-sensitive mutants with lesions in the vaccinia virus F10 kinase undergo arrest at the earliest stage of virion morphogenesis. J. Virol. 69, 6581-6587.
    • (1995) J. Virol. , vol.69 , pp. 6581-6587
    • Trakman, P.1    Caligiuri, A.2    Jesty, S.A.3    Liu, K.4    Sankar, U.5
  • 92
    • 0028172139 scopus 로고
    • A rapid protocol for DNA extraction and primer annealing for PCR sequencing
    • Trenick, S., and Dearden, P. (1994). A rapid protocol for DNA extraction and primer annealing for PCR sequencing. BioTechniques 17, 842-843.
    • (1994) BioTechniques , vol.17 , pp. 842-843
    • Trenick, S.1    Dearden, P.2
  • 93
    • 0028004462 scopus 로고
    • Molecular cloning and nucleotide sequence of the gene encoding chitinase II from Aeromonas sp. No. 10S-24
    • Ueda, M., Kawaguchi, T., and Arai, M. (1994). Molecular cloning and nucleotide sequence of the gene encoding chitinase II from Aeromonas sp. No. 10S-24. J. Ferment. Bioeng. 78, 205-211.
    • (1994) J. Ferment. Bioeng. , vol.78 , pp. 205-211
    • Ueda, M.1    Kawaguchi, T.2    Arai, M.3
  • 94
    • 0002201011 scopus 로고
    • Giant chlorella viruses
    • Van Etten, J. L. (1995). Giant chlorella viruses. Mol. Cells 5, 99-106.
    • (1995) Mol. Cells , vol.5 , pp. 99-106
    • Van Etten, J.L.1
  • 95
    • 0019456775 scopus 로고
    • Isolation and characterization of a virus from the intracellular green alga symbiotic with Hydra viridis
    • Van Etten, J. L., Meints, R. H., Burbank, D. E., Kuczmarski, D., Cuppels, D. A., and Lane, L. C. (1981). Isolation and characterization of a virus from the intracellular green alga symbiotic with Hydra viridis. Virology 113, 704-711.
    • (1981) Virology , vol.113 , pp. 704-711
    • Van Etten, J.L.1    Meints, R.H.2    Burbank, D.E.3    Kuczmarski, D.4    Cuppels, D.A.5    Lane, L.C.6
  • 96
    • 0020615927 scopus 로고
    • Growth cycle of a virus, PBCV-1, that infects Chlorella-like algae
    • Van Etten, J. L., Burbank, D. E., Xia, Y., and Meints, R. H. (1983). Growth cycle of a virus, PBCV-1, that infects Chlorella-like algae. Virology 126, 117-125.
    • (1983) Virology , vol.126 , pp. 117-125
    • Van Etten, J.L.1    Burbank, D.E.2    Xia, Y.3    Meints, R.H.4
  • 98
    • 0025833760 scopus 로고
    • Viruses and viruslike particles of eukaryotic algae
    • Van Etten, J. L., Lane, L. C., and Meints, R. H. (1991). Viruses and viruslike particles of eukaryotic algae. Microbiol. Rev. 55, 586-620.
    • (1991) Microbiol. Rev. , vol.55 , pp. 586-620
    • Van Etten, J.L.1    Lane, L.C.2    Meints, R.H.3
  • 101
    • 0027215228 scopus 로고
    • Evidence that SKI antiviral system of Saccharomyces cerevisiae acts by blocking expression of viral mRNA
    • Widner, W. R., and Wickner, R. B. (1993). Evidence that SKI antiviral system of Saccharomyces cerevisiae acts by blocking expression of viral mRNA. Mol. Cell. Biol. 13, 4331-4341.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4331-4341
    • Widner, W.R.1    Wickner, R.B.2
  • 103
    • 0028303483 scopus 로고
    • Self-splicing group I introns in eukaryotic viruses
    • Yamada, T., Tamura, K., Aimi, T., and Songsri, P. (1994). Self-splicing group I introns in eukaryotic viruses. Nucleic Acids Res. 20, 2532-2537.
    • (1994) Nucleic Acids Res. , vol.20 , pp. 2532-2537
    • Yamada, T.1    Tamura, K.2    Aimi, T.3    Songsri, P.4
  • 104
    • 0026707850 scopus 로고
    • Characterization of chlorella virus PBCV-1 CviAII restriction and modification system
    • Zhang, Y., Nelson, M., Nietfeldt, J. W., Burbank, D. E., and Van Etten, J. L. (1992). Characterization of chlorella virus PBCV-1 CviAII restriction and modification system. Nucleic Acids Res. 20, 5351-5356.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5351-5356
    • Zhang, Y.1    Nelson, M.2    Nietfeldt, J.W.3    Burbank, D.E.4    Van Etten, J.L.5
  • 105
    • 0027981687 scopus 로고
    • Hairpin loop structure at the termini of the chlorella virus PBCV-1 genome
    • Zhang, Y., Strasser, P., Grabherr, R., and Van Etten, J. L. (1994). Hairpin loop structure at the termini of the chlorella virus PBCV-1 genome. Virology 202, 1079-1082.
    • (1994) Virology , vol.202 , pp. 1079-1082
    • Zhang, Y.1    Strasser, P.2    Grabherr, R.3    Van Etten, J.L.4
  • 106
    • 0027510449 scopus 로고
    • Expression cloning of 2-5A-dependent RNAase: A uniquely regulated mediator of interferon action
    • Zhou, A., Hassel, B. A., and Silverman, R. H. (1993). Expression cloning of 2-5A-dependent RNAase: A uniquely regulated mediator of interferon action. Cell 72, 753-765.
    • (1993) Cell , vol.72 , pp. 753-765
    • Zhou, A.1    Hassel, B.A.2    Silverman, R.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.