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Volumn 317, Issue 1, 2003, Pages 73-83

Characterization of a chlorella virus PBCV-1 encoded ribonuclease III

Author keywords

Chlorella viruses; dsRNA; Phycodnaviridae; Ribonuclease; RNase III

Indexed keywords

AMINO ACID; CHITIN; INTEIN; MAGNESIUM ION; RIBONUCLEASE III;

EID: 0347627797     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virol.2003.08.044     Document Type: Article
Times cited : (23)

References (63)
  • 1
    • 0034804433 scopus 로고    scopus 로고
    • Escherichia coli ribonuclease III: Affinity purification of hexahistidine-tagged enzyme and assays for substrate binding and cleavage
    • Amarasinghe A.K., Calin-Jageman I., Harmouch A., Sun W., Nicholson A.W. Escherichia coli ribonuclease III affinity purification of hexahistidine-tagged enzyme and assays for substrate binding and cleavage . Methods Enzymol. 342:2001;143-158.
    • (2001) Methods Enzymol. , vol.342 , pp. 143-158
    • Amarasinghe, A.K.1    Calin-Jageman, I.2    Harmouch, A.3    Sun, W.4    Nicholson, A.W.5
  • 2
    • 0035800504 scopus 로고    scopus 로고
    • Dicing up RNAs
    • Ambros V. Dicing up RNAs. Science. 293:2001;811-813.
    • (2001) Science , vol.293 , pp. 811-813
    • Ambros, V.1
  • 3
    • 0034814879 scopus 로고    scopus 로고
    • A natural classification of ribonucleases
    • Aravind L., Koonin E.V. A natural classification of ribonucleases. Methods Enzymol. 341:2001;3-28.
    • (2001) Methods Enzymol. , vol.341 , pp. 3-28
    • Aravind, L.1    Koonin, E.V.2
  • 4
    • 0020393678 scopus 로고
    • Processing of bacteriophage T4 primary transcripts with ribonuclease III
    • Barkay T., Goldfarb A. Processing of bacteriophage T4 primary transcripts with ribonuclease III. J. Mol. Biol. 162:1982;299-315.
    • (1982) J. Mol. Biol. , vol.162 , pp. 299-315
    • Barkay, T.1    Goldfarb, A.2
  • 5
    • 0035905766 scopus 로고    scopus 로고
    • Role for a bidentate ribonuclease in the initiation step of RNA interference
    • Bernstein E., Caudy A.A., Hammond S.M., Hannon G.J. Role for a bidentate ribonuclease in the initiation step of RNA interference. Nature. 409:2001;363-366.
    • (2001) Nature , vol.409 , pp. 363-366
    • Bernstein, E.1    Caudy, A.A.2    Hammond, S.M.3    Hannon, G.J.4
  • 6
    • 0027249769 scopus 로고
    • Mutational analysis of a ribonuclease III processing signal
    • Chelladurai B., Li H., Zhang K., Nicholson A.W. Mutational analysis of a ribonuclease III processing signal. Biochemistry. 32:1993;7549-7558.
    • (1993) Biochemistry , vol.32 , pp. 7549-7558
    • Chelladurai, B.1    Li, H.2    Zhang, K.3    Nicholson, A.W.4
  • 7
    • 0037206569 scopus 로고    scopus 로고
    • Isolation and characterization of chlorella viruses from freshwater sources in Korea
    • Cho H.-H., Park H.-H., Kim J.-O., Choi T.-J. Isolation and characterization of chlorella viruses from freshwater sources in Korea. Mol. Cell. 14:2002;168-176.
    • (2002) Mol. Cell , vol.14 , pp. 168-176
    • Cho, H.-H.1    Park, H.-H.2    Kim, J.-O.3    Choi, T.-J.4
  • 8
    • 0036155107 scopus 로고    scopus 로고
    • Ribonuclease III: New sense from nuisance
    • Conrad C., Rauhut R. Ribonuclease III new sense from nuisance . Int. J. Biochem. Cell Biol. 34:2002;116-129.
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 116-129
    • Conrad, C.1    Rauhut, R.2
  • 9
    • 34250257369 scopus 로고
    • RNA processing and degradation by RNase III
    • J.G. Belasco, & G. Brawerman. NY: Academic Press
    • Court D.L. RNA processing and degradation by RNase III. Belasco J.G., Brawerman G. Control of Messenger RNA Stability. 1993;71-116 Academic Press, NY.
    • (1993) Control of Messenger RNA Stability , pp. 71-116
    • Court, D.L.1
  • 10
    • 0032574743 scopus 로고    scopus 로고
    • Unexpected electrophoretic migration of RNA with different 3′ termini causes a RNA sizing ambiguity that can be resolved using nuclease P1-generated sequencing ladders
    • Cruz-Reyes J., Piller K.J., Rusche L.N., Mukherjee M., Sollner-Webb B. Unexpected electrophoretic migration of RNA with different 3′ termini causes a RNA sizing ambiguity that can be resolved using nuclease P1-generated sequencing ladders. Biochemistry. 37:1998;6059-6064.
    • (1998) Biochemistry , vol.37 , pp. 6059-6064
    • Cruz-Reyes, J.1    Piller, K.J.2    Rusche, L.N.3    Mukherjee, M.4    Sollner-Webb, B.5
  • 11
    • 0000228203 scopus 로고
    • A model of evolutionary change in proteins
    • Dayhoff M.O. Washington, DC: National Biomedical Research Foundation
    • Dayhoff M.O., Schwartz R.M., Orcutt B.C. A model of evolutionary change in proteins. Dayhoff M.O. Atlas of Protein Sequence and Structure. Vol. 5:1978;345-352 National Biomedical Research Foundation, Washington, DC.
    • (1978) Atlas of Protein Sequence and Structure , vol.5 , pp. 345-352
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 13
    • 0017116036 scopus 로고
    • RNase III cleavage of single-stranded RNA: Effect of ionic strength on the fidelity of cleavage
    • Dunn J.J. RNase III cleavage of single-stranded RNA effect of ionic strength on the fidelity of cleavage . J. Biol. Chem. 25:1976;3807-3814.
    • (1976) J. Biol. Chem. , vol.25 , pp. 3807-3814
    • Dunn, J.J.1
  • 14
    • 0020964297 scopus 로고
    • Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements
    • Dunn J.J., Studier F.W. Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements. J. Mol. Biol. 166:1983;477-535.
    • (1983) J. Mol. Biol. , vol.166 , pp. 477-535
    • Dunn, J.J.1    Studier, F.W.2
  • 15
    • 0029919935 scopus 로고    scopus 로고
    • RNase III cleaves eukaryotic pre-ribosomal RNA at a U3 snoRNP-dependent site
    • Elela S.A., Igel H., Ares M. RNase III cleaves eukaryotic pre-ribosomal RNA at a U3 snoRNP-dependent site. Cell. 85:1996;115-124.
    • (1996) Cell , vol.85 , pp. 115-124
    • Elela, S.A.1    Igel, H.2    Ares, M.3
  • 17
    • 0003437299 scopus 로고
    • Seattle: Department of Genetics, University of Washington. Distributed by the author
    • Felsenstein J. PHYLIP (phylogeny inference package) 3.57c. 1993;Department of Genetics, University of Washington, Seattle. Distributed by the author.
    • (1993) PHYLIP (phylogeny inference package) 3.57c
    • Felsenstein, J.1
  • 18
    • 0034615578 scopus 로고    scopus 로고
    • A novel type of RNase III family proteins in eukaryotes
    • Filippov V., Solovyev V., Filippova M., Gill S.S. A novel type of RNase III family proteins in eukaryotes. Gene. 245:2000;213-221.
    • (2000) Gene , vol.245 , pp. 213-221
    • Filippov, V.1    Solovyev, V.2    Filippova, M.3    Gill, S.S.4
  • 19
    • 0141860062 scopus 로고    scopus 로고
    • Mouse ribonuclease III. cDNA structure, expression analysis, and chromosomal location
    • Fortin K.F., Nicholson R.H., Nicholson A.W. Mouse ribonuclease III. cDNA structure, expression analysis, and chromosomal location. BMC Genomics. 3:2002;26.
    • (2002) BMC Genomics , vol.3 , pp. 26
    • Fortin, K.F.1    Nicholson, R.H.2    Nicholson, A.W.3
  • 21
    • 0346594392 scopus 로고    scopus 로고
    • Madison WI: Version 10.1
    • Wisconsin Package. 2000;Version 10.1, Madison WI.
    • (2000) Wisconsin Package
  • 22
    • 0035811885 scopus 로고    scopus 로고
    • Molecular and genetic evidence for a virus-encoded glycosyltransferase involved in protein glycosylation
    • Graves M.V., Bernadt C.T., Cerny R., Van Etten J.L. Molecular and genetic evidence for a virus-encoded glycosyltransferase involved in protein glycosylation. Virology. 285:2001;332-345.
    • (2001) Virology , vol.285 , pp. 332-345
    • Graves, M.V.1    Bernadt, C.T.2    Cerny, R.3    Van Etten, J.L.4
  • 23
    • 0026691692 scopus 로고
    • Characterization of the major capsid protein and cloning of its gene from algal virus PBCV-1
    • Graves M.V., Meints R.H. Characterization of the major capsid protein and cloning of its gene from algal virus PBCV-1. Virology. 188:1992;198-207.
    • (1992) Virology , vol.188 , pp. 198-207
    • Graves, M.V.1    Meints, R.H.2
  • 24
    • 0023088801 scopus 로고
    • Structure of secondary cleavage sites of E. coli RNase III in A3t RNA from bacteriophage T7
    • Gross G., Dunn J.J. Structure of secondary cleavage sites of E. coli RNase III in A3t RNA from bacteriophage T7. Nucleic Acids Res. 15:1987;431-432.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 431-432
    • Gross, G.1    Dunn, J.J.2
  • 25
    • 0020568530 scopus 로고
    • Interplay among processing and degradative enzymes and a precursor ribonucleic acid in the selective maturation and maintenance of ribonucleic acid molecules
    • Gurevitz M., Apirion D. Interplay among processing and degradative enzymes and a precursor ribonucleic acid in the selective maturation and maintenance of ribonucleic acid molecules. Biochemistry. 22:1983;4000-4005.
    • (1983) Biochemistry , vol.22 , pp. 4000-4005
    • Gurevitz, M.1    Apirion, D.2
  • 26
    • 0035814498 scopus 로고    scopus 로고
    • Complete genome analysis of the mandarin fish infectious spleen and kidney necrosis iridovirus
    • He J.G., Deng M., Weng S.P., Li Z., Zhou S.Y., Long Q.X., Wang X.Z., Chan S.-M. Complete genome analysis of the mandarin fish infectious spleen and kidney necrosis iridovirus. Virology. 291:2001;126-139.
    • (2001) Virology , vol.291 , pp. 126-139
    • He, J.G.1    Deng, M.2    Weng, S.P.3    Li, Z.4    Zhou, S.Y.5    Long, Q.X.6    Wang, X.Z.7    Chan, S.-M.8
  • 29
    • 0026089369 scopus 로고
    • +, whose overexpression inhibits sexual development, encodes a ribonuclease III-like RNase
    • +, whose overexpression inhibits sexual development, encodes a ribonuclease III-like RNase. EMBO J. 10:1991;221-226.
    • (1991) EMBO J. , vol.10 , pp. 221-226
    • Iino, Y.1    Sugimoto, A.2    Yamamoto, M.3
  • 30
    • 0035919712 scopus 로고    scopus 로고
    • Analysis of the first complete DNA sequence of an invertebrate iridovirus: Coding strategy of the genome of Chilo iridescent virus
    • Jakob N.J., Muller K., Bahr U., Darai G. Analysis of the first complete DNA sequence of an invertebrate iridovirus coding strategy of the genome of Chilo iridescent virus . Virology. 286:2001;182-196.
    • (2001) Virology , vol.286 , pp. 182-196
    • Jakob, N.J.1    Muller, K.2    Bahr, U.3    Darai, G.4
  • 31
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones D.T., Taylor W.R., Thornton J.M. The rapid generation of mutation data matrices from protein sequences. CABIOS. 8:1992;275-282.
    • (1992) CABIOS , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 32
    • 0015386501 scopus 로고
    • Virus-associated nucleases: Location and properties of deoxyribonucleases and ribonucleases in purified frog virus 3
    • Kang H.S., McAuslan B.R. Virus-associated nucleases location and properties of deoxyribonucleases and ribonucleases in purified frog virus 3 . J. Virol. 10:1972;202-210.
    • (1972) J. Virol. , vol.10 , pp. 202-210
    • Kang, H.S.1    McAuslan, B.R.2
  • 33
    • 0030587386 scopus 로고    scopus 로고
    • Analysis of 76 kb of the chlorella virus PBCV-1 330-kb genome: Map positions 182 to 258
    • Kutish G.F., Li Y., Lu Z., Furuta M., Rock D.L., Van Etten J.L. Analysis of 76 kb of the chlorella virus PBCV-1 330-kb genome map positions 182 to 258 . Virology. 223:1996;303-317.
    • (1996) Virology , vol.223 , pp. 303-317
    • Kutish, G.F.1    Li, Y.2    Lu, Z.3    Furuta, M.4    Rock, D.L.5    Van Etten, J.L.6
  • 34
    • 0035155389 scopus 로고    scopus 로고
    • The RNase III family: A conserved structure and expanding functions in eukaryotic dsRNA metabolism
    • Lamontagne B., Larose S., Boulanger J., Elela S.A. The RNase III family a conserved structure and expanding functions in eukaryotic dsRNA metabolism . Curr. Issues Mol. Biol. 3:2001;71-78.
    • (2001) Curr. Issues Mol. Biol. , vol.3 , pp. 71-78
    • Lamontagne, B.1    Larose, S.2    Boulanger, J.3    Elela, S.A.4
  • 35
    • 0029976320 scopus 로고    scopus 로고
    • Defining the enzyme binding domain of a ribonuclease III processing signal. Ethylation interference and hydroxyl radical footprinting using catalytically inactive RNase III mutants
    • Li H., Nicholson A.W. Defining the enzyme binding domain of a ribonuclease III processing signal. Ethylation interference and hydroxyl radical footprinting using catalytically inactive RNase III mutants. EMBO J. 15:1996;1421-1433.
    • (1996) EMBO J. , vol.15 , pp. 1421-1433
    • Li, H.1    Nicholson, A.W.2
  • 36
    • 0027191132 scopus 로고
    • Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity, and specific anion effects
    • Li H.L., Chelladurai B.S., Zhang K., Nicholson A.W. Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity, and specific anion effects. Nucleic Acids Res. 21:1993;1919-1925.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1919-1925
    • Li, H.L.1    Chelladurai, B.S.2    Zhang, K.3    Nicholson, A.W.4
  • 38
    • 0018411950 scopus 로고
    • A role for ribonuclease III in synthesis of bacteriophage T4 transfer RNAs
    • McClain W.H. A role for ribonuclease III in synthesis of bacteriophage T4 transfer RNAs. Biochem. Biophys. Res. Commun. 86:1979;718-724.
    • (1979) Biochem. Biophys. Res. Commun. , vol.86 , pp. 718-724
    • McClain, W.H.1
  • 39
    • 0021970872 scopus 로고
    • DNA sequencing of the Escherichia coli ribonuclease III gene and its mutations
    • Nashimoto H., Uchida H. DNA sequencing of the Escherichia coli ribonuclease III gene and its mutations. Mol. Gen. Genet. 210:1985;25-29.
    • (1985) Mol. Gen. Genet. , vol.210 , pp. 25-29
    • Nashimoto, H.1    Uchida, H.2
  • 40
    • 0033609333 scopus 로고    scopus 로고
    • Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima
    • Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H. Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima. Nature. 399:1999;323-329.
    • (1999) Nature , vol.399 , pp. 323-329
    • Nelson, K.E.1    Clayton, R.A.2    Gill, S.R.3    Gwinn, M.L.4    Dodson, R.J.5    Haft, D.H.6
  • 41
    • 0029681842 scopus 로고    scopus 로고
    • Structure, reactivity and biology of double-stranded RNA
    • Nicholson A.W. Structure, reactivity and biology of double-stranded RNA. Prog. Nucl. Acids Res. Mol. Biol. 52:1996;1-65.
    • (1996) Prog. Nucl. Acids Res. Mol. Biol. , vol.52 , pp. 1-65
    • Nicholson, A.W.1
  • 42
    • 0032932638 scopus 로고    scopus 로고
    • Function, mechanism and regulation of bacterial ribonucleases
    • Nicholson A.W. Function, mechanism and regulation of bacterial ribonucleases. FEMS Microbiol. Rev. 23:1999;371-390.
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 371-390
    • Nicholson, A.W.1
  • 43
    • 0347224335 scopus 로고    scopus 로고
    • The ribonuclease III superfamily: Forms and functions in RNA maturation, decay, and gene silencing
    • G. Hannon. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Nicholson A.W. The ribonuclease III superfamily forms and functions in RNA maturation, decay, and gene silencing . Hannon G. RNAi A Guide to Gene Silencing . 2003;149-174 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2003) RNAi: A Guide to Gene Silencing , pp. 149-174
    • Nicholson, A.W.1
  • 44
    • 0033543952 scopus 로고    scopus 로고
    • Aminoacylation of tRNAs encoded by chlorella virus CVK2
    • Nishida K., Kawasaki T., Fujie M., Usami S., Yamada T. Aminoacylation of tRNAs encoded by chlorella virus CVK2. Virology. 263:1999;220-229.
    • (1999) Virology , vol.263 , pp. 220-229
    • Nishida, K.1    Kawasaki, T.2    Fujie, M.3    Usami, S.4    Yamada, T.5
  • 45
    • 0015309356 scopus 로고
    • Degradation of single- and double-stranded RNA by frog virus 3
    • Palese P., Koch G. Degradation of single- and double-stranded RNA by frog virus 3. Proc. Natl. Acad. Sci. USA. 69:1972;698-701.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 698-701
    • Palese, P.1    Koch, G.2
  • 46
    • 0019780395 scopus 로고
    • Processing of bacteriophage T4 tRNAs. The role of RNase III
    • Pragai B., Apirion D. Processing of bacteriophage T4 tRNAs. The role of RNase III. J. Mol. Biol. 153:1981;619-630.
    • (1981) J. Mol. Biol. , vol.153 , pp. 619-630
    • Pragai, B.1    Apirion, D.2
  • 47
    • 0029931692 scopus 로고    scopus 로고
    • Purification and characterization of the Pac1 ribonuclease of Schizosaccharomyces pombe
    • Rotondo G., Frendewey D. Purification and characterization of the Pac1 ribonuclease of Schizosaccharomyces pombe. Nucleic Acids Res. 24:1996;2377-2386.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2377-2386
    • Rotondo, G.1    Frendewey, D.2
  • 48
    • 0346908614 scopus 로고    scopus 로고
    • Molecular Cloning: A Laboratory Manual
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Sambrook J., Russell D.W. Molecular Cloning A Laboratory Manual . 3rd ed :2001;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2001) 3rd Ed
    • Sambrook, J.1    Russell, D.W.2
  • 49
    • 0029836454 scopus 로고    scopus 로고
    • Quartet puzzling: A quartet maximum likelihood method for reconstructing tree topologies
    • Strimmer K., Von Haeseler A. Quartet puzzling a quartet maximum likelihood method for reconstructing tree topologies . Mol. Biol. Evol. 13:1996;964-969.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 964-969
    • Strimmer, K.1    Von Haeseler, A.2
  • 50
    • 0035942357 scopus 로고    scopus 로고
    • 2+ rescue of the Glu117Asp mutant
    • 2+ rescue of the Glu117Asp mutant. Biochemistry. 40:2001;5102-5110.
    • (2001) Biochemistry , vol.40 , pp. 5102-5110
    • Sun, W.1    Nicholson, A.W.2
  • 51
    • 33749638541 scopus 로고    scopus 로고
    • PAUP*. Phylogenetic Analysis Using Parsimony (*and Other Methods)
    • Sunderland, MA: Sinauer Associates
    • Swofford D.L. PAUP*. Phylogenetic Analysis Using Parsimony (*and Other Methods). Version 4 ed :2002;Sinauer Associates, Sunderland, MA.
    • (2002) Version 4 Ed
    • Swofford, D.L.1
  • 52
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL X windows interface flexible strategies for multiple sequence alignment aided by quality analysis tools . Nucleic Acids Res. 25:1997;4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 53
    • 0031005423 scopus 로고    scopus 로고
    • The complete DNA sequence of lymphocystis disease virus
    • Tidona C.A., Darai G. The complete DNA sequence of lymphocystis disease virus. Virology. 230:1997;207-216.
    • (1997) Virology , vol.230 , pp. 207-216
    • Tidona, C.A.1    Darai, G.2
  • 54
    • 0001796706 scopus 로고    scopus 로고
    • Phycodnaviridae
    • Regenmortel, M.H.V., Fauquet, C.M., Bishop, D.H.L., et al. (Eds.), Academic Press, San Diego, CA
    • Van Etten J.L., 2000. Phycodnaviridae, in: "Virus Taxonomy," Regenmortel, M.H.V., Fauquet, C.M., Bishop, D.H.L., et al. (Eds.), Academic Press, San Diego, CA, pp. 183-193.
    • (2000) Virus Taxonomy , pp. 183-193
    • Van Etten, J.L.1
  • 55
    • 0346599192 scopus 로고    scopus 로고
    • Unusual life style of giant chlorella viruses
    • Van Etten J.L. Unusual life style of giant chlorella viruses. Annu. Rev. Genet. 37:2003;153-195.
    • (2003) Annu. Rev. Genet. , vol.37 , pp. 153-195
    • Van Etten, J.L.1
  • 56
    • 0020615927 scopus 로고
    • Growth cycle of a virus, PBCV-1, that infects chlorella-like algae
    • Van Etten J.L., Burbank D.E., Xia Y., Meints R.H. Growth cycle of a virus, PBCV-1, that infects chlorella-like algae. Virology. 126:1983;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
  • 57
    • 0021262414 scopus 로고
    • DNA synthesis in a chlorella-like alga following infection with the virus PBCV-1
    • Van Etten J.L., Burbank D.E., Xia Y., Meints R.H. DNA synthesis in a chlorella-like alga following infection with the virus PBCV-1. Virology. 134:1984;443-449.
    • (1984) Virology , vol.134 , pp. 443-449
    • Van Etten, J.L.1    Burbank, D.E.2    Xia, Y.3    Meints, R.H.4
  • 58
    • 0025833760 scopus 로고
    • Viruses and virus-like particles of eukaryotic algae
    • Van Etten J.L., Lane L.C., Meints R.H. Viruses and virus-like particles of eukaryotic algae. Microbiol. Revs. 55:1991;586-620.
    • (1991) Microbiol. Revs. , vol.55 , pp. 586-620
    • Van Etten, J.L.1    Lane, L.C.2    Meints, R.H.3
  • 60
    • 0019456775 scopus 로고
    • Isolation and characterization of a virus from the intracellular green algae symbiotic with Hydra viridis
    • Van Etten J.L., Meints R.H., Burbank D.E., Kuczmarski D., Cuppels D.A., Lane L.C. Isolation and characterization of a virus from the intracellular green algae symbiotic with Hydra viridis. Virology. 113:1981;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
  • 62
    • 0034711308 scopus 로고    scopus 로고
    • Human RNase III is a 160-kDa protein involved in preribosomal RNA processing
    • Wu H., Xu H., Miraglia L.J., Crooke S.T. Human RNase III is a 160-kDa protein involved in preribosomal RNA processing. J. Biol. Chem. 275:2000;36957-36965.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36957-36965
    • Wu, H.1    Xu, H.2    Miraglia, L.J.3    Crooke, S.T.4
  • 63
    • 0025164247 scopus 로고
    • A gene from S. pombe with homology to E. coli RNase III blocks conjugation and sporulation when overexpressed in wild-type cells
    • Xu H.P., Riggs M., Rodgers L., Wigler M. A gene from S. pombe with homology to E. coli RNase III blocks conjugation and sporulation when overexpressed in wild-type cells. Nucleic Acids Res. 18:1990;5304.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5304
    • Xu, H.P.1    Riggs, M.2    Rodgers, L.3    Wigler, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.