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Volumn 15, Issue 9, 2003, Pages 2003-2019

Domain analysis of the chloroplast polynucleotide phosphorylase reveals discrete functions in RNA degradation, polyadenylation, and sequence homology with exosome proteins

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; ENZYMES; PLANTS (BOTANY); POLYMERIZATION; RNA;

EID: 0141453035     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.013326     Document Type: Article
Times cited : (65)

References (48)
  • 3
    • 0035176037 scopus 로고    scopus 로고
    • Cold-temperature induction of Escherichia coli polynucleotide phosphorylase occurs by reversal of its autoregulation
    • Beran, R.K., and Simons, R.W. (2001). Cold-temperature induction of Escherichia coli polynucleotide phosphorylase occurs by reversal of its autoregulation. Mol. Microbiol. 39, 112-125.
    • (2001) Mol. Microbiol. , vol.39 , pp. 112-125
    • Beran, R.K.1    Simons, R.W.2
  • 4
    • 0033548140 scopus 로고    scopus 로고
    • Polyadenylation promotes degradation of 3′-structured RNA by the Escherichia coli mRNA degradosome in vitro
    • Blum, E., Carpousis, A.J., and Higgins, C.F. (1999). Polyadenylation promotes degradation of 3′-structured RNA by the Escherichia coli mRNA degradosome in vitro. J. Biol. Chem. 274, 4009-4016.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4009-4016
    • Blum, E.1    Carpousis, A.J.2    Higgins, C.F.3
  • 5
    • 0032916509 scopus 로고    scopus 로고
    • mRNA degradation, a tale of poly(A) and multiprotein machines
    • Carpousis, A.J., Vanzo, N.F., and Raynal, L.C. (1999). mRNA degradation, a tale of poly(A) and multiprotein machines. Trends Genet. 15, 24-28.
    • (1999) Trends Genet. , vol.15 , pp. 24-28
    • Carpousis, A.J.1    Vanzo, N.F.2    Raynal, L.C.3
  • 6
    • 0025064239 scopus 로고
    • The P30 movement protein of tobacco mosaic virus is a single-strand nucleic acid binding protein
    • Citovsky, V., Knorr, D., Schuster, G., and Zambryski, P. (1990). The P30 movement protein of tobacco mosaic virus is a single-strand nucleic acid binding protein. Cell 60, 637-647.
    • (1990) Cell , vol.60 , pp. 637-647
    • Citovsky, V.1    Knorr, D.2    Schuster, G.3    Zambryski, P.4
  • 8
    • 0032617132 scopus 로고    scopus 로고
    • Degradation of mRNA in Escherichia coli: An old problem with some new twists
    • Coburn, G.A., and Mackie, G.A. (1999). Degradation of mRNA in Escherichia coli: An old problem with some new twists. Prog. Nucleic Acids Res. 62, 55-108.
    • (1999) Prog. Nucleic Acids Res. , vol.62 , pp. 55-108
    • Coburn, G.A.1    Mackie, G.A.2
  • 9
    • 0026695513 scopus 로고
    • Identification of the rph (RNase PH) gene of Bacillus subtilis: Evidence for suppression of cold-sensitive mutations in Escherichia coli
    • Craven, M.G., Henner, D.J., Alessi, D., Schauer, A.T., Ost, K.A., Deutscher, M.P., and Friedman, D.I. (1992). Identification of the rph (RNase PH) gene of Bacillus subtilis: Evidence for suppression of cold-sensitive mutations in Escherichia coli. J. Bacteriol. 174, 4727-4735.
    • (1992) J. Bacteriol. , vol.174 , pp. 4727-4735
    • Craven, M.G.1    Henner, D.J.2    Alessi, D.3    Schauer, A.T.4    Ost, K.A.5    Deutscher, M.P.6    Friedman, D.I.7
  • 10
    • 0037449772 scopus 로고    scopus 로고
    • The yeast mitochondrial degradosome: Its composition, interplay between RNA helicase and RNase activities and the role in mitochondrial RNA metabolism
    • Dziembowski, A., Piwowarski, J., Hoser, R., Minczuk, M., Dmochowska, A., Siep, M., Van Der Spek, H., Grivell, L., and Stepien, P.P. (2002). The yeast mitochondrial degradosome: Its composition, interplay between RNA helicase and RNase activities and the role in mitochondrial RNA metabolism. J. Biol. Chem. 278, 1603-1611.
    • (2002) J. Biol. Chem. , vol.278 , pp. 1603-1611
    • Dziembowski, A.1    Piwowarski, J.2    Hoser, R.3    Minczuk, M.4    Dmochowska, A.5    Siep, M.6    Van Der Spek, H.7    Grivell, L.8    Stepien, P.P.9
  • 11
    • 0033168679 scopus 로고    scopus 로고
    • Polyadenylation accelerates the degradation of the mitochondrial mRNA associated with cytoplasmic male sterility in sunflower
    • Gagliardi, D., and Leaver, C.J. (1999). Polyadenylation accelerates the degradation of the mitochondrial mRNA associated with cytoplasmic male sterility in sunflower. EMBO J. 18, 3757-3766.
    • (1999) EMBO J. , vol.18 , pp. 3757-3766
    • Gagliardi, D.1    Leaver, C.J.2
  • 12
    • 0033368475 scopus 로고    scopus 로고
    • Messenger RNA stability and its role in control of gene expression in bacteria and phages
    • Grunberg-Manago, M. (1999). Messenger RNA stability and its role in control of gene expression in bacteria and phages. Annu. Rev. Genet. 33, 193-227.
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 193-227
    • Grunberg-Manago, M.1
  • 13
    • 0033133680 scopus 로고    scopus 로고
    • Degrading chloroplast mRNA: The role of polyadenylation
    • Hayes, R., Kudla, J., and Gruissem, W. (1999). Degrading chloroplast mRNA: The role of polyadenylation. Trends Biochem. Sci. 24, 199-202.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 199-202
    • Hayes, R.1    Kudla, J.2    Gruissem, W.3
  • 14
    • 0029917715 scopus 로고    scopus 로고
    • Chloroplast mRNA 3′-end processing by a high molecular weight protein complex is regulated by nuclear encoded RNA binding proteins
    • Hayes, R., Kudla, J., Schuster, G., Gabay, L., Maliga, P., and Gruissem, W. (1996). Chloroplast mRNA 3′-end processing by a high molecular weight protein complex is regulated by nuclear encoded RNA binding proteins. EMBO J. 18, 1132-1141.
    • (1996) EMBO J. , vol.18 , pp. 1132-1141
    • Hayes, R.1    Kudla, J.2    Schuster, G.3    Gabay, L.4    Maliga, P.5    Gruissem, W.6
  • 15
    • 0036382938 scopus 로고    scopus 로고
    • Mutational analysis of polynucleotide phosphorylase from Escherichia coli
    • Jarrige, A., Brechemier-Baey, D., Mathy, N., Duche, O., and Portier, C. (2002). Mutational analysis of polynucleotide phosphorylase from Escherichia coli. J. Mol. Biol. 321, 397-409.
    • (2002) J. Mol. Biol. , vol.321 , pp. 397-409
    • Jarrige, A.1    Brechemier-Baey, D.2    Mathy, N.3    Duche, O.4    Portier, C.5
  • 16
    • 0033993926 scopus 로고    scopus 로고
    • Polyadenylation of three classes of chloroplast RNA in Chlamydomonas reinhardtii
    • Komine, Y., Kwong, L., Anguera, M., Schuster, S., and Stern, D.B. (2000). Polyadenylation of three classes of chloroplast RNA in Chlamydomonas reinhardtii. RNA 6, 598-607.
    • (2000) RNA , vol.6 , pp. 598-607
    • Komine, Y.1    Kwong, L.2    Anguera, M.3    Schuster, S.4    Stern, D.B.5
  • 17
    • 0034745504 scopus 로고    scopus 로고
    • Prediction of the archaeal exosome and its connections with the proteasome and the translation and transcription machineries by a comparative-genomic approach
    • Koonin, E.V., Wolf, Y.I., and Aravind, L. (2001). Prediction of the archaeal exosome and its connections with the proteasome and the translation and transcription machineries by a comparative-genomic approach. Genome Res. 11, 240-252.
    • (2001) Genome Res. , vol.11 , pp. 240-252
    • Koonin, E.V.1    Wolf, Y.I.2    Aravind, L.3
  • 18
    • 0035138023 scopus 로고    scopus 로고
    • Transcript lifetime is balanced between stabilizing stem-loop structures and degradation-promoting polyadenylation in plant mitochondria
    • Kuhn, J., Tengler, U., and Binder, S. (2001). Transcript lifetime is balanced between stabilizing stem-loop structures and degradation-promoting polyadenylation in plant mitochondria. Mol. Cell. Biol. 21, 731-742.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 731-742
    • Kuhn, J.1    Tengler, U.2    Binder, S.3
  • 19
    • 0037168641 scopus 로고    scopus 로고
    • Identification and cloning of human polynucleotide phosphorylase, hPNPase old-35, in the context of terminal differentiation and cellular senescence
    • Leszczyniecka, M., Kang, D.C., Sarkar, D., Su, Z.Z., Holmes, M., Valerie, K., and Fisher, P.B. (2002). Identification and cloning of human polynucleotide phosphorylase, hPNPase old-35, in the context of terminal differentiation and cellular senescence. Proc. Natl. Acad. Sci. USA 99, 16636-16641.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16636-16641
    • Leszczyniecka, M.1    Kang, D.C.2    Sarkar, D.3    Su, Z.Z.4    Holmes, M.5    Valerie, K.6    Fisher, P.B.7
  • 20
    • 0037174922 scopus 로고    scopus 로고
    • DEAD box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E
    • Liou, G.G., Chang, H.Y., Lin, C.S., and Lin-Chao, S. (2002). DEAD box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E. J. Biol. Chem. 277, 41157-41162.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41157-41162
    • Liou, G.G.1    Chang, H.Y.2    Lin, C.S.3    Lin-Chao, S.4
  • 21
    • 0029828944 scopus 로고    scopus 로고
    • Addition of poly(A)-rich sequences to endonucleolytic cleavage sites in the degradation of spinach chloroplast mRNA
    • Lisitsky, I., Klaff, P., and Schuster, G. (1996). Addition of poly(A)-rich sequences to endonucleolytic cleavage sites in the degradation of spinach chloroplast mRNA. Proc. Natl. Acad. Sci. USA 93, 13398-13403.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13398-13403
    • Lisitsky, I.1    Klaff, P.2    Schuster, G.3
  • 22
    • 0031465234 scopus 로고    scopus 로고
    • Blocking polyadenylation of mRNA in the chloroplast inhibits its degradation
    • Lisitsky, I., Klaff, P., and Schuster, G. (1997a). Blocking polyadenylation of mRNA in the chloroplast inhibits its degradation. Plant J. 12, 1173-1178.
    • (1997) Plant J. , vol.12 , pp. 1173-1178
    • Lisitsky, I.1    Klaff, P.2    Schuster, G.3
  • 23
    • 0030748658 scopus 로고    scopus 로고
    • The mechanism of preferential degradation of polyadenylated RNA in the chloroplast: The exoribonuclease 100RNP/PNPase displays high binding affinity for poly(A) sequence
    • Lisitsky, I., Kotler, A., and Schuster, G. (1997b). The mechanism of preferential degradation of polyadenylated RNA in the chloroplast: The exoribonuclease 100RNP/PNPase displays high binding affinity for poly(A) sequence. J. Biol. Chem. 272, 17648-17653.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17648-17653
    • Lisitsky, I.1    Kotler, A.2    Schuster, G.3
  • 24
    • 0027998158 scopus 로고
    • RNA-binding activities of the different domains of a spinach chloroplast ribonucleoprotein
    • Lisitsky, I., Liveanu, V., and Schuster, G. (1994). RNA-binding activities of the different domains of a spinach chloroplast ribonucleoprotein. Nucleic Acids Res. 22, 4719-4724.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4719-4724
    • Lisitsky, I.1    Liveanu, V.2    Schuster, G.3
  • 25
    • 0033560992 scopus 로고    scopus 로고
    • Preferential degradation of polyadenylated and polyuridinylated RNAs by bacterial exoribonuclease polynucleotide phosphorylase (PNPase)
    • Lisitsky, I., and Schuster, G. (1999). Preferential degradation of polyadenylated and polyuridinylated RNAs by bacterial exoribonuclease polynucleotide phosphorylase (PNPase). Eur. J. Biochem. 261, 468-474.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 468-474
    • Lisitsky, I.1    Schuster, G.2
  • 26
    • 0004574825 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase
    • T.E. Creighton, ed (New York: John Wiley & Sons)
    • Littauer, U.Z., and Grunberg-Manago, M. (1999). Polynucleotide phosphorylase. In The Encyclopedia of Molecular Biology, T.E. Creighton, ed (New York: John Wiley & Sons), pp. 1911-1918.
    • (1999) The Encyclopedia of Molecular Biology , pp. 1911-1918
    • Littauer, U.Z.1    Grunberg-Manago, M.2
  • 27
    • 0033048415 scopus 로고    scopus 로고
    • The C-terminal half of RNase E, which organizes the Escherichia coli degradosome, participates in mRNA degradation but not rRNA processing in vivo
    • Lopez, P.J., Marchand, I., Joyce, S.A., and Dreyfus, M. (1999). The C-terminal half of RNase E, which organizes the Escherichia coli degradosome, participates in mRNA degradation but not rRNA processing in vivo. Mol. Microbiol. 33, 188-199.
    • (1999) Mol. Microbiol. , vol.33 , pp. 188-199
    • Lopez, P.J.1    Marchand, I.2    Joyce, S.A.3    Dreyfus, M.4
  • 28
    • 0345580792 scopus 로고    scopus 로고
    • Polyadenylation occurs at multiple sites in maize mitochondrial cox2 mRNA and is independent of editing status
    • Lupold, D.S., Caoile, A.G.F.S., and Stern, D.B. (1999). Polyadenylation occurs at multiple sites in maize mitochondrial cox2 mRNA and is independent of editing status. Plant Cell 11, 1565-1578.
    • (1999) Plant Cell , vol.11 , pp. 1565-1578
    • Lupold, D.S.1    Caoile, A.G.F.S.2    Stern, D.B.3
  • 29
    • 0034710943 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase functions both as a 3′ to 5′ exonuclease and a poly(A) polymerase in Escherichia coli
    • Mohanty, B.K., and Kushner, S.R. (2000). Polynucleotide phosphorylase functions both as a 3′ to 5′ exonuclease and a poly(A) polymerase in Escherichia coli. Proc. Natl. Acad. Sci. USA 97, 11966-11971.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11966-11971
    • Mohanty, B.K.1    Kushner, S.R.2
  • 30
    • 0033861250 scopus 로고    scopus 로고
    • Processing and degradation of chloroplast mRNA
    • Monde, R.A., Schuster, G., and Stern, D.B. (2000). Processing and degradation of chloroplast mRNA. Biochimie 82, 573-582.
    • (2000) Biochimie , vol.82 , pp. 573-582
    • Monde, R.A.1    Schuster, G.2    Stern, D.B.3
  • 31
    • 0037080834 scopus 로고    scopus 로고
    • The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements
    • Mukherjee, D., Gao, M., O'Connor, J.P., Raijmakers, R., Pruijn, G., Lutz, C.S., and Wilusz, J. (2002). The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements. EMBO J. 21, 165-174.
    • (2002) EMBO J. , vol.21 , pp. 165-174
    • Mukherjee, D.1    Gao, M.2    O'Connor, J.P.3    Raijmakers, R.4    Pruijn, G.5    Lutz, C.S.6    Wilusz, J.7
  • 32
    • 0027582419 scopus 로고
    • The 54 kDa RNA-binding protein from mustard chloroplasts mediates endonucleolytic transcript 3′ end formation in vitro
    • Nickelsen, J., and Link, G. (1993). The 54 kDa RNA-binding protein from mustard chloroplasts mediates endonucleolytic transcript 3′ end formation in vitro. Plant J. 3, 537-544.
    • (1993) Plant J. , vol.3 , pp. 537-544
    • Nickelsen, J.1    Link, G.2
  • 33
    • 0019444843 scopus 로고
    • tRNA punctuation model of RNA processing in human mitochondria
    • Ojala, D., Montoya, J., and Attardi, G. (1981). tRNA punctuation model of RNA processing in human mitochondria. Nature 290, 470-474.
    • (1981) Nature , vol.290 , pp. 470-474
    • Ojala, D.1    Montoya, J.2    Attardi, G.3
  • 34
    • 0036977391 scopus 로고    scopus 로고
    • Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring
    • Raijmakers, R., Egberts, W.V., van Venrooij, W.J., and Pruijn, G.J. (2002). Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring. J. Mol. Biol. 323, 653-663.
    • (2002) J. Mol. Biol. , vol.323 , pp. 653-663
    • Raijmakers, R.1    Egberts, W.V.2    Van Venrooij, W.J.3    Pruijn, G.J.4
  • 35
    • 0242400018 scopus 로고    scopus 로고
    • Degradation of mRNA in bacteria: Emergence of ubiquitous features
    • Regnier, P., and Arraiano, C.M. (2000). Degradation of mRNA in bacteria: Emergence of ubiquitous features. Bioessays 22, 235-244.
    • (2000) Bioessays , vol.22 , pp. 235-244
    • Regnier, P.1    Arraiano, C.M.2
  • 36
    • 0038182527 scopus 로고    scopus 로고
    • RNA polyadenylation and degradation in cyanobacteria are similar to the chloroplast but different from Escherichia coli
    • Rott, R., Zipor, G., Portnoy, V., Liveanu, V., and Schuster, G. (2003). RNA polyadenylation and degradation in cyanobacteria are similar to the chloroplast but different from Escherichia coli. J. Biol. Chem. 278, 15771-15777.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15771-15777
    • Rott, R.1    Zipor, G.2    Portnoy, V.3    Liveanu, V.4    Schuster, G.5
  • 37
    • 0031009317 scopus 로고    scopus 로고
    • Polyadenylation of mRNA in prokaryotes
    • Sarkar, N. (1997). Polyadenylation of mRNA in prokaryotes. Annu. Rev. Biochem. 66, 173-197.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 173-197
    • Sarkar, N.1
  • 38
    • 0033180187 scopus 로고    scopus 로고
    • Update on chloroplast molecular biology: Polyadenylation and degradation of mRNA in the chloroplast
    • Schuster, G., Lisitsky, I., and Klaff, P. (1999). Update on chloroplast molecular biology: Polyadenylation and degradation of mRNA in the chloroplast. Plant Physiol. 120, 937-944.
    • (1999) Plant Physiol. , vol.120 , pp. 937-944
    • Schuster, G.1    Lisitsky, I.2    Klaff, P.3
  • 39
    • 0027137145 scopus 로고
    • Conducting the G-quartet
    • Sundquist, W.I. (1993). Conducting the G-quartet. Curr. Biol 3, 893-895.
    • (1993) Curr. Biol. , vol.3 , pp. 893-895
    • Sundquist, W.I.1
  • 40
    • 0034435974 scopus 로고    scopus 로고
    • A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation
    • Symmons, M.F., Jones, G.H., and Luisi, B.F. (2000). A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation. Structure 8, 1215-1226.
    • (2000) Structure , vol.8 , pp. 1215-1226
    • Symmons, M.F.1    Jones, G.H.2    Luisi, B.F.3
  • 42
    • 0037121925 scopus 로고    scopus 로고
    • PNPase activity determines the efficiency of mRNA 3′-end processing, the degradation of tRNA and the extent of polyadenylation in chloroplasts
    • Walter, M., Kilian, J., and Kudla, J. (2002). PNPase activity determines the efficiency of mRNA 3′-end processing, the degradation of tRNA and the extent of polyadenylation in chloroplasts. EMBO J. 21, 6905-6914.
    • (2002) EMBO J. , vol.21 , pp. 6905-6914
    • Walter, M.1    Kilian, J.2    Kudla, J.3
  • 43
    • 0025601902 scopus 로고
    • Isolation and characterization of a new temperature-sensitive polynucleotide phosphorylase mutation in Escherichia coli K-12
    • Yancey, S.D., and Kushner, S.R. (1990). Isolation and characterization of a new temperature-sensitive polynucleotide phosphorylase mutation in Escherichia coli K-12. Biochimie 72, 835-843.
    • (1990) Biochimie , vol.72 , pp. 835-843
    • Yancey, S.D.1    Kushner, S.R.2
  • 44
    • 0030221344 scopus 로고    scopus 로고
    • CSP41, a sequence-specific chloroplast mRNA binding protein, is an endoribonuclease
    • Yang, J., Schuster, G., and Stern, D.B. (1996). CSP41, a sequence-specific chloroplast mRNA binding protein, is an endoribonuclease. Plant Cell 8, 1409-1420.
    • (1996) Plant Cell , vol.8 , pp. 1409-1420
    • Yang, J.1    Schuster, G.2    Stern, D.B.3
  • 45
    • 0034934778 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts
    • Yehudai-Resheff, S., Hirsh, M., and Schuster, G. (2001). Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts. Mol. Cell. Biol. 21, 5408-5416.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5408-5416
    • Yehudai-Resheff, S.1    Hirsh, M.2    Schuster, G.3
  • 46
    • 0034160029 scopus 로고    scopus 로고
    • Characterization of the E. coli poly(A)-polymerase: Specificity to nucleotides, RNA-binding affinities and RNA-structure dependence activity
    • Yehudai-Resheff, S., and Schuster, G. (2000). Characterization of the E. coli poly(A)-polymerase: Specificity to nucleotides, RNA-binding affinities and RNA-structure dependence activity. Nucleic Acids Res. 28, 1139-1144.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1139-1144
    • Yehudai-Resheff, S.1    Schuster, G.2
  • 47
    • 0030860690 scopus 로고    scopus 로고
    • An essential function for the phosphate-dependent exoribonucleases RNase PH and polynucleotide phosphorylase
    • Zhou, Z., and Deutscher, M.P. (1997). An essential function for the phosphate-dependent exoribonucleases RNase PH and polynucleotide phosphorylase. J. Bacteriol. 179, 4391-4395.
    • (1997) J. Bacteriol. , vol.179 , pp. 4391-4395
    • Zhou, Z.1    Deutscher, M.P.2
  • 48
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution
    • Zuo, Y., and Deutscher, M.P. (2001). Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution. Nucleic Acids Res. 29, 1017-1026.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.P.2


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