메뉴 건너뛰기




Volumn 40, Issue 9, 2012, Pages 4146-4157

Crystal structure of human polynucleotide phosphorylase: Insights into its domain function in RNA binding and degradation

Author keywords

[No Author keywords available]

Indexed keywords

POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE;

EID: 84861401113     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr1281     Document Type: Article
Times cited : (52)

References (52)
  • 1
    • 0034710943 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase functions both as a 30!50 exonuclease and a poly(A) polymerase in Escherichia coli
    • Mohanty, B.K. and Kushner, S.R. (2000) Polynucleotide phosphorylase functions both as a 30!50 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
  • 2
    • 32644435694 scopus 로고    scopus 로고
    • Degradation of RNA in bacteria: Comparison of mRNA and stable RNA
    • DOI 10.1093/nar/gkj472
    • Deutscher, M.P. (2006) Degradation of RNA in bacteria: comparison of mRNA and stable RNA. Nucleic Acids Res., 34, 659-666. (Pubitemid 43240252)
    • (2006) Nucleic Acids Research , vol.34 , Issue.2 , pp. 659-666
    • Deutscher, M.P.1
  • 4
    • 79954605509 scopus 로고    scopus 로고
    • Human polynucleotide phosphorylase (hPNPaseold-35): An evolutionary conserved gene with an expanding repertoire of RNA degradation functions
    • Das, S.K., Bhutia, S.K., Stokhi, U.K., Dash, R., Azab, B., Sarkar, D. and Fisher, P.B. (2011) Human polynucleotide phosphorylase (hPNPaseold-35): an evolutionary conserved gene with an expanding repertoire of RNA degradation functions. Oncogene, 30, 1733-1743.
    • (2011) Oncogene , vol.30 , pp. 1733-1743
    • Das, S.K.1    Bhutia, S.K.2    Stokhi, U.K.3    Dash, R.4    Azab, B.5    Sarkar, D.6    Fisher, P.B.7
  • 5
    • 33745838984 scopus 로고    scopus 로고
    • The RNA degradosome: life in the fast lane of adaptive molecular evolution
    • DOI 10.1016/j.tibs.2006.05.005, PII S0968000406001393
    • Marcaida, M.J., DePristo, M.A., Chandran, V., Carpousis, A.J. and Luisi, B.F. (2006) The RNA degradosome: life in the fast lane of adaptive molecular evolution. Trends Biochem. Sci., 31, 359-365. (Pubitemid 44038917)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.7 , pp. 359-365
    • Marcaida, M.J.1    DePristo, M.A.2    Chandran, V.3    Carpousis, A.J.4    Luisi, B.F.5
  • 6
    • 35548995356 scopus 로고    scopus 로고
    • The RNA degradosome of Escherichia coli: An mRNA-degrading machine assembled on RNase E
    • DOI 10.1146/annurev.micro.61.080706.093440
    • Carpousis, A.J. (2007) The RNA degradosome of Escherichia coli: an mRNA-degrading machine assembled on RNase E. Annu. Rev. Microbiol., 61, 71-87. (Pubitemid 350058200)
    • (2007) Annual Review of Microbiology , vol.61 , pp. 71-87
    • Carpousis, A.J.1
  • 8
    • 64049109732 scopus 로고    scopus 로고
    • RNA polyadenylation and decay in mitochondria and chloroplasts
    • Schuster, G. and Stern, D. (2009) RNA polyadenylation and decay in mitochondria and chloroplasts. Prog. Mol. Biol. Trans. Sci., 85, 393-422.
    • (2009) Prog. Mol. Biol. Trans. Sci. , vol.85 , pp. 393-422
    • Schuster, G.1    Stern, D.2
  • 9
    • 36249001217 scopus 로고    scopus 로고
    • Human polynucleotide phosphorylase: location matters
    • DOI 10.1016/j.tcb.2007.09.006, PII S0962892407002450
    • Chen, H.-W., Koehler, C.M. and Teitell, M.A. (2007) Human polynucleotide phosphorylase: location matters. Trends Cell Biol., 17, 600-608. (Pubitemid 350138435)
    • (2007) Trends in Cell Biology , vol.17 , Issue.12 , pp. 600-608
    • Chen, H.-W.1    Koehler, C.M.2    Teitell, M.A.3
  • 11
    • 23344451161 scopus 로고    scopus 로고
    • OLD-35) mediating cellular senescence
    • DOI 10.1128/MCB.25.16.7333-7343.2005
    • Sarkar, D., Park, E.S., Emdad, L., Randolph, A., Valerie, K. and Fisher, P.B. (2005) Defining the domains of human polynucleotide phosphorylase (hPNPaseOLD-35) mediating cellular senescence. Mol. Cell. Biol., 25, 7333-7343. (Pubitemid 41105928)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.16 , pp. 7333-7343
    • Sarkar, D.1    Park, E.S.2    Emdad, L.3    Randolph, A.4    Valerie, K.5    Fisher, P.B.6
  • 13
    • 33646794535 scopus 로고    scopus 로고
    • old-35)
    • DOI 10.1038/sj.cdd.4401829, PII 4401829
    • Sarkar, D., Park, E.S. and Fisher, P.B. (2006) Defining the mechanism by which IFN-b dowregulates c-myc expression in human melanoma cells: pivotal role for human polynucleotide phosphorylase (hPNPaseold-35). Cell Death Differ., 13, 1541-1553. (Pubitemid 44210357)
    • (2006) Cell Death and Differentiation , vol.13 , Issue.9 , pp. 1541-1553
    • Sarkar, D.1    Park, E.S.2    Fisher, P.B.3
  • 14
    • 77955384888 scopus 로고    scopus 로고
    • Human polynucleotide phosphorylase selectively and preferentially degrades microRNA-221 in human melanoma cells
    • Das, S.K., Sokhi, U.K., Bhutia, S.K., Azab, B., Su, Z.Z., Sarkar, D. and Fisher, P.B. (2010) Human polynucleotide phosphorylase selectively and preferentially degrades microRNA-221 in human melanoma cells. Proc. Natl Acad. Sci. USA, 107, 11948-11953.
    • (2010) Proc. Natl Acad Sci. USA , vol.107 , pp. 11948-11953
    • Das, S.K.1    Sokhi, U.K.2    Bhutia, S.K.3    Azab, B.4    Su, Z.Z.5    Sarkar, D.6    Fisher, P.B.7
  • 15
    • 34548593354 scopus 로고    scopus 로고
    • old-35) induces apoptosis
    • DOI 10.1158/0008-5472.CAN-07-0872
    • Sarkar, D., Park, E.S., Barber, G.N. and Fisher, P.B. (2007) Activation of double-stranded RNA-dependent protein kinase, a new pathway by which human polynucleotide phosphorylase (hPNPaseold-35) induces apoptosis. Cancer Res, 67, 7948-7953. (Pubitemid 47395123)
    • (2007) Cancer Research , vol.67 , Issue.17 , pp. 7948-7953
    • Sarkar, D.1    Eun, S.P.2    Barber, G.N.3    Fisher, P.B.4
  • 16
    • 33745384267 scopus 로고    scopus 로고
    • Molecular mechanisms of aging-associated inflammation
    • DOI 10.1016/j.canlet.2005.04.009, PII S0304383505003654
    • Sarkar, D. and Fisher, P.B. (2006) Molecular mechanisms of aging-associated inflammation. Cancer Lett., 236, 13-23. (Pubitemid 44382538)
    • (2006) Cancer Letters , vol.236 , Issue.1 , pp. 13-23
    • Sarkar, D.1    Fisher, P.B.2
  • 17
    • 38649115643 scopus 로고    scopus 로고
    • Stable PNPase RNAi silencing: Its effect on the processing and adenylation of human mitochondrial RNA
    • DOI 10.1261/rna.697308
    • Slomovic, S. and Schuster, G. (2008) Stable PNPase RNAi silencing: its effect on the processing and adenylation of human mitochondrial RNA. RNA, 14, 310-323. (Pubitemid 351171591)
    • (2008) RNA , vol.14 , Issue.2 , pp. 310-323
    • Slomovic, S.1    Schuster, G.2
  • 20
    • 68949108247 scopus 로고    scopus 로고
    • Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-kDa heteropentamer to cooperatively degrade double-stranded RNA with a 30-to-50directionality
    • Wang, D.D.-H., Shu, Z., Lieser, S.A., Chen, P.-L. and Lee, W.-H. (2009) Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-kDa heteropentamer to cooperatively degrade double-stranded RNA with a 30-to-50directionality. J. Biol. Chem., 284, 20812-20821.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20812-20821
    • Wang, D.D.-H.1    Shu, Z.2    Lieser, S.A.3    Chen, P.-L.4    Lee, W.-H.5
  • 22
    • 23044432699 scopus 로고    scopus 로고
    • Conserved domains in polynucleotide phosphorylase among eubacteria
    • DOI 10.1016/j.biochi.2005.03.005, PII S0300908405000775
    • Bermudez-Cruz, R.M., Ramirez, F., Kameyama-Kawabe, L. and Montanez, C. (2005) Conserved domains in polynucleotide phosphorylase among eubacteria. Biochimie, 87, 737-745. (Pubitemid 41058904)
    • (2005) Biochimie , vol.87 , Issue.8 , pp. 737-745
    • Bermudez-Cruz, R.M.1    Ramirez, F.2    Kameyama-Kawabe, L.3    Montanez, C.4
  • 23
    • 0034435974 scopus 로고    scopus 로고
    • A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation
    • DOI 10.1016/S0969-2126(00)00521-9, PII S0969212600005219
    • 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. (Pubitemid 32667486)
    • (2000) Structure , vol.8 , Issue.11 , pp. 1215-1226
    • Symmons, M.F.1    Jones, G.H.2    Luisi, B.F.3
  • 24
    • 55549093442 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli PNPase: Central channel residues are involved in processive RNA degradation
    • Shi, Z., Yang, W.-Z., Lin-Chao, S., Chak, K.-F. and Yuan, H.S. (2008) Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. RNA, 14, 2361-2371.
    • (2008) RNA , vol.14 , pp. 2361-2371
    • Shi, Z.1    Yang, W.-Z.2    Lin-Chao, S.3    Chak, K.-F.4    Yuan, H.S.5
  • 25
    • 67349257830 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase e RNA and manganese: Implications for catalytic mechanism and RNA degradosome assembly
    • Nurmohamed, S., Vaidialingam, B., Callaghan, A.J. and Luisi, B.F. (2009) Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: implications for catalytic mechanism and RNA degradosome assembly. J. Mol. Biol., 389, 17-33.
    • (2009) J. Mol. Biol. , vol.389 , pp. 17-33
    • Nurmohamed, S.1    Vaidialingam, B.2    Callaghan, A.J.3    Luisi, B.F.4
  • 26
    • 79960668648 scopus 로고    scopus 로고
    • Structural components and architectures of RNA exosomes
    • Januszyk, K. and Lima, C.D. (2010) Structural components and architectures of RNA exosomes. Adv. Exp. Med. Biol., 702, 9-28.
    • (2010) Adv. Exp. Med. Biol. , vol.702 , pp. 9-28
    • Januszyk, K.1    Lima, C.D.2
  • 27
    • 34447306927 scopus 로고    scopus 로고
    • The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines
    • DOI 10.1007/s11373-007-9178-y, Special Issue on Molecular Biology
    • Lin-Chao, S., Chiou, N.-T. and Schuster, G. (2007) The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines. J. Biomed. Sci., 14, 523-532. (Pubitemid 47063488)
    • (2007) Journal of Biomedical Science , vol.14 , Issue.4 , pp. 523-532
    • Lin-Chao, S.1    Chiou, N.-T.2    Schuster, G.3
  • 29
    • 33845407784 scopus 로고    scopus 로고
    • Reconstitution, Activities, and Structure of the Eukaryotic RNA Exosome
    • DOI 10.1016/j.cell.2006.10.037, PII S0092867406014279
    • Liu, Q., Greimann, J.C. and Lima, C.D. (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell, 127, 1223-1237. (Pubitemid 44894519)
    • (2006) Cell , vol.127 , Issue.6 , pp. 1223-1237
    • Liu, Q.1    Greimann, J.C.2    Lima, C.D.3
  • 30
    • 27644435644 scopus 로고    scopus 로고
    • Structural framework for the mechanism of archaeal exosomes in RNA processing
    • DOI 10.1016/j.molcel.2005.10.018, PII S1097276505017132
    • Buttner, K., Wenig, K. and Hopfner, K.-P. (2005) Structural framework for the mechanism of archaeal exosomes in RNA processing. Mol. Cell, 20, 461-471. (Pubitemid 41572302)
    • (2005) Molecular Cell , vol.20 , Issue.3 , pp. 461-471
    • Buttner, K.1    Wenig, K.2    Hopfner, K.-P.3
  • 31
    • 34247844604 scopus 로고    scopus 로고
    • RNA channelling by the archaeal exosome
    • DOI 10.1038/sj.embor.7400945, PII 7400945
    • Lorentzen, E., Dziembowski, A., Lindner, D., Seraphin, B. and Conti, E. (2007) RNA channelling by the archaeal exosome. EMBO Rep., 8, 470-476. (Pubitemid 46696517)
    • (2007) EMBO Reports , vol.8 , Issue.5 , pp. 470-476
    • Lorentzen, E.1    Dziembowski, A.2    Lindner, D.3    Seraphin, B.4    Conti, E.5
  • 32
    • 0036382938 scopus 로고    scopus 로고
    • Mutational analysis of polynucleotide phosphorylase form Escherichia coli
    • Jarrige, A.-C., Brechemier-Baey, D., Mathy, N., Cuche, O. and Portier, C. (2002) Mutational analysis of polynucleotide phosphorylase form Escherichia coli. J. Mol. Biol., 321, 397-409.
    • (2002) J. Mol. Biol. , vol.321 , pp. 397-409
    • Jarrige, A.-C.1    Brechemier-Baey, D.2    Mathy, N.3    Cuche, O.4    Portier, C.5
  • 33
    • 27144485749 scopus 로고    scopus 로고
    • Function of the conserved S1 and KH domains in polynucleotide phosphorylase
    • DOI 10.1128/JB.187.21.7214-7221.2005
    • Stickney, L.M., Hankins, J.S., Miao, S. and Mackie, G.A. (2005) Function of the conserved S1 and KH domains in polynucelotide phosphorylase. J. Bacteriol., 187, 7214-7221. (Pubitemid 41507779)
    • (2005) Journal of Bacteriology , vol.187 , Issue.21 , pp. 7214-7221
    • Stickney, L.M.1    Hankins, J.S.2    Miao, X.3    Mackie, G.A.4
  • 34
    • 38649100934 scopus 로고    scopus 로고
    • Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts
    • DOI 10.1261/rna.698108
    • Portnoy, V., Palnizky, G., Yehudai-Resheff, S., Glaser, F. and Schuster, G. (2008) Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts. RNA, 14, 297-309. (Pubitemid 351171590)
    • (2008) RNA , vol.14 , Issue.2 , pp. 297-309
    • Portnoy, V.1    Palnizky, G.2    Yehudai-Resheff, S.3    Glaser, F.4    Schuster, G.5
  • 35
    • 0031471204 scopus 로고    scopus 로고
    • The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid-binding fold
    • DOI 10.1016/S0092-8674(00)81844-9
    • Bycroft, M., Hubbard, T.J.P., Proctor, M., Freund, S.M.V. and Murzin, A.G. (1997) The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell, 88, 235-242. (Pubitemid 28015872)
    • (1997) Cell , vol.88 , Issue.2 , pp. 235-242
    • Bycroft, M.1    Hubbard, T.J.P.2    Proctor, M.3    Freund, S.M.V.4    Murzin, A.G.5
  • 36
    • 0034603208 scopus 로고    scopus 로고
    • Sequence-specific RNA binding by a Nova KH domain: Implications for paraneoplastic disease and the fragile X syndrome
    • Lewis, H.A., Musunuru, K., Jensen, K.B., Edo, C., Chen, H., Darnell, R.B. and Burley, S.K. (2000) Sequence-specific RNA binding by a Nova KH domain: implications for paraneoplastic disease and the fragile X syndrome. Cell, 100, 323-332. (Pubitemid 30353088)
    • (2000) Cell , vol.100 , Issue.3 , pp. 323-332
    • Lewis, H.A.1    Musunuru, K.2    Jensen, K.B.3    Edo, C.4    Chen, H.5    Darnell, R.B.6    Burley, S.K.7
  • 38
    • 43549124851 scopus 로고    scopus 로고
    • Structure and function of KH domains
    • DOI 10.1111/j.1742-4658.2008.06411.x
    • Regan, L., Valverde, R. and Edwards, L. (2008) Structure and function of KH domains. FEBS J., 275, 2712-2726. (Pubitemid 351678660)
    • (2008) FEBS Journal , vol.275 , Issue.11 , pp. 2712-2726
    • Valverde, R.1    Edwards, L.2    Regan, L.3
  • 39
    • 27144547978 scopus 로고    scopus 로고
    • Structure of a Mycobacterium tuberculosis NusA-RNA complex
    • DOI 10.1038/sj.emboj.7600829, PII 7600829
    • Beuth, B., Pennell, S., Arnvig, K.B., Martin, S.R. and Taylor, I.A. (2005) Structure of a Mycobacterium tuberculosis NusA-RNA complex. EMBO J., 24, 3576-3587. (Pubitemid 41509365)
    • (2005) EMBO Journal , vol.24 , Issue.20 , pp. 3576-3587
    • Beuth, B.1    Pennell, S.2    Arnvig, K.B.3    Martin, S.R.4    Taylor, I.A.5
  • 40
    • 70349301461 scopus 로고    scopus 로고
    • Structure of ERA in complex with the 30 end of 16S rRNA: Implications for ribosome biogenesis
    • Tu, C., Zhou, X.M., Tropea, J.E., Austin, B.P., Waugh, D.S., Court, D.L. and Ji, X.H. (2009) Structure of ERA in complex with the 30 end of 16S rRNA: implications for ribosome biogenesis. Proc. Natl Acad. Sci. USA, 106, 14843-14848.
    • (2009) Proc. Natl Acad Sci. USA , vol.106 , pp. 14843-14848
    • Tu, C.1    Zhou, X.M.2    Tropea, J.E.3    Austin, B.P.4    Waugh, D.S.5    Court, D.L.6    Ji, X.H.7
  • 41
    • 0027273728 scopus 로고
    • The pre-mRNA binding K protein contains a novel evolutionarily conserved motif
    • Siomi, H., Matunis, M.J., Michael, W.M. and Dreyfuss, G. (1993) The pre-mRNA binding K protein contains a novel evolutionarily conserved motif. Nucleic Acids Res., 21, 1193-1198. (Pubitemid 23155615)
    • (1993) Nucleic Acids Research , vol.21 , Issue.5 , pp. 1193-1198
    • Siomi, H.1    Matunis, M.J.2    Michael, W.M.3    Dreyfuss, G.4
  • 42
    • 34548430484 scopus 로고    scopus 로고
    • Fragile X Mental Retardation Syndrome: Structure of the KH1-KH2 Domains of Fragile X Mental Retardation Protein
    • DOI 10.1016/j.str.2007.06.022, PII S0969212607002808
    • Valverde, R., Pozdnyakova, I., Kajander, T., Venkatrarnan, J. and Regan, L. (2007) Fragile X mental retardation syndrome: structure of the KH1-KH2 domains of fragile X mental retardation protein. Structure, 15, 1090-1098. (Pubitemid 47362689)
    • (2007) Structure , vol.15 , Issue.9 , pp. 1090-1098
    • Valverde, R.1    Pozdnyakova, I.2    Kajander, T.3    Venkatraman, J.4    Regan, L.5
  • 43
    • 0031471204 scopus 로고    scopus 로고
    • The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid-binding fold
    • DOI 10.1016/S0092-8674(00)81844-9
    • Bycroft, M., Hubbard, T.J.P., Proctor, M., Freund, S.M.V. and Murzin, A.G. (1997) The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell, 88, 235-242. (Pubitemid 28015872)
    • (1997) Cell , vol.88 , Issue.2 , pp. 235-242
    • Bycroft, M.1    Hubbard, T.J.P.2    Proctor, M.3    Freund, S.M.V.4    Murzin, A.G.5
  • 44
    • 33748414894 scopus 로고    scopus 로고
    • Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex
    • DOI 10.1038/nature05080, PII NATURE05080
    • Frazao, C., Mcvey, C.E., Amblar, M., Barbas, A., Vonrhein, C., Arraiano, C.M. and Carrondo, M.A. (2006) Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex. Nature, 443, 110-114. (Pubitemid 44344058)
    • (2006) Nature , vol.443 , Issue.7107 , pp. 110-114
    • Frazao, C.1    McVey, C.E.2    Amblar, M.3    Barbas, A.4    Vonrhein, C.5    Arraiano, C.M.6    Carrondo, M.A.7
  • 45
    • 4143138726 scopus 로고    scopus 로고
    • Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces
    • DOI 10.1016/j.jmb.2004.05.061, PII S0022283604006412
    • Schubert, M., Edge, R.E., Lario, P., Cook, M.A., Strynadka, N.C.J., Mackie, G.A. and McIntosh, L.P. (2004) Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces. J. Mol. Biol., 341, 37-54. (Pubitemid 39090633)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.1 , pp. 37-54
    • Schubert, M.1    Edge, R.E.2    Lario, P.3    Cook, M.A.4    Strynadka, N.C.J.5    Mackie, G.A.6    McIntosh, L.P.7
  • 46
    • 0035861997 scopus 로고    scopus 로고
    • Crystal structure of the transcription elongation/antitermination factor NusA from Mycobacterium tuberculosis at 1.7 Aå resolution
    • DOI 10.1006/jmbi.2000.5144
    • Gopal, B., Haire, L.F., Gamblin, S.J., Dodson, E.J., Lane, A.N., Papavinasasundaram, K.G., Colston, M.J. and Dodson, G. (2001) Crystal structure of the transcription elongation/antitermination factor NusA from Mycobacterium tuberculosis at 1.7 angstrom resolution. J. Mol. Biol., 314, 1087-1095. (Pubitemid 34073072)
    • (2001) Journal of Molecular Biology , vol.314 , Issue.5 , pp. 1087-1095
    • Gopal, B.1    Haire, L.F.2    Gamblin, S.J.3    Dodson, E.J.4    Lane, A.N.5    Papavinasasundaram, K.G.6    Colston, M.J.7    Dodson, G.8
  • 48
    • 27644496002 scopus 로고    scopus 로고
    • Structural basis of 3' end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core
    • DOI 10.1016/j.molcel.2005.10.020, PII S1097276505017156
    • Lorentzen, E. and Conti, E. (2005) Structural basis of 30 end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH domain. Mol. Cell, 20, 473-481. (Pubitemid 41572303)
    • (2005) Molecular Cell , vol.20 , Issue.3 , pp. 473-481
    • Lorentzen, E.1    Conti, E.2
  • 49
    • 46649091980 scopus 로고    scopus 로고
    • Insights into the mechanism of progressive RNA degradation by the archaeal exosome
    • Navarro, M.V.A.S., Oliveira, C.C., Zanchin, N.I.T. and Guimara, B.G. (2008) Insights into the mechanism of progressive RNA degradation by the archaeal exosome. J. Biol. Chem., 283, 14120-14131.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14120-14131
    • Navarro, M.V.A.S.1    Oliveira, C.C.2    Zanchin, N.I.T.3    Guimara, B.G.4
  • 51
    • 0019558178 scopus 로고
    • Secondary structure of eukaryotic cytoplasmic 5S ribosomal RNA
    • Luehrsen, K.R. and Fox, G.E. (1981) Secondary structure of eukaryotic cytoplasmic 5S ribosomal RNA. Proc. Natl Acad. Sci. USA, 78, 2150-2154.
    • (1981) Proc. Natl Acad Sci. USA , vol.78 , pp. 2150-2154
    • Luehrsen, K.R.1    Fox, G.E.2
  • 52
    • 0027391688 scopus 로고
    • Secondary structure of RNase MRP RNA as predicted by phylogenetic comparison
    • Schmitt, M.E., Bennett, J.L., Dairaghi, D.J. and Clayton, D.A. (1993) Secondary structure of RNase MRP as predicted by phylogenetic comparison. FASEB J., 7, 208-213. (Pubitemid 23034036)
    • (1993) FASEB Journal , vol.7 , Issue.1 , pp. 208-213
    • Schmitt, M.E.1    Bennett, J.L.2    Dairaghi, D.J.3    Clayton, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.