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Volumn 19, Issue 9, 2008, Pages 1896-1906

Bacterial RNase P RNA is a drug target for aminoglycoside-arginine conjugates

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; ARGININE; BINDING ENERGY; PROTEINS;

EID: 52249097419     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc800191u     Document Type: Article
Times cited : (11)

References (64)
  • 1
    • 0032779273 scopus 로고    scopus 로고
    • RNA as a small-molecule drug target: Doubling the value of genomics
    • Ecker, D. J., and Griffey, J. (1999) RNA as a small-molecule drug target: doubling the value of genomics. Drug Discovery Today 4, 420-429.
    • (1999) Drug Discovery Today , vol.4 , pp. 420-429
    • Ecker, D.J.1    Griffey, J.2
  • 2
    • 0034783659 scopus 로고    scopus 로고
    • Targeting RNA with small-molecule drugs: Therapeutic promise and chemical challenges
    • Gallego, J., and Varani, G. (2001) Targeting RNA with small-molecule drugs: Therapeutic promise and chemical challenges. Acc. Chem. Res. 34, 836-843.
    • (2001) Acc. Chem. Res , vol.34 , pp. 836-843
    • Gallego, J.1    Varani, G.2
  • 3
    • 0041836268 scopus 로고    scopus 로고
    • Chemical and functional diversity of small molecule ligands for RNA
    • Hermann, T. (2003) Chemical and functional diversity of small molecule ligands for RNA. Biopolymers 70, 4-18.
    • (2003) Biopolymers , vol.70 , pp. 4-18
    • Hermann, T.1
  • 4
    • 0003120548 scopus 로고    scopus 로고
    • Ribonuclease P
    • Gesteland, R. F, Cech, T, and Atkins, J. F, Eds, pp, CSH Laboratory Press, Cold Spring Harbor, NY
    • Altman, S., and Kirsebom, L. (1999) Ribonuclease P, in The RNA World (Gesteland, R. F., Cech, T., and Atkins, J. F., Eds.), pp 351-380, CSH Laboratory Press, Cold Spring Harbor, NY.
    • (1999) The RNA World , pp. 351-380
    • Altman, S.1    Kirsebom, L.2
  • 5
    • 33645747326 scopus 로고    scopus 로고
    • Ribonuclease P; the evolution of an ancient RNA enzyme
    • Walker, S. C., and Engelke, D. R. (2006) Ribonuclease P; the evolution of an ancient RNA enzyme. Crit. Rev. Biochem. Mol. Biol. 41, 77-102.
    • (2006) Crit. Rev. Biochem. Mol. Biol , vol.41 , pp. 77-102
    • Walker, S.C.1    Engelke, D.R.2
  • 6
    • 0034814681 scopus 로고    scopus 로고
    • The ribonuclease P family
    • Hall, T. A., and Brown, J. W. (2001) The ribonuclease P family. Methods Enzymol. 341, 56-77.
    • (2001) Methods Enzymol , vol.341 , pp. 56-77
    • Hall, T.A.1    Brown, J.W.2
  • 9
    • 33645747326 scopus 로고    scopus 로고
    • Ribonuclease P; the evolution of an ancient RNA enzyme
    • Walker, S. C., and Engelke, D. R. (2006) Ribonuclease P; the evolution of an ancient RNA enzyme. Crit. Rev. Biochem. Mol. Biol. 41, 77-102.
    • (2006) Crit. Rev. Biochem. Mol. Biol , vol.41 , pp. 77-102
    • Walker, S.C.1    Engelke, D.R.2
  • 10
    • 39149107446 scopus 로고    scopus 로고
    • Studies on the mechanism of inhibition of bacterial ribonuclease P by aminoglycoside derivatives
    • Kawamoto, S. A., Sudhahar, C. G., Hatfield, C. L., Sun, J., Behrman, E. J., and Gopalan, V. (2008) Studies on the mechanism of inhibition of bacterial ribonuclease P by aminoglycoside derivatives. Nucleic Acids Res. 36, 697-704.
    • (2008) Nucleic Acids Res , vol.36 , pp. 697-704
    • Kawamoto, S.A.1    Sudhahar, C.G.2    Hatfield, C.L.3    Sun, J.4    Behrman, E.J.5    Gopalan, V.6
  • 11
    • 0021013526 scopus 로고
    • The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
    • Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N. R., and Altman, S. (1983) The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell 35, 849-857.
    • (1983) Cell , vol.35 , pp. 849-857
    • Guerrier-Takada, C.1    Gardiner, K.2    Marsh, T.3    Pace, N.R.4    Altman, S.5
  • 12
    • 0347763706 scopus 로고    scopus 로고
    • Roles of protein subunits in RNA-protein complexes: Lessons from ribonuclease P
    • Hsieh, J., Andrews, A. J., and Fierke, C. A. (2004) Roles of protein subunits in RNA-protein complexes: Lessons from ribonuclease P. Biopolymers 73, 79-89.
    • (2004) Biopolymers , vol.73 , pp. 79-89
    • Hsieh, J.1    Andrews, A.J.2    Fierke, C.A.3
  • 13
    • 0032076249 scopus 로고    scopus 로고
    • Ribonuclease P protein structure: Evolutionary origins in the translational apparatus
    • Stams, T., Niranjanakumari, S., Fierke, C. A., and Christianson, D. W. (1998) Ribonuclease P protein structure: Evolutionary origins in the translational apparatus. Science 280, 752-755.
    • (1998) Science , vol.280 , pp. 752-755
    • Stams, T.1    Niranjanakumari, S.2    Fierke, C.A.3    Christianson, D.W.4
  • 15
    • 0037199416 scopus 로고    scopus 로고
    • The affinity of magnesium binding sites in the Bacillus subtilis RNase Pxpre-tRNA complex is enhanced by the protein subunit
    • Kurz, J. C., and Fierke, C. A. (2002) The affinity of magnesium binding sites in the Bacillus subtilis RNase Pxpre-tRNA complex is enhanced by the protein subunit. Biochemistry 41, 9545-9558.
    • (2002) Biochemistry , vol.41 , pp. 9545-9558
    • Kurz, J.C.1    Fierke, C.A.2
  • 16
    • 33748361597 scopus 로고    scopus 로고
    • Evidence that substrate-specific effects of C5 protein lead to uniformity in binding and catalysis by RNase P
    • Sun, L., Campbell, F. E., Zahler, N. H., and Harris, M. E. (2006) Evidence that substrate-specific effects of C5 protein lead to uniformity in binding and catalysis by RNase P. EMBO J. 25, 3998-4007.
    • (2006) EMBO J , vol.25 , pp. 3998-4007
    • Sun, L.1    Campbell, F.E.2    Zahler, N.H.3    Harris, M.E.4
  • 18
    • 0034614360 scopus 로고    scopus 로고
    • The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA
    • Spitzfaden, C., Nicholson, N., Jones, J. J., Guth, S., Lehr, R., Prescott, C. D., Hegg, L. A., and Eggleston, D. S. (2000) The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA. J. Mol. Biol. 295, 105-115.
    • (2000) J. Mol. Biol , vol.295 , pp. 105-115
    • Spitzfaden, C.1    Nicholson, N.2    Jones, J.J.3    Guth, S.4    Lehr, R.5    Prescott, C.D.6    Hegg, L.A.7    Eggleston, D.S.8
  • 19
    • 0024529973 scopus 로고
    • Ribonuclease P: An enzyme with a catalytic RNA subunit
    • Altman, S. (1989) Ribonuclease P: An enzyme with a catalytic RNA subunit. Adv. Enzymol. Relat. Areas Mol. Biol. 62, 1-36.
    • (1989) Adv. Enzymol. Relat. Areas Mol. Biol , vol.62 , pp. 1-36
    • Altman, S.1
  • 20
    • 0031564661 scopus 로고    scopus 로고
    • Analysis of the functional role of conserved residues in the protein subunit of ribonuclease P from Escherichia coli
    • Gopalan, V., Baxevanis, A. D., Landsman, D., and Altman, S. (1997) Analysis of the functional role of conserved residues in the protein subunit of ribonuclease P from Escherichia coli. J. Mol. Biol. 267, 818-829.
    • (1997) J. Mol. Biol , vol.267 , pp. 818-829
    • Gopalan, V.1    Baxevanis, A.D.2    Landsman, D.3    Altman, S.4
  • 21
    • 0036920388 scopus 로고    scopus 로고
    • Elucidation of structure-function relationships in the protein subunit of bacterial RNase P using a genetic complementation approach
    • Jovanovic, M., Sanchez, R., Altman, S., and Gopalan, V. (2002) Elucidation of structure-function relationships in the protein subunit of bacterial RNase P using a genetic complementation approach. Nucleic Acids Res. 30, 5065-5073.
    • (2002) Nucleic Acids Res , vol.30 , pp. 5065-5073
    • Jovanovic, M.1    Sanchez, R.2    Altman, S.3    Gopalan, V.4
  • 22
    • 34247606403 scopus 로고    scopus 로고
    • New insights into aminoglycoside antibiotics and derivatives
    • Silva, J. G., and Carvalho, I. (2007) New insights into aminoglycoside antibiotics and derivatives. Curr. Med. Chem. 14, 1101-1119.
    • (2007) Curr. Med. Chem , vol.14 , pp. 1101-1119
    • Silva, J.G.1    Carvalho, I.2
  • 23
    • 0033524495 scopus 로고    scopus 로고
    • Aminoglycoside antibiotics are able to specifically bind the 5′- untranslated region of thymidylate synthase messenger RNA
    • Tok, J. B., Cho, J., and Rando, R. R. (1999) Aminoglycoside antibiotics are able to specifically bind the 5′- untranslated region of thymidylate synthase messenger RNA. Biochemistry 38, 199-206.
    • (1999) Biochemistry , vol.38 , pp. 199-206
    • Tok, J.B.1    Cho, J.2    Rando, R.R.3
  • 24
    • 0035005249 scopus 로고    scopus 로고
    • Aminoglycoside binding displaces a divalent metal ion in a tRNA-neomycin B complex
    • Mikkelsen, N. E., Johansson, K., Virtanen, A., and Kirsebom, L. A. (2001) Aminoglycoside binding displaces a divalent metal ion in a tRNA-neomycin B complex. Nat. Struct. Biol. 8, 510-514.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 510-514
    • Mikkelsen, N.E.1    Johansson, K.2    Virtanen, A.3    Kirsebom, L.A.4
  • 25
    • 0025917063 scopus 로고
    • The number of positively charged amino acids in the basic domain of Tat is critical for trans-activation and complex formation with TAR RNA
    • Delling, U., Roy, S., Sumner-Smith, M., Barnett, R., Reid, L., Rosen, C. A., and Sonenberg, N. (1991) The number of positively charged amino acids in the basic domain of Tat is critical for trans-activation and complex formation with TAR RNA. Proc. Natl. Acad. Sci. U.S.A. 88, 6234-6238.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 6234-6238
    • Delling, U.1    Roy, S.2    Sumner-Smith, M.3    Barnett, R.4    Reid, L.5    Rosen, C.A.6    Sonenberg, N.7
  • 26
    • 0027370433 scopus 로고
    • Small molecules that selectively block RNA binding of HIV-1 Rev protein inhibit Rev function and viral production
    • Zapp, M. L., Stern, S., and Green, M. R. (1993) Small molecules that selectively block RNA binding of HIV-1 Rev protein inhibit Rev function and viral production. Cell 74, 969-978.
    • (1993) Cell , vol.74 , pp. 969-978
    • Zapp, M.L.1    Stern, S.2    Green, M.R.3
  • 27
    • 0032554635 scopus 로고    scopus 로고
    • Binding of neomycin to the TAR element of HIV-1 RNA induces dissociation of Tat protein by an allosteric mechanism
    • Wang, S., Huber, P. W., Cui, M., Czarnik, A. W., and Mei, H. Y. (1998) Binding of neomycin to the TAR element of HIV-1 RNA induces dissociation of Tat protein by an allosteric mechanism. Biochemistry 37, 5549-5557.
    • (1998) Biochemistry , vol.37 , pp. 5549-5557
    • Wang, S.1    Huber, P.W.2    Cui, M.3    Czarnik, A.W.4    Mei, H.Y.5
  • 30
    • 0033028501 scopus 로고    scopus 로고
    • Arginine-aminoglycoside conjugates that bind to HIV transactivation responsive element RNA in vitro
    • Litovchick, A., Evdokimov, A. G., and Lapidot, A. (1999) Arginine-aminoglycoside conjugates that bind to HIV transactivation responsive element RNA in vitro. FEBS Lett. 445, 73-79.
    • (1999) FEBS Lett , vol.445 , pp. 73-79
    • Litovchick, A.1    Evdokimov, A.G.2    Lapidot, A.3
  • 31
    • 0034696520 scopus 로고    scopus 로고
    • Aminoglycoside-arginine conjugates that bind TAR RNA: Synthesis, characterization, and antiviral activity
    • Litovchick, A., Evdokimov, A. G., and Lapidot, A. (2000) Aminoglycoside-arginine conjugates that bind TAR RNA: Synthesis, characterization, and antiviral activity. Biochemistry 39, 2838-2852.
    • (2000) Biochemistry , vol.39 , pp. 2838-2852
    • Litovchick, A.1    Evdokimov, A.G.2    Lapidot, A.3
  • 32
    • 0035951091 scopus 로고    scopus 로고
    • Neomycin B-arginine conjugate, a novel HIV-1 Tat antagonist: Synthesis and anti-HIV activities
    • Litovchick, A., Lapidot, A., Eisenstein, M., Kalinkovich, A., and Borkow, G. (2001) Neomycin B-arginine conjugate, a novel HIV-1 Tat antagonist: Synthesis and anti-HIV activities. Biochemistry 40, 15612-15623.
    • (2001) Biochemistry , vol.40 , pp. 15612-15623
    • Litovchick, A.1    Lapidot, A.2    Eisenstein, M.3    Kalinkovich, A.4    Borkow, G.5
  • 33
    • 0344201924 scopus 로고    scopus 로고
    • Structure-activity relationship of neomycin, paromomycin, and neamine-arginine conjugates, targeting HIV-1 gp120-CXCR4 binding step
    • Borkow, G., Vijayabaskar, V., Lara, H. H., Kalinkovich, A., and Lapidot, A. (2003) Structure-activity relationship of neomycin, paromomycin, and neamine-arginine conjugates, targeting HIV-1 gp120-CXCR4 binding step. Antiviral Res. 60, 181-192.
    • (2003) Antiviral Res , vol.60 , pp. 181-192
    • Borkow, G.1    Vijayabaskar, V.2    Lara, H.H.3    Kalinkovich, A.4    Lapidot, A.5
  • 34
    • 0344926359 scopus 로고    scopus 로고
    • Mutations in gp41 and gp120 of HIV-1 isolates resistant to hexa-arginine neomycin B conjugate
    • Borkow, G., Lara, H. H., and Lapidot, A. (2003) Mutations in gp41 and gp120 of HIV-1 isolates resistant to hexa-arginine neomycin B conjugate. Biochem. Biophys. Res. Commun. 312, 1047-1052.
    • (2003) Biochem. Biophys. Res. Commun , vol.312 , pp. 1047-1052
    • Borkow, G.1    Lara, H.H.2    Lapidot, A.3
  • 35
    • 8844276772 scopus 로고    scopus 로고
    • Structure-activity relationships of aminoglycoside-arginine conjugates that bind HIV-1 RNAs as determined by fluorescence and NMR spectroscopy
    • Lapidot, A., Vijayabaskar, V., Litovchick, A., Yu, J., and James, T. L. (2004) Structure-activity relationships of aminoglycoside-arginine conjugates that bind HIV-1 RNAs as determined by fluorescence and NMR spectroscopy. FEBS Lett. 577, 415-421.
    • (2004) FEBS Lett , vol.577 , pp. 415-421
    • Lapidot, A.1    Vijayabaskar, V.2    Litovchick, A.3    Yu, J.4    James, T.L.5
  • 38
    • 0025168740 scopus 로고
    • Fragments of the HIV-1 Tat protein specifically bind TAR RNA
    • Weeks, K. M., Ampe, C., Schultz, S. C., Steitz, T. A., and Crothers, D. M. (1990) Fragments of the HIV-1 Tat protein specifically bind TAR RNA. Science 249, 1281-1285.
    • (1990) Science , vol.249 , pp. 1281-1285
    • Weeks, K.M.1    Ampe, C.2    Schultz, S.C.3    Steitz, T.A.4    Crothers, D.M.5
  • 40
    • 34548475769 scopus 로고    scopus 로고
    • Prediction of HIV-1 entry inhibitors neomycin-arginine conjugates interaction with the CD4-gp120 binding site by molecular modeling and multistep docking procedure
    • Berchanski, A., and Lapidot, A. (2007) Prediction of HIV-1 entry inhibitors neomycin-arginine conjugates interaction with the CD4-gp120 binding site by molecular modeling and multistep docking procedure. BBA-Biomembranes 1768, 2107-2119.
    • (2007) BBA-Biomembranes , vol.1768 , pp. 2107-2119
    • Berchanski, A.1    Lapidot, A.2
  • 41
    • 36749022789 scopus 로고    scopus 로고
    • Structure-function relationship of novel X4 HIV-1 entry inhibitors: L- and D-arginine peptides-aminoglycoside conjugates
    • Hegde, R., Borkow, G., Berchanski, A., and Lapidot, A. (2007) Structure-function relationship of novel X4 HIV-1 entry inhibitors: L- and D-arginine peptides-aminoglycoside conjugates. FEBS J. 274, 6523-6536.
    • (2007) FEBS J , vol.274 , pp. 6523-6536
    • Hegde, R.1    Borkow, G.2    Berchanski, A.3    Lapidot, A.4
  • 42
    • 0032546728 scopus 로고    scopus 로고
    • Derivation of the three-dimensional architecture of bacterial ribonuclease P RNAs from comparative sequence analysis
    • Massire, C., Jaeger, L., and Westhof, E. (1998) Derivation of the three-dimensional architecture of bacterial ribonuclease P RNAs from comparative sequence analysis. J. Mol. Biol. 279, 773-793.
    • (1998) J. Mol. Biol , vol.279 , pp. 773-793
    • Massire, C.1    Jaeger, L.2    Westhof, E.3
  • 43
    • 0037462929 scopus 로고    scopus 로고
    • Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme
    • Tsai, H. Y., Masquida, B., Biswas, R., Westhof, E., and Gopalan, V. (2003) Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme. J. Mol. Biol. 325, 661-675.
    • (2003) J. Mol. Biol , vol.325 , pp. 661-675
    • Tsai, H.Y.1    Masquida, B.2    Biswas, R.3    Westhof, E.4    Gopalan, V.5
  • 44
    • 34547892624 scopus 로고    scopus 로고
    • A view of RNase P
    • Altman, S. (2007) A view of RNase P. Mol. BioSyst. 3, 604-607.
    • (2007) Mol. BioSyst , vol.3 , pp. 604-607
    • Altman, S.1
  • 46
  • 47
    • 33947716757 scopus 로고    scopus 로고
    • Niranjanakumari, S., Day-Storms, J. J., Ahmed, M., Hsieh, J., Zahler, N. H., Venters, R. A., and Fierke, C. A. (2007) Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage. RNA 13, 521-535.
    • Niranjanakumari, S., Day-Storms, J. J., Ahmed, M., Hsieh, J., Zahler, N. H., Venters, R. A., and Fierke, C. A. (2007) Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage. RNA 13, 521-535.
  • 48
    • 8844263008 scopus 로고    scopus 로고
    • Docking and scoring in virtual screening for drug discovery: Methods and applications
    • Kitchen, D. B., Decornez, H., and Bajorath, J. (2004) Docking and scoring in virtual screening for drug discovery: methods and applications. Nature Rev. 3, 935-949.
    • (2004) Nature Rev , vol.3 , pp. 935-949
    • Kitchen, D.B.1    Decornez, H.2    Bajorath, J.3
  • 49
    • 0034617166 scopus 로고    scopus 로고
    • Faber, C., Sticht, H., Schweimer, K., and Rosch, P. (2000) Structural rearrangements of HIV-1 Tat-responsive RNA upon binding of neomycin B. J. Biol. Chem. 275, 20660-20666.
    • Faber, C., Sticht, H., Schweimer, K., and Rosch, P. (2000) Structural rearrangements of HIV-1 Tat-responsive RNA upon binding of neomycin B. J. Biol. Chem. 275, 20660-20666.
  • 50
    • 2642518000 scopus 로고    scopus 로고
    • Hydrophobic complementarity in protein-protein docking
    • Berchanski, A., Shapira, B., and Eisenstein, M. (2004) Hydrophobic complementarity in protein-protein docking. Proteins 56, 130-142.
    • (2004) Proteins , vol.56 , pp. 130-142
    • Berchanski, A.1    Shapira, B.2    Eisenstein, M.3
  • 52
    • 11844256433 scopus 로고    scopus 로고
    • The Pre-tRNA Nucleotide Base and 2′-Hydroxyl at N(-1) Contribute to Fidelity in tRNA Processing by RNase P
    • Zahler, N. H., Sun, L., Christian, E. L., and Harris, M. E. (2005) The Pre-tRNA Nucleotide Base and 2′-Hydroxyl at N(-1) Contribute to Fidelity in tRNA Processing by RNase P. J. Mol. Bio.l 345, 969-985.
    • (2005) J. Mol. Bio.l , vol.345 , pp. 969-985
    • Zahler, N.H.1    Sun, L.2    Christian, E.L.3    Harris, M.E.4
  • 53
    • 0029556990 scopus 로고
    • Probing of tertiary interactions in RNA: 2′-Hydroxyl-base contacts between the RNase P RNA and pre-tRNA
    • Pan, T., Loria, A., and Zhong, K. (1995) Probing of tertiary interactions in RNA: 2′-Hydroxyl-base contacts between the RNase P RNA and pre-tRNA. Proc. Natl. Acad. Sci. U.S.A. 92, 12510-12514.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 12510-12514
    • Pan, T.1    Loria, A.2    Zhong, K.3
  • 54
    • 33746538312 scopus 로고    scopus 로고
    • The P4 metal binding site in RNase P RNA affects active site metal affinity through substrate positioning
    • Christian, E. L., Smith, K. M., Perera, N., and Harris, M. E. (2006) The P4 metal binding site in RNase P RNA affects active site metal affinity through substrate positioning. RNA 12, 1463-1467.
    • (2006) RNA 12 , pp. 1463-1467
    • Christian, E.L.1    Smith, K.M.2    Perera, N.3    Harris, M.E.4
  • 55
    • 0037046152 scopus 로고    scopus 로고
    • NAIM and site-specific functional group modification analysis of RNase P RNA: Magnesium dependent structure within the conserved P1-P4 multihelix junction contributes to catalysis
    • Kaye, N. M., Christian, E. L., and Harris, M. E. (2002) NAIM and site-specific functional group modification analysis of RNase P RNA: magnesium dependent structure within the conserved P1-P4 multihelix junction contributes to catalysis. Biochemistry 41, 4533-4545.
    • (2002) Biochemistry , vol.41 , pp. 4533-4545
    • Kaye, N.M.1    Christian, E.L.2    Harris, M.E.3
  • 56
    • 33846443976 scopus 로고    scopus 로고
    • Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation
    • Getz, M. M., Andrews, A. J., Fierke, C. A., and Al-Hashimi, H. M. (2007) Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation. RNA 13, 251-266.
    • (2007) RNA 13 , pp. 251-266
    • Getz, M.M.1    Andrews, A.J.2    Fierke, C.A.3    Al-Hashimi, H.M.4
  • 57
    • 27144527101 scopus 로고    scopus 로고
    • Protein activation of a ribozyme: The role of bacterial RNase P protein
    • Buck, A. H., Dalby, A. B., Poole, A. W., Kazantsev, A. V., and Pace, N. R. (2005) Protein activation of a ribozyme: the role of bacterial RNase P protein. EMBO J. 24, 3360-3368.
    • (2005) EMBO J , vol.24 , pp. 3360-3368
    • Buck, A.H.1    Dalby, A.B.2    Poole, A.W.3    Kazantsev, A.V.4    Pace, N.R.5
  • 58
    • 34848863932 scopus 로고    scopus 로고
    • RNase P RNA mediated cleavage: Substrate recognition and catalysis
    • Kirsebom, L. A. (2007) RNase P RNA mediated cleavage: substrate recognition and catalysis. Biochimie 89, 1183-1194.
    • (2007) Biochimie , vol.89 , pp. 1183-1194
    • Kirsebom, L.A.1
  • 59
    • 0031849761 scopus 로고    scopus 로고
    • The P15-loop of Escherichia coli RNase P RNA is an autonomous divalent metal ion binding domain
    • Kufel, J., and Kirsebom, L. A. (1998) The P15-loop of Escherichia coli RNase P RNA is an autonomous divalent metal ion binding domain. RNA 4, 777-788.
    • (1998) RNA , vol.4 , pp. 777-788
    • Kufel, J.1    Kirsebom, L.A.2
  • 60
    • 28944452277 scopus 로고    scopus 로고
    • The 5′ leader of precursor tRNAAsp bound to the Bacillus subtilis RNase P holoenzyme has an extended conformation
    • Rueda, D., Hsieh, J., Day-Storms, J. J., Fierke, C. A., and Walter, N. G. (2005) The 5′ leader of precursor tRNAAsp bound to the Bacillus subtilis RNase P holoenzyme has an extended conformation. Biochemistry 44, 16130-16139.
    • (2005) Biochemistry , vol.44 , pp. 16130-16139
    • Rueda, D.1    Hsieh, J.2    Day-Storms, J.J.3    Fierke, C.A.4    Walter, N.G.5
  • 62
    • 0034731571 scopus 로고    scopus 로고
    • Synthesis and anti-HIV activity of guanidinoglycosides
    • Baker, T. J., Luedtke, N. W., Tor, Y., and Goodman, M. (2000) Synthesis and anti-HIV activity of guanidinoglycosides. J. Org. Chem. 65, 9054-9058.
    • (2000) J. Org. Chem , vol.65 , pp. 9054-9058
    • Baker, T.J.1    Luedtke, N.W.2    Tor, Y.3    Goodman, M.4
  • 63
    • 0031051477 scopus 로고    scopus 로고
    • Specificity of aminoglycoside-binding to RNA constructs derived from the 16S rRNA decoding region and the HIV-RRE activator region
    • Wang, Y., Hamasaki, K., and Rando, R. R. (1997) Specificity of aminoglycoside-binding to RNA constructs derived from the 16S rRNA decoding region and the HIV-RRE activator region. Biochemistry 36, 768-779.
    • (1997) Biochemistry , vol.36 , pp. 768-779
    • Wang, Y.1    Hamasaki, K.2    Rando, R.R.3
  • 64
    • 52249103351 scopus 로고    scopus 로고
    • Amino-Modified Polysaccharides and Methods of Generating and Using Same,
    • US Patent 10/831,224[PCT 2003027-00-01
    • Lapidot, A., Vijayabaskar, V and Borkow, G. (2004) Amino-Modified Polysaccharides and Methods of Generating and Using Same, US Patent 10/831,224[PCT 2003027-00-01].
    • (2004)
    • Lapidot, A.1    Vijayabaskar, V.2    Borkow, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.