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Volumn 7, Issue 10, 2012, Pages

Inhibition of Cell Division Induced by External Guide Sequences (EGS Technology) Targeting ftsZ

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; RIBONUCLEASE P; TRANSFER RNA;

EID: 84867869154     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0047690     Document Type: Article
Times cited : (13)

References (60)
  • 1
    • 21844441637 scopus 로고    scopus 로고
    • Diverse paths to midcell: assembly of the bacterial cell division machinery
    • Goehring NW, Beckwith J, (2005) Diverse paths to midcell: assembly of the bacterial cell division machinery. Curr Biol 15: R514-526.
    • (2005) Curr Biol , vol.15
    • Goehring, N.W.1    Beckwith, J.2
  • 2
    • 33745209434 scopus 로고    scopus 로고
    • The order of the ring: assembly of Escherichia coli cell division components
    • Vicente M, Rico AI, (2006) The order of the ring: assembly of Escherichia coli cell division components. Mol Microbiol 61: 5-8.
    • (2006) Mol Microbiol , vol.61 , pp. 5-8
    • Vicente, M.1    Rico, A.I.2
  • 4
    • 27644540151 scopus 로고    scopus 로고
    • FtsZ and the division of prokaryotic cells and organelles
    • Margolin W, (2005) FtsZ and the division of prokaryotic cells and organelles. Nat Rev Mol Cell Biol 6: 862-871.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 862-871
    • Margolin, W.1
  • 5
    • 34247859209 scopus 로고    scopus 로고
    • Interaction between cell division proteins FtsE and FtsZ
    • Corbin BD, Wang Y, Beuria TK, Margolin W, (2007) Interaction between cell division proteins FtsE and FtsZ. J Bacteriol 189: 3026-3035.
    • (2007) J Bacteriol , vol.189 , pp. 3026-3035
    • Corbin, B.D.1    Wang, Y.2    Beuria, T.K.3    Margolin, W.4
  • 7
    • 78649646536 scopus 로고    scopus 로고
    • Advances in understanding E. coli cell fission
    • de Boer PA, (2010) Advances in understanding E. coli cell fission. Curr Opin Microbiol 13: 730-737.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 730-737
    • de Boer, P.A.1
  • 9
    • 78650078263 scopus 로고    scopus 로고
    • FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one
    • Erickson HP, Anderson DE, Osawa M, (2010) FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one. Microbiol Mol Biol Rev 74: 504-528.
    • (2010) Microbiol Mol Biol Rev , vol.74 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 11
    • 0242582382 scopus 로고    scopus 로고
    • Discovery of a small molecule that inhibits cell division by blocking FtsZ, a novel therapeutic target of antibiotics
    • Wang J, Galgoci A, Kodali S, Herath KB, Jayasuriya H, et al. (2003) Discovery of a small molecule that inhibits cell division by blocking FtsZ, a novel therapeutic target of antibiotics. J Biol Chem 278: 44424-44428.
    • (2003) J Biol Chem , vol.278 , pp. 44424-44428
    • Wang, J.1    Galgoci, A.2    Kodali, S.3    Herath, K.B.4    Jayasuriya, H.5
  • 12
    • 67649479403 scopus 로고    scopus 로고
    • Concurrent growth rate and transcript analyses reveal essential gene stringency in Escherichia coli
    • Goh S, Boberek JM, Nakashima N, Stach J, Good L, (2009) Concurrent growth rate and transcript analyses reveal essential gene stringency in Escherichia coli. PLoS One 4: e6061.
    • (2009) PLoS One , vol.4
    • Goh, S.1    Boberek, J.M.2    Nakashima, N.3    Stach, J.4    Good, L.5
  • 13
    • 52249120794 scopus 로고    scopus 로고
    • An inhibitor of FtsZ with potent and selective anti-staphylococcal activity
    • Haydon DJ, Stokes NR, Ure R, Galbraith G, Bennett JM, et al. (2008) An inhibitor of FtsZ with potent and selective anti-staphylococcal activity. Science 321: 1673-1675.
    • (2008) Science , vol.321 , pp. 1673-1675
    • Haydon, D.J.1    Stokes, N.R.2    Ure, R.3    Galbraith, G.4    Bennett, J.M.5
  • 15
    • 80054829705 scopus 로고    scopus 로고
    • Antibiotic acyldepsipeptides activate ClpP peptidase to degrade the cell division protein FtsZ
    • Sass P, Josten M, Famulla K, Schiffer G, Sahl HG, et al. (2011) Antibiotic acyldepsipeptides activate ClpP peptidase to degrade the cell division protein FtsZ. Proc Natl Acad Sci U S A 108: 17474-17479.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 17474-17479
    • Sass, P.1    Josten, M.2    Famulla, K.3    Schiffer, G.4    Sahl, H.G.5
  • 16
    • 34147136107 scopus 로고    scopus 로고
    • Totarol inhibits bacterial cytokinesis by perturbing the assembly dynamics of FtsZ
    • Jaiswal R, Beuria TK, Mohan R, Mahajan SK, Panda D, (2007) Totarol inhibits bacterial cytokinesis by perturbing the assembly dynamics of FtsZ. Biochemistry 46: 4211-4220.
    • (2007) Biochemistry , vol.46 , pp. 4211-4220
    • Jaiswal, R.1    Beuria, T.K.2    Mohan, R.3    Mahajan, S.K.4    Panda, D.5
  • 17
    • 84857549874 scopus 로고    scopus 로고
    • Targeting the assembly of bacterial cell division protein FtsZ with small molecules
    • Schaffner-Barbero C, Martin-Fontecha M, Chacon P, Andreu JM, (2012) Targeting the assembly of bacterial cell division protein FtsZ with small molecules. ACS Chem Biol 7: 269-277.
    • (2012) ACS Chem Biol , vol.7 , pp. 269-277
    • Schaffner-Barbero, C.1    Martin-Fontecha, M.2    Chacon, P.3    Andreu, J.M.4
  • 18
    • 77952728317 scopus 로고    scopus 로고
    • Creating an antibacterial with in vivo efficacy: synthesis and characterization of potent inhibitors of the bacterial cell division protein FtsZ with improved pharmaceutical properties
    • Haydon DJ, Bennett JM, Brown D, Collins I, Galbraith G, et al. (2010) Creating an antibacterial with in vivo efficacy: synthesis and characterization of potent inhibitors of the bacterial cell division protein FtsZ with improved pharmaceutical properties. J Med Chem 53: 3927-3936.
    • (2010) J Med Chem , vol.53 , pp. 3927-3936
    • Haydon, D.J.1    Bennett, J.M.2    Brown, D.3    Collins, I.4    Galbraith, G.5
  • 20
    • 77952881006 scopus 로고    scopus 로고
    • Inhibition of gene expression by RNase P
    • Lundblad EW, Altman S, (2010) Inhibition of gene expression by RNase P. Nature Biotechnol. 27: 212-221.
    • (2010) Nature Biotechnol , vol.27 , pp. 212-221
    • Lundblad, E.W.1    Altman, S.2
  • 21
    • 0036510611 scopus 로고    scopus 로고
    • RNase P: variations and uses
    • Gopalan V, Vioque A, Altman S, (2002) RNase P: variations and uses. J Biol Chem 277: 6759-6762.
    • (2002) J Biol Chem , vol.277 , pp. 6759-6762
    • Gopalan, V.1    Vioque, A.2    Altman, S.3
  • 22
    • 56649123205 scopus 로고    scopus 로고
    • Inhibition of expression in Escherichia coli of a virulence regulator MglB of Francisella tularensis using external guide sequence technology
    • Xiao G, Lundblad EW, Izadjoo M, Altman S, (2008) Inhibition of expression in Escherichia coli of a virulence regulator MglB of Francisella tularensis using external guide sequence technology. PLoS One 3: e3719.
    • (2008) PLoS One , vol.3
    • Xiao, G.1    Lundblad, E.W.2    Izadjoo, M.3    Altman, S.4
  • 23
    • 47949087055 scopus 로고    scopus 로고
    • Inhibition of expression of virulence genes of Yersinia pestis in Escherichia coli by external guide sequences and RNase P
    • Ko JH, Izadjoo M, Altman S, (2008) Inhibition of expression of virulence genes of Yersinia pestis in Escherichia coli by external guide sequences and RNase P. RNA. 14: 1656-1662.
    • (2008) RNA , vol.14 , pp. 1656-1662
    • Ko, J.H.1    Izadjoo, M.2    Altman, S.3
  • 24
    • 1342285092 scopus 로고    scopus 로고
    • Disruption of type III secretion in Salmonella enterica serovar Typhimurium by external guide sequences
    • McKinney JS, Zhang H, Kubori T, Galan JE, Altman S, (2004) Disruption of type III secretion in Salmonella enterica serovar Typhimurium by external guide sequences. Nucleic Acids Res 32: 848-854.
    • (2004) Nucleic Acids Res , vol.32 , pp. 848-854
    • McKinney, J.S.1    Zhang, H.2    Kubori, T.3    Galan, J.E.4    Altman, S.5
  • 25
    • 0035810952 scopus 로고    scopus 로고
    • Inhibition of Escherichia coli viability by external guide sequences complementary to two essential genes
    • McKinney J, Guerrier-Takada C, Wesolowski D, Altman S, (2001) Inhibition of Escherichia coli viability by external guide sequences complementary to two essential genes. Proc Natl Acad Sci U S A 98: 6605-6610.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6605-6610
    • McKinney, J.1    Guerrier-Takada, C.2    Wesolowski, D.3    Altman, S.4
  • 26
    • 0030844329 scopus 로고    scopus 로고
    • Phenotypic conversion of drug-resistant bacteria to drug sensitivity
    • Guerrier-Takada C, Salavati R, Altman S, (1997) Phenotypic conversion of drug-resistant bacteria to drug sensitivity. Proc Natl Acad Sci U S A 94: 8468-8472.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8468-8472
    • Guerrier-Takada, C.1    Salavati, R.2    Altman, S.3
  • 27
    • 69449104409 scopus 로고    scopus 로고
    • Inhibition of aac(6′)-Ib-mediated amikacin resistance by nuclease-resistant external guide sequences in bacteria
    • Soler Bistue AJ, Martin FA, Vozza N, Ha H, Joaquin JC, et al. (2009) Inhibition of aac(6′)-Ib-mediated amikacin resistance by nuclease-resistant external guide sequences in bacteria. Proc Natl Acad Sci U S A 106: 13230-132235.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13230-132235
    • Soler Bistue, A.J.1    Martin, F.A.2    Vozza, N.3    Ha, H.4    Joaquin, J.C.5
  • 28
    • 34250222069 scopus 로고    scopus 로고
    • External guide sequences targeting the aac(6′)-Ib mRNA induce inhibition of amikacin resistance
    • Soler Bistue AJ, Ha H, Sarno R, Don M, Zorreguieta A, et al. (2007) External guide sequences targeting the aac(6′)-Ib mRNA induce inhibition of amikacin resistance. Antimicrob Agents Chemother 51: 1918-1925.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 1918-1925
    • Soler Bistue, A.J.1    Ha, H.2    Sarno, R.3    Don, M.4    Zorreguieta, A.5
  • 29
    • 66249131670 scopus 로고    scopus 로고
    • Inactivation of expression of several genes in a variety of bacterial species by EGS technology
    • Shen N, Ko JH, Xiao G, Wesolowski D, Shan G, et al. (2009) Inactivation of expression of several genes in a variety of bacterial species by EGS technology. Proc Natl Acad Sci U S A 106: 8163-8168.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8163-8168
    • Shen, N.1    Ko, J.H.2    Xiao, G.3    Wesolowski, D.4    Shan, G.5
  • 30
    • 0028856792 scopus 로고
    • Artificial regulation of gene expression in Escherichia coli by RNase P
    • Guerrier-Takada C, Li Y, Altman S, (1995) Artificial regulation of gene expression in Escherichia coli by RNase P. Proc Natl Acad Sci U S A. 92: 11115-11119.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 11115-11119
    • Guerrier-Takada, C.1    Li, Y.2    Altman, S.3
  • 33
    • 0141924827 scopus 로고    scopus 로고
    • Inhibition of aminoglycoside 6′-N-acetyltransferase type Ib-mediated amikacin resistance by antisense oligodeoxynucleotides
    • Sarno R, Ha H, Weinsetel N, Tolmasky ME, (2003) Inhibition of aminoglycoside 6′-N-acetyltransferase type Ib-mediated amikacin resistance by antisense oligodeoxynucleotides. Antimicrob Agents Chemother 47: 3296-3304.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 3296-3304
    • Sarno, R.1    Ha, H.2    Weinsetel, N.3    Tolmasky, M.E.4
  • 34
    • 0002287019 scopus 로고    scopus 로고
    • Algorithms and thermodynamics for RNA secondary structure prediction: A practical guide
    • Barciszewski J, Clark B, editors
    • Zuker M, Mathews DH, Turner DH (1999) Algorithms and thermodynamics for RNA secondary structure prediction: a practical guide. In: Barciszewski J, Clark B, editors. RNA biochemistry and Biotechnology: Kluwer Academic Publishers. 11-43.
    • (1999) RNA biochemistry and Biotechnology: Kluwer Academic Publishers , pp. 11-43
    • Zuker, M.1    Mathews, D.H.2    Turner, D.H.3
  • 35
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker M, (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 31: 3406-3415.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 36
    • 0026511121 scopus 로고
    • Targeted cleavage of mRNA in vitro by RNase P from Escherichia coli
    • Li Y, Guerrier-Takada C, Altman S, (1992) Targeted cleavage of mRNA in vitro by RNase P from Escherichia coli. Proc Natl Acad Sci U S A 89: 3185-3189.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 3185-3189
    • Li, Y.1    Guerrier-Takada, C.2    Altman, S.3
  • 37
    • 77956818245 scopus 로고
    • Molecular biology of bacterial septation
    • Ghuysen J, Hakenbeck R, editors, Amsterdam: Elsevier Science
    • Ayala J, Garrido T, de Pedro M, Vicente M (1994) Molecular biology of bacterial septation. In: Ghuysen J, Hakenbeck R, editors. Bacterial Cell Wall. Amsterdam: Elsevier Science. 73-101.
    • (1994) Bacterial Cell Wall , pp. 73-101
    • Ayala, J.1    Garrido, T.2    de Pedro, M.3    Vicente, M.4
  • 38
    • 0030805106 scopus 로고    scopus 로고
    • Contribution of individual promoters in the ddlB-ftsZ region to the transcription of the essential cell-division gene ftsZ in Escherichia coli
    • Flardh K, Garrido T, Vicente M, (1997) Contribution of individual promoters in the ddlB-ftsZ region to the transcription of the essential cell-division gene ftsZ in Escherichia coli. Molecular Microbiol 24: 927-936.
    • (1997) Molecular Microbiol , vol.24 , pp. 927-936
    • Flardh, K.1    Garrido, T.2    Vicente, M.3
  • 39
    • 0037315564 scopus 로고    scopus 로고
    • Global RNA half-life analysis in Escherichia coli reveals positional patterns of transcript degradation
    • Selinger DW, Saxena RM, Cheung KJ, Church GM, Rosenow C, (2003) Global RNA half-life analysis in Escherichia coli reveals positional patterns of transcript degradation. Genome research 13: 216-223.
    • (2003) Genome Research , vol.13 , pp. 216-223
    • Selinger, D.W.1    Saxena, R.M.2    Cheung, K.J.3    Church, G.M.4    Rosenow, C.5
  • 40
    • 0029744210 scopus 로고    scopus 로고
    • RNase E processing of essential cell division genes mRNA in Escherichia coli
    • Cam K, Rome G, Krisch HM, Bouche JP, (1996) RNase E processing of essential cell division genes mRNA in Escherichia coli. Nucleic Acids Res 24: 3065-3070.
    • (1996) Nucleic Acids Res , vol.24 , pp. 3065-3070
    • Cam, K.1    Rome, G.2    Krisch, H.M.3    Bouche, J.P.4
  • 41
    • 21144450388 scopus 로고    scopus 로고
    • Transcriptional analysis of the conserved ftsZ gene cluster in Mycoplasma genitalium and Mycoplasma pneumoniae
    • Benders GA, Powell BC, Hutchison CA, 3rd (2005) Transcriptional analysis of the conserved ftsZ gene cluster in Mycoplasma genitalium and Mycoplasma pneumoniae. J Bacteriol 187: 4542-4551.
    • (2005) J Bacteriol , vol.187 , pp. 4542-4551
    • Benders, G.A.1    Powell, B.C.2    Hutchison 3rd, C.A.3
  • 42
    • 0019476056 scopus 로고
    • Inactivation of the ribonucleic acid-processing enzyme ribonuclease E blocks cell division
    • Goldblum K, Apririon D, (1981) Inactivation of the ribonucleic acid-processing enzyme ribonuclease E blocks cell division. J Bacteriol 146: 128-132.
    • (1981) J Bacteriol , vol.146 , pp. 128-132
    • Goldblum, K.1    Apririon, D.2
  • 43
    • 0035117389 scopus 로고    scopus 로고
    • Transcription of the Escherichia coli dcw cluster: evidence for distal upstream transcripts being involved in the expression of the downstream ftsZ gene
    • de la Fuente A, Palacios P, Vicente M, (2001) Transcription of the Escherichia coli dcw cluster: evidence for distal upstream transcripts being involved in the expression of the downstream ftsZ gene. Biochimie 83: 109-115.
    • (2001) Biochimie , vol.83 , pp. 109-115
    • de la Fuente, A.1    Palacios, P.2    Vicente, M.3
  • 44
    • 33745885282 scopus 로고    scopus 로고
    • RNase E maintenance of proper FtsZ/FtsA ratio required for nonfilamentous growth of Escherichia coli cells but not for colony-forming ability
    • Tamura M, Lee K, Miller CA, Moore CJ, Shirako Y, et al. (2006) RNase E maintenance of proper FtsZ/FtsA ratio required for nonfilamentous growth of Escherichia coli cells but not for colony-forming ability. J Bacteriol 188: 5145-5152.
    • (2006) J Bacteriol , vol.188 , pp. 5145-5152
    • Tamura, M.1    Lee, K.2    Miller, C.A.3    Moore, C.J.4    Shirako, Y.5
  • 45
    • 77950255824 scopus 로고    scopus 로고
    • The 10×′20 Initiative: pursuing a global commitment to develop 10 new antibacterial drugs by 2020
    • Infectious Diseases Society of America
    • Infectious Diseases Society of America (2010) The 10×′20 Initiative: pursuing a global commitment to develop 10 new antibacterial drugs by 2020. Clin Infect Dis 50: 1081-1083.
    • (2010) Clin Infect Dis , vol.50 , pp. 1081-1083
  • 46
    • 78449256152 scopus 로고    scopus 로고
    • Progress and challenges in implementing the research on ESKAPE pathogens
    • Rice LB, (2010) Progress and challenges in implementing the research on ESKAPE pathogens. Infect Control Hospital Epidemiol 31Suppl 1: S7-10.
    • (2010) Infect Control Hospital Epidemiol , vol.31 , pp. 7-10
    • Rice, L.B.1
  • 47
    • 78149434123 scopus 로고    scopus 로고
    • Genetic evidence for inhibition of bacterial division protein FtsZ by berberine
    • Boberek JM, Stach J, Good L, (2010) Genetic evidence for inhibition of bacterial division protein FtsZ by berberine. PLoS One 5: e13745.
    • (2010) PLoS One , vol.5
    • Boberek, J.M.1    Stach, J.2    Good, L.3
  • 48
    • 57749110369 scopus 로고    scopus 로고
    • Antibacterial alkoxybenzamide inhibitors of the essential bacterial cell division protein FtsZ
    • Czaplewski LG, Collins I, Boyd EA, Brown D, East SP, et al. (2009) Antibacterial alkoxybenzamide inhibitors of the essential bacterial cell division protein FtsZ. Bioorg Med Chem Lett 19: 524-527.
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 524-527
    • Czaplewski, L.G.1    Collins, I.2    Boyd, E.A.3    Brown, D.4    East, S.P.5
  • 49
    • 67649997319 scopus 로고    scopus 로고
    • Novel anion liposome-encapsulated antisense oligonucleotide restores susceptibility of methicillin-resistant Staphylococcus aureus and rescues mice from lethal sepsis by targeting mecA
    • Meng J, Wang H, Hou Z, Chen T, Fu J, et al. (2009) Novel anion liposome-encapsulated antisense oligonucleotide restores susceptibility of methicillin-resistant Staphylococcus aureus and rescues mice from lethal sepsis by targeting mecA. Antimicrob Agents Chemother 53: 2871-2878.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 2871-2878
    • Meng, J.1    Wang, H.2    Hou, Z.3    Chen, T.4    Fu, J.5
  • 50
    • 77950345190 scopus 로고    scopus 로고
    • Cationic phosphorodiamidate morpholino oligomers efficiently prevent growth of Escherichia coli in vitro and in vivo
    • Mellbye BL, Weller DD, Hassinger JN, Reeves MD, Lovejoy CE, et al. (2010) Cationic phosphorodiamidate morpholino oligomers efficiently prevent growth of Escherichia coli in vitro and in vivo. J Antimicrob Chemother 65: 98-106.
    • (2010) J Antimicrob Chemother , vol.65 , pp. 98-106
    • Mellbye, B.L.1    Weller, D.D.2    Hassinger, J.N.3    Reeves, M.D.4    Lovejoy, C.E.5
  • 51
    • 0036510769 scopus 로고    scopus 로고
    • Cell permeabilization and uptake of antisense peptide-peptide nucleic acid (PNA) into Escherichia coli
    • Eriksson M, Nielsen PE, Good L, (2002) Cell permeabilization and uptake of antisense peptide-peptide nucleic acid (PNA) into Escherichia coli. J Biol Chem 277: 7144-7147.
    • (2002) J Biol Chem , vol.277 , pp. 7144-7147
    • Eriksson, M.1    Nielsen, P.E.2    Good, L.3
  • 53
    • 75649138331 scopus 로고    scopus 로고
    • Efficient gene silencing by delivery of locked nucleic acid antisense oligonucleotides, unassisted by transfection reagents
    • Stein CA, Hansen JB, Lai J, Wu S, Voskresenskiy A, et al. (2010) Efficient gene silencing by delivery of locked nucleic acid antisense oligonucleotides, unassisted by transfection reagents. Nucleic Acids Res 38: e3.
    • (2010) Nucleic Acids Res , vol.38
    • Stein, C.A.1    Hansen, J.B.2    Lai, J.3    Wu, S.4    Voskresenskiy, A.5
  • 54
    • 82455208055 scopus 로고    scopus 로고
    • Potent and sustained cellular inhibition of miR-122 by lysine-derivatized peptide nucleic acids (PNA) and phosphorothioate locked nucleic acid (LNA)/2′-O-methyl (OMe) mixmer anti-miRs in the absence of transfection agents
    • Torres AG, Threlfall RN, Gait MJ, (2011) Potent and sustained cellular inhibition of miR-122 by lysine-derivatized peptide nucleic acids (PNA) and phosphorothioate locked nucleic acid (LNA)/2′-O-methyl (OMe) mixmer anti-miRs in the absence of transfection agents. Artif DNA PNA XNA 2: 71-78.
    • (2011) Artif DNA PNA XNA , vol.2 , pp. 71-78
    • Torres, A.G.1    Threlfall, R.N.2    Gait, M.J.3
  • 55
    • 70849111210 scopus 로고    scopus 로고
    • Delivery of nucleic acids with a stearylated (RxR)4 peptide using a non-covalent co-incubation strategy
    • Lehto T, Abes R, Oskolkov N, Suhorutsenko J, Copolovici DM, et al. (2010) Delivery of nucleic acids with a stearylated (RxR)4 peptide using a non-covalent co-incubation strategy. J Control Release 141: 42-51.
    • (2010) J Control Release , vol.141 , pp. 42-51
    • Lehto, T.1    Abes, R.2    Oskolkov, N.3    Suhorutsenko, J.4    Copolovici, D.M.5
  • 56
    • 61349197462 scopus 로고    scopus 로고
    • A stearylated CPP for delivery of splice correcting oligonucleotides using a non-covalent co-incubation strategy
    • Mae M, El Andaloussi S, Lundin P, Oskolkov N, Johansson HJ, et al. (2009) A stearylated CPP for delivery of splice correcting oligonucleotides using a non-covalent co-incubation strategy. J Control Release 134: 221-227.
    • (2009) J Control Release , vol.134 , pp. 221-227
    • Mae, M.1    El Andaloussi, S.2    Lundin, P.3    Oskolkov, N.4    Johansson, H.J.5
  • 57
    • 77955051682 scopus 로고    scopus 로고
    • Design of a dual-ligand system using a specific ligand and cell penetrating peptide, resulting in a synergistic effect on selectivity and cellular uptake
    • Takara K, Hatakeyama H, Ohga N, Hida K, Harashima H, (2010) Design of a dual-ligand system using a specific ligand and cell penetrating peptide, resulting in a synergistic effect on selectivity and cellular uptake. Int J Pharm 396: 143-148.
    • (2010) Int J Pharm , vol.396 , pp. 143-148
    • Takara, K.1    Hatakeyama, H.2    Ohga, N.3    Hida, K.4    Harashima, H.5
  • 58
    • 84856077925 scopus 로고    scopus 로고
    • Influence of stearyl and trifluoromethylquinoline modifications of the cell penetrating peptide TP10 on its interaction with a lipid membrane
    • Anko M, Majhenc J, Kogej K, Sillard R, Langel U, et al. (2012) Influence of stearyl and trifluoromethylquinoline modifications of the cell penetrating peptide TP10 on its interaction with a lipid membrane. Biochim Biophys Acta 1818: 915-924.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 915-924
    • Anko, M.1    Majhenc, J.2    Kogej, K.3    Sillard, R.4    Langel, U.5
  • 59
    • 77949890248 scopus 로고    scopus 로고
    • Cell penetrating peptides: overview and applications to the delivery of oligonucleotides
    • Said Hassane F, Saleh AF, Abes R, Gait MJ, Lebleu B, (2010) Cell penetrating peptides: overview and applications to the delivery of oligonucleotides. Cell Mol Life Sci 67: 715-726.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 715-726
    • Said Hassane, F.1    Saleh, A.F.2    Abes, R.3    Gait, M.J.4    Lebleu, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.