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Volumn 19, Issue 16, 2013, Pages 2869-2877

Everything you always wanted to know about CADY-mediated siRNA delivery* (* But afraid to ask)

Author keywords

CADY; Cell penetrating peptide; Direct translocation; Non covalent delivery; SiRNA

Indexed keywords

CADY PEPTIDE; CELL PENETRATING PEPTIDE; MEMBRANE PHOSPHOLIPID; NANOPARTICLE; PEPTIDE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 84878631538     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/1381612811319160004     Document Type: Review
Times cited : (19)

References (71)
  • 1
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    • Fire A, Xu S, Montgomery MK, Kostas SA, Driver SE, Mello CC. Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature 1998; 391: 806-11.
    • (1998) Nature , vol.391 , pp. 806-811
    • Fire, A.1    Xu, S.2    Montgomery, M.K.3    Kostas, S.A.4    Driver, S.E.5    Mello, C.C.6
  • 2
    • 3242677639 scopus 로고    scopus 로고
    • siRNAs: Applications in functional genomics and potential as therapeutics
    • Dorsett Y, Tuschl T. siRNAs: applications in functional genomics and potential as therapeutics. Nat Rev Drug Discov 2004; 3: 318-29.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 318-329
    • Dorsett, Y.1    Tuschl, T.2
  • 3
    • 84856389509 scopus 로고    scopus 로고
    • RNA-based therapeutics: Current progress and future prospects
    • Burnett JC, Rossi JJ. RNA-based therapeutics: current progress and future prospects. Chem Biol 2012; 19: 60-71.
    • (2012) Chem Biol , vol.19 , pp. 60-71
    • Burnett, J.C.1    Rossi, J.J.2
  • 5
    • 58749104364 scopus 로고    scopus 로고
    • The promises and pitfalls of RNAinterference-based therapeutics
    • Castanotto D, Rossi JJ. The promises and pitfalls of RNAinterference-based therapeutics. Nature 2009; 457: 426-33.
    • (2009) Nature , vol.457 , pp. 426-433
    • Castanotto, D.1    Rossi, J.J.2
  • 7
    • 77649275761 scopus 로고    scopus 로고
    • Novel RNA-based strategies for therapeutic gene silencing
    • Sibley CR, Seow Y, Wood MJ. Novel RNA-based strategies for therapeutic gene silencing. Mol Ther 2010; 18: 466-76.
    • (2010) Mol Ther , vol.18 , pp. 466-476
    • Sibley, C.R.1    Seow, Y.2    Wood, M.J.3
  • 8
    • 84855876918 scopus 로고    scopus 로고
    • Non-viral vectors for the mediation of RNAi
    • Zhang S, Zhao Y, Zhi D, Zhang S. Non-viral vectors for the mediation of RNAi. Bioorg Chem 2012; 40: 10-8.
    • (2012) Bioorg Chem , vol.40 , pp. 10-18
    • Zhang, S.1    Zhao, Y.2    Zhi, D.3    Zhang, S.4
  • 10
    • 79955592687 scopus 로고    scopus 로고
    • Can non-viral technologies knockdown the barriers to siRNA delivery and achieve the next generation of cancer therapeutics?
    • Guo J, Bourre L, Soden DM, O'Sullivan GC, O'Driscoll C. Can non-viral technologies knockdown the barriers to siRNA delivery and achieve the next generation of cancer therapeutics? Biotechnol Adv 2011; 29: 402-17.
    • (2011) Biotechnol Adv , vol.29 , pp. 402-417
    • Guo, J.1    Bourre, L.2    Soden, D.M.3    O'Sullivan, G.C.4    O'Driscoll, C.5
  • 11
    • 67249096677 scopus 로고    scopus 로고
    • Nonviral methods for siRNA delivery
    • Gao K, Huang L. Nonviral methods for siRNA delivery. Mol Pharm 2009; 6: 651-8.
    • (2009) Mol Pharm , vol.6 , pp. 651-658
    • Gao, K.1    Huang, L.2
  • 12
    • 47249138782 scopus 로고    scopus 로고
    • Mechanisms and strategies for effective delivery of antisense and siRNA oligonucleotides
    • Juliano R, Alam MR, Dixit V, Kang H. Mechanisms and strategies for effective delivery of antisense and siRNA oligonucleotides. Nucleic Acids Res 2008; 36: 4158-71.
    • (2008) Nucleic Acids Res , vol.36 , pp. 4158-4171
    • Juliano, R.1    Alam, M.R.2    Dixit, V.3    Kang, H.4
  • 13
    • 67649408951 scopus 로고    scopus 로고
    • siRNA delivery using peptide transduction domains
    • Eguchi A, Dowdy SF. siRNA delivery using peptide transduction domains. Trends Pharmacol Sci 2009; 30: 341-5.
    • (2009) Trends Pharmacol Sci , vol.30 , pp. 341-345
    • Eguchi, A.1    Dowdy, S.F.2
  • 14
    • 77958153239 scopus 로고    scopus 로고
    • In vivo biodistribution and efficacy of peptide mediated delivery
    • Järver P, Mäger I, Langel Ü. In vivo biodistribution and efficacy of peptide mediated delivery. Trends Pharmacol Sci 2010; 31: 528-35.
    • (2010) Trends Pharmacol Sci , vol.31 , pp. 528-535
    • Järver, P.1    Mäger, I.2    Langel, U.3
  • 15
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cell-penetrating peptides: From molecular mechanisms to therapeutics
    • Heitz F, Morris MC, Divita G. Twenty years of cell-penetrating peptides: from molecular mechanisms to therapeutics. Br J Pharmacol 2009; 157: 195-206.
    • (2009) Br J Pharmacol , vol.157 , pp. 195-206
    • Heitz, F.1    Morris, M.C.2    Divita, G.3
  • 16
    • 13844254266 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Mechanism and kinetics of cargo delivery
    • Zorko M, Langel Ü. Cell-penetrating peptides: mechanism and kinetics of cargo delivery, Adv Drug Deliv Rev 2005; 57: 529-45.
    • (2005) Adv Drug Deliv Rev , vol.57 , pp. 529-545
    • Zorko, M.1    Langel, U.2
  • 17
    • 27744557054 scopus 로고    scopus 로고
    • Cell-penetrating peptides:Mechanism and applications
    • El-Andaloussi S, Holm T, Langel Ü. Cell-penetrating peptides:mechanism and applications, Curr Pharm Design 2005; 11: 3597-611
    • (2005) Curr Pharm Design , vol.11 , pp. 3597-3611
    • El-Andaloussi, S.1    Holm, T.2    Langel, U.3
  • 18
    • 33751251344 scopus 로고    scopus 로고
    • Influence of protein transduction domains on intracellular delivery of macromolecules
    • Murriel CL, Dowdy SF. Influence of protein transduction domains on intracellular delivery of macromolecules, Expert Opin Drug Deliv 2006; 3: 739-46.
    • (2006) Expert Opin Drug Deliv , vol.3 , pp. 739-746
    • Murriel, C.L.1    Dowdy, S.F.2
  • 19
    • 42049095153 scopus 로고    scopus 로고
    • Cell-penetrating peptides: From molecular mechanisms to therapeutics
    • Morris MC, Deshayes S, Heitz F, Divita G. Cell-penetrating peptides: from molecular mechanisms to therapeutics, Biol Cell 2008; 100: 201-17.
    • (2008) Biol Cell , vol.100 , pp. 201-217
    • Morris, M.C.1    Deshayes, S.2    Heitz, F.3    Divita, G.4
  • 21
    • 25144520907 scopus 로고    scopus 로고
    • On the mechanisms of the internalization of S4(13)-PV cellpenetrating peptide
    • Mano M, Teodósio C, Paiva A, Simões S, Pedroso de Lima MC. On the mechanisms of the internalization of S4(13)-PV cellpenetrating peptide, Biochem J 2005; 390: 603-12.
    • (2005) Biochem J , vol.390 , pp. 603-612
    • Mano, M.1    Teodósio, C.2    Paiva, A.3    Simões, S.4    de Pedroso Lima, M.C.5
  • 22
    • 58149217884 scopus 로고    scopus 로고
    • A new potent secondary amphipathic cell-penetrating peptide for siRNA delivery into mammalian cells
    • Crombez L, Aldrian-Herrada G, Konate K, et al. A new potent secondary amphipathic cell-penetrating peptide for siRNA delivery into mammalian cells. Mol Ther 2009; 17: 95-103.
    • (2009) Mol Ther , vol.17 , pp. 95-103
    • Crombez, L.1    Aldrian-Herrada, G.2    Konate, K.3
  • 23
    • 77951225648 scopus 로고    scopus 로고
    • Insight into the cellular uptake mechanism of a secondary amphipathic cell-penetrating peptide for siRNA delivery
    • Konate K, Crombez L, Deshayes S, et al. Insight into the cellular uptake mechanism of a secondary amphipathic cell-penetrating peptide for siRNA delivery. Biochemistry 2010; 49: 3393-402.
    • (2010) Biochemistry , vol.49 , pp. 3393-3402
    • Konate, K.1    Crombez, L.2    Deshayes, S.3
  • 24
    • 80053609746 scopus 로고    scopus 로고
    • Direct translocation as major cellular uptake for CADY self-assembling peptide-based nanoparticles
    • Rydström A, Deshayes S, Konate K, et al. Direct translocation as major cellular uptake for CADY self-assembling peptide-based nanoparticles. PLoS One 2011; 6: e25924.
    • (2011) PLoS One , vol.6
    • Rydström, A.1    Deshayes, S.2    Konate, K.3
  • 25
    • 79952201159 scopus 로고    scopus 로고
    • A non-covalent peptide-based strategy for siRNA delivery
    • Crombez L, Divita G. A non-covalent peptide-based strategy for siRNA delivery. Methods Mol Biol 2011; 683: 349-60.
    • (2011) Methods Mol Biol , vol.683 , pp. 349-360
    • Crombez, L.1    Divita, G.2
  • 26
    • 84864129837 scopus 로고    scopus 로고
    • Self-Assembling Peptide-Based Nanoparticles for siRNA Delivery in Primary Cell Lines
    • Deshayes S, Konate K, Rydström A, et al. Self-Assembling Peptide-Based Nanoparticles for siRNA Delivery in Primary Cell Lines. Small 2012; 8: 2184-8.
    • (2012) Small , vol.8 , pp. 2184-2188
    • Deshayes, S.1    Konate, K.2    Rydström, A.3
  • 27
    • 67149093390 scopus 로고    scopus 로고
    • Efficient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein
    • Eguchi A, Meade BR, Chang YC, et al. Efficient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein. Nat Biotechnol 2009; 27: 567-71.
    • (2009) Nat Biotechnol , vol.27 , pp. 567-571
    • Eguchi, A.1    Meade, B.R.2    Chang, Y.C.3
  • 28
    • 79956015439 scopus 로고    scopus 로고
    • Design of a peptide-based vector, PepFect6, for efficient delivery of siRNA in cell culture and systemically in vivo
    • Andaloussi SE, Lehto T, Mäger I, et al. Design of a peptide-based vector, PepFect6, for efficient delivery of siRNA in cell culture and systemically in vivo. Nucleic Acids Res 2011; 39: 3972-87.
    • (2011) Nucleic Acids Res , vol.39 , pp. 3972-3987
    • Andaloussi, S.E.1    Lehto, T.2    Mäger, I.3
  • 29
    • 84858701389 scopus 로고    scopus 로고
    • Effective endogenous gene silencing mediated by pH responsive peptides proceeds via multiple pathways
    • Lam JK, Liang W, Lan Y, et al. Effective endogenous gene silencing mediated by pH responsive peptides proceeds via multiple pathways. J Control Release 2012; 158: 293-303.
    • (2012) J Control Release , vol.158 , pp. 293-303
    • Lam, J.K.1    Liang, W.2    Lan, Y.3
  • 30
    • 0030804766 scopus 로고    scopus 로고
    • A new peptide vector for efficient delivery of oligonucleotides into mammalian cells
    • Morris MC, Vidal P, Chaloin L, Heitz F, Divita G. A new peptide vector for efficient delivery of oligonucleotides into mammalian cells. Nucleic Acids Res 1997; 25: 2730-6.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2730-2736
    • Morris, M.C.1    Vidal, P.2    Chaloin, L.3    Heitz, F.4    Divita, G.5
  • 31
    • 0033199787 scopus 로고    scopus 로고
    • A novel potent strategy for gene delivery using a single peptide vector as a carrier
    • Morris MC, Chaloin L, Méry J, Heitz F, Divita G. A novel potent strategy for gene delivery using a single peptide vector as a carrier. Nucleic Acids Res 1999; 27: 3510-7.
    • (1999) Nucleic Acids Res , vol.27 , pp. 3510-3517
    • Morris, M.C.1    Chaloin, L.2    Méry, J.3    Heitz, F.4    Divita, G.5
  • 32
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • Morris MC, Depollier J, Mery J, Heitz F, Divita G. A peptide carrier for the delivery of biologically active proteins into mammalian cells. Nat Biotechnol 2001; 19:1173-6.
    • (2001) Nat Biotechnol , vol.19 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 33
    • 77958152651 scopus 로고    scopus 로고
    • Structural polymorphism of non-covalent peptide-based delivery systems: Highway to cellular uptake
    • Deshayes S, Konate K, Aldrian G, Crombez L, Heitz F, Divita G. Structural polymorphism of non-covalent peptide-based delivery systems: highway to cellular uptake. Biochim Biophys Acta 2010; 1798: 2304-14.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 2304-2314
    • Deshayes, S.1    Konate, K.2    Aldrian, G.3    Crombez, L.4    Heitz, F.5    Divita, G.6
  • 34
    • 0021269089 scopus 로고
    • Sequence requirements for nuclear location of simian virus 40 large-T antigen
    • Kalderon D, Richardson WD, Markham AF, Smith AE. Sequence requirements for nuclear location of simian virus 40 large-T antigen. Nature 1984; 311: 33-8.
    • (1984) Nature , vol.311 , pp. 33-38
    • Kalderon, D.1    Richardson, W.D.2    Markham, A.F.3    Smith, A.E.4
  • 35
    • 0037592877 scopus 로고    scopus 로고
    • Insight into the mechanism of the peptide-based gene delivery system MPG: Implications for delivery of siRNA into mammalian cells
    • Simeoni F, Morris MC, Heitz F, Divita G. Insight into the mechanism of the peptide-based gene delivery system MPG: implications for delivery of siRNA into mammalian cells. Nucleic Acids Res 2003; 31: 2717-24.
    • (2003) Nucleic Acids Res , vol.31 , pp. 2717-2724
    • Simeoni, F.1    Morris, M.C.2    Heitz, F.3    Divita, G.4
  • 36
    • 0027191425 scopus 로고
    • Disulfide linkage to polyacrylic resin for automated Fmoc peptide synthesis. Immunochemical applications of peptide resins and mercaptoamide peptides
    • Méry J, Granier C, Juin M, Brugidou J. Disulfide linkage to polyacrylic resin for automated Fmoc peptide synthesis. Immunochemical applications of peptide resins and mercaptoamide peptides. Int J Pept Protein Res 1993; 42: 44-52.
    • (1993) Int J Pept Protein Res , vol.42 , pp. 44-52
    • Méry, J.1    Granier, C.2    Juin, M.3    Brugidou, J.4
  • 37
    • 0036169073 scopus 로고    scopus 로고
    • New basic membrane-destabilizing peptides for plasmid-based gene delivery in vitro and in vivo
    • Rittner K, Benavente A, Bompard-Sorlet A, et al. New basic membrane-destabilizing peptides for plasmid-based gene delivery in vitro and in vivo. Mol Ther 2002; 5: 104-14.
    • (2002) Mol Ther , vol.5 , pp. 104-114
    • Rittner, K.1    Benavente, A.2    Bompard-Sorlet, A.3
  • 38
    • 0029941321 scopus 로고    scopus 로고
    • A novel DNA-peptide complex for efficient gene transfer and expression in mammalian cells
    • Gottschalk S, Sparrow JT, Hauer J, et al. A novel DNA-peptide complex for efficient gene transfer and expression in mammalian cells. Gene Ther 1996; 3: 448-57.
    • (1996) Gene Ther , vol.3 , pp. 448-457
    • Gottschalk, S.1    Sparrow, J.T.2    Hauer, J.3
  • 39
    • 77952580991 scopus 로고    scopus 로고
    • Secondary structure of cell-penetrating peptides controls membrane interaction and insertion
    • Eiríksdóttir E, Konate K, Langel U, Divita G, Deshayes S. Secondary structure of cell-penetrating peptides controls membrane interaction and insertion. Biochim Biophys Acta 2010; 1798: 1119-28.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1119-1128
    • Eiríksdóttir, E.1    Konate, K.2    Langel, U.3    Divita, G.4    Deshayes, S.5
  • 40
    • 84870222380 scopus 로고    scopus 로고
    • Modeling of non-covalent complexes of the cell-penetrating peptide CADY and its siRNA cargo
    • Crowet JM, Lins L, Deshayes S, et al. Modeling of non-covalent complexes of the cell-penetrating peptide CADY and its siRNA cargo. Biochim Biophys Acta 2013; 1828: 499-509.
    • (2013) Biochim Biophys Acta , vol.1828 , pp. 499-509
    • Crowet, J.M.1    Lins, L.2    Deshayes, S.3
  • 41
    • 0027179487 scopus 로고
    • Phospholipids in animal eukaryotic membranes: Transverse asymmetry and movement
    • Zachowski A. Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement. Biochem J 1993; 294: 1-14.
    • (1993) Biochem J , vol.294 , pp. 1-14
    • Zachowski, A.1
  • 42
    • 20944447518 scopus 로고    scopus 로고
    • Cell-penetrating peptides: From inception to application
    • Magzoub M, Gräslund A. Cell-penetrating peptides: from inception to application. Q Rev Biophys 2004; 37: 147-95.
    • (2004) Q Rev Biophys , vol.37 , pp. 147-195
    • Magzoub, M.1    Gräslund, A.2
  • 43
    • 70350049076 scopus 로고    scopus 로고
    • Biophysical interactions with model lipid membranes: Applications in drug discovery and drug delivery
    • Peetla C, Stine A, Labhasetwar V. Biophysical interactions with model lipid membranes: applications in drug discovery and drug delivery. Mol Pharm 2009; 6: 1264-76.
    • (2009) Mol Pharm , vol.6 , pp. 1264-1276
    • Peetla, C.1    Stine, A.2    Labhasetwar, V.3
  • 44
    • 0033179620 scopus 로고    scopus 로고
    • Lipid monolayers: Why use half a membrane to characterize protein-membrane interactions?
    • Brockman H. Lipid monolayers: why use half a membrane to characterize protein-membrane interactions? Curr Opin Struct Biol 1999; 9: 438-43.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 438-443
    • Brockman, H.1
  • 45
    • 0032694324 scopus 로고    scopus 로고
    • The monolayer technique: A potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes
    • Maget-Dana R. The monolayer technique: a potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes. Biochim Biophys Acta 1999; 1462: 109-40.
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 109-140
    • Maget-Dana, R.1
  • 46
    • 67349258550 scopus 로고    scopus 로고
    • Parameters modulating the maximum insertion pressure of proteins and peptides in lipid monolayers
    • Calvez P, Bussières S, Eric Demers, Salesse C. Parameters modulating the maximum insertion pressure of proteins and peptides in lipid monolayers. Biochimie 2009; 91: 718-33.
    • (2009) Biochimie , vol.91 , pp. 718-733
    • Calvez, P.1    Bussières, S.2    Demers, E.3    Salesse, C.4
  • 47
    • 0037071786 scopus 로고    scopus 로고
    • Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: Effects of surface charge and peptide concentration
    • Magzoub M, Eriksson LE, Gräslund A. Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: effects of surface charge and peptide concentration. Biochim Biophys Acta 2002; 1563: 53-63.
    • (2002) Biochim Biophys Acta , vol.1563 , pp. 53-63
    • Magzoub, M.1    Eriksson, L.E.2    Gräslund, A.3
  • 48
    • 0037457905 scopus 로고    scopus 로고
    • Application of a novel analysis to measure the binding of the membranetranslocating peptide penetratin to negatively charged liposomes
    • Persson D, Thorén PE, Herner M, Lincoln P, Nordén B. Application of a novel analysis to measure the binding of the membranetranslocating peptide penetratin to negatively charged liposomes. Biochemistry 2003; 42: 421-9.
    • (2003) Biochemistry , vol.42 , pp. 421-429
    • Persson, D.1    Thorén, P.E.2    Herner, M.3    Lincoln, P.4    Nordén, B.5
  • 50
    • 78049324771 scopus 로고    scopus 로고
    • Cellpenetrating peptide induces leaky fusion of liposomes containing late endosome-specific anionic lipid
    • Yang ST, Zaitseva E, Chernomordik LV, Melikov K. Cellpenetrating peptide induces leaky fusion of liposomes containing late endosome-specific anionic lipid. Biophys J 2010; 99: 2525-33.
    • (2010) Biophys J , vol.99 , pp. 2525-2533
    • Yang, S.T.1    Zaitseva, E.2    Chernomordik, L.V.3    Melikov, K.4
  • 51
    • 9644291651 scopus 로고    scopus 로고
    • On the mechanism of non-endosomial peptide-mediated cellular delivery of nucleic acids
    • Deshayes S, Gerbal-Chaloin S, Morris MC, et al. On the mechanism of non-endosomial peptide-mediated cellular delivery of nucleic acids. Biochim Biophys Acta 2004; 1667: 141-7.
    • (2004) Biochim Biophys Acta , vol.1667 , pp. 141-147
    • Deshayes, S.1    Gerbal-Chaloin, S.2    Morris, M.C.3
  • 53
    • 70450169244 scopus 로고    scopus 로고
    • Self-assembled lipid nanomedicines for siRNA tumor targeting
    • Tseng YC, Huang L. Self-assembled lipid nanomedicines for siRNA tumor targeting. J Biomed Nanotechnol 2009; 5: 351-63.
    • (2009) J Biomed Nanotechnol , vol.5 , pp. 351-363
    • Tseng, Y.C.1    Huang, L.2
  • 54
    • 42049095153 scopus 로고    scopus 로고
    • Cell-penetrating peptides: From molecular mechanisms to therapeutics
    • Morris MC, Deshayes S, Heitz F, Divita G. Cell-penetrating peptides: from molecular mechanisms to therapeutics. Biol Cell 2008; 100: 201-17.
    • (2008) Biol Cell , vol.100 , pp. 201-217
    • Morris, M.C.1    Deshayes, S.2    Heitz, F.3    Divita, G.4
  • 55
    • 23944483437 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Tools for intracellular delivery of therapeutics
    • Deshayes S, Morris MC, Divita G, Heitz F. Cell-penetrating peptides: tools for intracellular delivery of therapeutics. Cell Mol Life Sci 2005; 62: 1839-49.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1839-1849
    • Deshayes, S.1    Morris, M.C.2    Divita, G.3    Heitz, F.4
  • 56
    • 3543051871 scopus 로고    scopus 로고
    • Role of membrane potential and hydrogen bonding in the mechanism of translocation of guanidinium-rich peptides into cells
    • Rothbard JB, Jessop TC, Lewis RS, Murray BA, Wender PA. Role of membrane potential and hydrogen bonding in the mechanism of translocation of guanidinium-rich peptides into cells. J Am Chem Soc 2004; 126: 9506-7.
    • (2004) J Am Chem Soc , vol.126 , pp. 9506-9507
    • Rothbard, J.B.1    Jessop, T.C.2    Lewis, R.S.3    Murray, B.A.4    Wender, P.A.5
  • 57
    • 38949116621 scopus 로고    scopus 로고
    • Thermodynamic studies and binding mechanisms of cell-penetrating peptides with lipids and glycosaminoglycans
    • Ziegler A. Thermodynamic studies and binding mechanisms of cell-penetrating peptides with lipids and glycosaminoglycans. Adv Drug Deliv Rev 2008; 60: 580-97.
    • (2008) Adv Drug Deliv Rev , vol.60 , pp. 580-597
    • Ziegler, A.1
  • 58
    • 10344221003 scopus 로고    scopus 로고
    • Cellular uptake of argininerich peptides: Roles for macropinocytosis and actin rearrangement
    • Nakase I, Niwa M, Takeuchi T, et al. Cellular uptake of argininerich peptides: roles for macropinocytosis and actin rearrangement. Mol Ther 2004; 10: 1011-22.
    • (2004) Mol Ther , vol.10 , pp. 1011-1022
    • Nakase, I.1    Niwa, M.2    Takeuchi, T.3
  • 59
    • 0031743946 scopus 로고    scopus 로고
    • Effect of bafilomycin A1 and nocodazole on endocytic transport in HeLa cells: Implications for viral uncoating and infection
    • Bayer N, Schober D, Prchla E, Murphy RF, Blaas D, Fuchs R. Effect of bafilomycin A1 and nocodazole on endocytic transport in HeLa cells: implications for viral uncoating and infection. J Virol 1998; 72: 9645-55.
    • (1998) J Virol , vol.72 , pp. 9645-9655
    • Bayer, N.1    Schober, D.2    Prchla, E.3    Murphy, R.F.4    Blaas, D.5    Fuchs, R.6
  • 60
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia JS, Stan RV, Dowdy SF. Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat Med 2004; 10: 310-5.
    • (2004) Nat Med , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 61
    • 0345306592 scopus 로고    scopus 로고
    • The GTP/GDP cycling of rho GTPase TCL is an essential regulator of the early endocytic pathway
    • de Toledo M, Senic-Matuglia F, Salamero J, et al. The GTP/GDP cycling of rho GTPase TCL is an essential regulator of the early endocytic pathway. Mol Biol Cell 2003; 14: 4846-56.
    • (2003) Mol Biol Cell , vol.14 , pp. 4846-4856
    • de Toledo, M.1    Senic-Matuglia, F.2    Salamero, J.3
  • 64
    • 0034762332 scopus 로고    scopus 로고
    • Internalization of cholera toxin by different endocytic mechanisms
    • Torgersen ML, Skretting G, van Deurs B, Sandvig K. Internalization of cholera toxin by different endocytic mechanisms. J Cell Sci 2001; 114: 3737-47.
    • (2001) J Cell Sci , vol.114 , pp. 3737-3747
    • Torgersen, M.L.1    Skretting, G.2    van Deurs, B.3    Sandvig, K.4
  • 65
    • 38149080449 scopus 로고    scopus 로고
    • Distinct role of clathrinmediated endocytosis in the functional uptake of cholera toxin
    • Broeck DV, Lagrou AR, De Wolf MJ. Distinct role of clathrinmediated endocytosis in the functional uptake of cholera toxin. Acta Biochim Pol 2007; 54: 757-67.
    • (2007) Acta Biochim Pol , vol.54 , pp. 757-767
    • Broeck, D.V.1    Lagrou, A.R.2    de Wolf, M.J.3
  • 66
    • 0023449563 scopus 로고
    • Ligands internalized through coated or noncoated invaginations follow a common intracellular pathway
    • Tran D, Carpentier JL, Sawano F, Gorden P, Orci L. Ligands internalized through coated or noncoated invaginations follow a common intracellular pathway. Proc Natl Acad Sci USA 1987; 84: 7957-61.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7957-7961
    • Tran, D.1    Carpentier, J.L.2    Sawano, F.3    Gorden, P.4    Orci, L.5
  • 67
    • 0345169052 scopus 로고    scopus 로고
    • Syndecans: Proteoglycan regulators of cell-surface microdomains?
    • Couchman JR. Syndecans: proteoglycan regulators of cell-surface microdomains? Nat Rev Mol Cell Biol 2003; 4: 926-37.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 926-937
    • Couchman, J.R.1
  • 68
    • 33750504883 scopus 로고    scopus 로고
    • Formation of transmembrane ionic channels of primary amphipathic cell-penetrating peptides. Consequences on the mechanism of cell penetration
    • Deshayes S, Plénat T, Charnet P, Divita G, Molle G, Heitz F. Formation of transmembrane ionic channels of primary amphipathic cell-penetrating peptides. Consequences on the mechanism of cell penetration. Biochim Biophys Acta 2006; 1758: 1846-51.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1846-1851
    • Deshayes, S.1    Plénat, T.2    Charnet, P.3    Divita, G.4    Molle, G.5    Heitz, F.6
  • 69
    • 42149177168 scopus 로고    scopus 로고
    • Translocation or membrane disintegration? Implication of peptide-membrane interactions in pep-1 activity
    • Henriques ST, Castanho MA. Translocation or membrane disintegration? Implication of peptide-membrane interactions in pep-1 activity. J Pept Sci 2008; 14: 482-7.
    • (2008) J Pept Sci , vol.14 , pp. 482-487
    • Henriques, S.T.1    Castanho, M.A.2
  • 70
    • 58249095956 scopus 로고    scopus 로고
    • The membrane repair response masks membrane disturbances caused by cell-penetrating peptide uptake
    • Palm-Apergi C, Lorents A, Padari K, Pooga M, Hällbrink M. The membrane repair response masks membrane disturbances caused by cell-penetrating peptide uptake. FASEB J 2009; 23: 214-23.
    • (2009) FASEB J , vol.23 , pp. 214-223
    • Palm-Apergi, C.1    Lorents, A.2    Padari, K.3    Pooga, M.4    Hällbrink, M.5
  • 71
    • 0344824647 scopus 로고    scopus 로고
    • Plasma membrane disruption: Repair, prevention, adaptation
    • McNeil PL, Steinhardt RA. Plasma membrane disruption: repair, prevention, adaptation. Annu Rev Cell Dev Biol 2003; 19: 697-731.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 697-731
    • McNeil, P.L.1    Steinhardt, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.