메뉴 건너뛰기




Volumn 13, Issue 1, 2012, Pages 93-104

Intracellular delivery: Exploiting viral membranotropic peptides

Author keywords

Cell penetrating peptides; Endocytosis; Intracellular delivery; Membrane fusion; Viral fusion proteins

Indexed keywords

ALAMETHICIN; ARGININE; CELL PENETRATING PEPTIDE; CLATHRIN; COAT PROTEIN; COAT PROTEIN GAMMA PEPTIDE; DRUG VEHICLE; GALANIN; GH625 PROTEIN; GLYCOPROTEIN; GLYCOPROTEIN GP 41; HEPATITIS B SURFACE ANTIGEN; LYSINE; MASTOPARAN; MELITTIN; MEMBRANE PROTEIN; MODEL AMPHIPATHIC PEPTIDE; PENETRATIN; PEP 1 PROTEIN; POLYARGININE; POLYPEPTIDE ANTIBIOTIC AGENT; PRES2 PROTEIN; PROTEIN VP22; SYNTHETIC PEPTIDE; TRANSACTIVATOR PROTEIN; TRANSPORTAN; TRYPTOPHAN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VIRUS FUSION PROTEIN; VIRUS PROTEIN;

EID: 84857613440     PISSN: 13892002     EISSN: 18755453     Source Type: Journal    
DOI: 10.2174/138920012798356961     Document Type: Review
Times cited : (43)

References (124)
  • 1
  • 2
    • 71249150257 scopus 로고    scopus 로고
    • The biological routes of gene delivery mediated by lipid-based non-viral vectors
    • Duan, Y.; Zhang, S.; Wang, B.; Yang, B.; Zhi, D. The biological routes of gene delivery mediated by lipid-based non-viral vectors. Expert Opin. Drug Deliv., 2009, 6, 1351-1361.
    • (2009) Expert Opin. Drug Deliv. , vol.6 , pp. 1351-1361
    • Duan, Y.1    Zhang, S.2    Wang, B.3    Yang, B.4    Zhi, D.5
  • 4
    • 73449101112 scopus 로고    scopus 로고
    • Recent trends in non-viral vectormediated gene delivery
    • Pathak A.; Patnaik S.; Gupta KC. Recent trends in non-viral vectormediated gene delivery. Biotechnol. J. 2009, 4, 1559-1572.
    • (2009) Biotechnol. J. , vol.4 , pp. 1559-1572
    • Pathak, A.1    Patnaik, S.2    Gupta, K.C.3
  • 7
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cellpenetrating peptides: From molecular mechanisms to therapeutics
    • Heitz; F.; M.C. Morris.; G. Divita.; Twenty years of cellpenetrating 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
  • 8
    • 38949184554 scopus 로고    scopus 로고
    • Delivery of proteins and nucleic acids using a non-covalent peptide-based strategy
    • DOI 10.1016/j.addr.2007.09.005, PII S0169409X07002888
    • Deshayes, S.; M.C. Morris.; F. Heitz.; G. Divita. Delivery of proteins and nucleic acids using a non-covalent peptide-based strategy. Adv. Drug Deliv. Rev. 2008; 60, 537-547. (Pubitemid 351222678)
    • (2008) Advanced Drug Delivery Reviews , vol.60 , Issue.4-5 , pp. 537-547
    • Deshayes, S.1    Morris, M.2    Heitz, F.3    Divita, G.4
  • 9
    • 23944483437 scopus 로고    scopus 로고
    • Cell-penetrating pep tides: Tools for intracellular delivery of therapeutics
    • DOI 10.1007/s00018-005-5109-0
    • Deshayes, S.; Morris, M.C.; Divita, G.; Heitz, F. Cell-penetrating peptides: Tools for intracellular delivery of therapeutics. Cell. Mol. Life Sci. 2005, 62,1839-1849. (Pubitemid 41188523)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.16 , pp. 1839-1849
    • Deshayes, S.1    Morris, M.C.2    Divita, G.3    Heitz, F.4
  • 10
    • 12344263736 scopus 로고    scopus 로고
    • Recent advances in the use of protein transduction domains for the delivery of peptides, proteins and nucleic acids in vivo
    • DOI 10.1517/17425247.2.1.43
    • Snyder, E.L.; S.F. Dowdy. Recent advances in the use of protein transduction domains for the delivery of peptides; proteins and nucleic acids in vivo. Expert Opin. Drug Deliv., 2005, 2,43-51. (Pubitemid 40123882)
    • (2005) Expert Opinion on Drug Delivery , vol.2 , Issue.1 , pp. 43-51
    • Snyder, E.L.1    Dowdy, S.F.2
  • 11
    • 67649408951 scopus 로고    scopus 로고
    • SiRNA delivery using peptide transduction domains
    • Eguchi, A.; S.F. Dowdy. siRNA delivery using peptide transduction domains. Trends Pharmacol. Sci., 2009, 30, 341-345.
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 341-345
    • Eguchi, A.1    Dowdy, S.F.2
  • 12
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • DOI 10.1016/0092-8674(88)90263-2
    • Frankel, A.D.; C.O. Pabo. Cellular uptake of the tat protein from human immunodeficiency virus. Cell, 1988, 55,1189-1193. (Pubitemid 19020071)
    • (1988) Cell , vol.55 , Issue.6 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 14
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi, D.; A.H. Joliot.; G. Chassaing.; A. Prochiantz. The third helix of the Antennapedia homeodomain translocates through biological membranes. J. Biol. Chem. 1994, 269, 10444-10450. (Pubitemid 24198241)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.14 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 15
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • DOI 10.1074/jbc.272.25.16010
    • Vives, E.; P. Brodin.; B. Lebleu. A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem., 1997, 272,16010-16017. (Pubitemid 27265584)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 16
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • DOI 10.1126/science.285.5433.1569
    • Schwarze, S.R.; A. Ho.; A. Vocero-Akbani.; S.F. Dowdy; In vivo protein transduction: Delivery of a biologically active protein into the mouse. Science, 1999, 285,1569-1572. (Pubitemid 29420581)
    • (1999) Science , vol.285 , Issue.5433 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 18
    • 0031471203 scopus 로고    scopus 로고
    • Intercellular trafficking and protein delivery by a herpesvirus structural protein
    • DOI 10.1016/S0092-8674(00)81843-7
    • Elliott, G.; P. O'Hare. Intercellular trafficking and protein delivery by a Herpesvirus structural protein. Cell, 1997, 88, 223-233. (Pubitemid 28015871)
    • (1997) Cell , vol.88 , Issue.2 , pp. 223-233
    • Elliott, G.1    O'Hare, P.2
  • 19
    • 0034021679 scopus 로고    scopus 로고
    • Novel cell permeable motif derived from the PreS2-domain of hepatitis-B virus surface antigens
    • DOI 10.1038/sj/gt/3301154
    • Oess, S.; Hildt, E. Novel cell permeable motif derived from the PreS2-domain of hepatitis-B virus surface antigens. Gene Ther., 2000, 7, 750-758. (Pubitemid 30255756)
    • (2000) Gene Therapy , vol.7 , Issue.9 , pp. 750-758
    • Oess, S.1    Hildt, E.2
  • 20
    • 39149101777 scopus 로고    scopus 로고
    • Calcitoinin-derived peptide carriers: Mechanisms and application
    • Rennert, R.; I. Neudorf.; A. Beck-Sickinger. Calcitoinin-derived peptide carriers: Mechanisms and application. Adv. Drug Deliv. Rev., 2008, 60, 485-499.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 485-499
    • Rennert, R.1    Neudorf, I.2    Beck-Sickinger, A.3
  • 21
    • 34548180403 scopus 로고    scopus 로고
    • Applications of cell-penetrating peptides in regulation of gene expression
    • Järver, P.; Langel, K.; El-Andaloussi, S.; Langel U. Applications of cell-penetrating peptides in regulation of gene expression. Biochem. Soc. Trans., 2007, 35, 770-774. (Pubitemid 47310365)
    • (2007) Biochemical Society Transactions , vol.35 , Issue.4 , pp. 770-774
    • Jarver, P.1    Langel, K.2    El-Andaloussi, S.3    Langel, U.4
  • 23
    • 45749120326 scopus 로고    scopus 로고
    • Cell-penetrating peptides as delivery vehicles for biology and medicine
    • DOI 10.1039/b719950c
    • Stewart, K.M.; K.L. Horton.; S.O. Kelley. Cell-penetrating peptides as delivery vehicles for biology and medicine. Org. Biomol. Chem., 2008, 6, 2242-2255. (Pubitemid 351863664)
    • (2008) Organic and Biomolecular Chemistry , vol.6 , Issue.13 , pp. 2242-2255
    • Stewart, K.M.1    Horton, K.L.2    Kelley, S.O.3
  • 24
    • 56049093057 scopus 로고    scopus 로고
    • Pelegrin. Cell-penetrating and celltargeting peptides in drug delivery
    • Vives, E. J. Schmidt.; A. Pelegrin. Cell-penetrating and celltargeting peptides in drug delivery. Biochim. Biophys. Acta, 2008, 1786,126-138.
    • (2008) Biochim. Biophys. Acta , vol.1786 , pp. 126-138
    • Vives, E.J.1    Schmidt, A.2
  • 25
    • 5644276383 scopus 로고    scopus 로고
    • Delivery of bioactive molecules into the cell: The Trojan horse approach
    • DOI 10.1016/j.mcn.2004.03.005, PII S1044743104000715
    • Dietz, G.P.; M. Bahr. Delivery of bioactive molecules into the cell: The Trojan horse approach. Mol. Cell. Neurosci., 2004, 27,85-131. (Pubitemid 39370094)
    • (2004) Molecular and Cellular Neuroscience , vol.27 , Issue.2 , pp. 85-131
    • Dietz, G.P.H.1    Bahr, M.2
  • 26
    • 0034237577 scopus 로고    scopus 로고
    • Protein transduction: Unrestricted delivery into all cells?
    • DOI 10.1016/S0962-8924(00)01771-2, PII S0962892400017712
    • Schwarze, S.R.; K.A. Hruska.; S.F. Dowdy.; Protein transduction: Unrestricted delivery into all cells? Trends Cell Biol., 2000, 10, 290-295. (Pubitemid 30387038)
    • (2000) Trends in Cell Biology , vol.10 , Issue.7 , pp. 290-295
    • Schwarze, S.R.1    Hruska, K.A.2    Dowdy, S.F.3
  • 27
    • 70349456654 scopus 로고    scopus 로고
    • Recent advances in the use of cell-penetrating peptides for medical and biological applications
    • (11
    • Fonseca, S.B.; Pereira, M.P.; Kelley, S.O. Recent advances in the use of cell-penetrating peptides for medical and biological applications. Adv. Drug Deliv. Rev., 2009, 30, 61(11), 953-964.
    • (2009) Adv. Drug Deliv. Rev. , vol.30 , Issue.61 , pp. 953-964
    • Fonseca, S.B.1    Pereira, M.P.2    Kelley, S.O.3
  • 28
    • 42049095153 scopus 로고    scopus 로고
    • Cell-penetrating peptides: From molecular mechanisms to therapeutics
    • DOI 10.1042/BC20070116
    • Morris, M.C.; Deshayes, S.; Heitz, F.; Divita, G. Cell-penetrating peptides: From molecular mechanism to therapeutics. Biol. Cell, 2008, 100, 201-217. (Pubitemid 351517084)
    • (2008) Biology of the Cell , vol.100 , Issue.4 , pp. 201-217
    • Morris, M.C.1    Deshayes, S.2    Heitz, F.3    Divita, G.4
  • 29
    • 77949741829 scopus 로고    scopus 로고
    • Intracellular transduction using cellpenetrating peptides
    • Sawant, R.; Torchilin, V. Intracellular transduction using cellpenetrating peptides. Mol. Biosyst., 2009, 6, 628-640.
    • (2009) Mol. Biosyst. , vol.6 , pp. 628-640
    • Sawant, R.1    Torchilin, V.2
  • 30
    • 0025767210 scopus 로고
    • Activating region of HIV-1 Tat protein: Vacuum UV circular dichroism and energy minimization
    • Loret, E. P.; Vives, E.; Ho, P. S.; Rochat, H.; Van Rietschoten, J.; Johnson Jr, W. C. Activating region of HIV-1 Tat protein: Vacuum UV circular dichroism and energy minimization. Biochem., 1991, 30, 6013-6023.
    • (1991) Biochem. , vol.30 , pp. 6013-6023
    • Loret, E.P.1    Vives, E.2    Ho, P.S.3    Rochat, H.4    Van Rietschoten, J.5    Johnson Jr., W.C.6
  • 31
    • 0027400035 scopus 로고
    • Antennapedia homeobox peptide enhances growth and branching of embryonic chicken motoneurons in vitro
    • DOI 10.1083/jcb.120.2.485
    • Bloch-Gallego, E.; Le Roux, I.; Joliot, A.H.; Volovitch, M.; Henderson, C.E.; Prochiantz, A. Antennapedia homeobox peptide enhances growth and branching of embryonic chicken motoneurons in vitro. J. Cell Biol., 1993, 120(2), 485-492. (Pubitemid 23040086)
    • (1993) Journal of Cell Biology , vol.120 , Issue.2 , pp. 485-492
    • Bloch-Gallego, E.1    Le Roux, I.2    Joliot, A.H.3    Volovitch, M.4    Henderson, C.E.5    Prochiantz, A.6
  • 33
    • 0034738570 scopus 로고    scopus 로고
    • Interaction of the third helix of Antennapedia homeodomain and a phospholipid monolayer, studied by ellipsometry and PM-IRRAS at the air-water interface
    • DOI 10.1016/S0005-2736(00)00218-2, PII S0005273600002182
    • Bellet-Amalric E.; Blaudez D.; Desbat B.; Graner F.; Gauthier F. and Renault A. Interaction of the third helix of Antennapedia homeodomain and a phospholipid monolayer; studied by ellipsometry and PM-IRRAS at the air-water interface. Biochim. Biophys. Acta, 2000, 1467, 131-143. (Pubitemid 30621592)
    • (2000) Biochimica et Biophysica Acta - Biomembranes , vol.1467 , Issue.1 , pp. 131-143
    • Bellet-Amalric, E.1    Blaudez, D.2    Desbat, B.3    Graner, F.4    Gauthier, F.5    Renault, A.6
  • 34
    • 0035795727 scopus 로고    scopus 로고
    • Interaction and structure induction of cell-penetrating peptides in the presence of phospholipid vesicles
    • DOI 10.1016/S0005-2736(01)00304-2, PII S0005273601003042
    • Magzoub, M.; Kilk, K.; Eriksson, L. E.; Langel, U. Graslund, A. Interaction and structure induction of cell-penetrating peptides in the presence of phospholipid vesicles. Biochim. Biophys. Acta, 2001, 1512, 77-89. (Pubitemid 32378784)
    • (2001) Biochimica et Biophysica Acta - Biomembranes , vol.1512 , Issue.1 , pp. 77-89
    • Magzoub, M.1    Kilk, K.2    Eriksson L.E.Goran3    Langel, U.4    Graslund, A.5
  • 35
    • 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
    • DOI 10.1016/S0005-2736(02)00373-5, PII S0005273602003735
    • Magzoub, M.; Eriksson, L. E.; Graslund 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. (Pubitemid 34455043)
    • (2002) Biochimica et Biophysica Acta - Biomembranes , vol.1563 , Issue.1-2 , pp. 53-63
    • Magzoub, M.1    Eriksson, L.E.G.2    Graslund, A.3
  • 37
    • 0035853015 scopus 로고    scopus 로고
    • Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR
    • DOI 10.1021/bi0008985
    • Lindberg, M.; Jarvet, J.; Langel, U.; Gräslund, A. Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR. Biochem., 2001, 40, 3141-3149 (Pubitemid 32205358)
    • (2001) Biochemistry , vol.40 , Issue.10 , pp. 3141-3149
    • Lindberg, M.1    Jarvet, J.2    Langel, U.3    Graslund, A.4
  • 38
    • 2942627932 scopus 로고    scopus 로고
    • NMR solution structure and position of transportan in neutral phospholipid bicelles
    • DOI 10.1016/j.febslet.2004.04.079, PII S0014579304005551
    • Bárány-Wallje, E.; Andersson, A.; Gräslund, A.; Mäler, L. NMR solution structure and position of transportan in neutral phospholipid bicelles. FEBS Lett., 2004, 567, 265-269. (Pubitemid 38748403)
    • (2004) FEBS Letters , vol.567 , Issue.2-3 , pp. 265-269
    • Barany-Wallje, E.1    Andersson, A.2    Graslund, A.3    Maler, L.4
  • 39
    • 0026093570 scopus 로고
    • Retention behaviour of a template-assembled synthetic protein and its amphiphilic building blocks on reversed-phase columns
    • Steiner, V.; Schar, M.; Bornsen, K.O.; Mutter, M. Retention behaviour of a template-assembled synthetic protein and its amphiphilic building blocks on reversed-phase columns. J. Chromatogr., 1991,586,43-50.
    • (1991) J. Chromatogr. , vol.586 , pp. 43-50
    • Steiner, V.1    Schar, M.2    Bornsen, K.O.3    Mutter, M.4
  • 40
    • 0032508926 scopus 로고    scopus 로고
    • Cellular uptake of an α-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically
    • DOI 10.1016/S0005-2736(98)00161-8, PII S0005273698001618
    • Oehlke, J.; Scheller, A.; Wiesner, B.; Krause, E.; Beyermann, M.; Klauschenz, E.; Melzig, M.; Bienert, M. Cellular uptake of an alpha-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically. Biochim. Biophys. Acta, 1998,1414, 127-139. (Pubitemid 28511045)
    • (1998) Biochimica et Biophysica Acta - Biomembranes , vol.1414 , Issue.1-2 , pp. 127-139
    • Oehlke, J.1    Scheller, A.2    Wiesner, B.3    Krause, E.4    Beyermann, M.5    Klauschenz, E.6    Melzig, M.7    Bienert, M.8
  • 41
    • 0030804766 scopus 로고    scopus 로고
    • A new peptide vector for efficient delivery of oligonucleotides into mammalian cells
    • DOI 10.1093/nar/25.14.2730
    • Morris, M.C.; 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, 2730-2736. (Pubitemid 27299785)
    • (1997) Nucleic Acids Research , vol.25 , Issue.14 , pp. 2730-2736
    • Morris, M.C.1    Vidal, P.2    Chaloin, L.3    Heitz, F.4    Divita, G.5
  • 42
    • 0033199787 scopus 로고    scopus 로고
    • A novel potent strategy for gene delivery using a single peptide vector as a carrier
    • DOI 10.1093/nar/27.17.3510
    • Morris, M.C.; 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, 27,3510-3517. (Pubitemid 29414679)
    • (1999) Nucleic Acids Research , vol.27 , Issue.17 , pp. 3510-3517
    • Morris, M.C.1    Chaloin, L.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 43
    • 0023669119 scopus 로고
    • Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus
    • Gallaher; W.R. Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus. Cell, 1987, 50,327-328.
    • (1987) Cell , vol.50 , pp. 327-328
    • Gallaher, W.R.1
  • 44
    • 0025297179 scopus 로고
    • Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41
    • Freed, E.O.; Myers, D.J. Risser, R. Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41.Proc. Natl. Acad. Sci. USA, 1990, 87, 4650-4654.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4650-4654
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 45
    • 0029968695 scopus 로고    scopus 로고
    • Mutational analysis of the fusion peptide of the human immunodeficiency virus type 1: Identification of critical glycine residues
    • DOI 10.1006/viro.1996.0169
    • Delahunty, M.D.; Rhee, I.; Freed, E.O.; Bonifacino, J.S. Mutational analysis of the fusion peptide of the human immunodeficiency virus type 1: Identification of critical glycine residues. Virology, 1996, 218, 94-102. (Pubitemid 26133090)
    • (1996) Virology , vol.218 , Issue.1 , pp. 94-102
    • Delahunty, M.D.1    Rhee, I.2    Freed, E.O.3    Bonifacino, J.S.4
  • 46
    • 0021269089 scopus 로고
    • In vitro mutagenesis of a putative DNA binding domain of SV40 large-T
    • Kalderon, D.; Richardson, W.D.; Markham, A.F. Smith, A.E. In vitro mutagenesis of a putative DNA binding domain of SV40 large-T. Nature, 1984,311, 33-38.
    • (1984) Nature , vol.311 , pp. 33-38
    • Kalderon, D.1    Richardson, W.D.2    Markham, A.F.3    Smith, A.E.4
  • 47
    • 0026458016 scopus 로고
    • The nuclear membrane
    • Dingwall, C.; Laskey, R. The nuclear membrane. Science, 1992, 258, 942-947.
    • (1992) Science , vol.258 , pp. 942-947
    • Dingwall, C.1    Laskey, R.2
  • 48
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • DOI 10.1038/nbt1201-1173
    • Morris, M. C.; 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, 1173-1176. (Pubitemid 33115705)
    • (2001) Nature Biotechnology , vol.19 , Issue.12 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 50
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides: An abundant source of membranepermeable peptides having potential as carriers for intracellular protein delivery
    • Futaki, S.; T. Suzuki.; W. Ohashi.; T. Yagami.; S. Tanaka.; K. Ueda. Arginine-rich peptides: An abundant source of membranepermeable peptides having potential as carriers for intracellular protein delivery; J. Biol. Chem., 2001, 276, 5836-5840.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6
  • 51
    • 0026521355 scopus 로고
    • The herpes simplex virus type 1 tegument protein VP22 is encoded by gene UL49
    • Elliott; G. D.; and D. M. Meredith. The herpes simplex virus type 1 tegument protein VP22 is encoded by gene UL49. J. Gen. Virol. 1992;73:723-726.
    • (1992) J. Gen. Virol. , vol.73 , pp. 723-726
    • Elliott, G.D.1    Meredith, D.M.2
  • 52
    • 0034863368 scopus 로고    scopus 로고
    • RNAs extracted from herpes simplex virus 1 virions: Apparent selectivity of viral but not cellular RNAs packaged in virions
    • DOI 10.1128/JVI.75.17.8105-8116.2001
    • Sciortino, M.T.; Suzuki, M.; Taddeo, B.; Roizman, B. RNAs extracted from herpes simplex virus 1 virions: Apparent selectivity of viral but not cellular RNAs packaged in virions. J. Virol.; 2001,75, 8105-8116. (Pubitemid 32743683)
    • (2001) Journal of Virology , vol.75 , Issue.17 , pp. 8105-8116
    • Sciortino, M.-T.1    Suzuki, M.2    Taddeo, B.3    Roizman, B.4
  • 53
    • 0035805581 scopus 로고    scopus 로고
    • Particle formation by a conserved domain of the herpes simplex virus protein VP22 facilitating protein and nucleic acid delivery
    • Normand, N.; van Leeuwen, H.; O'Hare, P. Particle formation by a conserved domain of the herpes simplex virus protein VP22 facilitating protein and nucleic acid delivery. J. Biol. Chem., 2001, 276, 15042-15050.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15042-15050
    • Normand, N.1    Van Leeuwen, H.2    O'Hare, P.3
  • 54
    • 0037062508 scopus 로고    scopus 로고
    • Of the three tegument proteins that package mRNA in herpes simplex virions, one (VP22) transports the mRNA to uninfected cells for expression prior to viral infection
    • DOI 10.1073/pnas.122231699
    • Sciortino, M. T.; Taddeo, B.; Poon, A. P. W.; Mastino, A.; Roizman, B. Of the three tegument proteins that package mRNA in herpes simplex virions; one (VP22) transports the mRNA to uninfected cells for expression prior to viral infection. Proc. Natl. Acad. Sci. USA., 2002, 99, 8318-8323. (Pubitemid 34651050)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.12 , pp. 8318-8323
    • Sciortino, M.T.1    Taddeo, B.2    Poon, A.P.W.3    Mastino, A.4    Roizman, B.5
  • 55
    • 0028806817 scopus 로고
    • Characterization of essential domains for the functionality of the MHBst transcriptional activator and identification of a minimal MHBst transactivator
    • Hildt, E.; Urban, S.; Hofschneider, P.H. Characterization of essential domains for the functionality of the MHBst transcriptional activator and identification of a minimal MHBst transactivator. Oncogene, 1995, 11, 2055-2066.
    • (1995) Oncogene , vol.11 , pp. 2055-2066
    • Hildt, E.1    Urban, S.2    Hofschneider, P.H.3
  • 56
    • 41949101389 scopus 로고    scopus 로고
    • Activation; exposure and penetration of virally encoded; membrane-active polypeptides during nonenveloped virus entry
    • Banerjee, M.; J. E. Johnson. Activation; exposure and penetration of virally encoded; membrane-active polypeptides during nonenveloped virus entry. Curr. Protein Pept. Sci., 2008, 916-927.
    • (2008) Curr. Protein Pept. Sci. , pp. 916-927
    • Banerjee, M.1    Johnson, J.E.2
  • 57
    • 0033608952 scopus 로고    scopus 로고
    • An animal virus-derived peptide switches membrane morphology: Possible relevance to nodaviral transfection processes
    • Janshoff, A.; D. T. Bong.; C. Steinem.; J. E. Johnson.; M. R. Ghadiri. An animal virus-derived peptide switches membrane morphology: Possible relevance to nodaviral transfection processes. Biochem.,1999, 38,5328-5336.
    • (1999) Biochem. , vol.38 , pp. 5328-5336
    • Janshoff, A.1    Bong, D.T.2    Steinem, C.3    Johnson, J.E.4    Ghadiri, M.R.5
  • 58
    • 0033168280 scopus 로고    scopus 로고
    • A highly membrane-active peptide in Flock House virus: Implications for the mechanism of nodavirus infection
    • DOI 10.1016/S1074-5521(99)80065-9
    • Bong, D. T.; C. Steinem.; A. Janshoff.; J. E. Johnson.; M. R. Ghadiri. A highly membrane active peptide in Flock House Virus: Implications for the mechanism of nodavirus infection. Chem. Biol., 1999,6,473-481. (Pubitemid 29311484)
    • (1999) Chemistry and Biology , vol.6 , Issue.7 , pp. 473-481
    • Bong, D.T.1    Steinem, C.2    Janshoff, A.3    Johnson, J.E.4    Ghadiri, M.R.5
  • 59
    • 0034117197 scopus 로고    scopus 로고
    • Membrane partitioning of the cleavage peptide in flock house virus
    • Bong, D.T.; Janshoff, A.; Steinem, C.; Ghadiri M.R. Membrane Partitioning of the Cleavage Peptide in Flock House Virus. Bioph. J., 2000, 78, 839-845. (Pubitemid 30211841)
    • (2000) Biophysical Journal , vol.78 , Issue.2 , pp. 839-845
    • Bong, D.T.1    Janshoff, A.2    Steinem, C.3    Ghadiri, M.R.4
  • 60
    • 70449120118 scopus 로고    scopus 로고
    • Cell-surface accumulation of flock house virus-derived peptide leads to efficient internalization via macropinocytosis
    • Nakase, I.; Hirose, H.; Tanaka, G.; Tadokoro, A.; Kobayashi, S.; Takeuchi, T.; Futaki, S. Cell-surface accumulation of flock house virus-derived peptide leads to efficient internalization via macropinocytosis. Mol. Ther., 2009, 17,1868-1876.
    • (2009) Mol. Ther. , vol.17 , pp. 1868-1876
    • Nakase, I.1    Hirose, H.2    Tanaka, G.3    Tadokoro, A.4    Kobayashi, S.5    Takeuchi, T.6    Futaki, S.7
  • 61
    • 77952758845 scopus 로고    scopus 로고
    • The presence of a single Nterminal histidine residue enhances the fusogenic properties of a membranotropic peptide derived from herpes simplex virus type 1 glycoprotein H
    • Galdiero, S.; A. Falanga.; M. Vitiello.; L. Raiola.; L. Russo.; C. Pedone.; C.Isernia.; M. Galdiero. "The presence of a single Nterminal histidine residue enhances the fusogenic properties of a membranotropic peptide derived from herpes simplex virus type 1 glycoprotein H. J. Biol. Chem, 2010, 285(22), 17123-17136.
    • (2010) J. Biol. Chem , vol.285 , Issue.22 , pp. 17123-17136
    • Galdiero, S.1    Falanga, A.2    Vitiello, M.3    Raiola, L.4    Russo, L.5    Pedone, C.6    Isernia, C.7    Galdiero, M.8
  • 62
    • 82255175122 scopus 로고    scopus 로고
    • A peptide derived from Herpes Simplex Virus type 1 glycoprotein H: Membrane translocation and applications to the delivery of quantum dots
    • doi:10.1016/j.n.nano.2011.04.009
    • Falanga; M. Vitiello; M. Cantisani; R. Tarallo; D. Guarnieri; E. Mignogna; P. Netti; C. Pedone; M. Galdiero; S. Galdiero. A peptide derived from Herpes Simplex Virus type 1 glycoprotein H: Membrane translocation and applications to the delivery of quantum dots. Nanomedicine; 2011, doi:10.1016/j.n.nano.2011.04.009.
    • (2011) Nanomedicine
    • Falanga, M.1    Vitiello, M.2    Cantisani, R.3    Tarallo, D.4    Guarnieri, E.5    Mignogna, P.6    Netti, C.7    Pedone, M.8    Galdiero, S.9    Galdiero10
  • 64
    • 0032487377 scopus 로고    scopus 로고
    • Application of membrane-active peptides for drug and gene delivery across cellular membranes
    • DOI 10.1016/S0169-409X(98)00005-2, PII S0169409X98000052
    • Plank, C.; Zauner, W.; Wagner, E.; Application of membraneactive peptides for drug and gene delivery across cellular membranes. Adv. Drug Deliv. Rev., 1998, 34, 21-35. (Pubitemid 28464476)
    • (1998) Advanced Drug Delivery Reviews , vol.34 , Issue.1 , pp. 21-35
    • Plank, C.1    Zauner, W.2    Wagner, E.3
  • 65
  • 66
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • DOI 10.1080/10409230802058320, PII 794225034
    • White, J.M.; Delos, S.E.; Brecher, M.; Schornberg, K. Structures and mechanisms of viral membrane fusion proteins: Multiple varia tions on a common theme. Crit. Rev. Biochem. Mol. Biol., 2008, 43(3),189-219. (Pubitemid 351883153)
    • (2008) Critical Reviews in Biochemistry and Molecular Biology , vol.43 , Issue.3 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 67
    • 38449106713 scopus 로고    scopus 로고
    • Penetration of non-enveloped viruses into the cytoplasm
    • Tsai, B.; Penetration of non-enveloped viruses into the cytoplasm. Annu. Rev. Cell Dev. Biol., 2007, 23,23-43.
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 23-43
    • Tsai, B.1
  • 68
    • 0028321381 scopus 로고
    • Capsid assembly in a family of animal viruses primes an autoproteolytic maturation that depends on a single aspartic acid residue
    • Zlotnick, A.; Reddy, V.S.; Dasgupta, R.; Schneemann, A.; Ray, W.J. Jr.; Rueckert, R.R.; Johnson, J.E. Capsid assembly in a family of animal viruses primes an autoproteolytic maturation that depends on a single aspartic acid residue. J. Biol. Chem., 1994, 6,269(18):13680-13684. (Pubitemid 24206149)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.18 , pp. 13680-13684
    • Zlotnick, A.1    Reddy, V.S.2    Dasgupta, R.3    Schneemann, A.4    Ray Jr., W.J.5    Rueckert, R.R.6    Johnson, J.E.7
  • 70
    • 42449151315 scopus 로고    scopus 로고
    • Peptides released from reovirus outer capsid form membrane pores that recruit virus particles
    • DOI 10.1038/emboj.2008.60, PII EMBOJ200860
    • Ivanovic, T.; Agosto, M. A.; Zhang, L.; Chandran, K.; Harrison, S. C.; Nibert, M. L. Peptides released from reovirus outer capsid form membrane pores that recruit virus particles. EMBO. J., 2008, 27,1289-1298. (Pubitemid 351574754)
    • (2008) EMBO Journal , vol.27 , Issue.8 , pp. 1289-1298
    • Ivanovic, T.1    Agosto, M.A.2    Zhang, L.3    Chandran, K.4    Harrison, S.C.5    Nibert, M.L.6
  • 71
    • 0029793570 scopus 로고    scopus 로고
    • Trypsin activation pathway of rotavirus infectivity
    • Arias, C. F.; Romero, P.; Alvarez, V.; Lopez, S. Trypsin activation pathway of rotavirus infectivity. J. Virol., 1996,70, 5832-5839. (Pubitemid 26266793)
    • (1996) Journal of Virology , vol.70 , Issue.9 , pp. 5832-5839
    • Arias, C.F.1    Romero, P.2    Alvarez, V.3    Lopez, S.4
  • 72
    • 0029983628 scopus 로고    scopus 로고
    • The role of the adenovirus protease in virus entry into cells
    • Greber, U. F.; Webster, P.; Weber, J.; Helenius, A. The role of the adenovirus protease on virus entry into cells. EMBO. J., 1996,15,1766-1777. (Pubitemid 26119212)
    • (1996) EMBO Journal , vol.15 , Issue.8 , pp. 1766-1777
    • Greber, U.F.1    Webster, P.2    Weber, J.3    Helenius, A.4
  • 73
    • 0036173429 scopus 로고    scopus 로고
    • The capsid of infectious bursal disease virus contains several small peptides arising from the maturation process of pVP2
    • DOI 10.1128/jvi.76.5.2393-2402.2002
    • Da Costa, B.; Chevalier, C.; Henry, C.; Huet, J. C.; Petit, S.; Lepault, J.; Boot, H.; Delmas, B. The capsid of infectious bursal disease virus contains several small peptides arising from the maturation process of pVP2. J. Virol., 2002, 76, 2393-2402. (Pubitemid 34150707)
    • (2002) Journal of Virology , vol.76 , Issue.5 , pp. 2393-2402
    • Da Costa, B.1    Chevalier, C.2    Henry, C.3    Huet, J.-C.4    Petit, S.5    Lepault, J.6    Boot, H.7    Delmas, B.8
  • 75
    • 26944466459 scopus 로고    scopus 로고
    • Mechanism of membrane fusion by viral envelope proteins
    • DOI 10.1016/S0065-3527(05)64007-9, PII S0065352705640079, Virus Structure and Assembly
    • Harrison, S.C. Mechanism of membrane fusion by viral envelope proteins. Adv. Virus. Res.; 2005, 64,231-261. (Pubitemid 43574760)
    • (2005) Advances in Virus Research , vol.64 , pp. 231-261
    • Harrison, S.C.1
  • 76
    • 29144460894 scopus 로고    scopus 로고
    • Paramyxovirus membrane fusion: Lessons from the F and HN atomic structures
    • DOI 10.1016/j.virol.2005.09.007, PII S0042682205005684
    • Lamb, R.A.; Paterson, R.G.; Jardetzky, T.S. Paramyxovirus membrane fusion: Lessons from the F and HN atomic structures. Virology, 2006, 344(1), 30-37. (Pubitemid 41814447)
    • (2006) Virology , vol.344 , Issue.1 , pp. 30-37
    • Lamb, R.A.1    Paterson, R.G.2    Jardetzky, T.S.3
  • 77
    • 33749042583 scopus 로고    scopus 로고
    • Flavivirus membrane fusion
    • DOI 10.1099/vir.0.82210-0
    • Stiasny, K.; Heinz, F.X. Flavivirus membrane fusion. J. Gen. Virol., 2006,87(10),2755-2766. (Pubitemid 44463884)
    • (2006) Journal of General Virology , vol.87 , Issue.10 , pp. 2755-2766
    • Stiasny, K.1    Heinz, F.X.2
  • 78
    • 29144497159 scopus 로고    scopus 로고
    • Class II virus membrane fusion proteins
    • DOI 10.1016/j.virol.2005.09.036, PII S0042682205006008
    • Kielian, M. Class II virus membrane fusion proteins. Virology, 2006, 344(1),38-47. (Pubitemid 41814448)
    • (2006) Virology , vol.344 , Issue.1 , pp. 38-47
    • Kielian, M.1
  • 79
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • DOI 10.1038/nrmicro1326, PII N1326
    • Kielian, M.; Rey, F.A. Virus membrane-fusion proteins: More than one way to make a hairpin. Nat. Rev. Microbiol., 2006, 4(1),67-76. (Pubitemid 43135288)
    • (2006) Nature Reviews Microbiology , vol.4 , Issue.1 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 80
    • 34248149810 scopus 로고    scopus 로고
    • Virus membrane fusion
    • DOI 10.1016/j.febslet.2007.01.093, PII S0014579307001664, Membrane Trafficking
    • Weissenhorn, W.; Hinz, A.; Gaudin, Y. Virus membrane fusion. FEBS Lett., 2007,581(11),2150-2155. (Pubitemid 46722604)
    • (2007) FEBS Letters , vol.581 , Issue.11 , pp. 2150-2155
    • Weissenhorn, W.1    Hinz, A.2    Gaudin, Y.3
  • 82
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson, I.A.; Skehel, J.J.; Wiley, D.C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature, 1981, 289(5796), 366-373.
    • (1981) Nature , vol.289 , Issue.5796 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 83
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1.7 angstrom resolution
    • Fass, D.; Harrison, S.C.; Kim, P.S. Retrovirus envelope domain at 1.7 angstrom resolution Nat. Struct. Biol.; 1996, 3(5), 465-469.
    • (1996) Nat. Struct. Biol. , vol.3 , Issue.5 , pp. 465-469
    • Fass, D.1    Harrison, S.C.2    Kim, P.S.3
  • 84
    • 0032214714 scopus 로고    scopus 로고
    • Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
    • Weissenhorn, W.; Carfi, A.; Lee, K.H.; Skehel, J.J.; Wiley, D.C. Crystal structure of the Ebola virus membrane fusion subunit; GP2; from the envelope glycoprotein ectodomain. Molecular. Cell.; 1998, 2(5), 605-616. (Pubitemid 128379086)
    • (1998) Molecular Cell , vol.2 , Issue.5 , pp. 605-616
    • Weissenhorn, W.1    Carfi, A.2    Lee, K.-H.3    Skehel, J.J.4    Wiley, D.C.5
  • 85
    • 3142663245 scopus 로고    scopus 로고
    • Structural basis for coronavirus-mediated membrane fusion: Crystal structure of mouse hepatitis virus spike protein fusion core
    • DOI 10.1074/jbc.M403760200
    • Xu, Y.; Liu, Y.; Lou, Z.; Qin, L.; Li, X.; Bai, Z.; Pang, H.; Tien, P.; Gao, G.F.; Rao, Z. Structural basis for coronavirus-mediated membrane fusion: Crystal structure of mouse hepatitis virus spike protein fusion core. J. Biol. Chem.; 2004, 279(29), 30514-30522. (Pubitemid 38937982)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.29 , pp. 30514-30522
    • Xu, Y.1    Liu, Y.2    Lou, Z.3    Qin, L.4    Li, X.5    Bai, Z.6    Pang, H.7    Tien, P.8    Gao, G.F.9    Rao, Z.10
  • 86
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • DOI 10.1038/nature04322
    • Yin, H.S.; Wen, X.; Paterson, R.G.; Lamb, R.A.; Jardetzky, T.S. Structure of the parainfluenza virus 5 F protein in its metastable; prefusion conformation. Nature, 2006, 439 (7072), 38-44. (Pubitemid 43053622)
    • (2006) Nature , vol.439 , Issue.7072 , pp. 38-44
    • Yin, H.-S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 87
    • 11144340301 scopus 로고    scopus 로고
    • Class I and class II viral fusion protein structures reveal similar principles in membrane fusion
    • DOI 10.1080/09687860400017784
    • Schibli, D.J.; Weissenhorn, W. Class I and class II viral fusion protein structures reveal similar principles in membrane fusion. Mol. Membr. Biol., 2004, 21(6), 361-371. (Pubitemid 40030212)
    • (2004) Molecular Membrane Biology , vol.21 , Issue.6 , pp. 361-371
    • Schibli, D.J.1    Weissenhorn, W.2
  • 88
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • Rey, F.A.; Heinz, F.X.; Mandl, C.; Kunz, C.; Harrison, S.C. The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature, 1995, 375(6529), 291-298.
    • (1995) Nature , vol.375 , Issue.6529 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 89
    • 0035815282 scopus 로고    scopus 로고
    • The fusion glycoprotein shell of Semliki Forest virus: An icosahedral assembly primed for fusogenic activation at endosomal pH
    • DOI 10.1016/S0092-8674(01)00303-8
    • Lescar, J.; Roussel, A.; Wien, M.W.; Navaza, J.; Fuller, S.D.; Wengler, G.; Wengler, G.; Rey, F.A. The Fusion glycoprotein shellof Semliki Forest virus: An icosahedral assembly primed for fusogenic activation at endosomal pH. Cell, 2001,105(1),137-148. (Pubitemid 32323923)
    • (2001) Cell , vol.105 , Issue.1 , pp. 137-148
    • Lescar, J.1    Roussel, A.2    Wien, M.W.3    Navaza, J.4    Fuller, S.D.5    Wengler, G.6    Wengler, G.7    Rey, F.A.8
  • 91
    • 33745974537 scopus 로고    scopus 로고
    • Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G
    • DOI 10.1126/science.1127683
    • Roche, S.; Bressanelli, S.; Rey, F.A.; Gaudin, Y. Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G. Science, 2006, 313(5784),187-191. (Pubitemid 44066243)
    • (2006) Science , vol.313 , Issue.5784 , pp. 187-191
    • Roche, S.1    Bressanelli, S.2    Rey, F.A.3    Gaudin, Y.4
  • 92
    • 33746005904 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein B from herpes simplex virus 1
    • DOI 10.1126/science.1126548
    • Heldwein, E.E.; Lou, H.; Bender, F.C.; Cohen, G.H.; Eisenberg, R.J.; Harrison, S.C. Crystal structure of glycoprotein B from herpes simplex virus 1. Science, 2006, 313(5784),217-220. (Pubitemid 44066251)
    • (2006) Science , vol.313 , Issue.5784 , pp. 217-220
    • Heldwein, E.E.1    Lou, H.2    Bender, F.C.3    Cohen, G.H.4    Eisenberg, R.J.5    Harrison, S.C.6
  • 93
    • 53549088587 scopus 로고    scopus 로고
    • The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
    • Kadlec, J.; Loureiro, S.; Abrescia, N.G.; Stuart, D.I.; Jones, I.M. The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines. Nat. Struct. Mol. Biol.; 2008, 15(10), 1024-1030.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , Issue.10 , pp. 1024-1030
    • Kadlec, J.1    Loureiro, S.2    Abrescia, N.G.3    Stuart, D.I.4    Jones, I.M.5
  • 94
    • 62449188223 scopus 로고    scopus 로고
    • Structure of a trimeric variant of the Epstein-Barr virus glycoprotein. B
    • Backovic, M.; Longnecker, R.; Jardetzky, T.S.: Structure of a trimeric variant of the Epstein-Barr virus glycoprotein. B. Proc. Natl. Acad. Sci., U S A, 2009,106,2880-2885.
    • (2009) Proc. Natl. Acad. Sci., U S A , vol.106 , pp. 2880-2885
    • Backovic, M.1    Longnecker, R.2    Jardetzky, T.S.3
  • 96
    • 33847292794 scopus 로고    scopus 로고
    • β-barrel membrane bacterial proteins: Structure, function, assembly and interaction with lipids
    • DOI 10.2174/138920307779941541
    • Galdiero, S.; M. Galdiero.; C. Pedone. β-barrel membrane bacterial proteins: Structure; function; assembly and interaction with lipids. Curr. Protein Pep. Sci., 2007, 8, 63-82. (Pubitemid 46322270)
    • (2007) Current Protein and Peptide Science , vol.8 , Issue.1 , pp. 63-82
    • Galdiero, S.1    Galdiero, M.2    Pedone, C.3
  • 98
    • 70349243416 scopus 로고    scopus 로고
    • Developments in membrane fusion
    • Galdiero, S. Developments In Membrane Fusion. Protein Pep. Lett., 2009, 16 (7),711.
    • (2009) Protein Pep. Lett. , vol.16 , Issue.7 , pp. 711
    • Galdiero, S.1
  • 99
    • 15844404886 scopus 로고    scopus 로고
    • Target cell-specific DNA transfer mediated by a chimeric multidomain protein: Novel non-viral gene delivery system
    • DOI 10.1074/jbc.271.18.10560
    • Fominaya, J.; Wels, W. Target cell-specific DNA transfer mediated by a chimeric multidomain protein-novel non-viral gene delivery system; J. Biol. Chem. 1996, 271,10560-10568. (Pubitemid 26145790)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.18 , pp. 10560-10568
    • Fominaya, J.1    Wels, W.2
  • 100
    • 0029941321 scopus 로고    scopus 로고
    • A novel DNA-peptide complex for efficient gene transfer and expression in mammalian cells
    • Gottschalk, S.; Sparrow, J.T.; Hauer, J.; M.P. Mims, M.P.; Leland, F.E.; Woo, S.L.C.; Smith, L.C. A novel DNA-peptide complex for efficient gene transfer and expression in mammalian cells; Gene Ther. 1996, 3, 448-457. (Pubitemid 26171343)
    • (1996) Gene Therapy , vol.3 , Issue.5 , pp. 448-457
    • Gottschalk, S.1    Sparrow, J.T.2    Hauer, J.3    Mims, M.P.4    Leland, F.E.5    Woo, S.L.C.6    Smith, L.C.7
  • 101
    • 0027496645 scopus 로고
    • Stepwise dismantling of adenovirus 2 during entry into cells
    • DOI 10.1016/0092-8674(93)90382-Z
    • Greber, U.F.; Willetts, M.; Webster, P.; Helenius, A. Stepwise dismantling of adenovirus 2 during entry into cells. Cell, 1993, 75, 477-486. (Pubitemid 23335073)
    • (1993) Cell , vol.75 , Issue.3 , pp. 477-486
    • Greber, U.F.1    Willetts, M.2    Webster, P.3    Helenius, A.4
  • 102
    • 0032502017 scopus 로고    scopus 로고
    • Fluorescent virions: Dynamic tracking of the pathway of adenoviral gene transfer vectors in living cells
    • Leopold, P.L.; Ferris,B.; Grinberg, I.; Worgall, S.; Hackett, N.R.; Crystal, R.G. Fluorescent virions: Dynamic tracking of the pathway of adenoviral gene transfer vectors in living cells; Hum. Gene Ther., 1998, 9, 367-378. (Pubitemid 28085024)
    • (1998) Human Gene Therapy , vol.9 , Issue.3 , pp. 367-378
    • Leopold, P.L.1    Ferris, B.2    Grinberg, I.3    Worgall, S.4    Hackett, N.R.5    Crystal, R.G.6
  • 104
    • 1542609485 scopus 로고    scopus 로고
    • Transduction peptides: From technology to physiology
    • DOI 10.1038/ncb0304-189
    • Joliot, A.; Prochiantz, A. Transduction peptides: From technology to physiology. Nat. Cell Biol., 2004, 6, 189-196. (Pubitemid 38344356)
    • (2004) Nature Cell Biology , vol.6 , Issue.3 , pp. 189-196
    • Joliot, A.1    Prochiantz, A.2
  • 105
    • 33748433244 scopus 로고    scopus 로고
    • Cell-penetrating peptides as vectors for peptide, protein and oligonucleotide delivery
    • DOI 10.1016/j.coph.2006.04.004, PII S1471489206001251, Anti-infectives/New Technologies
    • Mae, M.; Langel, U. Cell-penetrating peptides as vectors for peptide; protein and oligonucleotide delivery. Curr. Opin. Pharmacol., 2006, 6,509-514. (Pubitemid 44340662)
    • (2006) Current Opinion in Pharmacology , vol.6 , Issue.5 , pp. 509-514
    • Mae, M.1    Langel, U.2
  • 106
    • 1042288299 scopus 로고    scopus 로고
    • Insight into the Mechanism of Internalization of the Cell-Penetrating Carrier Peptide Pep-1 through Conformational Analysis
    • DOI 10.1021/bi035682s
    • Deshayes, S.; Heitz, A.; Morris, M.C.; Charnet, P.; Divita, G.; Heitz, F. Insight into the mechanism of internalization of the cellpenetrating carrier peptide Pep-1 through conformational analysis Biochem. 2004, 43, 1449-1457. (Pubitemid 38200550)
    • (2004) Biochemistry , vol.43 , Issue.6 , pp. 1449-1457
    • Deshayes, S.1    Heitz, A.2    Morris, M.C.3    Charnet, P.4    Divita, G.5    Heitz, F.6
  • 107
    • 2942715203 scopus 로고    scopus 로고
    • Primary amphipathic cell-penetrating peptides: Structural requirements and interactions with model membranes
    • DOI 10.1021/bi049298m
    • Deshayes, S.; Plenat, T.; Aldrian-Herrada, G.; Divita, G.; Le Grimellec, C.; Heitz, F.; Primary amphipathic cell-penetrating peptides: Structural requirements and interactions with model membranes Biochem. 2004, 43, 7698-7706. (Pubitemid 38787677)
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7698-7706
    • Deshayes, S.1    Plenat, T.2    Aldrian-Herrada, G.3    Divita, G.4    Le Grimellec, C.5    Heitz, F.6
  • 108
    • 33749385780 scopus 로고    scopus 로고
    • Cell-penetrating peptides and antimicrobial peptides: How different are they?
    • DOI 10.1042/BJ20061100
    • Henriques, S.T.; Melo, M.N; Castanho, M. Cell-penetrating peptides and antimicrobial peptides: How different they are? Biochem. J., 2006, 399, 1-7. (Pubitemid 44505401)
    • (2006) Biochemical Journal , vol.399 , Issue.1 , pp. 1-7
    • Henriques, S.T.1    Melo, M.N.2    Castanho, M.A.R.B.3
  • 110
    • 77951225648 scopus 로고    scopus 로고
    • Insight into the cellular uptake mechanism of a secondary amphipathic cellpenetrating peptide for siRNA delivery
    • Konate, K.; Crombez, L.; Deshayes, S.; Decaffmeyer, M.; Thomas, A.; Brasseur, R.; Aldrian, G.; Heitz, F.; Divita, G. Insight into the cellular uptake mechanism of a secondary amphipathic cellpenetrating peptide for siRNA delivery. Biochem., 2010, 49(16), 3393-3402.
    • (2010) Biochem. , vol.49 , Issue.16 , pp. 3393-3402
    • Konate, K.1    Crombez, L.2    Deshayes, S.3    Decaffmeyer, M.4    Thomas, A.5    Brasseur, R.6    Aldrian, G.7    Heitz, F.8    Divita, G.9
  • 111
    • 33646532237 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells: Application to the delivery of antibodies and therapeutic proteins
    • (Celis; J. E.; ed
    • Morris, M.C.; Depollier, J.; Mery, J.; Heitz, F.; Divita, G. A peptide carrier for the delivery of biologically active proteins into mammalian cells: Application to the delivery of antibodies and therapeutic proteins. In cell Biology: A Laboratory Handbook (Celis; J. E.; ed.) 2006, 4, 13-18.
    • (2006) Cell Biology: A Laboratory Handbook , vol.4 , pp. 13-18
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 112
    • 1542569535 scopus 로고    scopus 로고
    • Making proteins into drugs: Assisted delivery of proteins and peptides into living neurons
    • Gallo, G. Making proteins into drugs: Assisted delivery of proteins and peptides into living neurons. Methods Cell Biol., 2003, 71, 325-338.
    • (2003) Methods Cell Biol. , vol.71 , pp. 325-338
    • Gallo, G.1
  • 113
    • 42149177168 scopus 로고    scopus 로고
    • Translocation or membrane disintegration? Implication of peptide-membrane interactions in pep-1 activity
    • DOI 10.1002/psc.1003
    • Henriques, S.T.; Castanho, M. ARB.; translocation or membrane disintegration? Implication of peptide-membrane interactions in pep-1 activity. J. Pept. Sci., 2008, 14, 482-487. (Pubitemid 351540910)
    • (2008) Journal of Peptide Science , vol.14 , Issue.4 , pp. 482-487
    • Henriques, S.T.1    Castanho, M.A.R.B.2
  • 114
    • 67651211690 scopus 로고    scopus 로고
    • Enhanced gene expression by a novel stearylated INF7 peptide derivative through fusion independent endosomal escape
    • El-Sayed, A.; Masuda, T.; Khalil, I.; Akita, H.; Harashima, H. Enhanced gene expression by a novel stearylated INF7 peptide derivative through fusion independent endosomal escape. J.Control Release, 2009, 138(2), 160-167.
    • (2009) J.Control Release , vol.138 , Issue.2 , pp. 160-167
    • El-Sayed, A.1    Masuda, T.2    Khalil, I.3    Akita, H.4    Harashima, H.5
  • 115
    • 74549132183 scopus 로고    scopus 로고
    • Fusion of a short HA2-derived peptide sequence to cell-penetrating peptides improves cytosolyc uptake; but enhances cytotoxic activity
    • Neundorf, I.; Rennert, R.; Hoyer, J.; Schramm, F.; Lobner, K.; Kitanovic, I.; Wolfl, S. Fusion of a short HA2-derived peptide sequence to cell-penetrating peptides improves cytosolyc uptake; but enhances cytotoxic activity Pharmac., 2009, 2, 49-65.
    • (2009) Pharmac. , vol.2 , pp. 49-65
    • Neundorf, I.1    Rennert, R.2    Hoyer, J.3    Schramm, F.4    Lobner, K.5    Kitanovic, I.6    Wolfl, S.7
  • 117
    • 36849070485 scopus 로고    scopus 로고
    • Degradable-brushed pHEMA-pDMAEMA synthesized via ATRP and click chemistry for gene delivery
    • DOI 10.1021/bc0701186
    • Jiang, X.; Lok, M.C.; Hennink, W.E. Degradable-brushed pHEMA-pDMAEMA synthesized via ATRP and click chemistry for gene delivery; Bioconjugate Chemistry, 2007, 18 (6), 2077-2084. (Pubitemid 350220011)
    • (2007) Bioconjugate Chemistry , vol.18 , Issue.6 , pp. 2077-2084
    • Jiang, X.1    Lok, M.C.2    Hennink, W.E.3
  • 118
    • 0037178877 scopus 로고    scopus 로고
    • Functional characterization of an endosome-disruptive peptide and its application in cytosolic delivery of immunoliposome-entrapped proteins
    • DOI 10.1074/jbc.M200429200
    • Mastrobattista, E.; Koning, G.A.; Van Bloois, L.; Filipe, A.C.; Jiskoot, W.; Storm, G.; Functional characterization of an endosome-disruptive peptide and its application in cytosolic delivery of immunoliposome-entrapped proteins; J. Biol. Chem. 2002, 277 (30), 27135-27143. (Pubitemid 34951728)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 27135-27143
    • Mastrobattista, E.1    Koning, G.A.2    Van Bloois, L.3    Filipe, A.C.S.4    Jiskoot, W.5    Storm, G.6
  • 119
    • 21344450090 scopus 로고    scopus 로고
    • Strategies for cytosolic delivery of liposomal macromolecules
    • DOI 10.1016/j.ijpharm.2005.02.040, PII S0378517305002474, Selected Contribution from the 5th European Workshop on Particulate Systems
    • Fretz, M.M.; Mastrobattista, E., Koning, G.A.; Jiskoot, W.; Storm, G.; Strategies for cytosolic delivery of liposomal macromolecules; Int. J. Pharmac., 2005, 298 (2), 305-309. (Pubitemid 40910733)
    • (2005) International Journal of Pharmaceutics , vol.298 , Issue.2 , pp. 305-309
    • Fretz, M.M.1    Mastrobattista, E.2    Koning, G.A.3    Jiskoot, W.4    Storm, G.5
  • 120
    • 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
    • DOI 10.1093/nar/gkg385
    • Simeoni, F.; Morris, M. C.; 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, 2717-2724. (Pubitemid 37442116)
    • (2003) Nucleic Acids Research , vol.31 , Issue.11 , pp. 2717-2724
    • Simeoni, F.1    Morris, M.C.2    Heitz, F.3    Divita, G.4
  • 122
    • 76749147768 scopus 로고    scopus 로고
    • Role of membranotropic sequences from herpes simplex virus type I glycoproteins B and H in the fusion process
    • Galdiero, S.; Falanga, A.; Vitiello, G.; Vitiello, M.; Pedone, C.; D'Errico, G.; Galdiero, M. Role of membranotropic sequences from herpes simplex virus type I glycoproteins B and H in the fusion process. Biochim, Biophys, Acta. 2010, 1798(3), 579-591.
    • (2010) Biochim, Biophys, Acta. , vol.1798 , Issue.3 , pp. 579-591
    • Galdiero, S.1    Falanga, A.2    Vitiello, G.3    Vitiello, M.4    Pedone, C.5    D'Errico, G.6    Galdiero, M.7
  • 124
    • 46649091525 scopus 로고    scopus 로고
    • A fusogenic segment of glycoprotein H from herpes simplex virus enhances transfection efficiency of cationic liposomes
    • DOI 10.1002/jgm.1184
    • Tu, Y.; Kim, J.S. A fusogenic segment of glycoprotein H from herpes simplex virus enhances transfection efficiency of cationic liposomes. J. Gene Med., 2008,10, 646-654. (Pubitemid 351936537)
    • (2008) Journal of Gene Medicine , vol.10 , Issue.6 , pp. 646-654
    • Tu, Y.1    Kim, J.-S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.