메뉴 건너뛰기




Volumn 354, Issue 1-2, 2008, Pages 39-48

Octaarginine-modified liposomes: Enhanced cellular uptake and controlled intracellular trafficking

Author keywords

Endocytosis; Gene delivery; Intracellular trafficking; Liposomes; Octaarginine

Indexed keywords

AMILORIDE; ARGININE; CLATHRIN; CYTOCHALASIN D; GENISTEIN; LIPOFECTAMINE; LIPOSOME; METHYL BETA CYCLODEXTRIN; NUCLEIC ACID; NYSTATIN; OCTAARGININE; OLIGOARGININE DERIVATIVE; PENETRATIN; PEPTIDE; UNCLASSIFIED DRUG; VIRUS VECTOR;

EID: 40849140747     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2007.12.003     Document Type: Short Survey
Times cited : (101)

References (68)
  • 1
    • 1642443376 scopus 로고    scopus 로고
    • Quantitative three-dimensional analysis of the intracellular trafficking of plasmid DNA transfected by a nonviral gene delivery system using confocal laser scanning microscopy
    • Akita H., Ito R., Khalil I.A., Futaki S., and Harashima H. Quantitative three-dimensional analysis of the intracellular trafficking of plasmid DNA transfected by a nonviral gene delivery system using confocal laser scanning microscopy. Mol. Ther. 9 (2004) 443-451
    • (2004) Mol. Ther. , vol.9 , pp. 443-451
    • Akita, H.1    Ito, R.2    Khalil, I.A.3    Futaki, S.4    Harashima, H.5
  • 2
    • 0026545612 scopus 로고
    • Potocytosis: sequestration and transport of small molecules by caveolae
    • Anderson R.G., Kamen B.A., Rothberg K.G., and Lacey S.W. Potocytosis: sequestration and transport of small molecules by caveolae. Science 255 (1992) 410-411
    • (1992) Science , vol.255 , pp. 410-411
    • Anderson, R.G.1    Kamen, B.A.2    Rothberg, K.G.3    Lacey, S.W.4
  • 3
    • 0033756398 scopus 로고    scopus 로고
    • Transduction of TAT-HA-beta-galactosidase fusion protein into salivary gland-derived cells and organ cultures of the developing gland, and into rat submandibular gland in vivo
    • Barka T., Gresik E.W., and van Der Noen H. Transduction of TAT-HA-beta-galactosidase fusion protein into salivary gland-derived cells and organ cultures of the developing gland, and into rat submandibular gland in vivo. J. Histochem. Cytochem. 48 (2000) 1453-1460
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 1453-1460
    • Barka, T.1    Gresik, E.W.2    van Der Noen, H.3
  • 4
    • 0037333830 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan as a plasma membrane carrier
    • Belting M. Heparan sulfate proteoglycan as a plasma membrane carrier. Trends Biochem. Sci. 28 (2003) 145-151
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 145-151
    • Belting, M.1
  • 5
    • 13844256698 scopus 로고    scopus 로고
    • Tat peptide-mediated cellular delivery: back to basics
    • Brooks H., Lebleu B., and Vives E. Tat peptide-mediated cellular delivery: back to basics. Adv. Drug Deliv. Rev. 57 (2005) 559-577
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 559-577
    • Brooks, H.1    Lebleu, B.2    Vives, E.3
  • 7
    • 2442670068 scopus 로고    scopus 로고
    • Endosome disruption enhances the functional nuclear delivery of Tat-fusion proteins
    • Caron N.J., Quenneville S.P., and Tremblay J.P. Endosome disruption enhances the functional nuclear delivery of Tat-fusion proteins. Biochem. Biophys. Res. Commun. 319 (2004) 12-20
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 12-20
    • Caron, N.J.1    Quenneville, S.P.2    Tremblay, J.P.3
  • 8
    • 33646343208 scopus 로고    scopus 로고
    • Increased intracellular targeting to airway cells using octaarginine-coated liposomes: in vitro assessment of their suitability for inhalation
    • Cryan S.A., Devocelle M., Moran P.J., Hickey A.J., and Kelly J.G. Increased intracellular targeting to airway cells using octaarginine-coated liposomes: in vitro assessment of their suitability for inhalation. Mol. Pharm. 3 (2006) 104-112
    • (2006) Mol. Pharm. , vol.3 , pp. 104-112
    • Cryan, S.A.1    Devocelle, M.2    Moran, P.J.3    Hickey, A.J.4    Kelly, J.G.5
  • 9
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • Derossi D., Calvet S., Trembleau A., Brunissen A., Chassaing G., and Prochiantz A. Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J. Biol. Chem. 271 (1996) 18188-18193
    • (1996) J. Biol. Chem. , vol.271 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 10
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: the penetratin system for intracellular delivery
    • Derossi D., Chassaing G., and Prochiantz A. Trojan peptides: the penetratin system for intracellular delivery. Trends Cell Biol. 8 (1998) 84-87
    • (1998) Trends Cell Biol. , vol.8 , pp. 84-87
    • Derossi, D.1    Chassaing, G.2    Prochiantz, A.3
  • 11
    • 5644276383 scopus 로고    scopus 로고
    • Delivery of bioactive molecules into the cell: the Trojan horse approach
    • Dietz G.P., and Bahr M. Delivery of bioactive molecules into the cell: the Trojan horse approach. Mol. Cell Neurosci. 27 (2004) 85-131
    • (2004) Mol. Cell Neurosci. , vol.27 , pp. 85-131
    • Dietz, G.P.1    Bahr, M.2
  • 12
    • 0035078052 scopus 로고    scopus 로고
    • Physico-chemical requirements for cellular uptake of pAntp peptide. Role of lipid-binding affinity
    • Drin G., Mazel M., Clair P., Mathieu D., Kaczorek M., and Temsamani J. Physico-chemical requirements for cellular uptake of pAntp peptide. Role of lipid-binding affinity. Eur. J. Biochem. 268 (2001) 1304-1314
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1304-1314
    • Drin, G.1    Mazel, M.2    Clair, P.3    Mathieu, D.4    Kaczorek, M.5    Temsamani, J.6
  • 14
    • 14044250982 scopus 로고    scopus 로고
    • Formation and intracellular trafficking of lipoplexes and polyplexes
    • Elouahabi A., and Ruysschaert J.M. Formation and intracellular trafficking of lipoplexes and polyplexes. Mol. Ther. 11 (2005) 336-347
    • (2005) Mol. Ther. , vol.11 , pp. 336-347
    • Elouahabi, A.1    Ruysschaert, J.M.2
  • 15
    • 0029067792 scopus 로고
    • The role of dioleoyl phosphatidylethanolamine in cationic liposome mediated gene transfer
    • Farhood H., Serbina N., and Huang L. The role of dioleoyl phosphatidylethanolamine in cationic liposome mediated gene transfer. Biochim. Biophys. Acta 1235 (1995) 289-295
    • (1995) Biochim. Biophys. Acta , vol.1235 , pp. 289-295
    • Farhood, H.1    Serbina, N.2    Huang, L.3
  • 16
    • 0042355293 scopus 로고    scopus 로고
    • Caveolae-mediated internalization of extracellular HIV-1 tat fusion proteins visualized in real time
    • Ferrari A., Pellegrini V., Arcangeli C., Fittipaldi A., Giacca M., and Beltram F. Caveolae-mediated internalization of extracellular HIV-1 tat fusion proteins visualized in real time. Mol. Ther. 8 (2003) 284-294
    • (2003) Mol. Ther. , vol.8 , pp. 284-294
    • Ferrari, A.1    Pellegrini, V.2    Arcangeli, C.3    Fittipaldi, A.4    Giacca, M.5    Beltram, F.6
  • 17
    • 1842529513 scopus 로고    scopus 로고
    • A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides
    • Fischer R., Kohler K., Fotin-Mleczek M., and Brock R. A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides. J. Biol. Chem. 279 (2004) 12625-12635
    • (2004) J. Biol. Chem. , vol.279 , pp. 12625-12635
    • Fischer, R.1    Kohler, K.2    Fotin-Mleczek, M.3    Brock, R.4
  • 19
    • 11844302810 scopus 로고    scopus 로고
    • Decoding the entry of two novel cell-penetrating peptides in HeLa cells: lipid raft-mediated endocytosis and endosomal escape
    • Foerg C., Ziegler U., Fernandez-Carneado J., Giralt E., Rennert R., Beck-Sickinger A.G., and Merkle H.P. Decoding the entry of two novel cell-penetrating peptides in HeLa cells: lipid raft-mediated endocytosis and endosomal escape. Biochemistry 44 (2005) 72-81
    • (2005) Biochemistry , vol.44 , pp. 72-81
    • Foerg, C.1    Ziegler, U.2    Fernandez-Carneado, J.3    Giralt, E.4    Rennert, R.5    Beck-Sickinger, A.G.6    Merkle, H.P.7
  • 21
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • Futaki S., Suzuki T., Ohashi W., Yagami T., Tanaka S., Ueda K., and Sugiura Y. Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276 (2001) 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    Sugiura, Y.7
  • 23
    • 2442663176 scopus 로고    scopus 로고
    • Arginine carrier peptide bearing Ni(II) chelator to promote cellular uptake of histidine-tagged proteins
    • Futaki S., Niwa M., Nakase I., Tadokoro A., Zhang Y., Nagaoka M., Wakako N., and Sugiura Y. Arginine carrier peptide bearing Ni(II) chelator to promote cellular uptake of histidine-tagged proteins. Bioconjug. Chem. 15 (2004) 475-481
    • (2004) Bioconjug. Chem. , vol.15 , pp. 475-481
    • Futaki, S.1    Niwa, M.2    Nakase, I.3    Tadokoro, A.4    Zhang, Y.5    Nagaoka, M.6    Wakako, N.7    Sugiura, Y.8
  • 24
    • 13844272399 scopus 로고    scopus 로고
    • Membrane-permeable arginine-rich peptides and the translocation mechanisms
    • Futaki S. Membrane-permeable arginine-rich peptides and the translocation mechanisms. Adv. Drug Deliv. Rev. 57 (2005) 547-558
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 547-558
    • Futaki, S.1
  • 25
    • 13844298046 scopus 로고    scopus 로고
    • Intracellular delivery of large molecules and small particles by cell-penetrating proteins and peptides
    • Gupta B., Levchenko T.S., and Torchilin V.P. Intracellular delivery of large molecules and small particles by cell-penetrating proteins and peptides. Adv. Drug Deliv. Rev. 57 (2005) 637-651
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 637-651
    • Gupta, B.1    Levchenko, T.S.2    Torchilin, V.P.3
  • 26
    • 4644329186 scopus 로고    scopus 로고
    • HIV-1 Tat protein transduction domain peptide facilitates gene transfer in combination with cationic liposomes
    • Hyndman L., Lemoine J.L., Huang L., Porteous D.J., Boyd A.C., and Nan X. HIV-1 Tat protein transduction domain peptide facilitates gene transfer in combination with cationic liposomes. J. Control. Release 99 (2004) 435-444
    • (2004) J. Control. Release , vol.99 , pp. 435-444
    • Hyndman, L.1    Lemoine, J.L.2    Huang, L.3    Porteous, D.J.4    Boyd, A.C.5    Nan, X.6
  • 27
    • 33746084052 scopus 로고    scopus 로고
    • Cellular uptake and subsequent intracellular trafficking of R8-liposomes introduced at low temperature
    • Iwasa A., Akita H., Khalil I., Kogure K., Futaki S., and Harashima H. Cellular uptake and subsequent intracellular trafficking of R8-liposomes introduced at low temperature. Biochim. Biophys. Acta 1758 (2006) 713-720
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 713-720
    • Iwasa, A.1    Akita, H.2    Khalil, I.3    Kogure, K.4    Futaki, S.5    Harashima, H.6
  • 28
    • 11144356131 scopus 로고    scopus 로고
    • The use of cell-penetrating peptides as a tool for gene regulation
    • Jarver P., and Langel U. The use of cell-penetrating peptides as a tool for gene regulation. Drug Discov. Today 9 (2004) 395-402
    • (2004) Drug Discov. Today , vol.9 , pp. 395-402
    • Jarver, P.1    Langel, U.2
  • 29
    • 2442421428 scopus 로고    scopus 로고
    • Transferrin-modified liposomes equipped with a pH-sensitive fusogenic peptide: an artificial viral-like delivery system
    • Kakudo T., Chaki S., Futaki S., Nakase I., Akaji K., Kawakami T., Maruyama K., Kamiya H., and Harashima H. Transferrin-modified liposomes equipped with a pH-sensitive fusogenic peptide: an artificial viral-like delivery system. Biochemistry 43 (2004) 5618-5628
    • (2004) Biochemistry , vol.43 , pp. 5618-5628
    • Kakudo, T.1    Chaki, S.2    Futaki, S.3    Nakase, I.4    Akaji, K.5    Kawakami, T.6    Maruyama, K.7    Kamiya, H.8    Harashima, H.9
  • 30
    • 11844268027 scopus 로고    scopus 로고
    • Cationic TAT peptide transduction domain enters cells by macropinocytosis
    • Kaplan I.M., Wadia J.S., and Dowdy S.F. Cationic TAT peptide transduction domain enters cells by macropinocytosis. J. Control. Release 102 (2005) 247-253
    • (2005) J. Control. Release , vol.102 , pp. 247-253
    • Kaplan, I.M.1    Wadia, J.S.2    Dowdy, S.F.3
  • 31
    • 1642578411 scopus 로고    scopus 로고
    • Mechanism of improved gene transfer by the N-terminal stearylation of octaarginine: enhanced cellular association by hydrophobic core formation
    • Khalil I.A., Futaki S., Niwa M., Baba Y., Kaji N., Kamiya H., and Harashima H. Mechanism of improved gene transfer by the N-terminal stearylation of octaarginine: enhanced cellular association by hydrophobic core formation. Gene Ther. 11 (2004) 636-644
    • (2004) Gene Ther. , vol.11 , pp. 636-644
    • Khalil, I.A.1    Futaki, S.2    Niwa, M.3    Baba, Y.4    Kaji, N.5    Kamiya, H.6    Harashima, H.7
  • 32
    • 33644593889 scopus 로고    scopus 로고
    • Uptake pathways and subsequent intracellular trafficking in nonviral gene delivery
    • Khalil I.A., Kogure K., Akita H., and Harashima H. Uptake pathways and subsequent intracellular trafficking in nonviral gene delivery. Pharmacol. Rev. 58 (2006) 32-45
    • (2006) Pharmacol. Rev. , vol.58 , pp. 32-45
    • Khalil, I.A.1    Kogure, K.2    Akita, H.3    Harashima, H.4
  • 33
    • 33645640345 scopus 로고    scopus 로고
    • High density of octaarginine stimulates macropinocytosis leading to efficient intracellular trafficking for gene expression
    • Khalil I.A., Kogure K., Futaki S., and Harashima H. High density of octaarginine stimulates macropinocytosis leading to efficient intracellular trafficking for gene expression. J. Biol. Chem. 281 (2006) 3544-3551
    • (2006) J. Biol. Chem. , vol.281 , pp. 3544-3551
    • Khalil, I.A.1    Kogure, K.2    Futaki, S.3    Harashima, H.4
  • 35
    • 3242657221 scopus 로고    scopus 로고
    • Development of a non-viral multifunctional envelope-type nano device by a novel lipid film hydration method
    • Kogure K., Moriguchi R., Sasaki K., Ueno M., Futaki S., and Harashima H. Development of a non-viral multifunctional envelope-type nano device by a novel lipid film hydration method. J. Control. Release 98 (2004) 317-323
    • (2004) J. Control. Release , vol.98 , pp. 317-323
    • Kogure, K.1    Moriguchi, R.2    Sasaki, K.3    Ueno, M.4    Futaki, S.5    Harashima, H.6
  • 36
    • 0029117498 scopus 로고
    • The emergence of clathrin-independent pinocytic pathways
    • Lamaze C., and Schmid S.L. The emergence of clathrin-independent pinocytic pathways. Curr. Opin. Cell Biol. 7 (1995) 573-580
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 573-580
    • Lamaze, C.1    Schmid, S.L.2
  • 39
    • 0031800381 scopus 로고    scopus 로고
    • Novel applications of liposomes
    • Lasic D.D. Novel applications of liposomes. Trends Biotechnol. 16 (1998) 307-321
    • (1998) Trends Biotechnol. , vol.16 , pp. 307-321
    • Lasic, D.D.1
  • 41
    • 3843050301 scopus 로고    scopus 로고
    • Enhanced heparan sulfate proteoglycan-mediated uptake of cell-penetrating peptide-modified liposomes
    • Marty C., Meylan C., Schott H., Ballmer-Hofer K., and Schwendener R.A. Enhanced heparan sulfate proteoglycan-mediated uptake of cell-penetrating peptide-modified liposomes. Cell Mol. Life Sci. 61 (2004) 1785-1794
    • (2004) Cell Mol. Life Sci. , vol.61 , pp. 1785-1794
    • Marty, C.1    Meylan, C.2    Schott, H.3    Ballmer-Hofer, K.4    Schwendener, R.A.5
  • 42
    • 0037119944 scopus 로고    scopus 로고
    • Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake
    • Meier O., Boucke K., Hammer S.V., Keller S., Stidwill R.P., Hemmi S., and Greber U.F. Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake. J. Cell Biol. 158 (2002) 1119-1131
    • (2002) J. Cell Biol. , vol.158 , pp. 1119-1131
    • Meier, O.1    Boucke, K.2    Hammer, S.V.3    Keller, S.4    Stidwill, R.P.5    Hemmi, S.6    Greber, U.F.7
  • 43
    • 0032475867 scopus 로고    scopus 로고
    • Proteoglycans mediate cationic liposome-DNA complex-based gene delivery in vitro and in vivo
    • Mounkes L.C., Zhong W., Cipres-Palacin G., Heath T.D., and Debs R.J. Proteoglycans mediate cationic liposome-DNA complex-based gene delivery in vitro and in vivo. J. Biol. Chem. 273 (1998) 26164-26170
    • (1998) J. Biol. Chem. , vol.273 , pp. 26164-26170
    • Mounkes, L.C.1    Zhong, W.2    Cipres-Palacin, G.3    Heath, T.D.4    Debs, R.J.5
  • 46
    • 17644386231 scopus 로고    scopus 로고
    • Cellular uptake of unconjugated TAT peptide involves clathrin-dependent endocytosis and heparan sulfate receptors
    • Richard J.P., Melikov K., Brooks H., Prevot P., Lebleu B., and Chernomordik L.V. Cellular uptake of unconjugated TAT peptide involves clathrin-dependent endocytosis and heparan sulfate receptors. J. Biol. Chem. 280 (2005) 15300-15306
    • (2005) J. Biol. Chem. , vol.280 , pp. 15300-15306
    • Richard, J.P.1    Melikov, K.2    Brooks, H.3    Prevot, P.4    Lebleu, B.5    Chernomordik, L.V.6
  • 47
    • 0038176513 scopus 로고    scopus 로고
    • Oligomers of the arginine-rich motif of the HIV-1 TAT protein are capable of transferring plasmid DNA into cells
    • Rudolph C., Plank C., Lausier J., Schillinger U., Muller R.H., and Rosenecker J. Oligomers of the arginine-rich motif of the HIV-1 TAT protein are capable of transferring plasmid DNA into cells. J. Biol. Chem. 278 (2003) 11411-11418
    • (2003) J. Biol. Chem. , vol.278 , pp. 11411-11418
    • Rudolph, C.1    Plank, C.2    Lausier, J.3    Schillinger, U.4    Muller, R.H.5    Rosenecker, J.6
  • 48
    • 0344389048 scopus 로고    scopus 로고
    • Interactions of polymeric and liposomal gene delivery systems with extracellular glycosaminoglycans: physicochemical and transfection studies
    • Ruponen M., Yla-Herttuala S., and Urtti A. Interactions of polymeric and liposomal gene delivery systems with extracellular glycosaminoglycans: physicochemical and transfection studies. Biochim. Biophys. Acta 1415 (1999) 331-341
    • (1999) Biochim. Biophys. Acta , vol.1415 , pp. 331-341
    • Ruponen, M.1    Yla-Herttuala, S.2    Urtti, A.3
  • 50
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: an integrated process
    • Schmid S.L. Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu. Rev. Biochem. 66 (1997) 511-548
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 51
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: delivery of a biologically active protein into the mouse
    • Schwarze S.R., Ho A., Vocero-Akbani A., and Dowdy S.F. In vivo protein transduction: delivery of a biologically active protein into the mouse. Science 285 (1999) 1569-1572
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 52
    • 0034237577 scopus 로고    scopus 로고
    • Protein transduction: unrestricted delivery into all cells?
    • Schwarze S.R., Hruska K.A., and Dowdy S.F. Protein transduction: unrestricted delivery into all cells?. Trends Cell Biol. 10 (2000) 290-295
    • (2000) Trends Cell Biol. , vol.10 , pp. 290-295
    • Schwarze, S.R.1    Hruska, K.A.2    Dowdy, S.F.3
  • 53
    • 1542721107 scopus 로고    scopus 로고
    • Cell penetrating peptides in drug delivery
    • Snyder E.L., and Dowdy S.F. Cell penetrating peptides in drug delivery. Pharm. Res. 21 (2004) 389-393
    • (2004) Pharm. Res. , vol.21 , pp. 389-393
    • Snyder, E.L.1    Dowdy, S.F.2
  • 54
    • 0037169486 scopus 로고    scopus 로고
    • Possible existence of common internalization mechanisms among arginine-rich peptides
    • Suzuki T., Futaki S., Niwa M., Tanaka S., Ueda K., and Sugiura Y. Possible existence of common internalization mechanisms among arginine-rich peptides. J. Biol. Chem. 277 (2002) 2437-2443
    • (2002) J. Biol. Chem. , vol.277 , pp. 2437-2443
    • Suzuki, T.1    Futaki, S.2    Niwa, M.3    Tanaka, S.4    Ueda, K.5    Sugiura, Y.6
  • 56
    • 0035902477 scopus 로고    scopus 로고
    • TAT peptide on the surface of liposomes affords their efficient intracellular delivery even at low temperature and in the presence of metabolic inhibitors
    • Torchilin V.P., Rammohan R., Weissig V., and Levchenko T.S. TAT peptide on the surface of liposomes affords their efficient intracellular delivery even at low temperature and in the presence of metabolic inhibitors. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 8786-8791
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8786-8791
    • Torchilin, V.P.1    Rammohan, R.2    Weissig, V.3    Levchenko, T.S.4
  • 58
    • 3843092828 scopus 로고    scopus 로고
    • Chances and pitfalls of cell penetrating peptides for cellular drug delivery
    • Trehin R., and Merkle H.P. Chances and pitfalls of cell penetrating peptides for cellular drug delivery. Eur. J. Pharm. Biopharm. 58 (2004) 209-223
    • (2004) Eur. J. Pharm. Biopharm. , vol.58 , pp. 209-223
    • Trehin, R.1    Merkle, H.P.2
  • 59
    • 0036784335 scopus 로고    scopus 로고
    • Translocation of liposomes into cancer cells by cell-penetrating peptides penetratin and tat: a kinetic and efficacy study
    • Tseng Y.L., Liu J.J., and Hong R.L. Translocation of liposomes into cancer cells by cell-penetrating peptides penetratin and tat: a kinetic and efficacy study. Mol. Pharmacol. 62 (2002) 864-872
    • (2002) Mol. Pharmacol. , vol.62 , pp. 864-872
    • Tseng, Y.L.1    Liu, J.J.2    Hong, R.L.3
  • 60
    • 0035793619 scopus 로고    scopus 로고
    • Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans
    • Tyagi M., Rusnati M., Presta M., and Giacca M. Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans. J. Biol. Chem. 276 (2001) 3254-3261
    • (2001) J. Biol. Chem. , vol.276 , pp. 3254-3261
    • Tyagi, M.1    Rusnati, M.2    Presta, M.3    Giacca, M.4
  • 61
    • 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
    • Vives E., Brodin P., and Lebleu B. A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 272 (1997) 16010-16017
    • (1997) J. Biol. Chem. , vol.272 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 62
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia J.S., Stan R.V., and Dowdy S.F. Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat. Med. 10 (2004) 310-315
    • (2004) Nat. Med. , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 63
    • 33845190449 scopus 로고    scopus 로고
    • Cationic lipids, lipoplexes and intracellular delivery of genes
    • Wasungu L., and Hoekstra D. Cationic lipids, lipoplexes and intracellular delivery of genes. J. Control. Release 116 (2006) 255-264
    • (2006) J. Control. Release , vol.116 , pp. 255-264
    • Wasungu, L.1    Hoekstra, D.2
  • 64
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters
    • Wender P.A., Mitchell D.J., Pattabiraman K., Pelkey E.T., Steinman L., and Rothbard J.B. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 13003-13008
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13003-13008
    • Wender, P.A.1    Mitchell, D.J.2    Pattabiraman, K.3    Pelkey, E.T.4    Steinman, L.5    Rothbard, J.B.6
  • 65
    • 0037359709 scopus 로고    scopus 로고
    • Regulation of cytoskeletal organization by syndecan transmembrane proteoglycans
    • Yoneda A., and Couchman J.R. Regulation of cytoskeletal organization by syndecan transmembrane proteoglycans. Matrix Biol. 22 (2003) 25-33
    • (2003) Matrix Biol. , vol.22 , pp. 25-33
    • Yoneda, A.1    Couchman, J.R.2
  • 66
    • 27744590845 scopus 로고    scopus 로고
    • Cytosolic delivery of a p16-peptide oligoarginine conjugate for inhibiting proliferation of MCF7 cells
    • Zaro J.L., and Shen W.C. Cytosolic delivery of a p16-peptide oligoarginine conjugate for inhibiting proliferation of MCF7 cells. J. Control. Release 108 (2005) 409-417
    • (2005) J. Control. Release , vol.108 , pp. 409-417
    • Zaro, J.L.1    Shen, W.C.2
  • 67
    • 17644419268 scopus 로고    scopus 로고
    • Nonbilayer phase of lipoplex-membrane mixture determines endosomal escape of genetic cargo and transfection efficiency
    • Zuhorn I.S., Bakowsky U., Polushkin E., Visser W.H., Stuart M.C., Engberts J.B., and Hoekstra D. Nonbilayer phase of lipoplex-membrane mixture determines endosomal escape of genetic cargo and transfection efficiency. Mol. Ther. 11 (2005) 801-810
    • (2005) Mol. Ther. , vol.11 , pp. 801-810
    • Zuhorn, I.S.1    Bakowsky, U.2    Polushkin, E.3    Visser, W.H.4    Stuart, M.C.5    Engberts, J.B.6    Hoekstra, D.7
  • 68
    • 34247281921 scopus 로고    scopus 로고
    • Adhesion receptors mediate efficient non-viral gene delivery
    • Zuhorn I.S., Kalicharan D., Robillard G.T., and Hoekstra D. Adhesion receptors mediate efficient non-viral gene delivery. Mol. Ther. 15 (2007) 946-953
    • (2007) Mol. Ther. , vol.15 , pp. 946-953
    • Zuhorn, I.S.1    Kalicharan, D.2    Robillard, G.T.3    Hoekstra, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.