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Volumn 19, Issue 12, 2008, Pages 2363-2374

Comparison of cellular uptake using 22 CPPs in 4 different cell lines

Author keywords

[No Author keywords available]

Indexed keywords

CELL PENETRATING PEPTIDE; PROTEINASE INHIBITOR; TRYPSIN;

EID: 58149099412     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc800194e     Document Type: Article
Times cited : (165)

References (69)
  • 1
    • 33747038452 scopus 로고    scopus 로고
    • Cell-penetrating peptides - a brief introduction
    • Jarver, P., and Langel, U. (2006) Cell-penetrating peptides - a brief introduction. Biochim. Biophys. Acta 1758, 260-3.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 260-263
    • Jarver, P.1    Langel, U.2
  • 2
    • 23944483437 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Tools for intracellular delivery of therapeutics
    • Deshayes, S., Morris, M. C., Divita, G., and Heitz, F. (2005) Cell-penetrating peptides: tools for intracellular delivery of therapeutics. Cell. Mol. Life Sci. 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
  • 3
    • 0036792527 scopus 로고    scopus 로고
    • Peptide-mediated cell delivery: Application in protein target validation
    • Lindsay, M. A. (2002) Peptide-mediated cell delivery: application in protein target validation. Curr. Opin. Pharmacol. 2, 587-94.
    • (2002) Curr. Opin. Pharmacol , vol.2 , pp. 587-594
    • Lindsay, M.A.1
  • 4
    • 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. (2005) Cellular uptake of unconjugated TAT peptide involves clathrin-dependent endocytosis and heparan sulfate receptors. J. Biol. Chem. 280, 15300-6.
    • (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
  • 5
    • 0032501957 scopus 로고    scopus 로고
    • Analytical methods for the characterization of cationic lipid-nucleic acid complexes
    • Ferrari, M. E., Nguyen, C. M., Zelphati, O., Tsai, Y., and Felgner, P. L. (1998) Analytical methods for the characterization of cationic lipid-nucleic acid complexes. Hum. Gene Ther. 9, 341-51.
    • (1998) Hum. Gene Ther , vol.9 , pp. 341-351
    • Ferrari, M.E.1    Nguyen, C.M.2    Zelphati, O.3    Tsai, Y.4    Felgner, P.L.5
  • 7
    • 11844268027 scopus 로고    scopus 로고
    • Cationic TAT peptide transduction domain enters cells by macropinocytosis
    • Kaplan, I. M., Wadia, J. S., and Dowdy, S. F. (2005) Cationic TAT peptide transduction domain enters cells by macropinocytosis. J. Controlled Release 102, 247-53.
    • (2005) J. Controlled Release , vol.102 , pp. 247-253
    • Kaplan, I.M.1    Wadia, J.S.2    Dowdy, S.F.3
  • 8
    • 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. (2004) Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat. Med. 10, 310-5.
    • (2004) Nat. Med , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 9
    • 34250835903 scopus 로고    scopus 로고
    • A comprehensive model for the cellular uptake of cationic cell-penetrating peptides
    • Duchardt, F., Fotin-Mleczek, M., Schwarz, H., Fischer, R., and Brock, R. (2007) A comprehensive model for the cellular uptake of cationic cell-penetrating peptides. Traffic 8, 848-66.
    • (2007) Traffic , vol.8 , pp. 848-866
    • Duchardt, F.1    Fotin-Mleczek, M.2    Schwarz, H.3    Fischer, R.4    Brock, R.5
  • 10
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi, D., Joliot, A. H., Chassaing, G., and Prochiantz, A. (1994) The third helix of the Antennapedia homeodomain translocates through biological membranes. J. Biol. Chem. 269, 10444-50.
    • (1994) J. Biol. Chem , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 11
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • Frankel, A. D., and Pabo, C. O. (1988) Cellular uptake of the tat protein from human immunodeficiency virus. Cell 55, 1189-93.
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 12
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein
    • Green, M., and Loewenstein, P. M. (1988) Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein. Cell 55, 1179-88.
    • (1988) Cell , vol.55 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 14
    • 13844254266 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Mechanism and kinetics of cargo delivery
    • Zorko, M., and Langel, U. (2005) Cell-penetrating peptides: mechanism and kinetics of cargo delivery. Adv. Drug Delivery Rev. 57, 529-45.
    • (2005) Adv. Drug Delivery Rev , vol.57 , pp. 529-545
    • Zorko, M.1    Langel, U.2
  • 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
    • Vives, E., Brodin, P., and Lebleu, B. (1997) A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 272, 16010-7.
    • (1997) J. Biol. Chem , vol.272 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 16
    • 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
    • Oehlke, J., Scheller, A., Wiesner, B., Krause, E., Beyermann, M., Klauschenz, E., Melzig, M., and Bienert, M. (1998) Cellular uptake of an α-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically. Biochim. Biophys. Acta 1414, 127-39.
    • (1998) Biochim. Biophys. Acta , vol.1414 , 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
  • 17
    • 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. (2001) Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276, 5836-40.
    • (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
  • 19
    • 34548162679 scopus 로고    scopus 로고
    • Cell-surface proteoglycans as molecular portals for cationic peptide and polymer entry into cells
    • Poon, G. M., and Gariepy, J. (2007) Cell-surface proteoglycans as molecular portals for cationic peptide and polymer entry into cells. Biochem. Soc. Trans. 35, 788-93.
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 788-793
    • Poon, G.M.1    Gariepy, J.2
  • 20
    • 35048856889 scopus 로고    scopus 로고
    • Cargo-dependent cytotoxicity and delivery efficacy of cell-penetrating peptides: A comparative study
    • El-Andaloussi, S., Jarver, P., Johansson, H. J., and Langel, U. (2007) Cargo-dependent cytotoxicity and delivery efficacy of cell-penetrating peptides: a comparative study. Biochem. J. 407, 285-92.
    • (2007) Biochem. J , vol.407 , pp. 285-292
    • El-Andaloussi, S.1    Jarver, P.2    Johansson, H.J.3    Langel, U.4
  • 21
    • 24344448619 scopus 로고    scopus 로고
    • Cationic cell-penetrating peptides interfere with TNF signalling by induction of TNF receptor internalization
    • Fotin-Mleczek, M., Welte, S., Mader, O., Duchardt, F., Fischer, R., Hufnagel, H., Scheurich, P., and Brock, R. (2005) Cationic cell-penetrating peptides interfere with TNF signalling by induction of TNF receptor internalization. J. Cell Sci. 118, 3339-51.
    • (2005) J. Cell Sci , vol.118 , pp. 3339-3351
    • Fotin-Mleczek, M.1    Welte, S.2    Mader, O.3    Duchardt, F.4    Fischer, R.5    Hufnagel, H.6    Scheurich, P.7    Brock, R.8
  • 22
    • 20444403719 scopus 로고    scopus 로고
    • Effects of cargo molecules on the cellular uptake of arginine-rich cell-penetrating peptides
    • Maiolo, J. R., Ferrer, M., and Ottinger, E. A. (2005) Effects of cargo molecules on the cellular uptake of arginine-rich cell-penetrating peptides. Biochim. Biophys. Acta 1712, 161-72.
    • (2005) Biochim. Biophys. Acta , vol.1712 , pp. 161-172
    • Maiolo, J.R.1    Ferrer, M.2    Ottinger, E.A.3
  • 23
    • 0037908883 scopus 로고    scopus 로고
    • Extending the applicability of carboxyfluorescein in solid-phase synthesis
    • Fischer, R., Mader, O., Jung, G., and Brock, R. (2003) Extending the applicability of carboxyfluorescein in solid-phase synthesis. Bioconjugate Chem. 14, 653-60.
    • (2003) Bioconjugate Chem , vol.14 , pp. 653-660
    • Fischer, R.1    Mader, O.2    Jung, G.3    Brock, R.4
  • 25
    • 39149127301 scopus 로고    scopus 로고
    • Proline-rich, amphipathic cell-penetrating peptides
    • Pujals, S., and Giralt, E. (2008) Proline-rich, amphipathic cell-penetrating peptides. Adv. Drug Delivery Rev. 60, 473-84.
    • (2008) Adv. Drug Delivery Rev , vol.60 , pp. 473-484
    • Pujals, S.1    Giralt, E.2
  • 28
    • 0038743278 scopus 로고    scopus 로고
    • In vitro uptake and stability study of pVEC and its all-D analog
    • Elmquist, A., and Langel, U. (2003) In vitro uptake and stability study of pVEC and its all-D analog. Biol. Chem. 384, 387-93.
    • (2003) Biol. Chem , vol.384 , pp. 387-393
    • Elmquist, A.1    Langel, U.2
  • 29
    • 34249991192 scopus 로고    scopus 로고
    • Peptide degradation is a critical determinant for cell-penetrating peptide uptake
    • Palm, C., Jayamanne, M., Kjellander, M., and Hallbrink, M. (2007) Peptide degradation is a critical determinant for cell-penetrating peptide uptake. Biochim. Biophys. Acta 1768, 1769-76.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1769-1776
    • Palm, C.1    Jayamanne, M.2    Kjellander, M.3    Hallbrink, M.4
  • 30
    • 4744368322 scopus 로고    scopus 로고
    • Metabolic cleavage of cell-penetrating peptides in contact with epithelial models: Human calcitonin (hCT)-derived peptides, Tat(47-57) and penetratin(43-58)
    • Trehin, R., Nielsen, H. M., Jahnke, H. G., Krauss, U., Beck-Sickinger, A. G., and Merkle, H. P. (2004) Metabolic cleavage of cell-penetrating peptides in contact with epithelial models: human calcitonin (hCT)-derived peptides, Tat(47-57) and penetratin(43-58). Biochem. J. 382, 945-56.
    • (2004) Biochem. J , vol.382 , pp. 945-956
    • Trehin, R.1    Nielsen, H.M.2    Jahnke, H.G.3    Krauss, U.4    Beck-Sickinger, A.G.5    Merkle, H.P.6
  • 31
    • 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. (2004) A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides. J. Biol. Chem. 279, 12625-35.
    • (2004) J. Biol. Chem , vol.279 , pp. 12625-12635
    • Fischer, R.1    Kohler, K.2    Fotin-Mleczek, M.3    Brock, R.4
  • 32
    • 34548172649 scopus 로고    scopus 로고
    • Macropinocytosis: Searching for an endocytic identity and role in the uptake of cell penetrating peptides
    • Jones, A. T. (2007) Macropinocytosis: searching for an endocytic identity and role in the uptake of cell penetrating peptides. J. Cell Mol. Med. 11, 670-84.
    • (2007) J. Cell Mol. Med , vol.11 , pp. 670-684
    • Jones, A.T.1
  • 33
    • 34848892144 scopus 로고    scopus 로고
    • Cell penetrating peptides: Intracellular pathways and pharmaceutical perspectives
    • Patel, L. N., Zaro, J. L., and Shen, W. C. (2007) Cell penetrating peptides: intracellular pathways and pharmaceutical perspectives. Pharm. Res. 24, 1977-92.
    • (2007) Pharm. Res , vol.24 , pp. 1977-1992
    • Patel, L.N.1    Zaro, J.L.2    Shen, W.C.3
  • 34
    • 0020638326 scopus 로고
    • Differentiation between attached and ingested immune complexes by a fluorescence quenching cytofluorometric assay
    • Sahlin, S., Hed, J., and Rundquist, I. (1983) Differentiation between attached and ingested immune complexes by a fluorescence quenching cytofluorometric assay. J. Immunol. Methods 60, 115-24.
    • (1983) J. Immunol. Methods , vol.60 , pp. 115-124
    • Sahlin, S.1    Hed, J.2    Rundquist, I.3
  • 35
    • 0344946091 scopus 로고    scopus 로고
    • Uptake of chitosan and associated insulin in Caco-2 cell monolayers: A comparison between chitosan molecules and chitosan nanoparticles
    • Ma, Z., and Lim, L. Y. (2003) Uptake of chitosan and associated insulin in Caco-2 cell monolayers: a comparison between chitosan molecules and chitosan nanoparticles. Pharm. Res. 20, 1812-9.
    • (2003) Pharm. Res , vol.20 , pp. 1812-1819
    • Ma, Z.1    Lim, L.Y.2
  • 36
    • 0027318744 scopus 로고
    • A rapid and simple microfluorometric phagocytosis assay
    • Wan, C. P., Park, C. S., and Lau, B. H. (1993) A rapid and simple microfluorometric phagocytosis assay. J. Immunol. Methods 162, 1-7.
    • (1993) J. Immunol. Methods , vol.162 , pp. 1-7
    • Wan, C.P.1    Park, C.S.2    Lau, B.H.3
  • 38
    • 0033287045 scopus 로고    scopus 로고
    • 2′,7′-Bis-(2- carboxyethyl)-5(6)-carboxyfluorescein as a dual-emission fluorescent indicator of intracellular pH suitable for argon laser confocal microscopy
    • Lanz, E., Slavik, J., and Kotyk, A. (1999) 2′,7′-Bis-(2- carboxyethyl)-5(6)-carboxyfluorescein as a dual-emission fluorescent indicator of intracellular pH suitable for argon laser confocal microscopy. Folia Microbiol. (Praha) 44, 429-34.
    • (1999) Folia Microbiol. (Praha) , vol.44 , pp. 429-434
    • Lanz, E.1    Slavik, J.2    Kotyk, A.3
  • 39
    • 0030037217 scopus 로고    scopus 로고
    • Transbilayer transport of ions and lipids coupled with mastoparan X translocation
    • Matsuzaki, K., Yoneyama, S., Murase, O., and Miyajima, K. (1996) Transbilayer transport of ions and lipids coupled with mastoparan X translocation. Biochemistry 35, 8450-6.
    • (1996) Biochemistry , vol.35 , pp. 8450-8456
    • Matsuzaki, K.1    Yoneyama, S.2    Murase, O.3    Miyajima, K.4
  • 40
    • 9644303253 scopus 로고    scopus 로고
    • Uptake of cell-penetrating peptides is dependent on peptide-tocell ratio rather than on peptide concentration
    • Hallbrink, M., Oehlke, J., Papsdorf, G., and Bienert, M. (2004) Uptake of cell-penetrating peptides is dependent on peptide-tocell ratio rather than on peptide concentration. Biochim. Biophys. Acta 1667, 222-8.
    • (2004) Biochim. Biophys. Acta , vol.1667 , pp. 222-228
    • Hallbrink, M.1    Oehlke, J.2    Papsdorf, G.3    Bienert, M.4
  • 41
    • 33947097525 scopus 로고    scopus 로고
    • Differentiation restricted endocytosis of cell penetrating peptides in MDCK cells corresponds with activities of Rho-GTPases
    • Foerg, C., Ziegler, U., Fernandez-Carneado, J., Giralt, E., and Merkle, H. P. (2007) Differentiation restricted endocytosis of cell penetrating peptides in MDCK cells corresponds with activities of Rho-GTPases. Pharm. Res. 24, 628-42.
    • (2007) Pharm. Res , vol.24 , pp. 628-642
    • Foerg, C.1    Ziegler, U.2    Fernandez-Carneado, J.3    Giralt, E.4    Merkle, H.P.5
  • 42
    • 41149156893 scopus 로고    scopus 로고
    • Cellular internalization and distribution of arginine-rich peptides as a function of extracellular peptide concentration, serum, and plasma membrane associated proteoglycans
    • Kosuge, M., Takeuchi, T., Nakase, I., Jones, A. T., and Futaki, S. (2008) Cellular internalization and distribution of arginine-rich peptides as a function of extracellular peptide concentration, serum, and plasma membrane associated proteoglycans. Bioconjugate Chem. 19, 656-64.
    • (2008) Bioconjugate Chem , vol.19 , pp. 656-664
    • Kosuge, M.1    Takeuchi, T.2    Nakase, I.3    Jones, A.T.4    Futaki, S.5
  • 43
    • 25144520907 scopus 로고    scopus 로고
    • On the mechanisms of the internalization of S4(13)-PV cell-penetrating peptide
    • Mano, M., Teodosio, C., Paiva, A., Simoes, S., and Pedroso de Lima, M. C. (2005) On the mechanisms of the internalization of S4(13)-PV cell-penetrating peptide. Biochem. J. 390, 603-12.
    • (2005) Biochem. J , vol.390 , pp. 603-612
    • Mano, M.1    Teodosio, C.2    Paiva, A.3    Simoes, S.4    Pedroso de Lima, M.C.5
  • 44
    • 0035853015 scopus 로고    scopus 로고
    • Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR
    • Lindberg, M., Jarvet, J., Langel, U., and Graslund, A. (2001) Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR. Biochemistry 40, 3141-9.
    • (2001) Biochemistry , vol.40 , pp. 3141-3149
    • Lindberg, M.1    Jarvet, J.2    Langel, U.3    Graslund, A.4
  • 45
    • 0037466075 scopus 로고    scopus 로고
    • Comparison of the interaction, positioning, structure induction and membrane perturbation of cell-penetrating peptides and non-translocating variants with phospholipid vesicles
    • Magzoub, M., Eriksson, L. E., and Graslund, A. (2003) Comparison of the interaction, positioning, structure induction and membrane perturbation of cell-penetrating peptides and non-translocating variants with phospholipid vesicles. Biophys. Chem. 103, 271-88.
    • (2003) Biophys. Chem , vol.103 , pp. 271-288
    • Magzoub, M.1    Eriksson, L.E.2    Graslund, A.3
  • 46
    • 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. (2003) Caveolae-mediated internalization of extracellular HIV-1 tat fusion proteins visualized in real time. Mol. Ther. 8, 284-94.
    • (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
  • 47
    • 34247093930 scopus 로고    scopus 로고
    • Temperature-, concentration- and cholesterol-dependent translocation of L- and D-octa-arginine across the plasma and nuclear membrane of CD34+ leukaemia cells
    • Fretz, M. M., Penning, N. A., Al-Taei, S., Futaki, S., Takeuchi, T., Nakase, I., Storm, G., and Jones, A. T. (2007) Temperature-, concentration- and cholesterol-dependent translocation of L- and D-octa-arginine across the plasma and nuclear membrane of CD34+ leukaemia cells. Biochem. J. 403, 335-42.
    • (2007) Biochem. J , vol.403 , pp. 335-342
    • Fretz, M.M.1    Penning, N.A.2    Al-Taei, S.3    Futaki, S.4    Takeuchi, T.5    Nakase, I.6    Storm, G.7    Jones, A.T.8
  • 48
    • 11844293998 scopus 로고    scopus 로고
    • The cationic cell-penetrating peptide CPP(TAT) derived from the HIV-1 protein TAT is rapidly transported into living fibroblasts: Optical, biophysical, and metabolic evidence
    • Ziegler, A., Nervi, P., Durrenberger, M., and Seelig, J. (2005) The cationic cell-penetrating peptide CPP(TAT) derived from the HIV-1 protein TAT is rapidly transported into living fibroblasts: optical, biophysical, and metabolic evidence. Biochemistry 44, 138-48.
    • (2005) Biochemistry , vol.44 , pp. 138-148
    • Ziegler, A.1    Nervi, P.2    Durrenberger, M.3    Seelig, J.4
  • 49
    • 11244335404 scopus 로고    scopus 로고
    • Studies on the cellular uptake of substance P and lysine-rich, KLA-derived model peptides
    • Oehlke, J., Lorenz, D., Wiesner, B., and Bienert, M. (2005) Studies on the cellular uptake of substance P and lysine-rich, KLA-derived model peptides. J. Mol. Recognit. 18, 50-9.
    • (2005) J. Mol. Recognit , vol.18 , pp. 50-59
    • Oehlke, J.1    Lorenz, D.2    Wiesner, B.3    Bienert, M.4
  • 50
    • 31544458695 scopus 로고    scopus 로고
    • Endosome trapping limits the efficiency of splicing correction by PNA-oligolysine conjugates
    • Abes, S., Williams, D., Prevot, P., Thierry, A., Gait, M. J., and Lebleu, B. (2006) Endosome trapping limits the efficiency of splicing correction by PNA-oligolysine conjugates. J. Controlled Release 110, 595-604.
    • (2006) J. Controlled Release , vol.110 , pp. 595-604
    • Abes, S.1    Williams, D.2    Prevot, P.3    Thierry, A.4    Gait, M.J.5    Lebleu, B.6
  • 51
    • 33750498490 scopus 로고    scopus 로고
    • Induction of splice correction by cell-penetrating peptide nucleic acids
    • El-Andaloussi, S., Johansson, H. J., Lundberg, P., and Langel, U. (2006) Induction of splice correction by cell-penetrating peptide nucleic acids. J. Gene Med. 8, 1262-73.
    • (2006) J. Gene Med , vol.8 , pp. 1262-1273
    • El-Andaloussi, S.1    Johansson, H.J.2    Lundberg, P.3    Langel, U.4
  • 52
    • 0142149065 scopus 로고    scopus 로고
    • Complexes of plasmid DNA with basic domain 47-57 of the HIV-1 Tat protein are transferred to mammalian cells by endocytosis-mediated pathways
    • Ignatovich, I. A., Dizhe, E. B., Pavlotskaya, A. V., Akifiev, B. N., Burov, S. V., Orlov, S. V., and Perevozchikov, A. P. (2003) Complexes of plasmid DNA with basic domain 47-57 of the HIV-1 Tat protein are transferred to mammalian cells by endocytosis-mediated pathways. J. Biol. Chem. 278, 42625-36.
    • (2003) J. Biol. Chem , vol.278 , pp. 42625-42636
    • Ignatovich, I.A.1    Dizhe, E.B.2    Pavlotskaya, A.V.3    Akifiev, B.N.4    Burov, S.V.5    Orlov, S.V.6    Perevozchikov, A.P.7
  • 53
    • 0041816277 scopus 로고    scopus 로고
    • Antennapedia and HIV transactivator of transcription (TAT) "protein transduction domains" promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans
    • Console, S., Marty, C., Garcia-Echeverria, C., Schwendener, R., and Ballmer-Hofer, K. (2003) Antennapedia and HIV transactivator of transcription (TAT) "protein transduction domains" promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans. J. Biol. Chem. 278, 35109-14.
    • (2003) J. Biol. Chem , vol.278 , pp. 35109-35114
    • Console, S.1    Marty, C.2    Garcia-Echeverria, C.3    Schwendener, R.4    Ballmer-Hofer, K.5
  • 55
    • 0348010364 scopus 로고    scopus 로고
    • Cytoplasmic and nuclear delivery of a TAT-derived peptide and a beta-peptide after endocytic uptake into HeLa cells
    • Potocky, T. B., Menon, A. K., and Gellman, S. H. (2003) Cytoplasmic and nuclear delivery of a TAT-derived peptide and a beta-peptide after endocytic uptake into HeLa cells. J. Biol. Chem. 278, 50188-94.
    • (2003) J. Biol. Chem , vol.278 , pp. 50188-50194
    • Potocky, T.B.1    Menon, A.K.2    Gellman, S.H.3
  • 56
    • 33847036106 scopus 로고    scopus 로고
    • Vectorization of morpholino oligomers by the (R-Ahx-R)4 peptide allows efficient splicing correction in the absence of endosomolytic agents
    • Abes, S., Moulton, H. M., Clair, P., Prevot, P., Youngblood, D. S., Wu, R. P., Iversen, P. L., and Lebleu, B. (2006) Vectorization of morpholino oligomers by the (R-Ahx-R)4 peptide allows efficient splicing correction in the absence of endosomolytic agents. J. Controlled Release 116, 304-13.
    • (2006) J. Controlled Release , vol.116 , pp. 304-313
    • Abes, S.1    Moulton, H.M.2    Clair, P.3    Prevot, P.4    Youngblood, D.S.5    Wu, R.P.6    Iversen, P.L.7    Lebleu, B.8
  • 57
    • 0034126420 scopus 로고    scopus 로고
    • New advances in the transport of doxorubicin through the blood-brain barrier by a peptide vector-mediated strategy
    • Rousselle, C., Clair, P., Lefauconnier, J. M., Kaczorek, M., Scherrmann, J. M., and Temsamani, J. (2000) New advances in the transport of doxorubicin through the blood-brain barrier by a peptide vector-mediated strategy. Mol. Pharmacol. 57, 679-86.
    • (2000) Mol. Pharmacol , vol.57 , pp. 679-686
    • Rousselle, C.1    Clair, P.2    Lefauconnier, J.M.3    Kaczorek, M.4    Scherrmann, J.M.5    Temsamani, J.6
  • 58
    • 0039174260 scopus 로고    scopus 로고
    • Nuclear import of adenovirus DNA in vitro involves the nuclear protein import pathway and hsc70
    • Saphire, A. C., Guan, T., Schirmer, E. C., Nemerow, G. R., and Gerace, L. (2000) Nuclear import of adenovirus DNA in vitro involves the nuclear protein import pathway and hsc70. J. Biol. Chem. 275, 4298-304.
    • (2000) J. Biol. Chem , vol.275 , pp. 4298-4304
    • Saphire, A.C.1    Guan, T.2    Schirmer, E.C.3    Nemerow, G.R.4    Gerace, L.5
  • 59
    • 0037016020 scopus 로고    scopus 로고
    • Translocating proline-rich peptides from the antimicrobial peptide bactenecin 7
    • Sadler, K., Eom, K. D., Yang, J. L., Dimitrova, Y., and Tam, J. P. (2002) Translocating proline-rich peptides from the antimicrobial peptide bactenecin 7. Biochemistry 41, 14150-7.
    • (2002) Biochemistry , vol.41 , pp. 14150-14157
    • Sadler, K.1    Eom, K.D.2    Yang, J.L.3    Dimitrova, Y.4    Tam, J.P.5
  • 60
    • 0029006149 scopus 로고
    • Inhibition of nuclear translocation of transcription factor NF-kappa B by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence
    • Lin, Y. Z., Yao, S. Y., Veach, R. A., Torgerson, T. R., and Hawiger, J. (1995) Inhibition of nuclear translocation of transcription factor NF-kappa B by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence. J. Biol. Chem. 270, 14255-8.
    • (1995) J. Biol. Chem , vol.270 , pp. 14255-14258
    • Lin, Y.Z.1    Yao, S.Y.2    Veach, R.A.3    Torgerson, T.R.4    Hawiger, J.5
  • 61
    • 0022460644 scopus 로고
    • Induction of nuclear transport with a synthetic peptide homologous to the SV40 T antigen transport signal
    • Lanford, R. E., Kanda, P., and Kennedy, R. C. (1986) Induction of nuclear transport with a synthetic peptide homologous to the SV40 T antigen transport signal. Cell 46, 575-82.
    • (1986) Cell , vol.46 , pp. 575-582
    • Lanford, R.E.1    Kanda, P.2    Kennedy, R.C.3
  • 62
    • 0036669511 scopus 로고    scopus 로고
    • Cellular import mediated by nuclear localization signal peptide sequences
    • Ragin, A. D., Morgan, R. A., and Chmielewski, J. (2002) Cellular import mediated by nuclear localization signal peptide sequences. Chem. Biol. 9, 943-8.
    • (2002) Chem. Biol , vol.9 , pp. 943-948
    • Ragin, A.D.1    Morgan, R.A.2    Chmielewski, J.3
  • 63
    • 1642457360 scopus 로고    scopus 로고
    • Cellular internalization of human calcitonin derived peptides in MDCK monolayers: A comparative study with Tat(47-57) and penetratin(43-58)
    • Trehin, R., Krauss, U., Muff, R., Meinecke, M., Beck-Sickinger, A. G., and Merkle, H. P. (2004) Cellular internalization of human calcitonin derived peptides in MDCK monolayers: a comparative study with Tat(47-57) and penetratin(43-58). Pharm. Res. 21, 33-42.
    • (2004) Pharm. Res , vol.21 , pp. 33-42
    • Trehin, R.1    Krauss, U.2    Muff, R.3    Meinecke, M.4    Beck-Sickinger, A.G.5    Merkle, H.P.6
  • 64
    • 0035478616 scopus 로고    scopus 로고
    • VE-cadherin-derived cell-penetrating peptide, pVEC, with carrier functions
    • Elmquist, A., Lindgren, M., Bartfai, T., and Langel, U. (2001) VE-cadherin-derived cell-penetrating peptide, pVEC, with carrier functions. Exp. Cell Res. 269, 237-44.
    • (2001) Exp. Cell Res , vol.269 , pp. 237-244
    • Elmquist, A.1    Lindgren, M.2    Bartfai, T.3    Langel, U.4
  • 66
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • Morris, M. C., Depollier, J., Mery, J., Heitz, F., and Divita, G. (2001) A peptide carrier for the delivery of biologically active proteins into mammalian cells. Nat. Biotechnol. 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
  • 67
    • 0030804766 scopus 로고    scopus 로고
    • A new peptide vector for efficient delivery of oligonucleotides into mammalian cells
    • Morris, M. C., Vidal, P., Chaloin, L., Heitz, F., and Divita, G. (1997) A new peptide vector for efficient delivery of oligonucleotides into mammalian cells. Nucleic Acids Res. 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
  • 68
    • 3142774800 scopus 로고    scopus 로고
    • Potential peptide carriers: Amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein
    • Fernandez-Carneado, J., Kogan, M. J., Castel, S., and Giralt, E. (2004) Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein. Angew. Chem., Int. Ed. Engl. 43, 1811-4.
    • (2004) Angew. Chem., Int. Ed. Engl , vol.43 , pp. 1811-1814
    • Fernandez-Carneado, J.1    Kogan, M.J.2    Castel, S.3    Giralt, E.4
  • 69
    • 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. (2000) The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. Proc. Natl. Acad. Sci. U.S.A. 97, 13003-8.
    • (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


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