메뉴 건너뛰기




Volumn 62, Issue 3, 2010, Pages 183-193

Cell-penetrating peptides: Nanocarrier for macromolecule delivery in living cells

Author keywords

Cellular delivery; Macropinocytosis; Plant system; Protein transduction; Transfection

Indexed keywords

CELL PENETRATING PEPTIDE; NANOCARRIER; NUCLEIC ACID; OLIGONUCLEOTIDE;

EID: 77951144106     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.297     Document Type: Review
Times cited : (151)

References (105)
  • 1
    • 33748433244 scopus 로고    scopus 로고
    • Cell-penetrating peptides as vectors for peptide, protein and oligonucleotide delivery
    • Mae, M. and Langel, Ü. (2006) Cell-penetrating peptides as vectors for peptide, protein and oligonucleotide delivery. Curr. Opin. Pharmacol. 6, 509-514.
    • (2006) Curr. Opin. Pharmacol. , vol.6 , pp. 509-514
    • Mae, M.1    Langel, Ü.2
  • 2
    • 56049093057 scopus 로고    scopus 로고
    • Cell-penetrating and cell-targeting peptides in drug delivery
    • Vives, E., Schmidt, J., and Pelegrin, A. (2008) Cell-penetrating and cell-targeting peptides in drug delivery. Biochim. Biophys. Acta Rev. Cancer. 1786, 126-138.
    • (2008) Biochim. Biophys. Acta Rev. Cancer , vol.1786 , pp. 126-138
    • Vives, E.1    Schmidt, J.2    Pelegrin, A.3
  • 3
    • 42649087417 scopus 로고    scopus 로고
    • Study of uptake of cell penetrating peptides and their cargoes in permeabilized wheat immature embryos
    • DOI 10.1111/j.1742-4658.2008.06384.x
    • Chugh, A. and Eudes, F. (2008) Studies of uptake of cell-penetrating peptides and their cargoes in wheat immature embryos. FEBS J. 275, 2403-2414. (Pubitemid 351600079)
    • (2008) FEBS Journal , vol.275 , Issue.10 , pp. 2403-2414
    • Chugh, A.1    Eudes, F.2
  • 4
    • 24644458765 scopus 로고    scopus 로고
    • Synthesis of cell-penetrating peptides for cargo delivery
    • Pooga, M. and Langel, Ü. (2005) Synthesis of cell-penetrating peptides for cargo delivery. Methods Mol. Biol. 298, 77-89.
    • (2005) Methods Mol. Biol. , vol.298 , pp. 77-89
    • Pooga, M.1    Langel, Ü.2
  • 5
    • 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, E. T., 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. USA. 97, 13003-13008.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13003-13008
    • Wender, P.A.1    Mitchell, D.J.2    Pattabiraman, E.T.3    Pelkey, E.T.4    Steinman, L.5    Rothbard, J.B.6
  • 6
    • 20444403719 scopus 로고    scopus 로고
    • Effect of cargo molecules on cellular uptake of arginine-rich cell penetrating peptides
    • Maiolo, J. R., Ferrer, M., and Ottinger, E. A. (2005) Effect of cargo molecules on cellular uptake of arginine-rich cell penetrating peptides. Biochim. Biophys. Acta 1712, 161-172.
    • (2005) Biochim. Biophys. Acta , vol.1712 , pp. 161-172
    • Maiolo, J.R.1    Ferrer, M.2    Ottinger, E.A.3
  • 7
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intercellular 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 intercellular protein delivery. J. Biol. Chem. 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    Sugiura, Y.7
  • 8
    • 17144368106 scopus 로고    scopus 로고
    • Cellular internalization of fluorescent proteins via arginine-rich intracellular delivery peptide in plant cells
    • DOI 10.1093/pcp/pci046
    • Chang, M., Chou, J.-C., and Lee, H. J. (2005) Cellular internalization of fluorescent proteins via arginine-rich intracellular delivery peptide in plant cells. Plant Cell Physiol. 46, 482-488. (Pubitemid 40507529)
    • (2005) Plant and Cell Physiology , vol.46 , Issue.3 , pp. 482-488
    • Chang, M.1    Chou, J.-C.2    Lee, H.-J.3
  • 9
    • 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. (2001) Internalization of HIV-1 Tat requires cell surface heparan sulfate proteoglycans. J. Biol. Chem. 276, 3254-3261.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3254-3261
    • Tyagi, M.1    Rusnati, M.2    Presta, M.3    Giacca, M.4
  • 11
    • 13844256698 scopus 로고    scopus 로고
    • Tat peptide-mediated cellular delivery: Back to basics
    • Brooks, H., Lebleu, B., and Vivès, E. (2005) Tat peptide-mediated cellular delivery: back to basics. Adv. Drug Deliv. Rev. 57, 559-577.
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 559-577
    • Brooks, H.1    Lebleu, B.2    Vivès, E.3
  • 12
    • 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, 16010-16017.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 13
    • 33847075874 scopus 로고    scopus 로고
    • Translocation and nuclear accumulation of monomer and dimmer of HIV-1 Tat basic domain in triticale mesophyll protoplasts
    • Chugh, A. and Eudes, F. (2007) Translocation and nuclear accumulation of monomer and dimmer of HIV-1 Tat basic domain in triticale mesophyll protoplasts. Biochim. Biophys. Acta Biomembr. 1768, 419-426.
    • (2007) Biochim. Biophys. Acta Biomembr. , vol.1768 , pp. 419-426
    • Chugh, A.1    Eudes, F.2
  • 14
    • 0037440187 scopus 로고    scopus 로고
    • Cellular uptake of Antennapedia Penetratin peptides is a two-step process in which phase transfer precedes a tryptophan-dependent translocation
    • DOI 10.1093/nar/gkg160
    • Dom, G., Shaw-Jackson, C., Matis, C., Bouffioux, O., Picard, J. J., Prochiantz, A., Mingeot-Leclercq, M. P., Brasseur, R., and Rezsohazy, R. (2003) Cellular uptake of antennapedia penetratin peptides is a two-step process in which phase transfer precedes a tryptophan-dependent translocation. Nucleic Acids Res. 31, 556-561. (Pubitemid 36175944)
    • (2003) Nucleic Acids Research , vol.31 , Issue.2 , pp. 556-561
    • Dom, G.1    Shaw-Jackson, C.2    Matis, C.3    Bouffioux, O.4    Picard, J.J.5    Prochiantz, A.6    Mingeot-Leclerq, M.-P.7    Brasseur, R.8    Rezsohazy, R.9
  • 15
    • 0028239908 scopus 로고
    • The third helix of the antennapedia homeodornain translocates through biological membranes
    • Derossi, D., Joliot, A. H., Chassaing, G., and Prochiantz, A. (1994) The third helix of the antennapedia homeodornain translocates through biological membranes. J. Biol. Chem. 269, 10444-10450.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.A.3    Prochiantz, A.4
  • 17
    • 34548771163 scopus 로고    scopus 로고
    • A novel cell-penetrating peptide, M918, for efficient delivery of proteins and peptide nucleic acids
    • El-Andaloussi, S., Johansson, H. J., Holm, T., and Langel, Ü. (2007) A novel cell-penetrating peptide, M918, for efficient delivery of proteins and peptide nucleic acids. Mol. Ther. 15, 1820-1826.
    • (2007) Mol. Ther. , vol.15 , pp. 1820-1826
    • El-Andaloussi, S.1    Johansson, H.J.2    Holm, T.3    Langel, Ü.4
  • 18
    • 28444461040 scopus 로고    scopus 로고
    • Present and future of cell-penetrating peptide mediated delivery systems: Is the Trojan horse too wild to go only to Troy?
    • Vives, E. (2005) Present and future of cell-penetrating peptide mediated delivery systems: is the Trojan horse too wild to go only to Troy? J. Control. Release 109, 77-85.
    • (2005) J. Control. Release , vol.109 , pp. 77-85
    • Vives, E.1
  • 19
    • 0029006149 scopus 로고
    • Inhibition of nuclear translocation of transcription factor NF-κB 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-κB by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence. J. Biol. Chem. 270, 14255-14258.
    • (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
  • 20
    • 0030891149 scopus 로고    scopus 로고
    • Cellular import of functional peptides to block intracellular signaling
    • Hawiger, J. (1997) Cellular import of functional peptides to block intracellular signaling. Curr. Opin. Immunol. 9, 189-194.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 189-194
    • Hawiger, J.1
  • 21
    • 0029999551 scopus 로고    scopus 로고
    • Identification of a functionally important sequence in the cytoplasmic tail of integrin beta 3 by using cell-permeable peptide analogs
    • Liu, K. Y., Timmons, S., Lin, Y. Z., and Hawiger, J. (1996) Identification of a functionally important sequence in the cytoplasmic tail of integrin beta 3 by using cell-permeable peptide analogs. Proc. Natl. Acad. Sci. USA 93, 11819-11824.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11819-11824
    • Liu, K.Y.1    Timmons, S.2    Lin, Y.Z.3    Hawiger, J.4
  • 22
    • 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, 1977-1992.
    • (2007) Pharm. Res. , vol.24 , pp. 1977-1992
    • Patel, L.N.1    Zaro, J.L.2    Shen, W.C.3
  • 23
    • 0033802715 scopus 로고    scopus 로고
    • Evidence for an amphipathicity independent cellular uptake of amphipathic cell-penetrating peptides
    • Scheller, A., Wiesner, B., Melzig, M., Bienert, M., and Oehlke, J. (2000) Evidence for an amphipathicity independent cellular uptake of amphipathic cell-penetrating peptides. Eur. J. Biochem. 267, 6043-6050.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6043-6050
    • Scheller, A.1    Wiesner, B.2    Melzig, M.3    Bienert, M.4    Oehlke, J.5
  • 24
    • 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, 127-139.
    • (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
  • 25
    • 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, 1173-1176.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 26
    • 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, 1811-1814.
    • (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
  • 27
    • 34548162419 scopus 로고    scopus 로고
    • All-D proline-rich cell-penetrating peptides: A preliminary in vivo internalization study
    • Pujals, S., Sabidóo, E., Tarragó , T., and Giralt, E. (2007) All-D proline-rich cell-penetrating peptides: a preliminary in vivo internalization study. Biochem. Soc. Trans. 35, 794-796.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 794-796
    • Pujals, S.1    Sabidóo, E.2    Tarragó, T.3    Giralt, E.4
  • 29
    • 33749385780 scopus 로고    scopus 로고
    • Cell-penetrating peptides and antimicrobial peptides: How different are they?
    • Henriques, S. T., Melo, M. N., and Castanho, M. A. (2006) Cell-penetrating peptides and antimicrobial peptides: how different are they? Biochem. J. 399, 1-7.
    • (2006) Biochem. J. , vol.399 , pp. 1-7
    • Henriques, S.T.1    Melo, M.N.2    Castanho, M.A.3
  • 31
    • 0035478616 scopus 로고    scopus 로고
    • VE-cadherin derived cell-penetrating peptide, pVEC, with carrier functions
    • Elmquist, A., Lindgren, M., Bartfai, T., and Langel, Ü. (2001) VE-cadherin derived cell-penetrating peptide, pVEC, with carrier functions. Exp. Cell Res. 269, 237-244.
    • (2001) Exp. Cell Res. , vol.269 , pp. 237-244
    • Elmquist, A.1    Lindgren, M.2    Bartfai, T.3    Langel, Ü.4
  • 32
    • 42149175926 scopus 로고    scopus 로고
    • Cellular uptake of cell-penetrating peptides pVEC and transportan in plants
    • Chugh, A. and Eudes, F. (2008) Cellular uptake of cell-penetrating peptides pVEC and transportan in plants. J. Pept. Sci. 14, 477-481.
    • (2008) J. Pept. Sci. , vol.14 , pp. 477-481
    • Chugh, A.1    Eudes, F.2
  • 33
    • 0347624530 scopus 로고    scopus 로고
    • In vitro gene delivery by a novel human calcitonin (hCT)-derived carrier peptide
    • Krauss, U., Mueller, M., Stahl, M., and Beck-Sickinger, A. G. (2004) In vitro gene delivery by a novel human calcitonin (hCT)-derived carrier peptide. Bioorg. Med. Chem. Lett. 14, 51-54.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 51-54
    • Krauss, U.1    Mueller, M.2    Stahl, M.3    Beck-Sickinger, A.G.4
  • 36
    • 0038743278 scopus 로고    scopus 로고
    • In vitro uptake and stability study of pVEC and its all D-analog
    • Elmquist, A. and Langel, Ü. (2003) In vitro uptake and stability study of pVEC and its all D-analog. Biol. Chem. 384, 387-393.
    • (2003) Biol. Chem. , vol.384 , pp. 387-393
    • Elmquist, A.1    Langel, Ü.2
  • 37
    • 33646236541 scopus 로고    scopus 로고
    • Oligoarginine vectors for intracellular delivery: Design and cellular-uptake mechanisms
    • Futaki, S. (2006) Oligoarginine vectors for intracellular delivery: design and cellular-uptake mechanisms. Biopolymers 84, 241-249.
    • (2006) Biopolymers , vol.84 , pp. 241-249
    • Futaki, S.1
  • 38
    • 33750525085 scopus 로고    scopus 로고
    • An insight into the gene delivery mechanism of the arginine peptide system: Role of the peptide/DNA complex size
    • Choi, H. S., Kim, H. H., Yang, J. M., and Shin, S. (2006) An insight into the gene delivery mechanism of the arginine peptide system: role of the peptide/DNA complex size. Biochim. Biophys. Acta 1760, 1604-1612.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 1604-1612
    • Choi, H.S.1    Kim, H.H.2    Yang, J.M.3    Shin, S.4
  • 39
    • 0031566270 scopus 로고    scopus 로고
    • Gene transfer mediated by polyarginine requires formation of a big carrier-complex of DNA aggregate
    • Emi, N., Kidoaki, S., Yoshikawa, K., and Saito, H. (1997) Gene transfer mediated by polyarginine requires formation of a big carrier-complex of DNA aggregate. Biochem. Biophys. Res. Commun. 231, 421-424.
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 421-424
    • Emi, N.1    Kidoaki, S.2    Yoshikawa, K.3    Saito, H.4
  • 40
    • 0031788165 scopus 로고    scopus 로고
    • The size of DNA/transferrin-PEI complexes is an important factor for gene expression in cultured cells
    • Ogris, M., Steinlein, P., Kursa, M., Mechtler, K., Kircheis, R., and Wagner, E. (1998) The size of DNA/transferring-PEI complexes is an important factor for gene expression in cultured cells. Gene Ther. 5, 1425-1433. (Pubitemid 28482671)
    • (1998) Gene Therapy , vol.5 , Issue.10 , pp. 1425-1433
    • Ogris, M.1    Steinlein, P.2    Kursa, M.3    Mechtler, K.4    Kircheis, R.5    Wagner, E.6
  • 42
    • 35048856889 scopus 로고    scopus 로고
    • Cargo-dependent cytotoxicity and delivery efficacy of cell-penetrating peptides: A comparative study
    • DOI 10.1042/BJ20070507
    • El-Andaloussi, S., Järver, P., Johansson, H. J., and Langel, Ü. (2007) Cargo-dependent cytotoxicity and delivery efficacy of cell-penetrating peptides: a comparative study. Biochem. J. 407, 285-292. (Pubitemid 47556993)
    • (2007) Biochemical Journal , vol.407 , Issue.2 , pp. 285-292
    • El-Andaloussi, S.1    Jarver, P.2    Johansson, H.J.3    Langel, U.4
  • 43
    • 42649091044 scopus 로고    scopus 로고
    • Insight into the mechanism of internalization of the cell-penetrating peptide and recombinant proteins fused to Tat
    • Deshayes, S., Heitz, A., Morris, M. C., Charnet, P., Divita, G., and Heitz, F. (2004) Insight into the mechanism of internalization of the cell-penetrating peptide and recombinant proteins fused to Tat. Eur. J. Biochem. 269, 494-501.
    • (2004) Eur. J. Biochem. , vol.269 , pp. 494-501
    • Deshayes, S.1    Heitz, A.2    Morris, M.C.3    Charnet, P.4    Divita, G.5    Heitz, F.6
  • 44
    • 4344609460 scopus 로고    scopus 로고
    • Non-endocytic penetration of core histones into petunia protoplasts and cultured cells: A novel mechanism for the introduction of macromolecules into plant cells
    • Rosenbluh, J., Singh, S. K., Gafni, Y., Graessmann, A., and Loyter, A. (2004) Non-endocytic penetration of core histones into petunia protoplasts and cultured cells: a novel mechanism for the introduction of macromolecules into plant cells. Biochim. Biophys. Acta 1664, 230-240.
    • (2004) Biochim. Biophys. Acta , vol.1664 , pp. 230-240
    • Rosenbluh, J.1    Singh, S.K.2    Gafni, Y.3    Graessmann, A.4    Loyter, A.5
  • 45
    • 34147103472 scopus 로고    scopus 로고
    • First step of the cell-penetrating peptide mechanism involves Rac1 GTPase-dependent actin-network remodelling
    • DOI 10.1042/BC20060123
    • Gerbal-Chaloin, S., Gondeau, C., Aldrian-Herrada, G., Heitz, F., Gauthier-Rouviere, C., and Divita, G. (2007) First step of the cell-penetrating peptide mechanism involves Rac1 GTPase-dependent actin-network remodeling. Biol. Cell 99, 223-238. (Pubitemid 46567179)
    • (2007) Biology of the Cell , vol.99 , Issue.4 , pp. 223-238
    • Gerbal-Chaloin, S.1    Gondeau, C.2    Aldrian-Herrada, G.3    Heltz, F.4    Gauthier-Rouviere, C.5    Divita, G.6
  • 46
    • 33846223900 scopus 로고    scopus 로고
    • Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis
    • DOI 10.1021/bi0612824
    • Nakase, I., Tadokoro, A., Kawabata, N., Takeuchi, T., Katoh, H., Hiramoto, K., Negishi, M., Nomizu, M., Suguira, Y., and Futaki, S. (2007) Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis. Biochemistry 46, 492-501. (Pubitemid 46105438)
    • (2007) Biochemistry , vol.46 , Issue.2 , pp. 492-501
    • Nakase, I.1    Tadokoro, A.2    Kawabata, N.3    Takeuchi, T.4    Katoh, H.5    Hiramoto, K.6    Negishi, M.7    Nomizu, M.8    Sugiura, Y.9    Futaki, S.10
  • 47
    • 0036159271 scopus 로고    scopus 로고
    • Different mechanisms for cellular internalization of the HIV1-Tat-derived cell penetrating peptide and recombinant proteins fused to Tat
    • Silhol, M., Tyagi, M., Giacca, M., Lebleu, B., and Vives, E. (2002) Different mechanisms for cellular internalization of the HIV1-Tat-derived cell penetrating peptide and recombinant proteins fused to Tat. Eur. J. Biochem. 269, 494-501.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 494-501
    • Silhol, M.1    Tyagi, M.2    Giacca, M.3    Lebleu, B.4    Vives, E.5
  • 48
    • 0025967418 scopus 로고
    • Lipid-alginate interactions render changes in phospholipid bilayer permeability
    • Cohen, S., Bano, M. C., Chow, M., and Langer, R. (1991) Lipid-alginate interactions render changes in phospholipid bilayer permeability. Biochim. Biophys. Acta 1063, 95-102.
    • (1991) Biochim. Biophys. Acta , vol.1063 , pp. 95-102
    • Cohen, S.1    Bano, M.C.2    Chow, M.3    Langer, R.4
  • 49
    • 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. (2001) Physico-chemical requirements for cellular uptake of pAntp peptide: role of lipid-binding affinity. Eur. J. Biochem. 268, 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
  • 51
    • 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, 35109-35114.
    • (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
  • 52
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner, S. D. and Schmid, S. L. (2003) Regulated portals of entry into the cell. Nature 422, 37.
    • (2003) Nature , vol.422 , pp. 37
    • Conner, S.D.1    Schmid, S.L.2
  • 53
    • 33747038452 scopus 로고    scopus 로고
    • Cell-penetrating peptides - A brief introduction
    • Järver, P. and Langel, Ü. (2006) Cell-penetrating peptides - a brief introduction. Biochim. Biophys. Acta 1758, 260-263.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 260-263
    • Järver, P.1    Langel, Ü.2
  • 54
    • 0005907748 scopus 로고
    • Biotin-mediated delivery of exogenous macromolecules into soybean cells
    • Horn, M. A., Heinstein, P. F., and Low, P. S. (1990) Biotin-mediated delivery of exogenous macromolecules into soybean cells. Plant Physiol. 93, 1492-1496.
    • (1990) Plant Physiol. , vol.93 , pp. 1492-1496
    • Horn, M.A.1    Heinstein, P.F.2    Low, P.S.3
  • 55
    • 0001672151 scopus 로고
    • Characterization of parameters influencing receptor-mediated endocytosis in cultured soybean cells
    • Horn, M. A., Heinstein, P. F., and Low, P. S. (1992) Characterization of parameters influencing receptor-mediated endocytosis in cultured soybean cells. Plant Physiol. 98, 673-679.
    • (1992) Plant Physiol. , vol.98 , pp. 673-679
    • Horn, M.A.1    Heinstein, P.F.2    Low, P.S.3
  • 56
    • 0033909566 scopus 로고    scopus 로고
    • Protein sorting signals and prediction of subcellular localization
    • Nakai, K. and Peer, B. (2000) Protein sorting signals and prediction of subcellular localization. Adv. Protein Chem. 54, 277-344.
    • (2000) Adv. Protein Chem. , vol.54 , pp. 277-344
    • Nakai, K.1    Peer, B.2
  • 57
    • 0034126815 scopus 로고    scopus 로고
    • The nuclear pore complex: Mediator of translocation between nucleus and cytoplasm
    • Allen, T. D., Cronshaw, J. M., Bagley, S., Kiseleva, E., and Goldberg, M. W. (2000) The nuclear pore complex: mediator of translocation between nucleus and cytoplasm. J. Cell Sci. 113, 1651-1659. (Pubitemid 30333114)
    • (2000) Journal of Cell Science , vol.113 , Issue.10 , pp. 1651-1659
    • Allen, T.D.1    Cronshaw, J.M.2    Bagley, S.3    Kiseleva, E.4    Goldberg, M.W.5
  • 58
    • 0039468008 scopus 로고    scopus 로고
    • The protein kinase CK2 site (Ser(111/112)) enhances recognition of the simian virus 40 large T-antigen nuclear localization sequence by importin
    • Hubner, S., Xiao, C. Y., and Jans, D. A. (1997) The protein kinase CK2 site (Ser(111/112)) enhances recognition of the simian virus 40 large T-antigen nuclear localization sequence by importin. J. Biol. Chem. 272, 17191-17195.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17191-17195
    • Hubner, S.1    Xiao, C.Y.2    Jans, D.A.3
  • 59
    • 0028930155 scopus 로고
    • A nuclear localization domain in the hnRNP A1 protein
    • Siomi, H. and Dreyfuss, G. (1995) A nuclear localization domain in the hnRNP A1 protein. J. Cell. Biol. 129, 551-560.
    • (1995) J. Cell. Biol. , vol.129 , pp. 551-560
    • Siomi, H.1    Dreyfuss, G.2
  • 62
    • 67349259641 scopus 로고    scopus 로고
    • Translocation of cell-penetrating peptides and delivery of their cargoes in triticale microspores
    • Chugh, A., Amundsen, E., and Eudes, F. (2009) Translocation of cell-penetrating peptides and delivery of their cargoes in triticale microspores. Plant Cell Rep. 28, 801-810.
    • (2009) Plant Cell Rep. , vol.28 , pp. 801-810
    • Chugh, A.1    Amundsen, E.2    Eudes, F.3
  • 63
    • 17144368106 scopus 로고    scopus 로고
    • Cellular internalization of fluorescent proteins via arginine-rich intracellular delivery peptide in plant cells
    • DOI 10.1093/pcp/pci046
    • Chang, M., Chou, J.-C., and Lee, H.-J. (2005) Cellular internalization of fluorescent proteins via arginine-rich intracellular delivery peptide in plant cells. Plant Cell Physiol. 46, 482-488. (Pubitemid 40507529)
    • (2005) Plant and Cell Physiology , vol.46 , Issue.3 , pp. 482-488
    • Chang, M.1    Chou, J.-C.2    Lee, H.-J.3
  • 64
    • 2442467992 scopus 로고    scopus 로고
    • Cationic oligopeptide-mediated delivery of dsRNA for post-transcriptional gene silencing in plant cells
    • DOI 10.1016/j.febslet.2004.04.018, PII S0014579304004740
    • Unnamalai, N., Kang, B. G., and Lee, W. S. (2004) Cationic oligopeptide-mediated delivery of dsRNA for post-transcriptional gene silencing in plant cells. FEBS Lett. 566, 307-319. (Pubitemid 38625977)
    • (2004) FEBS Letters , vol.566 , Issue.1-3 , pp. 307-310
    • Unnamalai, N.1    Kang, B.G.2    Lee, W.S.3
  • 65
    • 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. (1999) In vivo protein transduction: delivery of a biologically active protein into the mouse. Science 285, 1569-1572.
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 66
    • 33847105943 scopus 로고    scopus 로고
    • (123) I-labeled HIV-1 tat peptide radioimmunoconjugates are imported into the nucleus of human breast cancer cells and functionally interact in vitro and in vivo with the cyclin dependent kinase inhibitor, p21(WAF-1/Cip-1)
    • Hu, M., Chen, P., Wang, J., Scollard, D. A., Vallis, K. A., and Reilly, R. M. (2006) (123) I-labeled HIV-1 tat peptide radioimmunoconjugates are imported into the nucleus of human breast cancer cells and functionally interact in vitro and in vivo with the cyclin dependent kinase inhibitor, p21(WAF-1/Cip-1). Eur. J. Nucl. Med. Mol. Imaging 34, 368-377.
    • (2006) Eur. J. Nucl. Med. Mol. Imaging , vol.34 , pp. 368-377
    • Hu, M.1    Chen, P.2    Wang, J.3    Scollard, D.A.4    Vallis, K.A.5    Reilly, R.M.6
  • 67
    • 23844524089 scopus 로고    scopus 로고
    • Intracellular protein therapy with SOCS3 inhibits inflammation and apoptosis
    • Jo, D., Liu, D., Yao, S., Collins, R. D., and Hawiger, J. (2005) Intracellular protein therapy with SOCS3 inhibits inflammation and apoptosis. Nat. Med. 11, 892-898.
    • (2005) Nat. Med. , vol.11 , pp. 892-898
    • Jo, D.1    Liu, D.2    Yao, S.3    Collins, R.D.4    Hawiger, J.5
  • 68
    • 0032883128 scopus 로고    scopus 로고
    • A disulfide conjugate between anti-tetanus antibodies and HIV (37-72) Tat neutralizes tetanus toxin inside chromaffin cells
    • Stein, S., Weiss, A., Adermann, K., Lazarovici, P., Hochman, J., and Wellhoner, H. (1999) A disulfide conjugate between anti-tetanus antibodies and HIV (37-72) Tat neutralizes tetanus toxin inside chromaffin cells. FEBS Lett. 458, 383-386.
    • (1999) FEBS Lett. , vol.458 , pp. 383-386
    • Stein, S.1    Weiss, A.2    Adermann, K.3    Lazarovici, P.4    Hochman, J.5    Wellhoner, H.6
  • 69
    • 40049101118 scopus 로고    scopus 로고
    • Co-transduction of sleeping beauty transposase and donor plasmid via a cell-penetrating peptide: A simple one step method
    • Jarver, P., Fernaeus, S., El-Andaloussi, S., Tjornhammar, M.-L., and Langel, Ü. (2008) Co-transduction of sleeping beauty transposase and donor plasmid via a cell-penetrating peptide: a simple one step method. Int. J. Pept. Res. Ther. 14, 58-63.
    • (2008) Int. J. Pept. Res. Ther. , vol.14 , pp. 58-63
    • Jarver, P.1    Fernaeus, S.2    El-Andaloussi, S.3    Tjornhammar, M.-L.4    Langel, Ü.5
  • 70
    • 0346157097 scopus 로고    scopus 로고
    • Intracellular delivery of bioactive peptides to RBL-2H3 cells induces β-hexosaminidase secretion and phospholipase D activation
    • Howl, J., Jones, S., and Farquhar, M. (2003) Intracellular delivery of bioactive peptides to RBL-2H3 cells induces β-hexosaminidase secretion and phospholipase D activation. Chembiochem. 4, 1312-1316.
    • (2003) Chembiochem. , vol.4 , pp. 1312-1316
    • Howl, J.1    Jones, S.2    Farquhar, M.3
  • 71
    • 40849120181 scopus 로고    scopus 로고
    • Gateways and tools for drug delivery: Endocytic pathways and the cellular dynamics of cell penetrating peptides
    • Jones, A. T. (2008) Gateways and tools for drug delivery: endocytic pathways and the cellular dynamics of cell penetrating peptides. Int. J. Pharm. 354, 34-38.
    • (2008) Int. J. Pharm. , vol.354 , pp. 34-38
    • Jones, A.T.1
  • 72
    • 38949151892 scopus 로고    scopus 로고
    • Multifunctional envelope-type nano device (MEND) as a non-viral gene delivery system
    • Kogure, K., Akita, H., Yamada, Y., and Harashima, H. (2008) Multifunctional envelope-type nano device (MEND) as a non-viral gene delivery system. Adv. Drug Deliv. Rev. 60, 559-571.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 559-571
    • Kogure, K.1    Akita, H.2    Yamada, Y.3    Harashima, H.4
  • 73
    • 34147100763 scopus 로고    scopus 로고
    • Efficient cytoplasmic protein delivery by means of a multifunctional envelope- Type nano device
    • Suzuki, R., Yamada, Y., and Harashima, H. (2007) Efficient cytoplasmic protein delivery by means of a multifunctional envelope- type nano device. Biol. Pharm. Bull. 30, 758-762.
    • (2007) Biol. Pharm. Bull. , vol.30 , pp. 758-762
    • Suzuki, R.1    Yamada, Y.2    Harashima, H.3
  • 74
    • 12844265426 scopus 로고    scopus 로고
    • Macro-branched cell-penetrating peptide design for gene delivery
    • DOI 10.1016/j.jconrel.2004.10.013, PII S0168365904004948
    • Liu, Z., Li, M., Cui, D., and Fei, J. (2005) Macro-branched cell-penetrating peptide design for gene delivery. J. Control. Release 102, 699-710. (Pubitemid 40170212)
    • (2005) Journal of Controlled Release , vol.102 , Issue.3 , pp. 699-710
    • Liu, Z.1    Li, M.2    Cui, D.3    Fei, J.4
  • 75
    • 13744259834 scopus 로고    scopus 로고
    • Synthesis, cellular uptake and HIV-1 Tat-dependant trans-activation inhibition activity of oligonucleotide analogue disulphide-conjugated to cell-penetrating peptides
    • Turner, J. J., Arzumanov, A. A., and Gait, M. J. (2005) Synthesis, cellular uptake and HIV-1 Tat-dependant trans-activation inhibition activity of oligonucleotide analogue disulphide-conjugated to cell-penetrating peptides. Nucleic Acids Res. 33, 27-42.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 27-42
    • Turner, J.J.1    Arzumanov, A.A.2    Gait, M.J.3
  • 76
    • 29344436510 scopus 로고    scopus 로고
    • Cell-penetrating peptide conjugates of peptide nucleic acids (PNA) as inhibitors of HIV-1 Tat-dependent trans-activation in cells
    • DOI 10.1093/nar/gki991
    • Turner, J. J., Ivanova, G. D., Verbeure, B., Williams, D., Arzumanov, A. A., Abes, S., Lebleu, B., and Gait, M. J. (2005) Cell-penetrating peptide conjugates of peptide nucleic acids (PNA) as inhibitors of HIV-1 Tatdependant trans-activation in cells. Nucleic Acids Res. 33, 6837-6849. (Pubitemid 43000315)
    • (2005) Nucleic Acids Research , vol.33 , Issue.21 , pp. 6837-6849
    • Turner, J.J.1    Ivanova, G.D.2    Verbeure, B.3    Williams, D.4    Arzumanov, A.A.5    Abes, S.6    Lebleu, B.7    Gait, M.J.8
  • 77
    • 0032485884 scopus 로고    scopus 로고
    • Up-regulation of luciferase gene expression with antisense oligonucleotides: Implications and applications in functional assay development
    • Kang, S. H., Cho, M. J., and Kole, R. (1998) Up-regulation of luciferase gene expression with antisense oligonucleotides: implications and applications in functional assay development. Biochemistry 37, 6235-6239.
    • (1998) Biochemistry , vol.37 , pp. 6235-6239
    • Kang, S.H.1    Cho, M.J.2    Kole, R.3
  • 78
    • 22644440063 scopus 로고    scopus 로고
    • Arginine-rich peptide conjugation to morphilino oligomers: Effects on antisense activity and specificity
    • Nelson, M. H., Stein, D. A., Kroeker, A. D., Hatievig, S. A., Iversen, P. L., and Moulton, H. M. (2005) Arginine-rich peptide conjugation to morphilino oligomers: effects on antisense activity and specificity. Bioconjug. Chem. 16, 959-966.
    • (2005) Bioconjug. Chem. , vol.16 , pp. 959-966
    • Nelson, M.H.1    Stein, D.A.2    Kroeker, A.D.3    Hatievig, S.A.4    Iversen, P.L.5    Moulton, H.M.6
  • 79
    • 32344441681 scopus 로고    scopus 로고
    • Photochemically enhanced cellular delivery of cell penetrating peptide-PNA conjugates
    • DOI 10.1016/j.febslet.2006.01.077, PII S0014579306001475
    • Shiraishi, T. and Nielsen, P. E. (2006) Photochemically enhanced cellular delivery of cell-penetrating peptide-PNA conjugates. FEBS Lett. 580, 1451-1456. (Pubitemid 43222014)
    • (2006) FEBS Letters , vol.580 , Issue.5 , pp. 1451-1456
    • Shiraishi, T.1    Nielsen, P.E.2
  • 80
    • 33750498490 scopus 로고    scopus 로고
    • Induction of splice correction by cell-penetrating peptide nucleic acids
    • DOI 10.1002/jgm.950
    • El-Andaloussi, S., Johansson, H. J., Lundberg, P., and Langel, Ü. (2006) Induction of splice correction by cell-penetrating peptide nucleic acids. J. Gene Med. 8, 1262-1273. (Pubitemid 44660525)
    • (2006) Journal of Gene Medicine , vol.8 , Issue.10 , pp. 1262-1273
    • El-Andaloussi, S.1    Johansson, H.J.2    Lundberg, P.3    Langel, U.4
  • 81
    • 31544458695 scopus 로고    scopus 로고
    • Endosome trapping limits the efficiency of splicing correction by PNA-oligolysine conjugates
    • DOI 10.1016/j.jconrel.2005.10.026, PII S0168365905005444
    • Abes, S., Williams, D., Prevot, P., Theirry, A., Gait, M. J., and Lebleu, B. (2006) Endosome trapping limits the efficiency of splice correction by PNA-oligolysine conjugates. J. Control. Release 110, 595-604. (Pubitemid 43163449)
    • (2006) Journal of Controlled Release , vol.110 , Issue.3 , pp. 595-604
    • Abes, S.1    Williams, D.2    Prevot, P.3    Thierry, A.4    Gait, M.J.5    Lebleu, B.6
  • 83
    • 4444361522 scopus 로고    scopus 로고
    • Cellular delivery of a double-stranded oligonucleotide NFkappaB decoy by hybridization to complementary PNA linked to a cell-penetrating peptide
    • DOI 10.1038/sj.gt.3302291
    • Fisher, L., Soomets, U., Cortes Toro, V., Chilton, L., Jiang, Y., Langel, Ü., and Iverfeldt, K. (2004) Cellular delivery of double-stranded oligonucleotide NFkappaB decoy by hybridisation to complementary PNA linked to a cell-penetrating peptide. Gene Ther. 11, 1264-1272. (Pubitemid 39173433)
    • (2004) Gene Therapy , vol.11 , Issue.16 , pp. 1264-1272
    • Fisher, L.1    Soomets, U.2    Cortes Toro, V.3    Chilton, L.4    Jiang, Y.5    Langel, U.6    Iverfeldt, K.7
  • 85
    • 33645569141 scopus 로고    scopus 로고
    • Significant and prolonged antisense effect of multifunctional envelope-type nano device encapsulating antisense oligodeoxynucleotide
    • Nakamura, Y., Kogure, K., Yamada, Y., Futaki, S., and Harashima, H. (2006) Significant and prolonged antisense effect of multifunctional envelope-type nano device encapsulating antisense oligodeoxynucleotide. J. Pharm. Pharmacol. 58, 341-437.
    • (2006) J. Pharm. Pharmacol. , vol.58 , pp. 341-437
    • Nakamura, Y.1    Kogure, K.2    Yamada, Y.3    Futaki, S.4    Harashima, H.5
  • 86
    • 0842346326 scopus 로고    scopus 로고
    • Conjugate for efficient delivery of short interfering RNA (siRNA) into mammalian cells
    • DOI 10.1016/S0014-5793(03)01505-9
    • Muratovska, A. and Eccles, M. R. (2004) Conjugate for efficient delivery of short interfering RNA (siRNA) into mammalian cells. FEBS Lett. 558, 63-68. (Pubitemid 38167411)
    • (2004) FEBS Letters , vol.558 , Issue.1-3 , pp. 63-68
    • Muratovska, A.1    Eccles, M.R.2
  • 87
    • 4344651353 scopus 로고    scopus 로고
    • Visualizing a correlation between siRNA localization, cellular uptake, and RNAi in living cells
    • Chiu, Y. L., Ali, A., Chu, C. Y., Cao, H., and Rana, T. M. (2004) Visualizing a correlation between siRNA localization, cellular uptake, and RNAi in living cells. Chem. Biol. 11, 1165-1175.
    • (2004) Chem. Biol. , vol.11 , pp. 1165-1175
    • Chiu, Y.L.1    Ali, A.2    Chu, C.Y.3    Cao, H.4    Rana, T.M.5
  • 88
    • 39149093340 scopus 로고    scopus 로고
    • Enhancing the cellular uptake of siRNA duplexes following noncovalent packaging with protein transduction domain peptides
    • Meade, B. R. and Dowdy, S. F. (2008) Enhancing the cellular uptake of siRNA duplexes following noncovalent packaging with protein transduction domain peptides. Adv. Drug Deliv. Rev. 60, 530-536.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 530-536
    • Meade, B.R.1    Dowdy, S.F.2
  • 89
    • 34248644581 scopus 로고    scopus 로고
    • Octaarginine-modified multifunctional envelope-type nano device for siRNA
    • DOI 10.1016/j.jconrel.2007.03.010, PII S0168365907001447
    • Nakamura, Y., Kogure, S., Futaki, S., and Harashima, H. (2007) Octarginine- modifies multifunctional envelope-type nano device for siRNA. J. Control. Release 119, 360-367. (Pubitemid 46770881)
    • (2007) Journal of Controlled Release , vol.119 , Issue.3 , pp. 360-367
    • Nakamura, Y.1    Kogure, K.2    Futaki, S.3    Harashima, H.4
  • 90
    • 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
    • Synder, E. L. and Dowdy, S. F. (2005) Recent advances in the use of protein transduction domains for the delivery of peptides, proteins and nucleic acids in vivo. Exp. Opin. Drug Deliv. 2, 43-51.
    • (2005) Exp. Opin. Drug Deliv. , vol.2 , pp. 43-51
    • Synder, E.L.1    Dowdy, S.F.2
  • 91
    • 17644397358 scopus 로고    scopus 로고
    • Selective induction of apoptosis through the FADD/Caspase-8 pathway by a p53 C-terminal peptide in human pre-malignant and malignant cells
    • DOI 10.1002/ijc.20838
    • Li, Y., Mao, Y., Rosal, R. V., Dinnen, R. D., Williams, A. C., Brandt-Raut, P. W., and Fine, R. L. (2005) Selective induction of apoptosis through the FADD/caspase-8 pathway by p53c-terminal peptide in human premalignant and malignant cells. Int. J. Cancer 115, 55-64. (Pubitemid 40559668)
    • (2005) International Journal of Cancer , vol.115 , Issue.1 , pp. 55-64
    • Li, Y.1    Mao, Y.2    Rosal, R.V.3    Dinnen, R.D.4    Williams, A.C.5    Brandt-Rauf, P.W.6    Fine, R.L.7
  • 93
    • 45749120326 scopus 로고    scopus 로고
    • Cell-penetrating peptides as delivery vehicles for biology and medicine
    • Stewart, K. M., Horton, K. L., and Kelley, S. O. (2008) Cell-penetrating peptides as delivery vehicles for biology and medicine. Org. Biomol. Chem. 6, 2242-2255.
    • (2008) Org. Biomol. Chem. , vol.6 , pp. 2242-2255
    • Stewart, K.M.1    Horton, K.L.2    Kelley, S.O.3
  • 95
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusognenic 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 fusognenic peptide enhances escape of Tat-fusion proteins after lipid raft macropinocytosis. Nat. Med. 10, 310-315.
    • (2004) Nat. Med. , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 96
    • 35248880092 scopus 로고    scopus 로고
    • Tat transduction: The molecular mechanism and therapeutic prospects
    • Gump, J. M. and Dowdy, S. F. (2007) Tat transduction: the molecular mechanism and therapeutic prospects. Trends Mol. Med. 13, 443-448.
    • (2007) Trends Mol. Med. , vol.13 , pp. 443-448
    • Gump, J.M.1    Dowdy, S.F.2
  • 97
    • 38949192863 scopus 로고    scopus 로고
    • Tat peptide-mediated intracellular delivery of pharmaceutical nanocarriers
    • Torchilin, V. P. (2008) Tat peptide-mediated intracellular delivery of pharmaceutical nanocarriers. Adv. Drug Deliv. Rev. 60, 548-558.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 548-558
    • Torchilin, V.P.1
  • 98
    • 0039547497 scopus 로고
    • Determination of the pore size of cell walls of living plant cells
    • Carpita, N., Sabularse, D., Montezinos, D., and Delmer, D. (1979) Determination of the pore size of cell walls of living plant cells. Science 205, 1144-1147.
    • (1979) Science , vol.205 , pp. 1144-1147
    • Carpita, N.1    Sabularse, D.2    Montezinos, D.3    Delmer, D.4
  • 99
    • 34247104947 scopus 로고    scopus 로고
    • Transfection and expression of plasmid DNA in plant cells by an arginine-rich intracellular delivery peptide without protoplast preparation
    • DOI 10.1016/j.febslet.2007.03.076, PII S0014579307003547
    • Chen, C.-P., Chou, J.-C., Liu, B. R., Chang, M., and Lee, H.-J. (2007) Transfection and expression of plasmid DNA in plant cells by arginine-rich intracellular delivery peptide without protoplast preparation. FEBS Lett. 581, 1891-1897. (Pubitemid 46602278)
    • (2007) FEBS Letters , vol.581 , Issue.9 , pp. 1891-1897
    • Chen, C.-P.1    Chou, J.-C.2    Liu, B.R.3    Chang, M.4    Lee, H.-J.5
  • 100
    • 39149096277 scopus 로고    scopus 로고
    • Cell membrane diversity in noncovalent protein transduction
    • Liu, B. R., Chou, J.-C., and Lee, H. J. (2008) Cell membrane diversity in noncovalent protein transduction. J. Membr. Biol. 222, 1-15.
    • (2008) J. Membr. Biol. , vol.222 , pp. 1-15
    • Liu, B.R.1    Chou, J.-C.2    Lee, H.J.3
  • 101
    • 33847351351 scopus 로고    scopus 로고
    • Noncovalent protein transduction in plant cells by macropinocytosis
    • DOI 10.1111/j.1469-8137.2007.01977.x
    • Chang, M., Chou, J.-C., Chen, C.-P., Liu, B. R., and Lee, H.-J. (2007) Noncovalent protein transduction in plant cells by macropinocytosis. New Phytol. 174, 46-56. (Pubitemid 46333287)
    • (2007) New Phytologist , vol.174 , Issue.1 , pp. 46-56
    • Chang, M.1    Chou, J.-C.2    Chen, C.-P.3    Liu, B.R.4    Lee, H.-J.5
  • 102
    • 0037244199 scopus 로고    scopus 로고
    • Direct delivery of bacterial avirulence proteins into resistant Arabidopsis protoplasts leads to hypersensitive cell death
    • DOI 10.1046/j.0960-7412.2002.001614.x
    • Wu, Y., Wood, M. D., Tao, Y., and Katagiri, F. (2003) Direct delivery of bacterial avirulence proteins into resistant arabidopsis protoplasts leads to hypersensitive death. Plant J. 33, 131-137. (Pubitemid 36117295)
    • (2003) Plant Journal , vol.33 , Issue.1 , pp. 131-137
    • Wu, Y.1    Wood, M.D.2    Tao, Y.3    Katagiri, F.4
  • 104
    • 77951100527 scopus 로고    scopus 로고
    • Isolated microspore embryogenesis in cereals: Aspects and prospects
    • (Kumar, A. and Sopory, S. K., eds.). IK International, New Delhi.
    • Chugh, A. and Eudes, F. (2008) Isolated microspore embryogenesis in cereals: aspects and prospects. In Recent Advances in Plant Biotechnology. (Kumar, A. and Sopory, S. K., eds.). pp. 205-226, IK International, New Delhi.
    • (2008) Recent Advances in Plant Biotechnology. , pp. 205-226
    • Chugh, A.1    Eudes, F.2
  • 105
    • 33645127973 scopus 로고    scopus 로고
    • Genetic transformation of barley (Hordeum vulgare L.) via infection of androgenetic pollen cultures with Agrobacterium tumefaciens
    • Kumlehn, J., Serazetdinova, L., Hensel, G., Becker, D., and Loerz, H. (2006) Genetic transformation of barley (Hordeum vulgare L.) via infection of androgenetic pollen cultures with Agrobacterium tumefaciens. Plant Biotechnol. J. 4, 251-261.
    • (2006) Plant Biotechnol. J. , vol.4 , pp. 251-261
    • Kumlehn, J.1    Serazetdinova, L.2    Hensel, G.3    Becker, D.4    Loerz, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.