메뉴 건너뛰기




Volumn , Issue , 2011, Pages 221-246

Peptide and Protein Delivery with Cell-penetrating Peptides

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84882561630     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-384935-9.10010-0     Document Type: Chapter
Times cited : (5)

References (137)
  • 1
    • 23944458820 scopus 로고    scopus 로고
    • Polyethyleneimine as a transmembrane carrier of fluorescently labeled proteins and antibodies
    • V.V. Didenko, H. Ngo and D.S. Baskin (2005) Polyethyleneimine as a transmembrane carrier of fluorescently labeled proteins and antibodies. Anal. Biochem. 344 168-173.
    • (2005) Anal. Biochem. , vol.344 , pp. 168-173
    • Didenko, V.V.1    Ngo, H.2    Baskin, D.S.3
  • 2
    • 20144389743 scopus 로고    scopus 로고
    • Intracellular delivery of proteins into mammalian living cells by polyethylenimine-cationization
    • J. Futami, M. Kitazoe, T. Maeda, E. Nukui, M. Sakaguchi, J. Kosaka, et al. (2005) Intracellular delivery of proteins into mammalian living cells by polyethylenimine-cationization. J. Biosci. Bioeng. 99 95-103.
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 95-103
    • Futami, J.1    Kitazoe, M.2    Maeda, T.3    Nukui, E.4    Sakaguchi, M.5    Kosaka, J.6
  • 3
    • 22344440313 scopus 로고    scopus 로고
    • Protein transduction assisted by polyethylenimine-cationized carrier proteins
    • M. Kitazoe, H. Murata, J. Futami, T. Maeda, M. Sakaguchi, M. Miyazaki, et al. (2005) Protein transduction assisted by polyethylenimine-cationized carrier proteins. J. Biochem. 137 693-701.
    • (2005) J. Biochem. , vol.137 , pp. 693-701
    • Kitazoe, M.1    Murata, H.2    Futami, J.3    Maeda, T.4    Sakaguchi, M.5    Miyazaki, M.6
  • 4
    • 0028789321 scopus 로고
    • Recent advances in liposomal drug-delivery systems
    • A. Chonn and P.R. Cullis (1995) Recent advances in liposomal drug-delivery systems. Curr. Opin. Biotechnol. 6 698-708.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 698-708
    • Chonn, A.1    Cullis, P.R.2
  • 5
    • 0035860724 scopus 로고    scopus 로고
    • Intracellular delivery of proteins with a new lipid-mediated delivery system
    • O. Zelphati, Y. Wang, S. Kitada, J.C. Reed, P.L. Felgner and J. Corbeil (2001) Intracellular delivery of proteins with a new lipid-mediated delivery system. J. Biol. Chem. 276 35103-35110.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35103-35110
    • Zelphati, O.1    Wang, Y.2    Kitada, S.3    Reed, J.C.4    Felgner, P.L.5    Corbeil, J.6
  • 6
    • 33845728507 scopus 로고    scopus 로고
    • Optimizing targeted gene delivery: Chemical modification of viral vectors and synthesis of artificial virus vector systems
    • S. Boeckle and E. Wagner (2006) Optimizing targeted gene delivery: Chemical modification of viral vectors and synthesis of artificial virus vector systems. AAPS J. 8 E731-E742.
    • (2006) AAPS J. , vol.8 , pp. E731-E742
    • Boeckle, S.1    Wagner, E.2
  • 8
    • 34548586993 scopus 로고    scopus 로고
    • Efficient electroporation of DNA and protein into confluent and differentiated epithelial cells in culture
    • A.A. Deora, F. Diaz, R. Schreiner and E. Rodriguez-Boulan (2007) Efficient electroporation of DNA and protein into confluent and differentiated epithelial cells in culture. Traffic 8 1304-1312.
    • (2007) Traffic , vol.8 , pp. 1304-1312
    • Deora, A.A.1    Diaz, F.2    Schreiner, R.3    Rodriguez-Boulan, E.4
  • 9
    • 0027496649 scopus 로고
    • Roles of kinesin and kinesin-like proteins in sea urchin embryonic cell division: Evaluation using antibody microinjection
    • B.D. Wright, M. Terasaki and J.M. Scholey (1993) Roles of kinesin and kinesin-like proteins in sea urchin embryonic cell division: Evaluation using antibody microinjection. J. Cell Biol. 123 681-689.
    • (1993) J. Cell Biol. , vol.123 , pp. 681-689
    • Wright, B.D.1    Terasaki, M.2    Scholey, J.M.3
  • 10
    • 52049108490 scopus 로고    scopus 로고
    • Microinjection into cultured hippocampal neurons: A straightforward approach for controlled cellular delivery of nucleic acids, peptides and antibodies
    • C. Lappe-Siefke, C. Maas and M. Kneussel (2008) Microinjection into cultured hippocampal neurons: A straightforward approach for controlled cellular delivery of nucleic acids, peptides and antibodies. J. Neurosci. Methods 175 88-95.
    • (2008) J. Neurosci. Methods , vol.175 , pp. 88-95
    • Lappe-Siefke, C.1    Maas, C.2    Kneussel, M.3
  • 11
    • 0032813559 scopus 로고    scopus 로고
    • Variability of human systemic humoral immune responses to adenovirus gene transfer vectors administered to different organs
    • B.G. Harvey, N.R. Hackett, T. El-Sawy, T.K. Rosengart, E.A. Hirschowitz, M.D. Lieberman, et al. (1999) Variability of human systemic humoral immune responses to adenovirus gene transfer vectors administered to different organs. J. Virol. 73 6729-6742.
    • (1999) J. Virol. , vol.73 , pp. 6729-6742
    • Harvey, B.G.1    Hackett, N.R.2    El-Sawy, T.3    Rosengart, T.K.4    Hirschowitz, E.A.5    Lieberman, M.D.6
  • 12
    • 11144248909 scopus 로고    scopus 로고
    • The innate immune response to adenovirus vectors
    • D.A. Muruve (2004) The innate immune response to adenovirus vectors. Hum. Gene Ther. 15 1157-1166.
    • (2004) Hum. Gene Ther. , vol.15 , pp. 1157-1166
    • Muruve, D.A.1
  • 13
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • A.D. Frankel and C.O. Pabo (1988) Cellular uptake of the tat protein from human immunodeficiency virus. Cell 55 1189-1193.
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 14
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein
    • M. Green and P.M. Loewenstein (1988) Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein. Cell 55 1179-1188.
    • (1988) Cell , vol.55 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.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
    • E. Vivés, P. Brodin and B. Lebleu (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
    • Vivés, E.1    Brodin, P.2    Lebleu, B.3
  • 16
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters
    • P.A. Wender, D.J. Mitchell, K. Pattabiraman, E.T. Pelkey, L. Steinman and J.B. Rothbard (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 13003-13008.
    • (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
  • 18
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • D. Derossi, A.H. Joliot, G. Chassaing and A. Prochiantz (1994) The third helix of the Antennapedia homeodomain 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.3    Prochiantz, A.4
  • 19
    • 0031471203 scopus 로고    scopus 로고
    • Intercellular trafficking and protein delivery by a herpesvirus structural protein
    • G. Elliott and P. O'Hare (1997) Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell 88 223-233.
    • (1997) Cell , vol.88 , pp. 223-233
    • Elliott, G.1    O'Hare, P.2
  • 20
    • 0035478616 scopus 로고    scopus 로고
    • VE-cadherin-derived cell-penetrating peptide, pVEC, with carrier functions
    • A. Elmquist, M. Lindgren, T. Bartfai and Ü Langel (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, A.4
  • 23
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • M.C. Morris, J. Depollier, J. Mery, F. Heitz and G. Divita (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
  • 24
    • 0033794501 scopus 로고    scopus 로고
    • Polyarginine enters cells more efficiently than other polycationic homopolymers
    • D.J. Mitchell, D.T. Kim, L. Steinman, C.G. Fathman and J.B. Rothbard (2000) Polyarginine enters cells more efficiently than other polycationic homopolymers. J. Pept. Res. 56 318-325.
    • (2000) J. Pept. Res. , vol.56 , pp. 318-325
    • Mitchell, D.J.1    Kim, D.T.2    Steinman, L.3    Fathman, C.G.4    Rothbard, J.B.5
  • 25
    • 10344221003 scopus 로고    scopus 로고
    • Cellular uptake of arginine-rich peptides: Roles for macropinocytosis and actin rearrangement
    • I. Nakase, M. Niwa, T. Takeuchi, K. Sonomura, N. Kawabata, Y. Koike, et al. (2004) Cellular uptake of arginine-rich peptides: Roles for macropinocytosis and actin rearrangement. Mol. Ther. 10 1011-1022.
    • (2004) Mol. Ther. , vol.10 , pp. 1011-1022
    • Nakase, I.1    Niwa, M.2    Takeuchi, T.3    Sonomura, K.4    Kawabata, N.5    Koike, Y.6
  • 26
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • J.D. Lear, Z.R. Wasserman and W.F. DeGrado (1988) Synthetic amphiphilic peptide models for protein ion channels. Science 240 1177-1181.
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    DeGrado, W.F.3
  • 27
    • 0025724956 scopus 로고
    • Interaction with phospholipid bilayers, ion channel formation, and antimicrobial activity of basic amphipathic alpha-helical model peptides of various chain lengths
    • Y. Agawa, S. Lee, S. Ono, H. Aoyagi, M. Ohno, T. Taniguchi, et al. (1991) Interaction with phospholipid bilayers, ion channel formation, and antimicrobial activity of basic amphipathic alpha-helical model peptides of various chain lengths. J. Biol. Chem. 266 20218-20222.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20218-20222
    • Agawa, Y.1    Lee, S.2    Ono, S.3    Aoyagi, H.4    Ohno, M.5    Taniguchi, T.6
  • 28
    • 0026093570 scopus 로고
    • Retention behaviour of a template-assembled synthetic protein and its amphiphilic building blocks on reversed-phase columns
    • V. Steiner, M. Schar, K.O. Bornsen and M. Mutter (1991) Retention behaviour of a template-assembled synthetic protein and its amphiphilic building blocks on reversed-phase columns. J. Chromatogr. 586 43-50.
    • (1991) J. Chromatogr. , vol.586 , pp. 43-50
    • Steiner, V.1    Schar, M.2    Bornsen, K.O.3    Mutter, M.4
  • 29
    • 0032508926 scopus 로고    scopus 로고
    • Cellular uptake of an alpha-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically
    • J. Oehlke, A. Scheller, B. Wiesner, E. Krause, M. Beyermann, E. Klauschenz, et al. (1998) Cellular uptake of an alpha-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically. Biochim. Biophys. Acta 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
  • 33
    • 0034237577 scopus 로고    scopus 로고
    • Protein transduction: Unrestricted delivery into all cells?
    • S.R. Schwarze, K.A. Hruska and S.F. Dowdy (2000) Protein transduction: Unrestricted delivery into all cells? Trends Cell Biol. 10 290-295.
    • (2000) Trends Cell Biol. , vol.10 , pp. 290-295
    • Schwarze, S.R.1    Hruska, K.A.2    Dowdy, S.F.3
  • 35
    • 9244255342 scopus 로고    scopus 로고
    • Protein cargo delivery properties of cell-penetrating peptides. A comparative study
    • P. Säälik, A. Elmquist, M. Hansen, K. Padari, K. Saar, K. Viht, et al. (2004) Protein cargo delivery properties of cell-penetrating peptides. A comparative study. Bioconjug. Chem. 15 1246-1253.
    • (2004) Bioconjug. Chem. , vol.15 , pp. 1246-1253
    • Säälik, P.1    Elmquist, A.2    Hansen, M.3    Padari, K.4    Saar, K.5    Viht, K.6
  • 37
    • 69949138136 scopus 로고    scopus 로고
    • CPP-protein constructs induce a population of non-acidic vesicles during trafficking through endo-lysosomal pathway
    • H. Räägel, P. Säälik, M. Hansen, Ü Langel and M. Pooga (2009) CPP-protein constructs induce a population of non-acidic vesicles during trafficking through endo-lysosomal pathway. J. Control. Release 139 108-117.
    • (2009) J. Control. Release , vol.139 , pp. 108-117
    • Räägel, H.1    Säälik, P.2    Hansen, M.3    Langel, A.4    Pooga, M.5
  • 38
    • 23044485527 scopus 로고    scopus 로고
    • Translocation of beta-galactosidase mediated by the cell-penetrating peptide pep-1 into lipid vesicles and human HeLa cells is driven by membrane electrostatic potential
    • S.T. Henriques, J. Costa and M.A. Castanho (2005) Translocation of beta-galactosidase mediated by the cell-penetrating peptide pep-1 into lipid vesicles and human HeLa cells is driven by membrane electrostatic potential. Biochemistry 44 10189-10198.
    • (2005) Biochemistry , vol.44 , pp. 10189-10198
    • Henriques, S.T.1    Costa, J.2    Castanho, M.A.3
  • 39
    • 28544450399 scopus 로고    scopus 로고
    • Biophysical and biological studies of end-group-modified derivatives of Pep-1
    • K. Weller, S. Lauber, M. Lerch, A. Renaud, H.P. Merkle and O. Zerbe (2005) Biophysical and biological studies of end-group-modified derivatives of Pep-1. Biochemistry 44 15799-15811.
    • (2005) Biochemistry , vol.44 , pp. 15799-15811
    • Weller, K.1    Lauber, S.2    Lerch, M.3    Renaud, A.4    Merkle, H.P.5    Zerbe, O.6
  • 40
    • 33846436425 scopus 로고    scopus 로고
    • Protein delivery by the cell-penetrating peptide YTA2
    • H. Myrberg, M. Lindgren and Ü Langel (2007) Protein delivery by the cell-penetrating peptide YTA2. Bioconjug. Chem. 18 170-174.
    • (2007) Bioconjug. Chem. , vol.18 , pp. 170-174
    • Myrberg, H.1    Lindgren, M.2    Langel, A.3
  • 41
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • J.S. Wadia, R.V. Stan and S.F. Dowdy (2004) Transducible TAT-HA fusogenic 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
  • 42
    • 74049160383 scopus 로고    scopus 로고
    • Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction
    • J.M. Gump, R.K. June and S.F. Dowdy (2010) Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction. J. Biol. Chem. 285 1500-1507.
    • (2010) J. Biol. Chem. , vol.285 , pp. 1500-1507
    • Gump, J.M.1    June, R.K.2    Dowdy, S.F.3
  • 43
    • 65649131227 scopus 로고    scopus 로고
    • Efficient CPP-mediated Cre protein delivery to developing and adult CNS tissues
    • Y. Gitton, L. Tibaldi, E. Dupont, G. Levi and A. Joliot (2009) Efficient CPP-mediated Cre protein delivery to developing and adult CNS tissues. BMC Biotechnol. 9 40.
    • (2009) BMC Biotechnol. , vol.9 , pp. 40
    • Gitton, Y.1    Tibaldi, L.2    Dupont, E.3    Levi, G.4    Joliot, A.5
  • 44
    • 38549110556 scopus 로고    scopus 로고
    • Comparison of protein transduction domains in mediating cell delivery of a secreted CRE protein
    • P.A. Shaw, I.R. Catchpole, C.A. Goddard and W.H. Colledge (2008) Comparison of protein transduction domains in mediating cell delivery of a secreted CRE protein. Biochemistry 47 1157-1166.
    • (2008) Biochemistry , vol.47 , pp. 1157-1166
    • Shaw, P.A.1    Catchpole, I.R.2    Goddard, C.A.3    Colledge, W.H.4
  • 45
    • 0141446039 scopus 로고    scopus 로고
    • Cell membrane lipid rafts mediate caveolar endocytosis of HIV-1 Tat fusion proteins
    • A. Fittipaldi, A. Ferrari, M. Zoppe, C. Arcangeli, V. Pellegrini, F. Beltram, et al. (2003) Cell membrane lipid rafts mediate caveolar endocytosis of HIV-1 Tat fusion proteins. J. Biol. Chem. 278 34141-34149.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34141-34149
    • Fittipaldi, A.1    Ferrari, A.2    Zoppe, M.3    Arcangeli, C.4    Pellegrini, V.5    Beltram, F.6
  • 46
    • 20444403719 scopus 로고    scopus 로고
    • Effects of cargo molecules on the cellular uptake of arginine-rich cell-penetrating peptides
    • J.R. Maiolo, M. Ferrer and E.A. Ottinger (2005) Effects of cargo molecules on the 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
  • 47
    • 35048856889 scopus 로고    scopus 로고
    • Cargo-dependent cytotoxicity and delivery efficacy of cell-penetrating peptides: A comparative study
    • S. El-Andaloussi, P. Järver, H.J. Johansson and Ü Langel (2007) Cargo-dependent cytotoxicity and delivery efficacy of cell-penetrating peptides: A comparative study. Biochem. J. 407 285-292.
    • (2007) Biochem. J. , vol.407 , pp. 285-292
    • El-Andaloussi, S.1    Järver, P.2    Johansson, H.J.3    Langel, A.4
  • 48
    • 33748648777 scopus 로고    scopus 로고
    • Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells
    • G. TÜnnemann, R.M. Martin, S. Haupt, C. Patsch, F. Edenhofer and M.C. Cardoso (2006) Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells. FASEB J. 20 1775-1784.
    • (2006) FASEB J. , vol.20 , pp. 1775-1784
    • TÜnnemann, G.1    Martin, R.M.2    Haupt, S.3    Patsch, C.4    Edenhofer, F.5    Cardoso, M.C.6
  • 49
    • 77958150359 scopus 로고    scopus 로고
    • Peptide-mediated protein delivery – Which pathways are penetrable?
    • H. Räägel, P. Säälik and M. Pooga (2010) Peptide-mediated protein delivery – Which pathways are penetrable? Biochim. Biophys. Acta 1798 2240-2248.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 2240-2248
    • Räägel, H.1    Säälik, P.2    Pooga, M.3
  • 50
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • D. Derossi, S. Calvet, A. Trembleau, A. Brunissen, G. Chassaing and A. Prochiantz (1996) Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J. Biol. Chem. 271 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
  • 52
    • 0035208275 scopus 로고    scopus 로고
    • Cellular internalization of a cargo complex with a novel peptide derived from the third helix of the islet-1 homeodomain. Comparison with the penetratin peptide
    • K. Kilk, M. Magzoub, M. Pooga, L.E. Eriksson, Ü Langel and A. Gräslund (2001) Cellular internalization of a cargo complex with a novel peptide derived from the third helix of the islet-1 homeodomain. Comparison with the penetratin peptide. Bioconjug. Chem. 12 911-916.
    • (2001) Bioconjug. Chem. , vol.12 , pp. 911-916
    • Kilk, K.1    Magzoub, M.2    Pooga, M.3    Eriksson, L.E.4    Langel, A.5    Gräslund, A.6
  • 53
    • 0036289650 scopus 로고    scopus 로고
    • Positively charged DNA-binding proteins cause apparent cell membrane translocation
    • M. Lundberg and M. Johansson (2002) Positively charged DNA-binding proteins cause apparent cell membrane translocation. Biochem. Biophys. Res. Commun. 291 367-371.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 367-371
    • Lundberg, M.1    Johansson, M.2
  • 54
    • 0346460957 scopus 로고    scopus 로고
    • Cell-penetrating peptides. A reevaluation of the mechanism of cellular uptake
    • J.P. Richard, K. Melikov, E. Vives, C. Ramos, B. Verbeure, M.J. Gait, et al. (2003) Cell-penetrating peptides. A reevaluation of the mechanism of cellular uptake. J. Biol. Chem. 278 585-590.
    • (2003) J. Biol. Chem. , vol.278 , pp. 585-590
    • Richard, J.P.1    Melikov, K.2    Vives, E.3    Ramos, C.4    Verbeure, B.5    Gait, M.J.6
  • 56
    • 38949116621 scopus 로고    scopus 로고
    • Thermodynamic studies and binding mechanisms of cell-penetrating peptides with lipids and glycosaminoglycans
    • A. Ziegler (2008) Thermodynamic studies and binding mechanisms of cell-penetrating peptides with lipids and glycosaminoglycans. Adv. Drug Deliv. Rev. 60 580-597.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 580-597
    • Ziegler, A.1
  • 57
    • 70350023192 scopus 로고    scopus 로고
    • Arginine-rich peptides destabilize the plasma membrane, consistent with a pore formation translocation mechanism of cell-penetrating peptides
    • H.D. Herce, A.E. Garcia, J. Litt, R.S. Kane, P. Martin, N. Enrique, et al. (2009) Arginine-rich peptides destabilize the plasma membrane, consistent with a pore formation translocation mechanism of cell-penetrating peptides. Biophys. J. 97 1917-1925.
    • (2009) Biophys. J. , vol.97 , pp. 1917-1925
    • Herce, H.D.1    Garcia, A.E.2    Litt, J.3    Kane, R.S.4    Martin, P.5    Enrique, N.6
  • 58
    • 75449096829 scopus 로고    scopus 로고
    • Molecular electroporation and the transduction of oligoarginines
    • K. Cahill (2009) Molecular electroporation and the transduction of oligoarginines. Phys. Biol. 7 16001.
    • (2009) Phys. Biol. , vol.7 , pp. 16001
    • Cahill, K.1
  • 59
    • 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
    • S. Console, C. Marty, C. Garcia-Echeverria, R. Schwendener and K. Ballmer-Hofer (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
  • 60
    • 3843050301 scopus 로고    scopus 로고
    • Enhanced heparan sulfate proteoglycan-mediated uptake of cell-penetrating peptide-modified liposomes
    • C. Marty, C. Meylan, H. Schott, K. Ballmer-Hofer and R.A. Schwendener (2004) Enhanced heparan sulfate proteoglycan-mediated uptake of cell-penetrating peptide-modified liposomes. Cell Mol. Life Sci. 61 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
  • 61
    • 14044270161 scopus 로고    scopus 로고
    • Binding of oligoarginine to membrane lipids and heparan sulfate: Structural and thermodynamic characterization of a cell-penetrating peptide
    • E. Goncalves, E. Kitas and J. Seelig (2005) Binding of oligoarginine to membrane lipids and heparan sulfate: Structural and thermodynamic characterization of a cell-penetrating peptide. Biochemistry 44 2692-2702.
    • (2005) Biochemistry , vol.44 , pp. 2692-2702
    • Goncalves, E.1    Kitas, E.2    Seelig, J.3
  • 62
    • 34548162679 scopus 로고    scopus 로고
    • Cell-surface proteoglycans as molecular portals for cationic peptide and polymer entry into cells
    • G.M. Poon and J. Gariepy (2007) Cell-surface proteoglycans as molecular portals for cationic peptide and polymer entry into cells. Biochem. Soc. Trans. 35 788-793.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 788-793
    • Poon, G.M.1    Gariepy, J.2
  • 63
    • 66149183010 scopus 로고    scopus 로고
    • Protein delivery with transportans is mediated by caveolae rather than flotillin-dependent pathways
    • P. Säälik, K. Padari, A. Niinep, A. Lorents, M. Hansen, E. Jokitalo, et al. (2009) Protein delivery with transportans is mediated by caveolae rather than flotillin-dependent pathways. Bioconjug. Chem. 20 877-887.
    • (2009) Bioconjug. Chem. , vol.20 , pp. 877-887
    • Säälik, P.1    Padari, K.2    Niinep, A.3    Lorents, A.4    Hansen, M.5    Jokitalo, E.6
  • 64
    • 0035943423 scopus 로고    scopus 로고
    • Emerging themes in lipid rafts and caveolae
    • F. Galbiati, B. Razani and M.P. Lisanti (2001) Emerging themes in lipid rafts and caveolae. Cell 106 403-411.
    • (2001) Cell , vol.106 , pp. 403-411
    • Galbiati, F.1    Razani, B.2    Lisanti, M.P.3
  • 66
    • 33846223900 scopus 로고    scopus 로고
    • Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis
    • I. Nakase, A. Tadokoro, N. Kawabata, T. Takeuchi, H. Katoh, K. Hiramoto, et al. (2007) Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis. Biochemistry 46 492-501.
    • (2007) Biochemistry , vol.46 , pp. 492-501
    • Nakase, I.1    Tadokoro, A.2    Kawabata, N.3    Takeuchi, T.4    Katoh, H.5    Hiramoto, K.6
  • 68
    • 70350347712 scopus 로고    scopus 로고
    • Imaging endocytic clathrin structures in living cells
    • T. Kirchhausen (2009) Imaging endocytic clathrin structures in living cells. Trends Cell Biol. 19 596-605.
    • (2009) Trends Cell Biol. , vol.19 , pp. 596-605
    • Kirchhausen, T.1
  • 69
    • 24344448619 scopus 로고    scopus 로고
    • Cationic cell-penetrating peptides interfere with TNF signalling by induction of TNF receptor internalization
    • M. Fotin-Mleczek, S. Welte, O. Mader, F. Duchardt, R. Fischer, H. Hufnagel, et al. (2005) Cationic cell-penetrating peptides interfere with TNF signalling by induction of TNF receptor internalization. J. Cell Sci. 118 3339-3351.
    • (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
  • 70
    • 0024595608 scopus 로고
    • Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation
    • J.E. Heuser and R.G. Anderson (1989) Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation. J. Cell Biol. 108 389-400.
    • (1989) J. Cell Biol. , vol.108 , pp. 389-400
    • Heuser, J.E.1    Anderson, R.G.2
  • 72
    • 0037684840 scopus 로고    scopus 로고
    • Caveolae/raft-dependent endocytosis
    • I.R. Nabi and P.U. Le (2003) Caveolae/raft-dependent endocytosis. J. Cell Biol. 161 673-677.
    • (2003) J. Cell Biol. , vol.161 , pp. 673-677
    • Nabi, I.R.1    Le, P.U.2
  • 73
    • 55449129956 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis of ErbB2 in geldanamycin-treated human breast cancer cells
    • D.J. Barr, A.G. Ostermeyer-Fay, R.A. Matundan and D.A. Brown (2008) Clathrin-independent endocytosis of ErbB2 in geldanamycin-treated human breast cancer cells. J. Cell Sci. 121 3155-3166.
    • (2008) J. Cell Sci. , vol.121 , pp. 3155-3166
    • Barr, D.J.1    Ostermeyer-Fay, A.G.2    Matundan, R.A.3    Brown, D.A.4
  • 74
    • 13444273098 scopus 로고    scopus 로고
    • Clathrin- and caveolin-1-independent endocytosis: Entry of simian virus 40 into cells devoid of caveolae
    • E.M. Damm, L. Pelkmans, J. Kartenbeck, A. Mezzacasa, T. Kurzchalia and A. Helenius (2005) Clathrin- and caveolin-1-independent endocytosis: Entry of simian virus 40 into cells devoid of caveolae. J. Cell Biol. 168 477-488.
    • (2005) J. Cell Biol. , vol.168 , pp. 477-488
    • Damm, E.M.1    Pelkmans, L.2    Kartenbeck, J.3    Mezzacasa, A.4    Kurzchalia, T.5    Helenius, A.6
  • 75
    • 0042355293 scopus 로고    scopus 로고
    • Caveolae-mediated internalization of extracellular HIV-1 tat fusion proteins visualized in real time
    • A. Ferrari, V. Pellegrini, C. Arcangeli, A. Fittipaldi, M. Giacca and F. Beltram (2003) Caveolae-mediated internalization of extracellular HIV-1 tat fusion proteins visualized in real time. Mol. Ther. 8 284-294.
    • (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
  • 77
    • 33746338257 scopus 로고    scopus 로고
    • A novel type of PTD, common helix-loop-helix motif, could efficiently mediate protein transduction into mammalian cells
    • J. Chen, G. Li, J. Lu, L. Chen, Y. Huang, H. Wu, et al. (2006) A novel type of PTD, common helix-loop-helix motif, could efficiently mediate protein transduction into mammalian cells. Biochem. Biophys. Res. Commun. 347 931-940.
    • (2006) Biochem. Biophys. Res. Commun. , vol.347 , pp. 931-940
    • Chen, J.1    Li, G.2    Lu, J.3    Chen, L.4    Huang, Y.5    Wu, H.6
  • 78
    • 34247481907 scopus 로고    scopus 로고
    • Acid wash in determining cellular uptake of Fab/cell-permeating peptide conjugates
    • S. Kameyama, M. Horie, T. Kikuchi, T. Omura, A. Tadokoro, T. Takeuchi, et al. (2007) Acid wash in determining cellular uptake of Fab/cell-permeating peptide conjugates. Biopolymers 88 98-107.
    • (2007) Biopolymers , vol.88 , pp. 98-107
    • Kameyama, S.1    Horie, M.2    Kikuchi, T.3    Omura, T.4    Tadokoro, A.5    Takeuchi, T.6
  • 79
    • 36448986388 scopus 로고    scopus 로고
    • Transdermal delivery of proteins mediated by non-covalently associated arginine-rich intracellular delivery peptides
    • Y.W. Hou, M.H. Chan, H.R. Hsu, B.R. Liu, C.P. Chen, H.H. Chen, et al. (2007) Transdermal delivery of proteins mediated by non-covalently associated arginine-rich intracellular delivery peptides. Exp. Dermatol. 16 999-1006.
    • (2007) Exp. Dermatol. , vol.16 , pp. 999-1006
    • Hou, Y.W.1    Chan, M.H.2    Hsu, H.R.3    Liu, B.R.4    Chen, C.P.5    Chen, H.H.6
  • 80
    • 34147103472 scopus 로고    scopus 로고
    • First step of the cell-penetrating peptide mechanism involves Rac1 GTPase-dependent actin-network remodelling
    • S. Gerbal-Chaloin, C. Gondeau, G. Aldrian-Herrada, F. Heitz, C. Gauthier-Rouviere and G. Divita (2007) First step of the cell-penetrating peptide mechanism involves Rac1 GTPase-dependent actin-network remodelling. Biol. Cell 99 223-238.
    • (2007) Biol. Cell , vol.99 , pp. 223-238
    • Gerbal-Chaloin, S.1    Gondeau, C.2    Aldrian-Herrada, G.3    Heitz, F.4    Gauthier-Rouviere, C.5    Divita, G.6
  • 81
    • 56349133196 scopus 로고    scopus 로고
    • The GTPase-activating protein GRAF1 regulates the CLIC/GEEC endocytic pathway
    • R. Lundmark, G.J. Doherty, M.T. Howes, K. Cortese, Y. Vallis, R.G. Parton, et al. (2008) The GTPase-activating protein GRAF1 regulates the CLIC/GEEC endocytic pathway. Curr. Biol. 18 1802-1808.
    • (2008) Curr. Biol. , vol.18 , pp. 1802-1808
    • Lundmark, R.1    Doherty, G.J.2    Howes, M.T.3    Cortese, K.4    Vallis, Y.5    Parton, R.G.6
  • 83
    • 0036232040 scopus 로고    scopus 로고
    • GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway
    • S. Sabharanjak, P. Sharma, R.G. Parton and S. Mayor (2002) GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway. Dev. Cell 2 411-423.
    • (2002) Dev. Cell , vol.2 , pp. 411-423
    • Sabharanjak, S.1    Sharma, P.2    Parton, R.G.3    Mayor, S.4
  • 84
    • 69449093833 scopus 로고    scopus 로고
    • Steric and not structure-specific factors dictate the endocytic mechanism of glycosylphosphatidylinositol-anchored proteins
    • P. Bhagatji, R. Leventis, J. Comeau, M. Refaei and J.R. Silvius (2009) Steric and not structure-specific factors dictate the endocytic mechanism of glycosylphosphatidylinositol-anchored proteins. J. Cell Biol. 186 615-628.
    • (2009) J. Cell Biol. , vol.186 , pp. 615-628
    • Bhagatji, P.1    Leventis, R.2    Comeau, J.3    Refaei, M.4    Silvius, J.R.5
  • 85
    • 69449087070 scopus 로고    scopus 로고
    • Endocytosis of lipid-anchored proteins: Excluding GEECs from the crowd
    • B. Nichols (2009) Endocytosis of lipid-anchored proteins: Excluding GEECs from the crowd. J. Cell Biol. 186 457-459.
    • (2009) J. Cell Biol. , vol.186 , pp. 457-459
    • Nichols, B.1
  • 86
    • 13444310587 scopus 로고    scopus 로고
    • Ultrastructural identification of uncoated caveolin-independent early endocytic vehicles
    • M. Kirkham, A. Fujita, R. Chadda, S.J. Nixon, T.V. Kurzchalia, D.K. Sharma, et al. (2005) Ultrastructural identification of uncoated caveolin-independent early endocytic vehicles. J. Cell Biol. 168 465-476.
    • (2005) J. Cell Biol. , vol.168 , pp. 465-476
    • Kirkham, M.1    Fujita, A.2    Chadda, R.3    Nixon, S.J.4    Kurzchalia, T.V.5    Sharma, D.K.6
  • 87
    • 0035171631 scopus 로고    scopus 로고
    • Glycosylphosphatidyl inositol-anchored proteins and fyn kinase assemble in noncaveolar plasma membrane microdomains defined by reggie-1 and -2
    • C.A. Stuermer, D.M. Lang, F. Kirsch, M. Wiechers, S.O. Deininger and H. Plattner (2001) Glycosylphosphatidyl inositol-anchored proteins and fyn kinase assemble in noncaveolar plasma membrane microdomains defined by reggie-1 and -2. Mol. Biol. Cell 12 3031-3045.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3031-3045
    • Stuermer, C.A.1    Lang, D.M.2    Kirsch, F.3    Wiechers, M.4    Deininger, S.O.5    Plattner, H.6
  • 88
    • 30344486984 scopus 로고    scopus 로고
    • Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells
    • O.O. Glebov, N.A. Bright and B.J. Nichols (2006) Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells. Nat. Cell. Biol. 8 46-54.
    • (2006) Nat. Cell. Biol. , vol.8 , pp. 46-54
    • Glebov, O.O.1    Bright, N.A.2    Nichols, B.J.3
  • 89
    • 28844454642 scopus 로고    scopus 로고
    • Arginine-rich cell penetrating peptides: From endosomal uptake to nuclear delivery
    • K. Melikov and L.V. Chernomordik (2005) Arginine-rich cell penetrating peptides: From endosomal uptake to nuclear delivery. Cell Mol. Life Sci. 62 2739-2749.
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 2739-2749
    • Melikov, K.1    Chernomordik, L.V.2
  • 90
    • 0029117498 scopus 로고
    • The emergence of clathrin-independent pinocytic pathways
    • C. Lamaze and S.L. Schmid (1995) The emergence of clathrin-independent pinocytic pathways. Curr. Opin. Cell Biol. 7 573-580.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 573-580
    • Lamaze, C.1    Schmid, S.L.2
  • 93
    • 31544479580 scopus 로고    scopus 로고
    • Intracellular traffic and fate of protein transduction domains HIV-1 TAT peptide and octaarginine. Implications for their utilization as drug delivery vectors
    • S. Al-Taei, N.A. Penning, J.C. Simpson, S. Futaki, T. Takeuchi, I. Nakase, et al. (2006) Intracellular traffic and fate of protein transduction domains HIV-1 TAT peptide and octaarginine. Implications for their utilization as drug delivery vectors. Bioconjug. Chem. 17 90-100.
    • (2006) Bioconjug. Chem. , vol.17 , pp. 90-100
    • Al-Taei, S.1    Penning, N.A.2    Simpson, J.C.3    Futaki, S.4    Takeuchi, T.5    Nakase, I.6
  • 94
    • 59849091278 scopus 로고    scopus 로고
    • Peptide-mediated cellular delivery of oligonucleotide-based therapeutics in vitro: Quantitative evaluation of overall efficacy employing easy to handle reporter systems
    • S.D. Laufer and T. Restle (2008) Peptide-mediated cellular delivery of oligonucleotide-based therapeutics in vitro: Quantitative evaluation of overall efficacy employing easy to handle reporter systems. Curr. Pharm. Des. 14 3637-3655.
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 3637-3655
    • Laufer, S.D.1    Restle, T.2
  • 95
    • 0348010364 scopus 로고    scopus 로고
    • Cytoplasmic and nuclear delivery of a TAT-derived peptide and a beta-peptide after endocytic uptake into HeLa cells
    • T.B. Potocky, A.K. Menon and S.H. Gellman (2003) Cytoplasmic and nuclear delivery of a TAT-derived peptide and a beta-peptide after endocytic uptake into HeLa cells. J. Biol. Chem. 278 50188-50194.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50188-50194
    • Potocky, T.B.1    Menon, A.K.2    Gellman, S.H.3
  • 96
    • 2442670068 scopus 로고    scopus 로고
    • Endosome disruption enhances the functional nuclear delivery of Tat-fusion proteins
    • N.J. Caron, S.P. Quenneville and J.P. Tremblay (2004) Endosome disruption enhances the functional nuclear delivery of Tat-fusion proteins. Biochem. Biophys. Res. Commun. 319 12-20.
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 12-20
    • Caron, N.J.1    Quenneville, S.P.2    Tremblay, J.P.3
  • 98
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • L. Pelkmans, J. Kartenbeck and A. Helenius (2001) Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat. Cell Biol. 3 473-483.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 99
    • 77951285705 scopus 로고    scopus 로고
    • S4(13)-PV cell-penetrating peptide forms nanoparticle-like structures to gain entry into cells
    • K. Padari, K. Koppel, A. Lorents, M. Hällbrink, M. Mano, M.C. Pedroso de Lima, et al. (2010) S4(13)-PV cell-penetrating peptide forms nanoparticle-like structures to gain entry into cells. Bioconjug. Chem. 21 774-783.
    • (2010) Bioconjug. Chem. , vol.21 , pp. 774-783
    • Padari, K.1    Koppel, K.2    Lorents, A.3    Hällbrink, M.4    Mano, M.5    Pedroso de Lima, M.C.6
  • 100
    • 1542327642 scopus 로고    scopus 로고
    • Pathway for polyarginine entry into mammalian cells
    • S.M. Fuchs and R.T. Raines (2004) Pathway for polyarginine entry into mammalian cells. Biochemistry 43 2438-2444.
    • (2004) Biochemistry , vol.43 , pp. 2438-2444
    • Fuchs, S.M.1    Raines, R.T.2
  • 101
    • 14844323999 scopus 로고    scopus 로고
    • The NH2 terminus of influenza virus hemagglutinin-2 subunit peptides enhances the antitumor potency of polyarginine-mediated p53 protein transduction
    • H. Michiue, K. Tomizawa, F.Y. Wei, M. Matsushita, Y.F. Lu, T. Ichikawa, et al. (2005) The NH2 terminus of influenza virus hemagglutinin-2 subunit peptides enhances the antitumor potency of polyarginine-mediated p53 protein transduction. J. Biol. Chem. 280 8285-8289.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8285-8289
    • Michiue, H.1    Tomizawa, K.2    Wei, F.Y.3    Matsushita, M.4    Lu, Y.F.5    Ichikawa, T.6
  • 102
    • 76649130213 scopus 로고    scopus 로고
    • Delivery of macromolecules into live cells by simple co-incubation with a peptide
    • Y.J. Lee, A. Erazo-Oliveras and J.P. Pellois (2010) Delivery of macromolecules into live cells by simple co-incubation with a peptide. Chem. Bio. Chem. 11 325-330.
    • (2010) Chem. Bio. Chem. , vol.11 , pp. 325-330
    • Lee, Y.J.1    Erazo-Oliveras, A.2    Pellois, J.P.3
  • 103
    • 65549133368 scopus 로고    scopus 로고
    • Delivery of macromolecules using arginine-rich cell-penetrating peptides: Ways to overcome endosomal entrapment
    • A. El-Sayed, S. Futaki and H. Harashima (2009) Delivery of macromolecules using arginine-rich cell-penetrating peptides: Ways to overcome endosomal entrapment. AAPS J. 11 13-22.
    • (2009) AAPS J. , vol.11 , pp. 13-22
    • El-Sayed, A.1    Futaki, S.2    Harashima, H.3
  • 104
    • 70350116119 scopus 로고    scopus 로고
    • Transduction of the MPG-tagged fusion protein into mammalian cells and oocytes depends on amiloride-sensitive endocytic pathway
    • S.J. Kwon, K. Han, S. Jung, J.E. Lee, S. Park, Y.P. Cheon, et al. (2009) Transduction of the MPG-tagged fusion protein into mammalian cells and oocytes depends on amiloride-sensitive endocytic pathway. BMC Biotechnol. 9 73.
    • (2009) BMC Biotechnol. , vol.9 , pp. 73
    • Kwon, S.J.1    Han, K.2    Jung, S.3    Lee, J.E.4    Park, S.5    Cheon, Y.P.6
  • 105
    • 1842529513 scopus 로고    scopus 로고
    • A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides
    • R. Fischer, K. Köhler, M. Fotin–Mleczek and R. Brock (2004) A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides. J. Biol. Chem. 279 12625-12635.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12625-12635
    • Fischer, R.1    Köhler, K.2    Fotin–Mleczek, M.3    Brock, R.4
  • 106
    • 0034948814 scopus 로고    scopus 로고
    • Differential regulation of retinoblastoma tumor suppressor protein by G(1) cyclin-dependent kinase complexes in vivo
    • S.A. Ezhevsky, A. Ho, M. Becker-Hapak, P.K. Davis and S.F. Dowdy (2001) Differential regulation of retinoblastoma tumor suppressor protein by G(1) cyclin-dependent kinase complexes in vivo. Mol. Cell Biol. 21 4773-4784.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 4773-4784
    • Ezhevsky, S.A.1    Ho, A.2    Becker-Hapak, M.3    Davis, P.K.4    Dowdy, S.F.5
  • 107
    • 0030961889 scopus 로고    scopus 로고
    • Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain
    • G. Selivanova, V. Iotsova, I. Okan, M. Fritsche, M. Ström, B. Groner, et al. (1997) Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain. Nat. Med. 3 632-638.
    • (1997) Nat. Med. , vol.3 , pp. 632-638
    • Selivanova, G.1    Iotsova, V.2    Okan, I.3    Fritsche, M.4    Ström, M.5    Groner, B.6
  • 108
    • 0030615324 scopus 로고    scopus 로고
    • p21WAF1-derived peptides linked to an internalization peptide inhibit human cancer cell growth
    • M. Bonfanti, S. Taverna, M. Salmona, M. D'Incalci and M. Broggini (1997) p21WAF1-derived peptides linked to an internalization peptide inhibit human cancer cell growth. Cancer Res. 57 1442-1446.
    • (1997) Cancer Res. , vol.57 , pp. 1442-1446
    • Bonfanti, M.1    Taverna, S.2    Salmona, M.3    D'Incalci, M.4    Broggini, M.5
  • 109
    • 0033531926 scopus 로고    scopus 로고
    • Bak BH3 peptides antagonize Bcl-xL function and induce apoptosis through cytochrome c-independent activation of caspases
    • E.P. Holinger, T. Chittenden and R.J. Lutz (1999) Bak BH3 peptides antagonize Bcl-xL function and induce apoptosis through cytochrome c-independent activation of caspases. J. Biol. Chem. 274 13298-13304.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13298-13304
    • Holinger, E.P.1    Chittenden, T.2    Lutz, R.J.3
  • 110
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • S.R. Schwarze, A. Ho, A. Vocero-Akbani and S.F. Dowdy (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
  • 112
    • 0035207025 scopus 로고    scopus 로고
    • Pharmacokinetics and delivery of tat and tat-protein conjugates to tissues in vivo
    • H.J. Lee and W.M. Pardridge (2001) Pharmacokinetics and delivery of tat and tat-protein conjugates to tissues in vivo. Bioconjug. Chem. 12 995-999.
    • (2001) Bioconjug. Chem. , vol.12 , pp. 995-999
    • Lee, H.J.1    Pardridge, W.M.2
  • 113
    • 39749105912 scopus 로고    scopus 로고
    • Applications of mesenchymal stem cells labeled with Tat peptide conjugated quantum dots to cell tracking in mouse body
    • Y. Lei, H. Tang, L. Yao, R. Yu, M. Feng and B. Zou (2008) Applications of mesenchymal stem cells labeled with Tat peptide conjugated quantum dots to cell tracking in mouse body. Bioconjug. Chem. 19 421-427.
    • (2008) Bioconjug. Chem. , vol.19 , pp. 421-427
    • Lei, Y.1    Tang, H.2    Yao, L.3    Yu, R.4    Feng, M.5    Zou, B.6
  • 114
    • 0242442127 scopus 로고    scopus 로고
    • Inhibition of delta-protein kinase c protects against reperfusion injury of the ischemic heart in vivo
    • K. Inagaki, L. Chen, F. Ikeno, F.H. Lee, K.I. Imahashi, D.M. Bouley, et al. (2003) Inhibition of delta-protein kinase c protects against reperfusion injury of the ischemic heart in vivo. Circulation 108 2304-2307.
    • (2003) Circulation , vol.108 , pp. 2304-2307
    • Inagaki, K.1    Chen, L.2    Ikeno, F.3    Lee, F.H.4    Imahashi, K.I.5    Bouley, D.M.6
  • 115
    • 37349013170 scopus 로고    scopus 로고
    • Properties of [(111)In]-labeled HIV-1 tat peptide radioimmunoconjugates in tumor-bearing mice following intravenous or intratumoral injection
    • B. Cornelissen, K. McLarty, V. Kersemans, D.A. Scollard and R.M. Reilly (2008) Properties of [(111)In]-labeled HIV-1 tat peptide radioimmunoconjugates in tumor-bearing mice following intravenous or intratumoral injection. Nucl. Med. Biol. 35 101-110.
    • (2008) Nucl. Med. Biol. , vol.35 , pp. 101-110
    • Cornelissen, B.1    McLarty, K.2    Kersemans, V.3    Scollard, D.A.4    Reilly, R.M.5
  • 116
    • 34848848833 scopus 로고    scopus 로고
    • Inhibition of experimental allergic airways disease by local application of a cell-penetrating dominant-negative STAT-6 peptide
    • C.T. McCusker, Y. Wang, J. Shan, M.W. Kinyanjui, A. Villeneuve, H. Michael, et al. (2007) Inhibition of experimental allergic airways disease by local application of a cell-penetrating dominant-negative STAT-6 peptide. J. Immunol. 179 2556-2564.
    • (2007) J. Immunol. , vol.179 , pp. 2556-2564
    • McCusker, C.T.1    Wang, Y.2    Shan, J.3    Kinyanjui, M.W.4    Villeneuve, A.5    Michael, H.6
  • 117
    • 33646587029 scopus 로고    scopus 로고
    • Intranasal delivery of the cytoplasmic domain of CTLA-4 using a novel protein transduction domain prevents allergic inflammation
    • J.M. Choi, M.H. Ahn, W.J. Chae, Y.G. Jung, J.C. Park, H.M. Song, et al. (2006) Intranasal delivery of the cytoplasmic domain of CTLA-4 using a novel protein transduction domain prevents allergic inflammation. Nat. Med. 12 574-579.
    • (2006) Nat. Med. , vol.12 , pp. 574-579
    • Choi, J.M.1    Ahn, M.H.2    Chae, W.J.3    Jung, Y.G.4    Park, J.C.5    Song, H.M.6
  • 118
    • 0035581420 scopus 로고    scopus 로고
    • Transduction of human catalase mediated by an HIV-1 TAT protein basic domain and arginine-rich peptides into mammalian cells
    • L.H. Jin, J.H. Bahn, W.S. Eum, H.Y. Kwon, S.H. Jang, K.H. Han, et al. (2001) Transduction of human catalase mediated by an HIV-1 TAT protein basic domain and arginine-rich peptides into mammalian cells. Free Radic. Biol. Med. 31 1509-1519.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1509-1519
    • Jin, L.H.1    Bahn, J.H.2    Eum, W.S.3    Kwon, H.Y.4    Jang, S.H.5    Han, K.H.6
  • 120
    • 77952901022 scopus 로고    scopus 로고
    • Coadministration of a tumor-penetrating peptide enhances the efficacy of cancer drugs
    • K.N. Sugahara, T. Teesalu, P.P. Karmali, V.R. Kotamraju, L. Agemy, D.R. Greenwald, et al. (2010) Coadministration of a tumor-penetrating peptide enhances the efficacy of cancer drugs. Science 328 1031-1035.
    • (2010) Science , vol.328 , pp. 1031-1035
    • Sugahara, K.N.1    Teesalu, T.2    Karmali, P.P.3    Kotamraju, V.R.4    Agemy, L.5    Greenwald, D.R.6
  • 122
    • 75949098347 scopus 로고    scopus 로고
    • In vivo characterization of activatable cell penetrating peptides for targeting protease activity in cancer
    • E.S. Olson, T.A. Aguilera, T. Jiang, L.G. Ellies, Q.T. Nguyen, E.H. Wong, et al. (2009) In vivo characterization of activatable cell penetrating peptides for targeting protease activity in cancer. Integr. Biol. 1 382-393.
    • (2009) Integr. Biol. , vol.1 , pp. 382-393
    • Olson, E.S.1    Aguilera, T.A.2    Jiang, T.3    Ellies, L.G.4    Nguyen, Q.T.5    Wong, E.H.6
  • 123
    • 0029594498 scopus 로고
    • Contributions of tumor and stromal matrix metalloproteinases to tumor progression, invasion and metastasis
    • J.R. MacDougall and L.M. Matrisian (1995) Contributions of tumor and stromal matrix metalloproteinases to tumor progression, invasion and metastasis. Cancer Metastasis Rev. 14 351-362.
    • (1995) Cancer Metastasis Rev. , vol.14 , pp. 351-362
    • MacDougall, J.R.1    Matrisian, L.M.2
  • 124
    • 77749297971 scopus 로고    scopus 로고
    • Activatable cell penetrating peptides linked to nanoparticles as dual probes for in vivo fluorescence and MR imaging of proteases
    • E.S. Olson, T. Jiang, T.A. Aguilera, Q.T. Nguyen, L.G. Ellies, M. Scadeng, et al. (2010) Activatable cell penetrating peptides linked to nanoparticles as dual probes for in vivo fluorescence and MR imaging of proteases. Proc. Natl. Acad. Sci. U.S.A. 107 4311-4316.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 4311-4316
    • Olson, E.S.1    Jiang, T.2    Aguilera, T.A.3    Nguyen, Q.T.4    Ellies, L.G.5    Scadeng, M.6
  • 125
    • 77749254873 scopus 로고    scopus 로고
    • Surgery with molecular fluorescence imaging using activatable cell-penetrating peptides decreases residual cancer and improves survival
    • Q.T. Nguyen, E.S. Olson, T.A. Aguilera, T. Jiang, M. Scadeng, L.G. Ellies, et al. (2010) Surgery with molecular fluorescence imaging using activatable cell-penetrating peptides decreases residual cancer and improves survival. Proc. Natl. Acad. Sci. U.S.A. 107 4317-4322.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 4317-4322
    • Nguyen, Q.T.1    Olson, E.S.2    Aguilera, T.A.3    Jiang, T.4    Scadeng, M.5    Ellies, L.G.6
  • 126
    • 0037174635 scopus 로고    scopus 로고
    • Treatment of ischemic brain damage by perturbing NMDA receptor-PSD-95 protein interactions
    • M. Aarts, Y. Liu, L. Liu, S. Besshoh, M. Arundine, J.W. Gurd, et al. (2002) Treatment of ischemic brain damage by perturbing NMDA receptor-PSD-95 protein interactions. Science 298 846-850.
    • (2002) Science , vol.298 , pp. 846-850
    • Aarts, M.1    Liu, Y.2    Liu, L.3    Besshoh, S.4    Arundine, M.5    Gurd, J.W.6
  • 127
    • 0038743278 scopus 로고    scopus 로고
    • In vitro uptake and stability study of pVEC and its all-D analog
    • A. Elmquist and Ü Langel (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, A.2
  • 128
    • 33846434072 scopus 로고    scopus 로고
    • Stability of cell-penetrating peptide-morpholino oligomer conjugates in human serum and in cells
    • D.S. Youngblood, S.A. Hatlevig, J.N. Hassinger, P.L. Iversen and H.M. Moulton (2007) Stability of cell-penetrating peptide-morpholino oligomer conjugates in human serum and in cells. Bioconjug. Chem. 18 50-60.
    • (2007) Bioconjug. Chem. , vol.18 , pp. 50-60
    • Youngblood, D.S.1    Hatlevig, S.A.2    Hassinger, J.N.3    Iversen, P.L.4    Moulton, H.M.5
  • 129
    • 0035152487 scopus 로고    scopus 로고
    • Cell-permeable peptide inhibitors of JNK: Novel blockers of beta-cell death
    • C. Bonny, A. Oberson, S. Negri, C. Sauser and D.F. Schorderet (2001) Cell-permeable peptide inhibitors of JNK: Novel blockers of beta-cell death. Diabetes 50 77-82.
    • (2001) Diabetes , vol.50 , pp. 77-82
    • Bonny, C.1    Oberson, A.2    Negri, S.3    Sauser, C.4    Schorderet, D.F.5
  • 132
    • 1542721107 scopus 로고    scopus 로고
    • Cell penetrating peptides in drug delivery
    • E.L. Snyder and S.F. Dowdy (2004) Cell penetrating peptides in drug delivery. Pharm. Res. 21 389-393.
    • (2004) Pharm. Res. , vol.21 , pp. 389-393
    • Snyder, E.L.1    Dowdy, S.F.2
  • 133
    • 57749189130 scopus 로고    scopus 로고
    • Caveolae and transcytosis in endothelial cells: role in atherosclerosis
    • P.G. Frank, S. Pavlides and M.P. Lisanti (2009) Caveolae and transcytosis in endothelial cells: role in atherosclerosis. Cell Tissue Res. 335 41-47.
    • (2009) Cell Tissue Res. , vol.335 , pp. 41-47
    • Frank, P.G.1    Pavlides, S.2    Lisanti, M.P.3
  • 134
    • 0031754150 scopus 로고    scopus 로고
    • Cell penetrating PNA constructs regulate galanin receptor levels and modify pain transmission in vivo
    • M. Pooga, U. Soomets, M. Hällbrink, A. Valkna, K. Saar, K. Rezaei, et al. (1998) Cell penetrating PNA constructs regulate galanin receptor levels and modify pain transmission in vivo. Nat. Biotechnol. 16 857-861.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 857-861
    • Pooga, M.1    Soomets, U.2    Hällbrink, M.3    Valkna, A.4    Saar, K.5    Rezaei, K.6
  • 135
    • 42249103388 scopus 로고    scopus 로고
    • Tat-Hsp70 protects dopaminergic neurons in midbrain cultures and in the substantia nigra in models of Parkinson's disease
    • F. Nagel, B.H. Falkenburger, L. Tonges, S. Kowsky, C. Poppelmeyer, J.B. Schulz, et al. (2008) Tat-Hsp70 protects dopaminergic neurons in midbrain cultures and in the substantia nigra in models of Parkinson's disease. J. Neurochem. 105 853-864.
    • (2008) J. Neurochem. , vol.105 , pp. 853-864
    • Nagel, F.1    Falkenburger, B.H.2    Tonges, L.3    Kowsky, S.4    Poppelmeyer, C.5    Schulz, J.B.6
  • 136
    • 67349287017 scopus 로고    scopus 로고
    • TAT-Hsp70-mediated neuroprotection and increased survival of neuronal precursor cells after focal cerebral ischemia in mice
    • T.R. Doeppner, F. Nagel, G.P. Dietz, J. Weise, L. Tonges, S. Schwarting, et al. (2009) TAT-Hsp70-mediated neuroprotection and increased survival of neuronal precursor cells after focal cerebral ischemia in mice. J. Cereb. Blood Flow Metab. 29 1187-1196.
    • (2009) J. Cereb. Blood Flow Metab. , vol.29 , pp. 1187-1196
    • Doeppner, T.R.1    Nagel, F.2    Dietz, G.P.3    Weise, J.4    Tonges, L.5    Schwarting, S.6
  • 137
    • 62149092900 scopus 로고    scopus 로고
    • TAT-Bcl-x(L) improves survival of neuronal precursor cells in the lesioned striatum after focal cerebral ischemia
    • T.R. Doeppner, G.P. Dietz, M. El Aanbouri, J. Gerber, O.W. Witte, M. Bähr, et al. (2009) TAT-Bcl-x(L) improves survival of neuronal precursor cells in the lesioned striatum after focal cerebral ischemia. Neurobiol. Dis. 34 87-94.
    • (2009) Neurobiol. Dis. , vol.34 , pp. 87-94
    • Doeppner, T.R.1    Dietz, G.P.2    El Aanbouri, M.3    Gerber, J.4    Witte, O.W.5    Bähr, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.