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Volumn 70, Issue 24, 2013, Pages 4825-4839

Cell-penetrating peptide secures an efficient endosomal escape of an intact cargo upon a brief photo-induction

Author keywords

CPP; Degradation; Effective delivery; Endosomal release; Photo induction; Protein transduction domain; PTD; Stability

Indexed keywords

CELL PENETRATING PEPTIDE; CELL PROTEIN; TRANSPORTAN 10; TUBULIN; UNCLASSIFIED DRUG;

EID: 84889889091     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-013-1416-z     Document Type: Article
Times cited : (19)

References (58)
  • 1
    • 33748433244 scopus 로고    scopus 로고
    • Cell-penetrating peptides as vectors for peptide, protein and oligonucleotide delivery
    • 16860608 10.1016/j.coph.2006.04.004
    • Mäe M, Langel Ü (2006) Cell-penetrating peptides as vectors for peptide, protein and oligonucleotide delivery. Curr Opin Pharmacol 6(5):509-514
    • (2006) Curr Opin Pharmacol , vol.6 , Issue.5 , pp. 509-514
    • Mäe, M.1    Langel, Ü.2
  • 2
    • 77958153239 scopus 로고    scopus 로고
    • In vivo biodistribution and efficacy of peptide mediated delivery
    • 20828841 10.1016/j.tips.2010.07.006
    • Järver P, Mäger I, Langel Ü (2010) In vivo biodistribution and efficacy of peptide mediated delivery. Trends Pharmacol Sci 31(11):528-535
    • (2010) Trends Pharmacol Sci , vol.31 , Issue.11 , pp. 528-535
    • Järver, P.1    Mäger, I.2    Langel, Ü.3
  • 3
    • 42049095153 scopus 로고    scopus 로고
    • Cell-penetrating peptides: From molecular mechanisms to therapeutics
    • 18341479 10.1042/BC20070116 1:CAS:528:DC%2BD1cXjtl2gs7c%3D
    • Morris MC, Deshayes S, Heitz F, Divita G (2008) Cell-penetrating peptides: from molecular mechanisms to therapeutics. Biol Cell 100(4):201-217
    • (2008) Biol Cell , vol.100 , Issue.4 , pp. 201-217
    • Morris, M.C.1    Deshayes, S.2    Heitz, F.3    Divita, G.4
  • 4
    • 84857781844 scopus 로고    scopus 로고
    • Cell-penetrating peptides as versatile vehicles for oligonucleotide delivery
    • 22233581 10.1038/mt.2011.284 1:CAS:528:DC%2BC38XlsF2iuw%3D%3D
    • Margus H, Padari K, Pooga M (2012) Cell-penetrating peptides as versatile vehicles for oligonucleotide delivery. Mol Ther 20(3):525-533
    • (2012) Mol Ther , vol.20 , Issue.3 , pp. 525-533
    • Margus, H.1    Padari, K.2    Pooga, M.3
  • 5
    • 27744528180 scopus 로고    scopus 로고
    • Endocytosis and cationic cell-penetrating peptides-a merger of concepts and methods
    • 16305498 10.2174/138161205774580778 1:CAS:528:DC%2BD2MXhtFOrt7jN
    • Fotin-Mleczek M, Fischer R, Brock R (2005) Endocytosis and cationic cell-penetrating peptides-a merger of concepts and methods. Curr Pharm Des 11(28):3613-3628
    • (2005) Curr Pharm des , vol.11 , Issue.28 , pp. 3613-3628
    • Fotin-Mleczek, M.1    Fischer, R.2    Brock, R.3
  • 6
    • 66149183010 scopus 로고    scopus 로고
    • Protein delivery with transportans is mediated by caveolae rather than flotillin-dependent pathways
    • 19348413 10.1021/bc800416f
    • Säälik P, Padari K, Niinep A, Lorents A, Hansen M, Jokitalo E, Langel Ü, Pooga M (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    Langel, Ü.7    Pooga, M.8
  • 7
    • 77958150359 scopus 로고    scopus 로고
    • Peptide-mediated protein delivery-which pathways are penetrable?
    • 20170627 10.1016/j.bbamem.2010.02.013
    • Räägel H, Säälik P, Pooga M (2010) Peptide-mediated protein delivery-which pathways are penetrable? Biochim Biophys Acta 1798(12):2240-2248
    • (2010) Biochim Biophys Acta , vol.1798 , Issue.12 , pp. 2240-2248
    • Räägel, H.1    Säälik, P.2    Pooga, M.3
  • 8
    • 0042199010 scopus 로고    scopus 로고
    • Cell surface adherence and endocytosis of protein transduction domains
    • 12842437 10.1016/S1525-0016(03)00135-7 1:CAS:528:DC%2BD3sXkvFGmsrw%3D
    • Lundberg M, Wikström S, Johansson M (2003) Cell surface adherence and endocytosis of protein transduction domains. Mol Ther 8(1):143-150
    • (2003) Mol Ther , vol.8 , Issue.1 , pp. 143-150
    • Lundberg, M.1    Wikström, S.2    Johansson, M.3
  • 9
    • 31544458695 scopus 로고    scopus 로고
    • Endosome trapping limits the efficiency of splicing correction by PNA-oligolysine conjugates
    • 16377019 10.1016/j.jconrel.2005.10.026 1:CAS:528:DC%2BD28XhtVaiur0%3D
    • Abes S, Williams D, Prevot P, Thierry A, Gait MJ, Lebleu B (2006) Endosome trapping limits the efficiency of splicing correction by PNA-oligolysine conjugates. J Control Release 110(3):595-604
    • (2006) J Control 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
  • 10
    • 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
    • 16321967 10.1093/nar/gki991 1:CAS:528:DC%2BD2MXhtlagtbfJ
    • Turner JJ, Ivanova GD, Verbeure B, Williams D, Arzumanov AA, Abes S, Lebleu B, Gait MJ (2005) Cell-penetrating peptide conjugates of peptide nucleic acids (PNA) as inhibitors of HIV-1 Tat-dependent trans-activation in cells. Nucleic Acids Res 33(21):6837-6849
    • (2005) Nucleic Acids Res , 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
  • 11
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • 14770178 10.1038/nm996 1:CAS:528:DC%2BD2cXhs1Wnurg%3D
    • Wadia JS, Stan RV, Dowdy SF (2004) Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat Med 10(3):310-315
    • (2004) Nat Med , vol.10 , Issue.3 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 12
    • 71749100835 scopus 로고    scopus 로고
    • Elucidating cell-penetrating peptide mechanisms of action for membrane interaction, cellular uptake, and translocation utilizing the hydrophobic counter-anion pyrenebutyrate
    • Guterstam P, Madani F, Hirose H, Takeuchi T, Futaki S, El-Andaloussi S, Gräslund A, Langel Ü (2009) Elucidating cell-penetrating peptide mechanisms of action for membrane interaction, cellular uptake, and translocation utilizing the hydrophobic counter-anion pyrenebutyrate. Biochemica et Biophysica Acta 1778:2509-2517
    • (2009) Biochemica et Biophysica Acta , vol.1778 , pp. 2509-2517
    • Guterstam, P.1    Madani, F.2    Hirose, H.3    Takeuchi, T.4    Futaki, S.5    El-Andaloussi, S.6    Gräslund, A.7    Langel, Ü.8
  • 13
    • 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
    • 16417256 10.1021/bc050274h 1:CAS:528:DC%2BD2MXhtlClsbrK
    • Al-Taei S, Penning NA, Simpson JC, Futaki S, Takeuchi T, Nakase I, Jones AT (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(1):90-100
    • (2006) Bioconjug Chem , vol.17 , Issue.1 , pp. 90-100
    • Al-Taei, S.1    Penning, N.A.2    Simpson, J.C.3    Futaki, S.4    Takeuchi, T.5    Nakase, I.6    Jones, A.T.7
  • 15
    • 33847036106 scopus 로고    scopus 로고
    • Vectorization of morpholino oligomers by the (R-Ahx-R)4 peptide allows efficient splicing correction in the absence of endosomolytic agents
    • 17097177 10.1016/j.jconrel.2006.09.011 1:CAS:528:DC%2BD28Xht1KitL%2FP
    • Abes S, Moulton HM, Clair P, Prevot P, Youngblood DS, Wu RP, Iversen PL, Lebleu B (2006) Vectorization of morpholino oligomers by the (R-Ahx-R)4 peptide allows efficient splicing correction in the absence of endosomolytic agents. J Control Release 116(3):304-313
    • (2006) J Control Release , vol.116 , Issue.3 , pp. 304-313
    • Abes, S.1    Moulton, H.M.2    Clair, P.3    Prevot, P.4    Youngblood, D.S.5    Wu, R.P.6    Iversen, P.L.7    Lebleu, B.8
  • 16
    • 9744276742 scopus 로고    scopus 로고
    • Specific redistribution of cell-penetrating peptides from endosomes to the cytoplasm and nucleus upon laser illumination
    • 15563153 10.1021/ja044867z 1:CAS:528:DC%2BD2cXpt1SktLc%3D
    • Maiolo JR 3rd, Ottinger EA, Ferrer M (2004) Specific redistribution of cell-penetrating peptides from endosomes to the cytoplasm and nucleus upon laser illumination. J Am Chem Soc 126(47):15376-15377
    • (2004) J Am Chem Soc , vol.126 , Issue.47 , pp. 15376-15377
    • Maiolo III, J.R.1    Ottinger, E.A.2    Ferrer, M.3
  • 17
    • 78649529393 scopus 로고    scopus 로고
    • Photochemical internalization provides time- and space-controlled endolysosomal escape of therapeutic molecules
    • 20600406 10.1016/j.jconrel.2010.06.008 1:CAS:528:DC%2BC3cXhsVCmsbzN
    • Selbo PK, Weyergang A, Hogset A, Norum OJ, Berstad MB, Vikdal M, Berg K (2010) Photochemical internalization provides time- and space-controlled endolysosomal escape of therapeutic molecules. J Control Release 148(1):2-12
    • (2010) J Control Release , vol.148 , Issue.1 , pp. 2-12
    • Selbo, P.K.1    Weyergang, A.2    Hogset, A.3    Norum, O.J.4    Berstad, M.B.5    Vikdal, M.6    Berg, K.7
  • 18
    • 32344441681 scopus 로고    scopus 로고
    • Photochemically enhanced cellular delivery of cell-penetrating peptide-PNA conjugates
    • 16460737 10.1016/j.febslet.2006.01.077 1:CAS:528:DC%2BD28Xhs1SntLw%3D
    • Shiraishi T, Nielsen PE (2006) Photochemically enhanced cellular delivery of cell-penetrating peptide-PNA conjugates. FEBS Lett 580(5):1451-1456
    • (2006) FEBS Lett , vol.580 , Issue.5 , pp. 1451-1456
    • Shiraishi, T.1    Nielsen, P.E.2
  • 19
    • 84855782572 scopus 로고    scopus 로고
    • Photochemical internalisation of a macromolecular protein toxin using a cell-penetrating peptide-photosensitiser conjugate
    • Wang JT, Giuntini F, Eggleston IM, Bown SG, Macrobert AJ (2012) Photochemical internalisation of a macromolecular protein toxin using a cell-penetrating peptide-photosensitiser conjugate. J Control Release 157(2):305-313
    • (2012) J Control Release , vol.157 , Issue.2 , pp. 305-313
    • Wang, J.T.1    Giuntini, F.2    Eggleston, I.M.3    Bown, S.G.4    Macrobert, A.J.5
  • 20
    • 28244477911 scopus 로고    scopus 로고
    • TP10, a delivery vector for decoy oligonucleotides targeting the Myc protein
    • 16253378 10.1016/j.jconrel.2005.09.012 1:CAS:528:DC%2BD2MXht1KlurrE
    • El-Andaloussi S, Johansson H, Magnusdottir A, Järver P, Lundberg P, Langel Ü (2005) TP10, a delivery vector for decoy oligonucleotides targeting the Myc protein. J Control Release 110(1):189-201
    • (2005) J Control Release , vol.110 , Issue.1 , pp. 189-201
    • El-Andaloussi, S.1    Johansson, H.2    Magnusdottir, A.3    Järver, P.4    Lundberg, P.5    Langel, Ü.6
  • 21
    • 34047238809 scopus 로고    scopus 로고
    • Mechanism of the cell-penetrating peptide transportan 10 permeation of lipid bilayers
    • 17218466 10.1529/biophysj.106.100198 1:CAS:528:DC%2BD2sXjs1Kjsbc%3D
    • Yandek LE, Pokorny A, Florén A, Knoelke K, Langel Ü, Almeida PF (2007) Mechanism of the cell-penetrating peptide transportan 10 permeation of lipid bilayers. Biophys J 92(7):2434-2444
    • (2007) Biophys J , vol.92 , Issue.7 , pp. 2434-2444
    • Yandek, L.E.1    Pokorny, A.2    Florén, A.3    Knoelke, K.4    Langel, Ü.5    Almeida, P.F.6
  • 22
    • 79952840265 scopus 로고    scopus 로고
    • Molecular dynamics studies of transportan 10 (Tp10) interacting with a POPC lipid bilayer
    • 21194203 10.1021/jp107763b 1:CAS:528:DC%2BC3MXmsVeg
    • Dunkin CM, Pokorny A, Almeida PF, Lee HS (2011) Molecular dynamics studies of transportan 10 (Tp10) interacting with a POPC lipid bilayer. J Phys Chem B 115(5):1188-1198
    • (2011) J Phys Chem B , vol.115 , Issue.5 , pp. 1188-1198
    • Dunkin, C.M.1    Pokorny, A.2    Almeida, P.F.3    Lee, H.S.4
  • 23
    • 79960104118 scopus 로고    scopus 로고
    • Penetration without cells: Membrane translocation of cell-penetrating peptides in the model giant plasma membrane vesicles
    • 21420454 10.1016/j.jconrel.2011.03.011
    • Säälik P, Niinep A, Pae J, Hansen M, Lubenets D, Langel Ü, Pooga M (2011) Penetration without cells: membrane translocation of cell-penetrating peptides in the model giant plasma membrane vesicles. J Control Release 153(2):117-125
    • (2011) J Control Release , vol.153 , Issue.2 , pp. 117-125
    • Säälik, P.1    Niinep, A.2    Pae, J.3    Hansen, M.4    Lubenets, D.5    Langel, Ü.6    Pooga, M.7
  • 24
    • 34548161524 scopus 로고    scopus 로고
    • Studying the uptake of cell-penetrating peptides
    • 17406337 10.1038/nprot.2006.174 1:CAS:528:DC%2BD28XhtFOitb%2FK
    • Holm T, Johansson H, Lundberg P, Pooga M, Lindgren M, Langel Ü (2006) Studying the uptake of cell-penetrating peptides. Nat Protoc 1(2):1001-1005
    • (2006) Nat Protoc , vol.1 , Issue.2 , pp. 1001-1005
    • Holm, T.1    Johansson, H.2    Lundberg, P.3    Pooga, M.4    Lindgren, M.5    Langel, Ü.6
  • 25
    • 47049117171 scopus 로고    scopus 로고
    • The same primary structure of the prion protein yields two distinct self-propagating states
    • 18400757 10.1074/jbc.M800562200 1:CAS:528:DC%2BD1cXmsFertLc%3D
    • Makarava N, Baskakov IV (2008) The same primary structure of the prion protein yields two distinct self-propagating states. J Biol Chem 283(23):15988-15996
    • (2008) J Biol Chem , vol.283 , Issue.23 , pp. 15988-15996
    • Makarava, N.1    Baskakov, I.V.2
  • 29
    • 84862849271 scopus 로고    scopus 로고
    • Self-assembling mini cell-penetrating peptides enter by both direct translocation and glycosaminoglycan-dependent endocytosis
    • 10.1039/c2cc33240j 1:CAS:528:DC%2BC38XovFWmtb8%3D
    • Bode SA, Thevenin M, Bechara C, Sagan S, Bregant S, Lavielle S, Chassaing G, Burlina F (2012) Self-assembling mini cell-penetrating peptides enter by both direct translocation and glycosaminoglycan-dependent endocytosis. Chem Commun (Camb) 48(57):7179-7181
    • (2012) Chem Commun (Camb) , vol.48 , Issue.57 , pp. 7179-7181
    • Bode, S.A.1    Thevenin, M.2    Bechara, C.3    Sagan, S.4    Bregant, S.5    Lavielle, S.6    Chassaing, G.7    Burlina, F.8
  • 30
    • 3543051871 scopus 로고    scopus 로고
    • Role of membrane potential and hydrogen bonding in the mechanism of translocation of guanidinium-rich peptides into cells
    • 15291531 10.1021/ja0482536 1:CAS:528:DC%2BD2cXlvVSktr8%3D
    • Rothbard JB, Jessop TC, Lewis RS, Murray BA, Wender PA (2004) Role of membrane potential and hydrogen bonding in the mechanism of translocation of guanidinium-rich peptides into cells. J Am Chem Soc 126(31):9506-9507
    • (2004) J Am Chem Soc , vol.126 , Issue.31 , pp. 9506-9507
    • Rothbard, J.B.1    Jessop, T.C.2    Lewis, R.S.3    Murray, B.A.4    Wender, P.A.5
  • 31
    • 33748648777 scopus 로고    scopus 로고
    • Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells
    • 16940149 10.1096/fj.05-5523com
    • Tünnemann G, Martin RM, Haupt S, Patsch C, Edenhofer F, Cardoso MC (2006) Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells. FASEB J 20(11):1775-1784
    • (2006) FASEB J , vol.20 , Issue.11 , pp. 1775-1784
    • Tünnemann, G.1    Martin, R.M.2    Haupt, S.3    Patsch, C.4    Edenhofer, F.5    Cardoso, M.C.6
  • 32
    • 79952632412 scopus 로고    scopus 로고
    • Conjugation to the cell-penetrating peptide TAT potentiates the photodynamic effect of carboxytetramethylrhodamine
    • 21423812 10.1371/journal.pone.0017732 1:CAS:528:DC%2BC3MXjvVClsbk%3D
    • Srinivasan D, Muthukrishnan N, Johnson GA, Erazo-Oliveras A, Lim J, Simanek EE, Pellois JP (2011) Conjugation to the cell-penetrating peptide TAT potentiates the photodynamic effect of carboxytetramethylrhodamine. PLoS One 6(3):e17732
    • (2011) PLoS One , vol.6 , Issue.3 , pp. 17732
    • Srinivasan, D.1    Muthukrishnan, N.2    Johnson, G.A.3    Erazo-Oliveras, A.4    Lim, J.5    Simanek, E.E.6    Pellois, J.P.7
  • 33
    • 0142134227 scopus 로고    scopus 로고
    • Cell damage and reactive oxygen species production induced by fluorescence microscopy: Effect on mitosis and guidelines for non-invasive fluorescence microscopy
    • 14535891 10.1046/j.1365-313X.2003.01868.x 1:CAS:528:DC%2BD3sXpt1Ogtb8%3D
    • Dixit R, Cyr R (2003) Cell damage and reactive oxygen species production induced by fluorescence microscopy: effect on mitosis and guidelines for non-invasive fluorescence microscopy. Plant J 36(2):280-290
    • (2003) Plant J , vol.36 , Issue.2 , pp. 280-290
    • Dixit, R.1    Cyr, R.2
  • 34
    • 33847659570 scopus 로고    scopus 로고
    • The peptide carrier Pep-1 forms biologically efficient nanoparticle complexes
    • 17331466 10.1016/j.bbrc.2007.02.046 1:CAS:528:DC%2BD2sXivVagsrs%3D
    • Munoz-Morris MA, Heitz F, Divita G, Morris MC (2007) The peptide carrier Pep-1 forms biologically efficient nanoparticle complexes. Biochem Biophys Res Commun 355(4):877-882
    • (2007) Biochem Biophys Res Commun , vol.355 , Issue.4 , pp. 877-882
    • Munoz-Morris, M.A.1    Heitz, F.2    Divita, G.3    Morris, M.C.4
  • 35
    • 77956641791 scopus 로고    scopus 로고
    • Cellular internalization kinetics of (luciferin-)cell-penetrating peptide conjugates
    • 20684543 10.1021/bc100174y 1:CAS:528:DC%2BC3cXpslWhtr0%3D
    • Eiriksdottir E, Mäger I, Lehto T, El Andaloussi S, Langel Ü (2010) Cellular internalization kinetics of (luciferin-)cell-penetrating peptide conjugates. Bioconjug Chem 21(9):1662-1672
    • (2010) Bioconjug Chem , vol.21 , Issue.9 , pp. 1662-1672
    • Eiriksdottir, E.1    Mäger, I.2    Lehto, T.3    El Andaloussi, S.4    Langel, Ü.5
  • 36
    • 11844293998 scopus 로고    scopus 로고
    • The cationic cell-penetrating peptide CPP(TAT) derived from the HIV-1 protein TAT is rapidly transported into living fibroblasts: Optical, biophysical, and metabolic evidence
    • 15628854 10.1021/bi0491604 1:CAS:528:DC%2BD2cXhtVOjtrfL
    • Ziegler A, Nervi P, Dürrenberger M, Seelig J (2005) The cationic cell-penetrating peptide CPP(TAT) derived from the HIV-1 protein TAT is rapidly transported into living fibroblasts: optical, biophysical, and metabolic evidence. Biochemistry 44(1):138-148
    • (2005) Biochemistry , vol.44 , Issue.1 , pp. 138-148
    • Ziegler, A.1    Nervi, P.2    Dürrenberger, M.3    Seelig, J.4
  • 37
    • 0028470454 scopus 로고
    • Barriers to drug delivery in solid tumors
    • 8066425 10.1038/scientificamerican0794-58 1:STN:280:DyaK2czksFenuw%3D%3D
    • Jain RK (1994) Barriers to drug delivery in solid tumors. Sci Am 271(1):58-65
    • (1994) Sci Am , vol.271 , Issue.1 , pp. 58-65
    • Jain, R.K.1
  • 38
    • 0036307898 scopus 로고    scopus 로고
    • Limited penetration of anticancer drugs through tumor tissue: A potential cause of resistance of solid tumors to chemotherapy
    • 11895922 1:CAS:528:DC%2BD38XislOqurw%3D
    • Tannock IF, Lee CM, Tunggal JK, Cowan DS, Egorin MJ (2002) Limited penetration of anticancer drugs through tumor tissue: a potential cause of resistance of solid tumors to chemotherapy. Clin Cancer Res 8(3):878-884
    • (2002) Clin Cancer Res , vol.8 , Issue.3 , pp. 878-884
    • Tannock, I.F.1    Lee, C.M.2    Tunggal, J.K.3    Cowan, D.S.4    Egorin, M.J.5
  • 39
    • 33644990966 scopus 로고    scopus 로고
    • DNA delivery for vaccination and therapeutics through the skin
    • 16472090 10.2174/156720106775197493 1:CAS:528:DC%2BD28XktlCjtQ%3D%3D
    • Foldvari M, Babiuk S, Badea I (2006) DNA delivery for vaccination and therapeutics through the skin. Curr Drug Deliv 3(1):17-28
    • (2006) Curr Drug Deliv , vol.3 , Issue.1 , pp. 17-28
    • Foldvari, M.1    Babiuk, S.2    Badea, I.3
  • 40
    • 79955020401 scopus 로고    scopus 로고
    • Cellular trafficking and photochemical internalization of cell-penetrating peptide linked cargo proteins: A dual fluorescent labeling study
    • 21405111 10.1021/bc900445g 1:CAS:528:DC%2BC3MXjtFers78%3D
    • Gillmeister MP, Betenbaugh MJ, Fishman PS (2011) Cellular trafficking and photochemical internalization of cell-penetrating peptide linked cargo proteins: a dual fluorescent labeling study. Bioconjug Chem 22(4):556-566
    • (2011) Bioconjug Chem , vol.22 , Issue.4 , pp. 556-566
    • Gillmeister, M.P.1    Betenbaugh, M.J.2    Fishman, P.S.3
  • 41
    • 69249142709 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: From kinetics to thermodynamics
    • 19655791 10.1021/bi900914g 1:CAS:528:DC%2BD1MXpsFaltr4%3D
    • Almeida PF, Pokorny A (2009) Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics. Biochemistry 48(34):8083-8093
    • (2009) Biochemistry , vol.48 , Issue.34 , pp. 8083-8093
    • Almeida, P.F.1    Pokorny, A.2
  • 42
    • 33748950268 scopus 로고    scopus 로고
    • Molecular mechanism of antimicrobial peptides: The origin of cooperativity
    • 16542637 10.1016/j.bbamem.2006.02.001 1:CAS:528:DC%2BD28XhtVanu7jO
    • Huang HW (2006) Molecular mechanism of antimicrobial peptides: the origin of cooperativity. Biochim Biophys Acta 1758(9):1292-1302
    • (2006) Biochim Biophys Acta , vol.1758 , Issue.9 , pp. 1292-1302
    • Huang, H.W.1
  • 43
    • 38049156027 scopus 로고    scopus 로고
    • Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes
    • 18093956 10.1073/pnas.0706574105 1:CAS:528:DC%2BD1cXks1yjug%3D%3D
    • Herce HD, Garcia AE (2007) Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes. Proc Natl Acad Sci USA 104(52):20805-20810
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.52 , pp. 20805-20810
    • Herce, H.D.1    Garcia, A.E.2
  • 44
    • 70350023192 scopus 로고    scopus 로고
    • Arginine-rich peptides destabilize the plasma membrane, consistent with a pore formation translocation mechanism of cell-penetrating peptides
    • 19804722 10.1016/j.bpj.2009.05.066 1:CAS:528:DC%2BD1MXhsVCiu7bP
    • Herce HD, Garcia AE, Litt J, Kane RS, Martin P, Enrique N, Rebolledo A, Milesi V (2009) Arginine-rich peptides destabilize the plasma membrane, consistent with a pore formation translocation mechanism of cell-penetrating peptides. Biophys J 97(7):1917-1925
    • (2009) Biophys J , vol.97 , Issue.7 , pp. 1917-1925
    • Herce, H.D.1    Garcia, A.E.2    Litt, J.3    Kane, R.S.4    Martin, P.5    Enrique, N.6    Rebolledo, A.7    Milesi, V.8
  • 45
    • 78049324771 scopus 로고    scopus 로고
    • Cell-penetrating peptide induces leaky fusion of liposomes containing late endosome-specific anionic lipid
    • 20959093 10.1016/j.bpj.2010.08.029 1:CAS:528:DC%2BC3cXhtlShsbbM
    • Yang ST, Zaitseva E, Chernomordik LV, Melikov K (2010) Cell-penetrating peptide induces leaky fusion of liposomes containing late endosome-specific anionic lipid. Biophys J 99(8):2525-2533
    • (2010) Biophys J , vol.99 , Issue.8 , pp. 2525-2533
    • Yang, S.T.1    Zaitseva, E.2    Chernomordik, L.V.3    Melikov, K.4
  • 46
    • 0037339402 scopus 로고    scopus 로고
    • Plasmon-waveguide resonance and impedance spectroscopy studies of the interaction between penetratin and supported lipid bilayer membranes
    • 12609881 10.1016/S0006-3495(03)74987-X 1:CAS:528:DC%2BD3sXit1ehs7Y%3D
    • Salamon Z, Lindblom G, Tollin G (2003) Plasmon-waveguide resonance and impedance spectroscopy studies of the interaction between penetratin and supported lipid bilayer membranes. Biophys J 84(3):1796-1807
    • (2003) Biophys J , vol.84 , Issue.3 , pp. 1796-1807
    • Salamon, Z.1    Lindblom, G.2    Tollin, G.3
  • 47
    • 84856077925 scopus 로고    scopus 로고
    • Influence of stearyl and trifluoromethylquinoline modifications of the cell-penetrating peptide TP10 on its interaction with a lipid membrane
    • 22240008 10.1016/j.bbamem.2011.12.028 1:CAS:528:DC%2BC38XhvFarsbk%3D
    • Anko M, Majhenc J, Kogej K, Sillard R, Langel U, Anderluh G, Zorko M (2012) Influence of stearyl and trifluoromethylquinoline modifications of the cell-penetrating peptide TP10 on its interaction with a lipid membrane. Biochim Biophys Acta 1818(3):915-924
    • (2012) Biochim Biophys Acta , vol.1818 , Issue.3 , pp. 915-924
    • Anko, M.1    Majhenc, J.2    Kogej, K.3    Sillard, R.4    Langel, U.5    Anderluh, G.6    Zorko, M.7
  • 48
    • 0042266431 scopus 로고    scopus 로고
    • Lipids in endocytic membrane transport and sorting
    • 12892777 10.1016/S0955-0674(03)00078-4 1:CAS:528:DC%2BD3sXlvVGjsbs%3D
    • Gruenberg J (2003) Lipids in endocytic membrane transport and sorting. Curr Opin Cell Biol 15(4):382-388
    • (2003) Curr Opin Cell Biol , vol.15 , Issue.4 , pp. 382-388
    • Gruenberg, J.1
  • 51
    • 46349095009 scopus 로고    scopus 로고
    • Membrane interaction and perturbation mechanisms induced by two cationic cell-penetrating peptides with distinct charge distribution
    • 18498774 10.1016/j.bbagen.2008.04.004 1:CAS:528:DC%2BD1cXmvFSis7o%3D
    • Alves ID, Goasdoue N, Correia I, Aubry S, Galanth C, Sagan S, Lavielle S, Chassaing G (2008) Membrane interaction and perturbation mechanisms induced by two cationic cell-penetrating peptides with distinct charge distribution. Biochim Biophys Acta 1780(7-8):948-959
    • (2008) Biochim Biophys Acta , vol.1780 , Issue.7-8 , pp. 948-959
    • Alves, I.D.1    Goasdoue, N.2    Correia, I.3    Aubry, S.4    Galanth, C.5    Sagan, S.6    Lavielle, S.7    Chassaing, G.8
  • 53
    • 0242268532 scopus 로고    scopus 로고
    • Lipid rafts and caveolae as portals for endocytosis: New insights and common mechanisms
    • 14617356 10.1034/j.1600-0854.2003.00128.x 1:CAS:528:DC%2BD3sXovVGqt7c%3D
    • Parton RG, Richards AA (2003) Lipid rafts and caveolae as portals for endocytosis: new insights and common mechanisms. Traffic 4(11):724-738
    • (2003) Traffic , vol.4 , Issue.11 , pp. 724-738
    • Parton, R.G.1    Richards, A.A.2
  • 54
    • 0037684840 scopus 로고    scopus 로고
    • Caveolae/raft-dependent endocytosis
    • 12771123 10.1083/jcb.200302028 1:CAS:528:DC%2BD3sXktlWiur4%3D
    • Nabi IR, Le PU (2003) Caveolae/raft-dependent endocytosis. J Cell Biol 161(4):673-677
    • (2003) J Cell Biol , vol.161 , Issue.4 , pp. 673-677
    • Nabi, I.R.1    Le, P.U.2
  • 55
    • 69949138136 scopus 로고    scopus 로고
    • CPP-protein constructs induce a population of non-acidic vesicles during trafficking through endo-lysosomal pathway
    • 19577599 10.1016/j.jconrel.2009.06.028
    • Räägel H, Säälik P, Hansen M, Langel Ü, Pooga M (2009) CPP-protein constructs induce a population of non-acidic vesicles during trafficking through endo-lysosomal pathway. J Control Release 139(2):108-117
    • (2009) J Control Release , vol.139 , Issue.2 , pp. 108-117
    • Räägel, H.1    Säälik, P.2    Hansen, M.3    Langel, Ü.4    Pooga, M.5
  • 56
    • 20444396903 scopus 로고    scopus 로고
    • A review of progress in clinical photodynamic therapy
    • 15896084 1:CAS:528:DC%2BD2MXmtVaisLc%3D
    • Huang Z (2005) A review of progress in clinical photodynamic therapy. Technol Cancer Res Treat 4(3):283-293
    • (2005) Technol Cancer Res Treat , vol.4 , Issue.3 , pp. 283-293
    • Huang, Z.1
  • 57
    • 56549129972 scopus 로고    scopus 로고
    • Guidelines for topical photodynamic therapy: Update
    • 18945319 10.1111/j.1365-2133.2008.08882.x 1:CAS:528: DC%2BD1MXps1eltw%3D%3D
    • Morton CA, McKenna KE, Rhodes LE (2008) Guidelines for topical photodynamic therapy: update. Br J Dermatol 159(6):1245-1266
    • (2008) Br J Dermatol , vol.159 , Issue.6 , pp. 1245-1266
    • Morton, C.A.1    McKenna, K.E.2    Rhodes, L.E.3
  • 58
    • 12944249210 scopus 로고    scopus 로고
    • Effectiveness of different light sources for 5-aminolevulinic acid photodynamic therapy
    • 15503248 10.1007/s10103-004-0314-x
    • Juzeniene A, Juzenas P, Ma LW, Iani V, Moan J (2004) Effectiveness of different light sources for 5-aminolevulinic acid photodynamic therapy. Lasers Med Sci 19(3):139-149
    • (2004) Lasers Med Sci , vol.19 , Issue.3 , pp. 139-149
    • Juzeniene, A.1    Juzenas, P.2    Ma, L.W.3    Iani, V.4    Moan, J.5


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