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Volumn 3, Issue 1, 2011, Pages 3-16

Targeting antibodies to the cytoplasm

Author keywords

Cell penetrating peptides; Cytosolic delivery; Intrabodies; Intracellular antibody; Intracellular delivery; Live cell imaging; Profection; Protein transduction domains; Protein transfection; Transbodies

Indexed keywords

ANTIBODY; CELL PROTEIN; HYBRID PROTEIN; IMMUNOGLOBULIN; IMMUNOGLOBULIN F(AB')2 FRAGMENT; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY;

EID: 78651396493     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.4161/mabs.3.1.14110     Document Type: Review
Times cited : (94)

References (209)
  • 1
    • 0036500993 scopus 로고    scopus 로고
    • Systems biology: A brief overview
    • Kitano H. Systems biology: A brief overview. Science 2002; 295:1662-4.
    • (2002) Science , vol.295 , pp. 1662-1664
    • Kitano, H.1
  • 6
    • 33947315300 scopus 로고    scopus 로고
    • Blocking translocation of cell surface molecules from the ER to the cell surface by intracellular antibodies targeted to the ER
    • DOI 10.1111/j.1582-4934.2007.00002.x
    • Böldicke T. Blocking translocation of cell surface molecules from the ER to the cell surface by intracellular antibodies targeted to the ER. J Cell Mol Med 2007; 11:54-70. (Pubitemid 46439625)
    • (2007) Journal of Cellular and Molecular Medicine , vol.11 , Issue.1 , pp. 54-70
    • Boldicke, T.1
  • 8
    • 0019804382 scopus 로고
    • Coiling of intermediate filaments induced by microinjection of a vimentin-specific antibody does not interfere with locomotion and mitosis
    • Gawlitta W, Osborn M, Weber K. Coiling of intermediate filaments induced by microinjection of a vimentin-specific antibody does not interfere with locomotion and mitosis. Eur J Cell Biol 1981; 26:83-90. (Pubitemid 12172689)
    • (1981) European Journal of Cell Biology , vol.26 , Issue.1 , pp. 83-90
    • Gawlitta, W.1    Osborn, M.2    Weber, K.3
  • 9
    • 0019436188 scopus 로고
    • Disruption of the in vivo distribution of the intermediate filaments in fibroblasts through the microinjection of a specific monoclonal antibody
    • Lin JJ, Feramisco JR. Disruption of the in vivo distribution of the intermediate filaments in fibroblasts through the microinjection of a specific monoclonal antibody. Cell 1981; 24:185-93.
    • (1981) Cell , vol.24 , pp. 185-193
    • Lin, J.J.1    Feramisco, J.R.2
  • 10
    • 0021352916 scopus 로고
    • 10 nm filaments are induced to collapse in living cells microinjected with monoclonal and polyclonal antibodies against tubulin
    • Blose SH, Meltzer DI, Feramisco JR. 10 nm filaments are induced to collapse in living cells microinjected with monoclonal and polyclonal antibodies against tubulin. J Cell Biol 1984; 98:847-58.
    • (1984) J Cell Biol , vol.98 , pp. 847-858
    • Blose, S.H.1    Meltzer, D.I.2    Feramisco, J.R.3
  • 11
    • 0023425213 scopus 로고
    • An investigation of microtubule organization and functions in living Drosophila embryos by injection of a fluorescently labeled antibody against tyrosinated alpha-tubulin
    • Warn RM, Flegg L, Warn A. An investigation of microtubule organization and functions in living Drosophila embryos by injection of a fluorescently labeled antibody against tyrosinated alpha-tubulin. J Cell Biol 1987; 105:1721-30.
    • (1987) J Cell Biol , vol.105 , pp. 1721-1730
    • Warn, R.M.1    Flegg, L.2    Warn, A.3
  • 12
    • 0027466863 scopus 로고
    • Microinjection of a monoclonal antibody against SPN antigen, now identified by peptide sequences as the NuMA protein, induces micronuclei in PtK2 cells
    • Kallajoki M, Harborth J, Weber K, Osborn M. Microinjection of a monoclonal antibody against SPN antigen, now identified by peptide sequences as the NuMA protein, induces micronuclei in PtK2 cells. J Cell Sci 1993; 104:139-50. (Pubitemid 23073176)
    • (1993) Journal of Cell Science , vol.104 , Issue.1 , pp. 139-150
    • Kallajoki, M.1    Harborth, J.2    Weber, K.3    Osborn, M.4
  • 13
    • 77953916958 scopus 로고    scopus 로고
    • Generating recombinant antibodies to the complete human proteome
    • Dubel S, Stoevesandt O, Taussig MJ, Hust M. Generating recombinant antibodies to the complete human proteome. Trends Biotechnol 2010; 28:333-9.
    • (2010) Trends Biotechnol , vol.28 , pp. 333-339
    • Dubel, S.1    Stoevesandt, O.2    Taussig, M.J.3    Hust, M.4
  • 14
    • 22544471858 scopus 로고    scopus 로고
    • Intrabodies as drug discovery tools and therapeutics
    • DOI 10.1016/j.cbpa.2005.06.003, PII S1367593105000803, Next-Generation Therapeutics
    • Stocks M. Intrabodies as drug discovery tools and therapeutics. Curr Opin Chem Biol 2005; 9:359-65. (Pubitemid 41019681)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.4 , pp. 359-365
    • Stocks, M.1
  • 15
    • 0029147496 scopus 로고
    • Heavy-chain dimers as well as complete antibodies are efficiently formed and secreted from Drosophila via a bip-mediated pathway
    • Kirkpatrick RB, Ganguly S, Angelichio M, Griego S, Shatzman A, Silverman C, et al. Heavy-chain dimers as well as complete antibodies are efficiently formed and secreted from Drosophila via a bip-mediated pathway. J Biol Chem 1995; 270:19800-5.
    • (1995) J Biol Chem , vol.270 , pp. 19800-19805
    • Kirkpatrick, R.B.1    Ganguly, S.2    Angelichio, M.3    Griego, S.4    Shatzman, A.5    Silverman, C.6
  • 16
    • 0034703009 scopus 로고    scopus 로고
    • BiP and PDI cooperate in the oxidative folding of antibodies in vitro
    • DOI 10.1074/jbc.M002655200
    • Mayer M, Kies U, Kammermeier R, Buchner J. BiP and PDI cooperate in the oxidative folding of antibodies in vitro. J Biol Chem 2000; 275:29421-5. (Pubitemid 32043816)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.38 , pp. 29421-29425
    • Mayer, M.1    Kies, U.2    Kammermeier, R.3    Buchner, J.4
  • 17
    • 0028148050 scopus 로고
    • Intracellular expression of single chain antibodies reverts ErbB-2 transformation
    • Beerli RR, Wels W, Hynes NE. Intracellular expression of single chain antibodies reverts ErbB-2 transformation. J Biol Chem 1994; 269:23931-6.
    • (1994) J Biol Chem , vol.269 , pp. 23931-23936
    • Beerli, R.R.1    Wels, W.2    Hynes, N.E.3
  • 18
    • 0028955535 scopus 로고
    • Phenotypic knockout of the high-affinity human interleukin 2 receptor by intracellular single-chain antibodies against the alpha subunit of the receptor
    • Richardson JH, Sodroski JG, Waldmann TA, Marasco WA. Phenotypic knockout of the high-affinity human interleukin 2 receptor by intracellular single-chain antibodies against the alpha subunit of the receptor. Proc Natl Acad Sci USA 1995; 92:3137-41.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3137-3141
    • Richardson, J.H.1    Sodroski, J.G.2    Waldmann, T.A.3    Marasco, W.A.4
  • 19
    • 4143121134 scopus 로고    scopus 로고
    • Intrabodies as therapeutic agents
    • Kontermann R. Intrabodies as therapeutic agents. Methods 2004; 34:163-70.
    • (2004) Methods , vol.34 , pp. 163-170
    • Kontermann, R.1
  • 20
    • 15444374558 scopus 로고    scopus 로고
    • Beta-site specific intrabodies to decrease and prevent generation of Alzheimer's Abeta peptide
    • Paganetti P, Calanca V, Galli C, Stefani M, Molinari M. beta-site specific intrabodies to decrease and prevent generation of Alzheimer's Abeta peptide. J Cell Biol 2005; 168:863-8.
    • (2005) J Cell Biol , vol.168 , pp. 863-868
    • Paganetti, P.1    Calanca, V.2    Galli, C.3    Stefani, M.4    Molinari, M.5
  • 21
    • 59249102344 scopus 로고    scopus 로고
    • Functional knockdown of VCAM-1 at the posttranslational level with ER retained antibodies
    • Strebe N, Guse A, Schungel M, Schirrmann T, Hafner M, Jostock T, et al. Functional knockdown of VCAM-1 at the posttranslational level with ER retained antibodies. J Immunol Methods 2008; 341: 30-40.
    • (2008) J Immunol Methods , vol.341 , pp. 30-40
    • Strebe, N.1    Guse, A.2    Schungel, M.3    Schirrmann, T.4    Hafner, M.5    Jostock, T.6
  • 22
    • 0031038715 scopus 로고    scopus 로고
    • An integrated vector system for the eukaryotic expression of antibodies or their fragments after selection from phage display libraries
    • Persic L, Roberts A, Wilton J, Cattaneo A, Bradbury A, Hoogenboom HR. An integrated vector system for the eukaryotic expression of antibodies or their fragments after selection from phage display libraries. Gene 1997; 187:9-18.
    • (1997) Gene , vol.187 , pp. 9-18
    • Persic, L.1    Roberts, A.2    Wilton, J.3    Cattaneo, A.4    Bradbury, A.5    Hoogenboom, H.R.6
  • 23
    • 0028883709 scopus 로고
    • Redox state of single chain Fv fragments targeted to the endoplasmic reticulum, cytosol and mitochondria
    • Biocca S, Ruberti F, Tafani M, Pierandrei-Amaldi P, Cattaneo A. Redox state of single chain Fv fragments targeted to the endoplasmic reticulum, cytosol and mitochondria. Biotechnology 1995; 13:1110-5.
    • (1995) Biotechnology , vol.13 , pp. 1110-1115
    • Biocca, S.1    Ruberti, F.2    Tafani, M.3    Pierandrei-Amaldi, P.4    Cattaneo, A.5
  • 24
    • 4143103580 scopus 로고    scopus 로고
    • Antigen-independent selection of intracellular stable antibody frameworks
    • Auf der Maur A, Tissot K, Barberis A. Antigen-independent selection of intracellular stable antibody frameworks. Methods 2004; 34:215-24.
    • (2004) Methods , vol.34 , pp. 215-224
    • Auf Der Maur, A.1    Tissot, K.2    Barberis, A.3
  • 25
    • 4143109060 scopus 로고    scopus 로고
    • The intracellular antibody capture technology: Towards the high-throughput selection of functional intracellular antibodies for target validation
    • DOI 10.1016/j.ymeth.2004.04.008, PII S104620230400074X
    • Visintin M, Quondam M, Cattaneo A. The intracellular antibody capture technology: Towards the highthroughput selection of functional intracellular antibodies for target validation. Methods 2004; 34:200-14. (Pubitemid 39092814)
    • (2004) Methods , vol.34 , Issue.2 , pp. 200-214
    • Visintin, M.1    Quondam, M.2    Cattaneo, A.3
  • 27
    • 0037416179 scopus 로고    scopus 로고
    • Intrabodies based on intracellular capture frameworks that bind the RAS protein with high affinity and impair oncogenic transformation
    • Tanaka T, Rabbitts TH. Intrabodies based on intracellular capture frameworks that bind the RAS protein with high affinity and impair oncogenic transformation. EMBO J 2003; 22:1025-35.
    • (2003) EMBO J , vol.22 , pp. 1025-1035
    • Tanaka, T.1    Rabbitts, T.H.2
  • 28
    • 0035212756 scopus 로고    scopus 로고
    • Immunomodulation of phytohormones and functional proteins in plant cells
    • Conrad U, Manteuffel R. Immunomodulation of phytohormones and functional proteins in plant cells. Trends Plant Sci 2001; 6:399-402.
    • (2001) Trends Plant Sci , vol.6 , pp. 399-402
    • Conrad, U.1    Manteuffel, R.2
  • 29
    • 38449115445 scopus 로고    scopus 로고
    • Intracellular antibodies (intrabodies) and their therapeutic potential
    • Lo AS, Zhu Q, Marasco WA. Intracellular antibodies (intrabodies) and their therapeutic potential. Handb Exp Pharmacol 2008; 343-73.
    • (2008) Handb Exp Pharmacol , pp. 343-373
    • Lo, A.S.1    Zhu, Q.2    Marasco, W.A.3
  • 30
    • 33644812859 scopus 로고    scopus 로고
    • Intracellular expression of recombinant antibody fluorescent protein fusions for localization of target antigens in Schizosaccharomyces pombe
    • Alting-Mees MA, Risseeuw EP, Liu E, Desautels M, Crosby WA, Hemmingsen SM. Intracellular expression of recombinant antibody fluorescent protein fusions for localization of target antigens in Schizosaccharomyces pombe. Methods Mol Biol 2006; 313:97-105.
    • (2006) Methods Mol Biol , vol.313 , pp. 97-105
    • Alting-Mees, M.A.1    Risseeuw, E.P.2    Liu, E.3    Desautels, M.4    Crosby, W.A.5    Hemmingsen, S.M.6
  • 31
    • 38649116010 scopus 로고    scopus 로고
    • Functional Intracellular Antibody Fragments Do Not Require Invariant Intradomain Disulfide Bonds
    • Tanaka T, Rabbitts TH. Functional Intracellular Antibody Fragments Do Not Require Invariant Intradomain Disulfide Bonds. J Mol Biol 2008; 794-57.
    • (2008) J Mol Biol , pp. 794-857
    • Tanaka, T.1    Rabbitts, T.H.2
  • 32
    • 0036299007 scopus 로고    scopus 로고
    • Intracellular antibody capture technology: Application to selection of intracellular antibodies recognising the BCR-ABL oncogenic protein
    • Tse E, Lobato MN, Forster A, Tanaka T, Chung GTY, Rabbitts TH. Intracellular antibody capture technology: Application to selection of intracellular antibodies recognising the BCR-ABL oncogenic protein. J Mol Biol 2002; 85-94.
    • (2002) J Mol Biol , pp. 85-94
    • Tse, E.1    Lobato, M.N.2    Forster, A.3    Tanaka, T.4    Chung, G.T.Y.5    Rabbitts, T.H.6
  • 33
    • 0036299049 scopus 로고    scopus 로고
    • The intracellular antibody capture technology (IACT): Towards a consensus sequence for intracellular antibodies
    • DOI 10.1006/jmbi.2002.5392
    • Visintin M, Settani G, Maritan A, Graziosi S, Marks JD, Cattaneo A. The intracellular antibody capture technology (IACT): Towards a consensus sequence for intracellular antibodies. J Mol Biol 2002; 317:73-83. (Pubitemid 34722200)
    • (2002) Journal of Molecular Biology , vol.317 , Issue.1 , pp. 73-83
    • Visintin, M.1    Settanni, G.2    Maritan, A.3    Graziosi, S.4    Marks, J.D.5    Cattaneo, A.6
  • 35
    • 7944230671 scopus 로고    scopus 로고
    • Intrabodies: Production and promise
    • Stocks M. Intrabodies: Production and promise. Drug Discovery Today 2004; 9:960-6.
    • (2004) Drug Discovery Today , vol.9 , pp. 960-966
    • Stocks, M.1
  • 37
    • 57749194881 scopus 로고    scopus 로고
    • Efficient isolation of soluble intracellular single-chain antibodies using the twinarginine translocation machinery
    • Fisher A, DeLisa MP. Efficient isolation of soluble intracellular single-chain antibodies using the twinarginine translocation machinery. J Mol Biol 2009; 385:299-311.
    • (2009) J Mol Biol , vol.385 , pp. 299-311
    • Fisher, A.1    DeLisa, M.P.2
  • 39
    • 0032511990 scopus 로고    scopus 로고
    • Characterization of a new intrabody directed against the N-terminal region of human p53
    • Cohen PA, Mani JC, Lane DP. Characterization of a new intrabody directed against the N-terminal region of human p53. Oncogene 1998; 17:2445-56.
    • (1998) Oncogene , vol.17 , pp. 2445-2456
    • Cohen, P.A.1    Mani, J.C.2    Lane, D.P.3
  • 40
    • 0028914482 scopus 로고
    • Inhibition of HIV-1 Tatmediated LTR transactivation and HIV-1 infection vy anti-Tat single chain intrabodies
    • Mhashilkar AM, Bagley J, Chen SY, Szilvay AM, Helland DG, Marasco WA. Inhibition of HIV-1 Tatmediated LTR transactivation and HIV-1 infection vy anti-Tat single chain intrabodies. EMBO J 1995; 14:1542-51.
    • (1995) EMBO J , vol.14 , pp. 1542-1551
    • Mhashilkar, A.M.1    Bagley, J.2    Chen, S.Y.3    Szilvay, A.M.4    Helland, D.G.5    Marasco, W.A.6
  • 41
    • 0038308559 scopus 로고    scopus 로고
    • Production of a functional catalytic antibody ScFv-NusA fusion protein in bacterial cytoplasm
    • Zheng L, Baumann U, Reymond JL. Production of a functional catalytic antibody ScFv-NusA fusion protein in bacterial cytoplasm. J Biochem 2003; 133:577-81.
    • (2003) J Biochem , vol.133 , pp. 577-581
    • Zheng, L.1    Baumann, U.2    Reymond, J.L.3
  • 42
    • 0031566160 scopus 로고    scopus 로고
    • Characterization of scFv-421, a single-chain antibody targeted to p53
    • Jannot CB, Hynes NE. Characterization of scFv-421, a single-chain antibody targeted to p53. Biochem Biophys Res Commun 1997; 230:242-6.
    • (1997) Biochem Biophys Res Commun , vol.230 , pp. 242-246
    • Jannot, C.B.1    Hynes, N.E.2
  • 43
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust RB, Waugh DS. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci 1999; 1668-74.
    • (1999) Protein Sci , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 44
    • 28844481147 scopus 로고    scopus 로고
    • Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners
    • Nallamsetty S, Waugh DS. Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners. Protein Expr Purif 2006; 45:175-82.
    • (2006) Protein Expr Purif , vol.45 , pp. 175-182
    • Nallamsetty, S.1    Waugh, D.S.2
  • 45
    • 33746744319 scopus 로고    scopus 로고
    • Enhancement of soluble protein expression through the use of fusion tags
    • DOI 10.1016/j.copbio.2006.06.003, PII S0958166906000875
    • Esposito D, Chatterjee DK. Enhancement of soluble protein expression through the use of fusion tags. Curr Opin Biotechnol 2006; 17:353-8. (Pubitemid 44163452)
    • (2006) Current Opinion in Biotechnology , vol.17 , Issue.4 , pp. 353-358
    • Esposito, D.1    Chatterjee, D.K.2
  • 46
    • 38749142906 scopus 로고    scopus 로고
    • Protein production and purification
    • Gräslund S. Protein production and purification. Nat Meth 2008; 5:135-46.
    • (2008) Nat Meth , vol.5 , pp. 135-146
    • Gräslund, S.1
  • 47
    • 0034817979 scopus 로고    scopus 로고
    • Aggresome formation by anti-Ras intracellular scFv fragments: The fate of the antigen-antibody complex
    • DOI 10.1046/j.1432-1327.2001.01876.x
    • Cardinale A, Filesi I, Biocca S. Aggresome formation by anti-Ras intracellular scFv fragments - the fate of the antigen antibody complex. Eur J Biochem 2001; 268-77. (Pubitemid 32862656)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.2 , pp. 268-277
    • Cardinale, A.1    Filesi, I.2    Biocca, S.3
  • 48
    • 0032479180 scopus 로고    scopus 로고
    • Expression of an antibody fragment at high levels in the bacterial cytoplasm
    • Martineau P, Jones P, Winter G. Expression of an antibody fragment at high levels in the bacterial cytoplasm. J Mol Biol 1998; 280:117-27.
    • (1998) J Mol Biol , vol.280 , pp. 117-127
    • Martineau, P.1    Jones, P.2    Winter, G.3
  • 49
    • 0035823143 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies
    • Bach H, Mazor Y, Shaky S, Shoham-Lev A, Berdichevsky Y, Gutnick DL, et al. Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies. J Mol Biol 2001; 312:79-93.
    • (2001) J Mol Biol , vol.312 , pp. 79-93
    • Bach, H.1    Mazor, Y.2    Shaky, S.3    Shoham-Lev, A.4    Berdichevsky, Y.5    Gutnick, D.L.6
  • 50
  • 51
    • 0024597585 scopus 로고
    • Increased expression of DNA cointroduced with nuclear protein in adult rat liver
    • Kaneda Y, Iwai K, Uchida T. Increased expression of DNA cointroduced with nuclear protein in adult rat liver. Science 1989; 243:375-8.
    • (1989) Science , vol.243 , pp. 375-378
    • Kaneda, Y.1    Iwai, K.2    Uchida, T.3
  • 53
    • 0025857661 scopus 로고
    • Expression of hepatitis B virus surface antigen in adult rat liver: Co-introduction of DNA and nuclear protein by a simplified liposome method
    • Kato K, Nakanishi M, Kaneda Y, Uchida T, Okada Y. Expression of hepatitis B virus surface antigen in adult rat liver. Co-introduction of DNA and nuclear protein by a simplified liposome method. J Biol Chem 1991; 266:3361-4. (Pubitemid 21909217)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.6 , pp. 3361-3364
    • Kato, K.1    Nakanishi, M.2    Kaneda, Y.3    Uchida, T.4    Okada, Y.5
  • 54
    • 0027264139 scopus 로고
    • Genomic targeting with purified Cre recombinase
    • Baubonis W, Sauer B. Genomic targeting with purified Cre recombinase. Nucleic Acids Res 1993; 21:2025-9. (Pubitemid 23160716)
    • (1993) Nucleic Acids Research , vol.21 , Issue.9 , pp. 2025-2029
    • Baubonis, W.1    Sauer, B.2
  • 55
    • 0027290777 scopus 로고
    • Cytoplasmic expression of a reporter gene by co-delivery of T7 RNA polymerase and T7 promoter sequence with cationic liposomes
    • Gao X, Huang L. Cytoplasmic expression of a reporter gene by co-delivery of T7 RNA polymerase and T7 promoter sequence with cationic liposomes. Nucleic Acids Res 1993; 21:2867-72. (Pubitemid 23220438)
    • (1993) Nucleic Acids Research , vol.21 , Issue.12 , pp. 2867-2872
    • Gao, X.1    Huang, L.2
  • 56
    • 0025059563 scopus 로고
    • Efficiency of cytoplasmic delivery by pH-sensitive liposomes to cells in culture
    • Chu CJ, Dijkstra J, Lai MZ, Hong K, Szoka FC. Efficiency of cytoplasmic delivery by pH-sensitive liposomes to cells in culture. Pharm Res 1990; 7:824-43. (Pubitemid 20332534)
    • (1990) Pharmaceutical Research , vol.7 , Issue.8 , pp. 824-834
    • Chu, C.-J.1    Dijkstra, J.2    Lai, M.-Z.3    Hong, K.4    Szoka, F.C.5
  • 57
    • 0026713158 scopus 로고
    • Class I restricted CTL recognition of a soluble protein delivered by liposomes containing lipophilic polylysines
    • Nair S, Zhou X, Huang L, Rouse BT. Class I restricted CTL recognition of a soluble protein delivered by liposomes containing lipophilic polylysines. J Immunol Methods 1992; 237-43.
    • (1992) J Immunol Methods , pp. 237-243
    • Nair, S.1    Zhou, X.2    Huang, L.3    Rouse, B.T.4
  • 58
    • 0027183359 scopus 로고
    • Cationic liposomemediated incorporation of prostatic acid phosphatase protein into human prostate carcinoma cells
    • Lin MF, DaVolio J, Garcia R. Cationic liposomemediated incorporation of prostatic acid phosphatase protein into human prostate carcinoma cells. Biochem Biophys Res Commun 1993; 192:413-9.
    • (1993) Biochem Biophys Res Commun , vol.192 , pp. 413-419
    • Lin, M.F.1    DaVolio, J.2    Garcia, R.3
  • 59
    • 0029065036 scopus 로고
    • Delivery of protein into cells using polycationic liposomes
    • Sells MA, Li J, Chernoff J. Delivery of protein into cells using polycationic liposomes. Biotechniques 1995; 19:72-6.
    • (1995) Biotechniques , vol.19 , pp. 72-76
    • Sells, M.A.1    Li, J.2    Chernoff, J.3
  • 60
    • 0029997423 scopus 로고    scopus 로고
    • Delivery of macromolecules into cytosol using liposomes containing hemolysin from Listeria monocytogenes
    • Lee KD, Oh YK, Portnoy DA, Swanson JA. Delivery of macromolecules into cytosol using liposomes containing hemolysin from Listeria monocytogenes. J Biol Chem 1996; 271:7249-52.
    • (1996) J Biol Chem , vol.271 , pp. 7249-7252
    • Lee, K.D.1    Oh, Y.K.2    Portnoy, D.A.3    Swanson, J.A.4
  • 61
    • 0031847226 scopus 로고    scopus 로고
    • Lipofection of purified adeno-associated virus Rep68 protein: Toward a chromosome-targeting nonviral particle
    • Lamartina S, Roscilli G, Rinaudo D, Delmastro P, Toniatti C. Lipofection of purified adeno-associated virus Rep68 protein: toward a chromosome-targeting nonviral particle. J Virol 1998; 72:7653-8.
    • (1998) J Virol , vol.72 , pp. 7653-7658
    • Lamartina, S.1    Roscilli, G.2    Rinaudo, D.3    Delmastro, P.4    Toniatti, C.5
  • 62
    • 0035860724 scopus 로고    scopus 로고
    • Intracellular delivery of proteins with a new lipid-mediated delivery system
    • Zelphati O, Wang Y, Kitada S, Reed JC, Felgner PL, Corbeil J. Intracellular delivery of proteins with a new lipid-mediated delivery system. J Biol Chem 2001; 276:35103-10.
    • (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
  • 63
    • 0037112944 scopus 로고    scopus 로고
    • Syndapins integrate N-WASP in receptor-mediated endocytosis
    • Kessels MM, Qualmann B. Syndapins integrate N-WASP in receptor-mediated endocytosis. EMBO J 2002; 21:6083-94.
    • (2002) EMBO J , vol.21 , pp. 6083-6094
    • Kessels, M.M.1    Qualmann, B.2
  • 65
    • 1642546240 scopus 로고    scopus 로고
    • c-Fos activated phospholipid synthesis is required for neurite elongation in differentiating PC12 cells
    • Gil GA, Bussolino DF, Portal MM, Pecchio AA, Renner ML, Borioli GA, et al. c-Fos activated phospholipid synthesis is required for neurite elongation in differentiating PC12 cells. Mol Biol Cell 2004; 15:1881-94.
    • (2004) Mol Biol Cell , vol.15 , pp. 1881-1894
    • Gil, G.A.1    Bussolino, D.F.2    Portal, M.M.3    Pecchio, A.A.4    Renner, M.L.5    Borioli, G.A.6
  • 67
    • 33750577279 scopus 로고    scopus 로고
    • Escherichia coli cyclomodulin Cif induces G2 arrest of the host cell cycle without activation of the DNA-damage checkpoint-signalling pathway
    • Taieb F, Nougayrede JP, Watrin C, Samba-Louaka A, Oswald E. Escherichia coli cyclomodulin Cif induces G2 arrest of the host cell cycle without activation of the DNA-damage checkpoint-signalling pathway. Cell Microbiol 2006; 8:1910-21.
    • (2006) Cell Microbiol , vol.8 , pp. 1910-1921
    • Taieb, F.1    Nougayrede, J.P.2    Watrin, C.3    Samba-Louaka, A.4    Oswald, E.5
  • 68
  • 69
    • 53449095486 scopus 로고    scopus 로고
    • Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse
    • Lofgren S, Fernando MR, Xing KY, Wang Y, Kuszynski CA, Ho YS, et al. Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse. Invest Ophthalmol Vis Sci 2008; 49:4497-505.
    • (2008) Invest Ophthalmol Vis Sci , vol.49 , pp. 4497-4505
    • Lofgren, S.1    Fernando, M.R.2    Xing, K.Y.3    Wang, Y.4    Kuszynski, C.A.5    Ho, Y.S.6
  • 70
    • 72149119358 scopus 로고    scopus 로고
    • Exogenous alpha-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells
    • Luk KC, Song C, O'Brien P, Stieber A, Branch JR, Brunden KR, et al. Exogenous alpha-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells. Proc Natl Acad Sci USA 2009; 106:20051-6.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20051-20056
    • Luk, K.C.1    Song, C.2    O'Brien, P.3    Stieber, A.4    Branch, J.R.5    Brunden, K.R.6
  • 72
    • 0031785492 scopus 로고    scopus 로고
    • Efficient protein transfection of cultured coronary venular endothelial cells
    • Tinsley JH, Hawker J, Yuan Y. Efficient protein transfection of cultured coronary venular endothelial cells. Am J Physiol Heart Circ Physiol 1998:1873-8.
    • (1998) Am J Physiol Heart Circ Physiol , pp. 1873-1878
    • Tinsley, J.H.1    Hawker, J.2    Yuan, Y.3
  • 73
    • 0035743222 scopus 로고    scopus 로고
    • Protein transfection of intact microvessels specifically modulates vasoreactivity and permeability
    • Tinsley JH, Zawieja DC, Wu MH, Ustinova EE, Xu W, Yuan SY. Protein transfection of intact microvessels specifically modulates vasoreactivity and permeability. J Vasc Res 2001; 444-52.
    • (2001) J Vasc Res , pp. 444-452
    • Tinsley, J.H.1    Zawieja, D.C.2    Wu, M.H.3    Ustinova, E.E.4    Xu, W.5    Yuan, S.Y.6
  • 75
    • 0036472994 scopus 로고    scopus 로고
    • Survivin exists in immunochemically distinct subcellular pools and is involved in spindle microtubule function
    • Fortugno P, Wall NR, Giodini A, O'Connor DS, Plescia J, Padgett KM, et al. Survivin exists in immunochemically distinct subcellular pools and is involved in spindle microtubule function. J Cell Sci 2002; 115:575-85.
    • (2002) J Cell Sci , vol.115 , pp. 575-585
    • Fortugno, P.1    Wall, N.R.2    Giodini, A.3    O'Connor, D.S.4    Plescia, J.5    Padgett, K.M.6
  • 76
    • 3042852733 scopus 로고    scopus 로고
    • Intracytoplasmic delivery of anionic proteins
    • Dalkara D, Zuber G, Behr JP. Intracytoplasmic delivery of anionic proteins. Mol Ther 2004; 9:964-9.
    • (2004) Mol Ther , vol.9 , pp. 964-969
    • Dalkara, D.1    Zuber, G.2    Behr, J.P.3
  • 77
    • 2542421751 scopus 로고    scopus 로고
    • Dynein motors transport activated Trks to promote survival of target-dependent neurons
    • Heerssen HM, Pazyra MF, Segal RA. Dynein motors transport activated Trks to promote survival of target-dependent neurons. Nat Neurosci 2004; 7:596-604.
    • (2004) Nat Neurosci , vol.7 , pp. 596-604
    • Heerssen, H.M.1    Pazyra, M.F.2    Segal, R.A.3
  • 78
    • 23944458820 scopus 로고    scopus 로고
    • Polyethyleneimine as a transmembrane carrier of fluorescently labeled proteins and antibodies
    • Didenko VV, Ngo H, Baskin DS. Polyethyleneimine as a transmembrane carrier of fluorescently labeled proteins and antibodies. Anal Biochem 2005; 168-73.
    • (2005) Anal Biochem , pp. 168-173
    • Didenko, V.V.1    Ngo, H.2    Baskin, D.S.3
  • 79
    • 33644754665 scopus 로고    scopus 로고
    • Impaired Crkl expression contributes to the defective DNA binding of Stat5b in nonobese diabetic mice
    • Laloraya M, Davoodi-Semiromi A, Kumar GP, McDuffie M, She JX. Impaired Crkl expression contributes to the defective DNA binding of Stat5b in nonobese diabetic mice. Diabetes 2006; 55:734-41.
    • (2006) Diabetes , vol.55 , pp. 734-741
    • Laloraya, M.1    Davoodi-Semiromi, A.2    Kumar, G.P.3    McDuffie, M.4    She, J.X.5
  • 80
    • 36749006634 scopus 로고    scopus 로고
    • Chlamydia pneumoniae inclusion membrane protein Cpn0585 interacts with multiple Rab GTPases
    • Cortes C, Rzomp KA, Tvinnereim A, Scidmore MA, Wizel B. Chlamydia pneumoniae inclusion membrane protein Cpn0585 interacts with multiple Rab GTPases. Infect Immun 2007; 75:5586-96.
    • (2007) Infect Immun , vol.75 , pp. 5586-5596
    • Cortes, C.1    Rzomp, K.A.2    Tvinnereim, A.3    Scidmore, M.A.4    Wizel, B.5
  • 82
    • 84876189469 scopus 로고    scopus 로고
    • Cationic lipid-mediated intracellular delivery of antibodies into live cells
    • Weill CO, Biri S, Erbacher P. Cationic lipid-mediated intracellular delivery of antibodies into live cells. Biotechniques 2008; 44:7-9.
    • (2008) Biotechniques , vol.44 , pp. 7-9
    • Weill, C.O.1    Biri, S.2    Erbacher, P.3
  • 83
    • 2342444942 scopus 로고    scopus 로고
    • Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival
    • Shimura H, Miura-Shimura Y, Kosik KS. Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival. J Biol Chem 2004; 279:17957-62.
    • (2004) J Biol Chem , vol.279 , pp. 17957-17962
    • Shimura, H.1    Miura-Shimura, Y.2    Kosik, K.S.3
  • 86
    • 33749575548 scopus 로고    scopus 로고
    • Inhibition of c-Met and prevention of spontaneous metastatic spreading by the 2-indolinone RPI-1
    • Cassinelli G, Lanzi C, Petrangolini G, Tortoreto M, Pratesi G, Cuccuru G, et al. Inhibition of c-Met and prevention of spontaneous metastatic spreading by the 2-indolinone RPI-1. Mol Cancer Ther 2006; 5:2388-97.
    • (2006) Mol Cancer Ther , vol.5 , pp. 2388-2397
    • Cassinelli, G.1    Lanzi, C.2    Petrangolini, G.3    Tortoreto, M.4    Pratesi, G.5    Cuccuru, G.6
  • 87
    • 34249690833 scopus 로고    scopus 로고
    • Nuclear import of human sexual regulator DMRT1 is mediated by importin-beta
    • Ying M, Chen B, Tian Y, Hou Y, Li Q, Shang X, et al. Nuclear import of human sexual regulator DMRT1 is mediated by importin-beta. Biochim Biophys Acta 2007; 1773:804-13.
    • (2007) Biochim Biophys Acta , vol.1773 , pp. 804-813
    • Ying, M.1    Chen, B.2    Tian, Y.3    Hou, Y.4    Li, Q.5    Shang, X.6
  • 88
    • 58249112736 scopus 로고    scopus 로고
    • RET/PTC1-driven neoplastic transformation and proinvasive phenotype of human thyrocytes involve Met induction and beta-catenin nuclear translocation
    • Cassinelli G, Favini E, Degl'Innocenti D, Salvi A, De Petro G, Pierotti MA, et al. RET/PTC1-driven neoplastic transformation and proinvasive phenotype of human thyrocytes involve Met induction and beta-catenin nuclear translocation. Neoplasia 2009; 11:10-21.
    • (2009) Neoplasia , vol.11 , pp. 10-21
    • Cassinelli, G.1    Favini, E.2    Degl'Innocenti, D.3    Salvi, A.4    De Petro, G.5    Pierotti, M.A.6
  • 89
    • 70349684157 scopus 로고    scopus 로고
    • O-antigen delays lipopolysaccharide recognition and impairs antibacterial host defense in murine intestinal epithelial cells
    • Duerr CU, Zenk SF, Chassin C, Pott J, Gutle D, Hensel M, et al. O-antigen delays lipopolysaccharide recognition and impairs antibacterial host defense in murine intestinal epithelial cells. PLoS Pathog 2009; 5:1000567.
    • (2009) PLoS Pathog , vol.5 , pp. 1000567
    • Duerr, C.U.1    Zenk, S.F.2    Chassin, C.3    Pott, J.4    Gutle, D.5    Hensel, M.6
  • 90
    • 77950220028 scopus 로고    scopus 로고
    • Efficient delivery of bioactive antibodies into the cytoplasm of living cells by charge-conversional polyion complex micelles
    • Lee Y, Ishii T, Kim HJ, Nishiyama N, Hayakawa Y, Itaka K, et al. Efficient delivery of bioactive antibodies into the cytoplasm of living cells by charge-conversional polyion complex micelles. Angew Chem Int Ed Engl 2010; 49:2552-5.
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 2552-2555
    • Lee, Y.1    Ishii, T.2    Kim, H.J.3    Nishiyama, N.4    Hayakawa, Y.5    Itaka, K.6
  • 91
    • 34848904314 scopus 로고    scopus 로고
    • Intracellular protein delivery with a dimerizable amphiphile for improved complex stability and prolonged protein release in the cytoplasm of adherent cell lines
    • Dalkara D, Chandrashekhar C, Zuber G. Intracellular protein delivery with a dimerizable amphiphile for improved complex stability and prolonged protein release in the cytoplasm of adherent cell lines. J Control Release 2006; 116:353-9.
    • (2006) J Control Release , vol.116 , pp. 353-359
    • Dalkara, D.1    Chandrashekhar, C.2    Zuber, G.3
  • 93
    • 38349076002 scopus 로고    scopus 로고
    • Efficient intracellular delivery of functional proteins using cationic polymer core/shell nanoparticles
    • Lee AL, Wang Y, Ye WH, Yoon HS, Chan SY, Yang YY. Efficient intracellular delivery of functional proteins using cationic polymer core/shell nanoparticles. Biomaterials 2008; 29:1224-32.
    • (2008) Biomaterials , vol.29 , pp. 1224-1232
    • Lee, A.L.1    Wang, Y.2    Ye, W.H.3    Yoon, H.S.4    Chan, S.Y.5    Yang, Y.Y.6
  • 94
    • 68849091330 scopus 로고    scopus 로고
    • Intracellular protein delivery by glucose-coated polymeric beads
    • Camb
    • Jung S, Huh S, Cheon YP, Park S. Intracellular protein delivery by glucose-coated polymeric beads. Chem Commun (Camb) 2009; 7:5003-5.
    • (2009) Chem Commun , vol.7 , pp. 5003-5005
    • Jung, S.1    Huh, S.2    Cheon, Y.P.3    Park, S.4
  • 96
    • 72149106160 scopus 로고    scopus 로고
    • pHsensitive carbonate apatite as an intracellular protein transporter
    • Tada S, Chowdhury EH, Cho CS, Akaike T. pHsensitive carbonate apatite as an intracellular protein transporter. Biomaterials 2010; 31:1453-9.
    • (2010) Biomaterials , vol.31 , pp. 1453-1459
    • Tada, S.1    Chowdhury, E.H.2    Cho, C.S.3    Akaike, T.4
  • 97
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • Morris MC, Depollier J, Mery J, Heitz F, Divita G. A peptide carrier for the delivery of biologically active proteins into mammalian cells. Nat Biotechnol 2001; 19: 1173-6.
    • (2001) Nat Biotechnol , vol.19 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 99
    • 0001120209 scopus 로고
    • Bloodbrain barrier transport of cationized immunoglobulin G: Enhanced delivery compared to native protein
    • Triguero D, Buciak JB, Yang J, Pardridge WM. Bloodbrain barrier transport of cationized immunoglobulin G: Enhanced delivery compared to native protein. Proc Natl Acad Sci USA 1989; 4761-5.
    • (1989) Proc Natl Acad Sci USA , pp. 4761-4765
    • Triguero, D.1    Buciak, J.B.2    Yang, J.3    Pardridge, W.M.4
  • 100
    • 20144389743 scopus 로고    scopus 로고
    • Intracellular delivery of proteins into mammalian living cells by polyethyleneiminecationization
    • Futami J, Kitazoe M, Maeda T, Nukui E, Sakaguchi M, Kosaka J, et al. Intracellular delivery of proteins into mammalian living cells by polyethyleneiminecationization. J Biosci Bioeng 2005; 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
  • 101
    • 0029981092 scopus 로고    scopus 로고
    • Evidence for the role of proteoglycans in cation-mediated gene transfer
    • Mislick KA, Baldeschwieler JD. Evidence for the role of proteoglycans in cation-mediated gene transfer. Proc Natl Acad Sci USA 1996; 93:12349-54.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12349-12354
    • Mislick, K.A.1    Baldeschwieler, J.D.2
  • 102
    • 3042857264 scopus 로고    scopus 로고
    • A model for non-viral gene delivery: Through syndecan adhesion molecules and powered by actin
    • Kopatz I, Remy JS, Behr JP. A model for non-viral gene delivery: Through syndecan adhesion molecules and powered by actin. J Gene Med 2004; 6:769-76.
    • (2004) J Gene Med , vol.6 , pp. 769-776
    • Kopatz, I.1    Remy, J.S.2    Behr, J.P.3
  • 103
    • 33644593889 scopus 로고    scopus 로고
    • Uptake pathways and subsequent intracellular trafficking in nonviral gene delivery
    • Khalil IA, Kogure K, Akita H, Harashima H. Uptake pathways and subsequent intracellular trafficking in nonviral gene delivery. Pharmacol Rev 2006; 32-45.
    • (2006) Pharmacol Rev , pp. 32-45
    • Khalil, I.A.1    Kogure, K.2    Akita, H.3    Harashima, H.4
  • 104
    • 78650476432 scopus 로고    scopus 로고
    • The proton sponge: A trick to enter cells the viruses did not exploit
    • Behr JP. The proton sponge: A trick to enter cells the viruses did not exploit. Chimia 1997; 51:34-6.
    • (1997) Chimia , vol.51 , pp. 34-36
    • Behr, J.P.1
  • 105
    • 0029743560 scopus 로고    scopus 로고
    • Retroviral infection is limited by Brownian motion
    • Chuck AS, Clarke MF, Palsson BO. Retroviral infection is limited by Brownian motion. Hum Gene Ther 1996; 7:1527-34.
    • (1996) Hum Gene Ther , vol.7 , pp. 1527-1534
    • Chuck, A.S.1    Clarke, M.F.2    Palsson, B.O.3
  • 106
    • 0031722107 scopus 로고    scopus 로고
    • Chitosan-based vector/DNA complexes for gene delivery: Biophysical characteristics and transfection ability
    • Erbacher P, Zou S, Bettinger T, Steffan AM, Remy JS. Chitosan-based vector/DNA complexes for gene delivery: Biophysical characteristics and transfection ability. Pharm Res 1998; 15:1332-9.
    • (1998) Pharm Res , vol.15 , pp. 1332-1339
    • Erbacher, P.1    Zou, S.2    Bettinger, T.3    Steffan, A.M.4    Remy, J.S.5
  • 107
    • 0033898807 scopus 로고    scopus 로고
    • Enhancement of transfection by physical concentration of DNA at the cell surface
    • Luo D, Saltzman WM. Enhancement of transfection by physical concentration of DNA at the cell surface. Nat Biotechnol 2000; 18:893-5.
    • (2000) Nat Biotechnol , vol.18 , pp. 893-895
    • Luo, D.1    Saltzman, W.M.2
  • 108
    • 0032931623 scopus 로고    scopus 로고
    • Lipoplex size is a major determinant of in vitro lipofection efficiency
    • Ross PC, Hui SW. Lipoplex size is a major determinant of in vitro lipofection efficiency. Gene Ther 1999; 6:651-9.
    • (1999) Gene Ther , vol.6 , pp. 651-659
    • Ross, P.C.1    Hui, S.W.2
  • 109
    • 71249150257 scopus 로고    scopus 로고
    • The biological routes of gene delivery mediated by lipid-based non-viral vectors
    • Duan Y, Zhang S, Wang B, Yang B, Zhi D. The biological routes of gene delivery mediated by lipid-based non-viral vectors. Expert Opin Drug Deliv 2009; 6:1351-61.
    • (2009) Expert Opin Drug Deliv , vol.6 , pp. 1351-1361
    • Duan, Y.1    Zhang, S.2    Wang, B.3    Yang, B.4    Zhi, D.5
  • 110
    • 0029118325 scopus 로고
    • High-efficiency retroviral-mediated gene transfer into human and nonhuman primate peripheral blood lymphocytes
    • Bunnell BA, Muul LM, Donahue RE, Blaese RM, Morgan RA. High-efficiency retroviral-mediated gene transfer into human and nonhuman primate peripheral blood lymphocytes. Proc Natl Acad Sci USA 1995; 92:7739-43.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7739-7743
    • Bunnell, B.A.1    Muul, L.M.2    Donahue, R.E.3    Blaese, R.M.4    Morgan, R.A.5
  • 112
    • 23844462026 scopus 로고    scopus 로고
    • Role of clathrin-and caveolae-mediated endocytosis in gene transfer mediated by lipo- And polyplexes
    • Rejman J, Bragonzi A, Conese M. Role of clathrin-and caveolae-mediated endocytosis in gene transfer mediated by lipo- and polyplexes. Mol Ther 2005; 12:468-74.
    • (2005) Mol Ther , vol.12 , pp. 468-474
    • Rejman, J.1    Bragonzi, A.2    Conese, M.3
  • 113
    • 1642575957 scopus 로고    scopus 로고
    • Size-dependent internalization of particles via the pathways of clathrin- and caveolae-mediated endocytosis
    • Rejman J, Oberle V, Zuhorn IS, Hoekstra D. Size-dependent internalization of particles via the pathways of clathrin- and caveolae-mediated endocytosis. Biochem J 2004; 377:159-69.
    • (2004) Biochem J , vol.377 , pp. 159-169
    • Rejman, J.1    Oberle, V.2    Zuhorn, I.S.3    Hoekstra, D.4
  • 114
    • 34547114456 scopus 로고    scopus 로고
    • Pathways of clathrin-independent endocytosis
    • Mayor S, Pagano RE. Pathways of clathrin-independent endocytosis. Nat Rev Mol Cell Biol 2007; 603-12.
    • (2007) Nat Rev Mol Cell Biol , pp. 603-612
    • Mayor, S.1    Pagano, R.E.2
  • 116
    • 47749131189 scopus 로고    scopus 로고
    • Design of cytotoxic ribonucleases by cationization to enhance intracellular protein delivery
    • Futami J, Yamada H. Design of cytotoxic ribonucleases by cationization to enhance intracellular protein delivery. Curr Pharm Biotechnol 2008; 9:180-4.
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 180-184
    • Futami, J.1    Yamada, H.2
  • 117
    • 0036744916 scopus 로고    scopus 로고
    • Evaluation of strategies for the intracellular delivery of proteins
    • Ye D, Xu D, Singer AU, Juliano RL. Evaluation of strategies for the intracellular delivery of proteins. Pharm Res 2002; 19:1302-9.
    • (2002) Pharm Res , vol.19 , pp. 1302-1309
    • Ye, D.1    Xu, D.2    Singer, A.U.3    Juliano, R.L.4
  • 118
    • 0141891450 scopus 로고    scopus 로고
    • Can transcription factors function as cell-cell signalling molecules?
    • Prochiantz A, Joliot A. Can transcription factors function as cell-cell signalling molecules? Nat Rev Mol Cell Biol 2003; 4:814-9.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 814-819
    • Prochiantz, A.1    Joliot, A.2
  • 119
    • 23844453399 scopus 로고    scopus 로고
    • Cationic sites on granzyme B contribute to cytotoxicity by promoting its uptake into target cells
    • Bird CH, Sun J, Ung K, Karambalis D, Whisstock JC, Trapani JA, et al. Cationic sites on granzyme B contribute to cytotoxicity by promoting its uptake into target cells. Mol Cell Biol 2005; 25:7854-67.
    • (2005) Mol Cell Biol , vol.25 , pp. 7854-7867
    • Bird, Ch.1    Sun, J.2    Ung, K.3    Karambalis, D.4    Whisstock, J.C.5    Trapani, J.A.6
  • 120
    • 0033948268 scopus 로고    scopus 로고
    • Messenger proteins: Homeoproteins, TAT and others
    • Prochiantz A. Messenger proteins: Homeoproteins, TAT and others. Curr Opin Cell Biol 2000; 12:400-6.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 400-406
    • Prochiantz, A.1
  • 121
    • 35648941282 scopus 로고    scopus 로고
    • Cellular uptake mechanisms and potential therapeutic utility of peptidic cell delivery vectors: Progress 2001-2006
    • Fischer PM. Cellular uptake mechanisms and potential therapeutic utility of peptidic cell delivery vectors: Progress 2001-2006. Med Res Rev 2007; 27:755-95.
    • (2007) Med Res Rev , vol.27 , pp. 755-795
    • Fischer, P.M.1
  • 123
    • 34250835903 scopus 로고    scopus 로고
    • A comprehensive model for the cellular uptake of cationic cell-penetrating peptides
    • Duchardt F, Fotin-Mleczek M, Schwarz H, Fischer R, Brock R. A comprehensive model for the cellular uptake of cationic cell-penetrating peptides. Traffic 2007; 8:848-66.
    • (2007) Traffic , vol.8 , pp. 848-866
    • Duchardt, F.1    Fotin-Mleczek, M.2    Schwarz, H.3    Fischer, R.4    Brock, R.5
  • 124
    • 74049160383 scopus 로고    scopus 로고
    • Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction
    • Gump JM, June RK, Dowdy SF. Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction. J Biol Chem 2010; 285:1500-7.
    • (2010) J Biol Chem , vol.285 , pp. 1500-1507
    • Gump, J.M.1    June, R.K.2    Dowdy, S.F.3
  • 125
    • 38949188925 scopus 로고    scopus 로고
    • Methodological and cellular aspects that govern the internalization mechanisms of arginine-rich cell-penetrating peptides
    • Nakase I, Takeuchi T, Tanaka G, Futaki S. Methodological and cellular aspects that govern the internalization mechanisms of arginine-rich cell-penetrating peptides. Adv Drug Deliv Rev 2008; 60:598-607.
    • (2008) Adv Drug Deliv Rev , vol.60 , pp. 598-607
    • Nakase, I.1    Takeuchi, T.2    Tanaka, G.3    Futaki, S.4
  • 126
    • 0037333830 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan as a plasma membrane carrier
    • Belting M. Heparan sulfate proteoglycan as a plasma membrane carrier. Trends Biochem Sci 2003; 28:145-51.
    • (2003) Trends Biochem Sci , vol.28 , pp. 145-151
    • Belting, M.1
  • 127
    • 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, Ballmer-Hofer K. 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 2003; 278:35109-14.
    • (2003) J Biol Chem , vol.278 , pp. 35109-35114
    • Console, S.1    Marty, C.2    Garcia-Echeverria, C.3    Schwendener, R.4    Ballmer-Hofer, K.5
  • 128
    • 41149156893 scopus 로고    scopus 로고
    • Cellular internalization and distribution of argininerich peptides as a function of extracellular peptide concentration, serum and plasma membrane associated proteoglycans
    • Kosuge M, Takeuchi T, Nakase I, Jones AT, Futaki S. Cellular internalization and distribution of argininerich peptides as a function of extracellular peptide concentration, serum and plasma membrane associated proteoglycans. Bioconjug Chem 2008; 19:656-64.
    • (2008) Bioconjug Chem , vol.19 , pp. 656-664
    • Kosuge, M.1    Takeuchi, T.2    Nakase, I.3    Jones, A.T.4    Futaki, S.5
  • 129
    • 0035793619 scopus 로고    scopus 로고
    • Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans
    • Tyagi M, Rusnati M, Presta M, Giacca M. Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans. J Biol Chem 2001; 276:3254-61.
    • (2001) J Biol Chem , vol.276 , pp. 3254-3261
    • Tyagi, M.1    Rusnati, M.2    Presta, M.3    Giacca, M.4
  • 130
    • 38049156027 scopus 로고    scopus 로고
    • Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes
    • Herce HD, Garcia AE. Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes. Proc Natl Acad Sci USA 2007; 104:20805-10.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20805-20810
    • Herce, H.D.1    Garcia, A.E.2
  • 131
    • 68949116150 scopus 로고    scopus 로고
    • Alternative mechanisms for the interaction of the cell-penetrating peptides penetratin and the TAT peptide with lipid bilayers
    • Yesylevskyy S, Marrink SJ, Mark AE. Alternative mechanisms for the interaction of the cell-penetrating peptides penetratin and the TAT peptide with lipid bilayers. Biophys J 2009; 97:40-9.
    • (2009) Biophys J , vol.97 , pp. 40-49
    • Yesylevskyy, S.1    Marrink, S.J.2    Mark, A.E.3
  • 132
    • 77954374712 scopus 로고    scopus 로고
    • Cell-penetrating HIV1 TAT peptides can generate pores in model membranes
    • Ciobanasu C, Siebrasse JP, Kubitscheck U. Cell-penetrating HIV1 TAT peptides can generate pores in model membranes. Biophys J 2010; 99:153-62.
    • (2010) Biophys J , vol.99 , pp. 153-162
    • Ciobanasu, C.1    Siebrasse, J.P.2    Kubitscheck, U.3
  • 133
  • 134
    • 20444403719 scopus 로고    scopus 로고
    • Effects of cargo molecules on the cellular uptake of arginine-rich cell-penetrating peptides
    • Maiolo JR, Ferrer M, Ottinger EA. Effects of cargo molecules on the cellular uptake of arginine-rich cell-penetrating peptides. Biochim Biophys Acta 2005; 1712:161-72.
    • (2005) Biochim Biophys Acta , vol.1712 , pp. 161-172
    • Maiolo, J.R.1    Ferrer, M.2    Ottinger, E.A.3
  • 136
    • 33748648777 scopus 로고    scopus 로고
    • Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells
    • Tunnemann G, Martin RM, Haupt S, Patsch C, Edenhofer F, Cardoso MC. Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells. FASEB J 2006; 20:1775-84.
    • (2006) FASEB J , vol.20 , pp. 1775-1784
    • Tunnemann, G.1    Martin, R.M.2    Haupt, S.3    Patsch, C.4    Edenhofer, F.5    Cardoso, M.C.6
  • 137
    • 17044398110 scopus 로고    scopus 로고
    • Making cell-permeable antibodies (Transbody) through fusion of protein transduction domains (PTD) with single chain variable fragment (scFv) antibodies: Potential advantages over antibodies expressed within the intracellular environment (Intrabody)
    • Heng BC, Cao T. Making cell-permeable antibodies (Transbody) through fusion of protein transduction domains (PTD) with single chain variable fragment (scFv) antibodies: Potential advantages over antibodies expressed within the intracellular environment (Intrabody). Medical Hypotheses 2005; 6:1105-8.
    • (2005) Medical Hypotheses , vol.6 , pp. 1105-1108
    • Heng, B.C.1    Cao, T.2
  • 140
    • 0035427589 scopus 로고    scopus 로고
    • Chemical engineering of cell penetrating antibodies
    • Zhao Y, Lou D, Burkett J, Kohler H. Chemical engineering of cell penetrating antibodies. J Immunol Methods 2001; 254:137-45.
    • (2001) J Immunol Methods , vol.254 , pp. 137-145
    • Zhao, Y.1    Lou, D.2    Burkett, J.3    Kohler, H.4
  • 141
    • 0036074754 scopus 로고    scopus 로고
    • Quantitation of the tumor-targeting properties of antibody fragments conjugated to cell-permeating HIV-1 TAT peptides
    • Niesner U, Halin C, Lozzi L, Gunthert M, Neri P, Wunderli-Allenspach H, et al. Quantitation of the tumor-targeting properties of antibody fragments conjugated to cell-permeating HIV-1 TAT peptides. Bioconjug Chem 2002; 13:729-36.
    • (2002) Bioconjug Chem , vol.13 , pp. 729-736
    • Niesner, U.1    Halin, C.2    Lozzi, L.3    Gunthert, M.4    Neri, P.5    Wunderli-Allenspach, H.6
  • 142
    • 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, Weissb A, Adermannc K, Lazarovicid P, Hochmane J, Wellhöner H. A disulfide conjugate between anti-tetanus antibodies and HIV (37-72). Tat neutralizes tetanus toxin inside chromaffin cells. FEBS Lett 1999; 458: 383-6.
    • (1999) FEBS Lett , vol.458 , pp. 383-386
    • Stein, S.1    Weissb, A.2    Adermannc, K.3    Lazarovicid, P.4    Hochmane, J.5    Wellhöner, H.6
  • 143
    • 0037152154 scopus 로고    scopus 로고
    • Intracellular delivery of monoclonal antibodies
    • Chen BX, Erlanger BF. Intracellular delivery of monoclonal antibodies. Immunol Lett 2002; 84:63-7.
    • (2002) Immunol Lett , vol.84 , pp. 63-67
    • Chen, B.X.1    Erlanger, B.F.2
  • 144
    • 0242551445 scopus 로고    scopus 로고
    • MTS-conjugated-antiactive caspase 3 antibodies inhibit actinomycin D-induced apoptosis
    • DOI 10.1023/A:1026139627930
    • Zhao Y, Brown TL, Kohler H, Muller S. MTS-conjugated-antiactive caspase 3 antibodies inhibit actinomycin D-induced apoptosis. Apoptosis 2003; 8:631-7. (Pubitemid 37411747)
    • (2003) Apoptosis , vol.8 , Issue.6 , pp. 631-637
    • Zhao, Y.1    Brown, T.L.2    Kohler, H.3    Muller, S.4
  • 145
    • 0141816702 scopus 로고    scopus 로고
    • A novel strategy using single-chain antibody to show the importance of Bcl-2 in mast cell survival
    • Cohen-Saidon C, Nechushtan H, Kahlon S, Livni N, Nissim A, Razin E. A novel strategy using single-chain antibody to show the importance of Bcl-2 in mast cell survival. Blood 2003; 102:2506-12.
    • (2003) Blood , vol.102 , pp. 2506-2512
    • Cohen-Saidon, C.1    Nechushtan, H.2    Kahlon, S.3    Livni, N.4    Nissim, A.5    Razin, E.6
  • 147
    • 1542319211 scopus 로고    scopus 로고
    • Site of Docking and Fusion of Insulin Secretory Granules in Live MIN6 beta Cells Analyzed by TAT-conjugated Anti-syntaxin 1 Antibody and Total Internal Reflection Fluorescence Microscopy
    • DOI 10.1074/jbc.M308954200
    • Ohara-Imaizumi M, Nishiwaki C, Kikuta T, Kumakura K, Nakamichi Y, Nagamatsu S. Site of docking and fusion of insulin secretory granules in live MIN6 beta cells analyzed by TAT-conjugated anti-syntaxin 1 antibody and total internal reflection fluorescence microscopy. J Biol Chem 2004; 279:8403-8. (Pubitemid 38294733)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 8403-8408
    • Ohara-Imaizumi, M.1    Nishiwaki, C.2    Kikuta, T.3    Kumakura, K.4    Nakamichi, Y.5    Nagamatsu, S.6
  • 148
    • 16844381988 scopus 로고    scopus 로고
    • Proapoptotic activity of cell-permeable anti-Akt single-chain antibodies
    • DOI 10.1158/0008-5472.CAN-04-2898
    • Shin I, Edl J, Biswas S, Lin PC, Mernaugh R, Arteaga CL. Proapoptotic activity of cell-permeable anti-Akt single-chain antibodies. Cancer Res 2005; 65:2815-24. (Pubitemid 40490084)
    • (2005) Cancer Research , vol.65 , Issue.7 , pp. 2815-2824
    • Shin, I.1    Edl, J.2    Biswas, S.3    Lin, P.C.4    Mernaugh, R.5    Arteaga, C.L.6
  • 150
    • 33646383091 scopus 로고    scopus 로고
    • Distribution of immunoglobulin Fab fragment conjugated with HIV-1 REV peptide following intravenous administration in rats
    • DOI 10.1021/mp050064m
    • Kameyama S, Okada R, Kikuchi T, Omura T, Nakase I, Takeuchi T, et al. Distribution of immunoglobulin Fab fragment conjugated with HIV-1 REV peptide following intravenous administration in rats. Mol Pharm 2006; 3:174-80. (Pubitemid 43672253)
    • (2006) Molecular Pharmaceutics , vol.3 , Issue.2 , pp. 174-180
    • Kameyama, S.1    Okada, R.2    Kikuchi, T.3    Omura, T.4    Nakase, I.5    Takeuchi, T.6    Sugiura, Y.7    Futaki, S.8
  • 151
    • 33749243325 scopus 로고    scopus 로고
    • Cell cycle inhibition by an anti-cyclin D1 antibody chemically modified for intracellular delivery
    • Chen BC, Erlanger BF. Cell cycle inhibition by an anti-cyclin D1 antibody chemically modified for intracellular delivery. Cancer Lett 2006; 244:71-5.
    • (2006) Cancer Lett , vol.244 , pp. 71-75
    • Chen, B.C.1    Erlanger, B.F.2
  • 152
    • 33645055376 scopus 로고    scopus 로고
    • Targeting of HIV-1 Tat traffic and function by transduction-competent single chain antibodies
    • Theisen DM, Pongratz C, Wiegmann K, Rivero F, Krut O, Kronke M. Targeting of HIV-1 Tat traffic and function by transduction-competent single chain antibodies. Vaccine 2006; 24:3127-36.
    • (2006) Vaccine , vol.24 , pp. 3127-3136
    • Theisen, D.M.1    Pongratz, C.2    Wiegmann, K.3    Rivero, F.4    Krut, O.5    Kronke, M.6
  • 153
    • 34247481907 scopus 로고    scopus 로고
    • Acid wash in determining cellular uptake of Fab/cell-permeating peptide conjugates
    • Kameyama S, Horie M, Kikuchi T, Omura T, Tadokoro A, Takeuchi T, et al. Acid wash in determining cellular uptake of Fab/cell-permeating peptide conjugates. Biopolymers 2007; 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
  • 154
    • 33847105943 scopus 로고    scopus 로고
    • 123I-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)
    • 123I-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 2007; 34:368-77.
    • (2007) 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
  • 155
    • 42049097657 scopus 로고    scopus 로고
    • Internalization via Antennapedia protein transduction domain of an scFv antibody toward c-Myc protein
    • Avignolo C, Bagnasco L, Biasotti B, Melchiori A, Tomati V, Bauer I, et al. Internalization via Antennapedia protein transduction domain of an scFv antibody toward c-Myc protein. FASEB J 2008; 22:1237-45.
    • (2008) FASEB J , vol.22 , pp. 1237-1245
    • Avignolo, C.1    Bagnasco, L.2    Biasotti, B.3    Melchiori, A.4    Tomati, V.5    Bauer, I.6
  • 156
    • 77954885702 scopus 로고    scopus 로고
    • A human single chain transbody specific to matrix protein (M1) interferes with the replication of influenza A virus
    • Poungpair O, Pootong A, Maneewatch S, Srimanote P, Tongtawe P, Songserm T, et al. A human single chain transbody specific to matrix protein (M1) interferes with the replication of influenza A virus. Bioconjug Chem 2010; 21:1134-41.
    • (2010) Bioconjug Chem , vol.21 , pp. 1134-1141
    • Poungpair, O.1    Pootong, A.2    Maneewatch, S.3    Srimanote, P.4    Tongtawe, P.5    Songserm, T.6
  • 157
  • 158
    • 58149187809 scopus 로고    scopus 로고
    • Secretion and uptake of TAT-fusion proteins produced by engineered mammalian cells
    • Koutsokeras A, Kabouridis PS. Secretion and uptake of TAT-fusion proteins produced by engineered mammalian cells. Biochim Biophys Acta 2009; 1790:147-53.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 147-153
    • Koutsokeras, A.1    Kabouridis, P.S.2
  • 159
    • 38549110556 scopus 로고    scopus 로고
    • Comparison of protein transduction domains in mediating cell delivery of a secreted CRE protein
    • Shaw PA, Catchpole IR, Goddard CA, Colledge WH. Comparison of protein transduction domains in mediating cell delivery of a secreted CRE protein. Biochemistry 2008; 47:1157-66.
    • (2008) Biochemistry , vol.47 , pp. 1157-1166
    • Shaw, P.A.1    Catchpole, I.R.2    Goddard, C.A.3    Colledge, W.H.4
  • 160
    • 33846591495 scopus 로고    scopus 로고
    • The taming of the cell penetrating domain of the HIV Tat: Myths and realities
    • DOI 10.1016/j.jconrel.2006.10.031, PII S0168365906006146
    • Chauhan A, Tikoo A, Kapur AK, Singh M. The taming of the cell penetrating domain of the HIV Tat: myths and realities. J Control Release 2007; 117:148-62. (Pubitemid 46172502)
    • (2007) Journal of Controlled Release , vol.117 , Issue.2 , pp. 148-162
    • Chauhan, A.1    Tikoo, A.2    Kapur, A.K.3    Singh, M.4
  • 161
    • 0030725756 scopus 로고    scopus 로고
    • Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins
    • Nakayama K. Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem J 1997; 327:625-35.
    • (1997) Biochem J , vol.327 , pp. 625-635
    • Nakayama, K.1
  • 164
    • 0035836609 scopus 로고    scopus 로고
    • Ability of the Tat basic domain and VP22 to mediate cell binding, but not membrane translocation of the diphtheria toxin A-fragment
    • Falnes PO, Wesche J, Olsnes S. Ability of the Tat basic domain and VP22 to mediate cell binding, but not membrane translocation of the diphtheria toxin A-fragment. Biochemistry 2001; 40:4349-58.
    • (2001) Biochemistry , vol.40 , pp. 4349-4358
    • Falnes, P.O.1    Wesche, J.2    Olsnes, S.3
  • 165
    • 0029550235 scopus 로고
    • Class I MHC presentation of exogenous soluble antigen via macropinocytosis in bone marrow macrophages
    • Norbury CC, Hewlett LJ, Prescott AR, Shastri N, Watts C. Class I MHC presentation of exogenous soluble antigen via macropinocytosis in bone marrow macrophages. Immunity 1995; 3:783-91.
    • (1995) Immunity , vol.3 , pp. 783-791
    • Norbury, C.C.1    Hewlett, L.J.2    Prescott, A.R.3    Shastri, N.4    Watts, C.5
  • 166
    • 0037119944 scopus 로고    scopus 로고
    • Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake
    • Meier O, Boucke K, Hammer SV, Keller S, Stidwill RP, Hemmi S, et al. Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake. J Cell Biol 2002; 158:1119-31.
    • (2002) J Cell Biol , vol.158 , pp. 1119-1131
    • Meier, O.1    Boucke, K.2    Hammer, S.V.3    Keller, S.4    Stidwill, R.P.5    Hemmi, S.6
  • 167
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia JS, Stan RV, Dowdy SF. Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat Med 2004; 10:310-5.
    • (2004) Nat Med , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 168
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cell-penetrating peptides: From molecular mechanisms to therapeutics
    • Heitz F, Morris MC, Divita G. Twenty years of cell-penetrating peptides: From molecular mechanisms to therapeutics. Br J Pharmacol 2009; 157:195-206.
    • (2009) Br J Pharmacol , vol.157 , pp. 195-206
    • Heitz, F.1    Morris, M.C.2    Divita, G.3
  • 170
    • 33746075548 scopus 로고    scopus 로고
    • Delivery of antibody-captured proteins into living cells using PTD-fused protein A
    • Mie M, Mori K, Funabashi H, Kobatake E. Delivery of antibody-captured proteins into living cells using PTD-fused protein A. Biotechnol Lett 2006; 28:1209-14.
    • (2006) Biotechnol Lett , vol.28 , pp. 1209-1214
    • Mie, M.1    Mori, K.2    Funabashi, H.3    Kobatake, E.4
  • 171
    • 18344381440 scopus 로고    scopus 로고
    • A TAT-streptavidin fusion protein directs uptake of biotinylated cargo into mammalian cells
    • Albarran B, To R, Stayton PS. A TAT-streptavidin fusion protein directs uptake of biotinylated cargo into mammalian cells. Protein Eng Des Sel 2005; 18:147-52.
    • (2005) Protein Eng des Sel , vol.18 , pp. 147-152
    • Albarran, B.1    To, R.2    Stayton, P.S.3
  • 172
    • 65549133368 scopus 로고    scopus 로고
    • Delivery of Macromolecules Using arginine-rich cell-penetrating peptides: Ways to overcome endosomal entrapment
    • El-Sayed A, Futaki S, Harashima H. Delivery of Macromolecules Using arginine-rich cell-penetrating peptides: Ways to overcome endosomal entrapment. AAPS J 2009; 11:13-22.
    • (2009) AAPS J , vol.11 , pp. 13-22
    • El-Sayed, A.1    Futaki, S.2    Harashima, H.3
  • 173
    • 0020352681 scopus 로고
    • Weak bases and ionophores rapidly and reversibly raise the pH of endocytic vesicles in cultured mouse fibroblasts
    • Maxfield FR. Weak bases and ionophores rapidly and reversibly raise the pH of endocytic vesicles in cultured mouse fibroblasts. J Cell Biol 1982; 95:676-81.
    • (1982) J Cell Biol , vol.95 , pp. 676-681
    • Maxfield, F.R.1
  • 174
    • 0029979929 scopus 로고    scopus 로고
    • Putative role of chloroquine in gene transfer into a human hepatoma cell line by DNA lactosylated polylysine complexes
    • Erbacher P, Roche AC, Monsigny M, Midoux P. Putative role of chloroquine in gene transfer into a human hepatoma cell line by DNA lactosylated polylysine complexes. Exp Cell Res 1996; 225:186-94.
    • (1996) Exp Cell Res , vol.225 , pp. 186-194
    • Erbacher, P.1    Roche, A.C.2    Monsigny, M.3    Midoux, P.4
  • 175
    • 0035821383 scopus 로고    scopus 로고
    • Enhanced plasmid DNA transfection with lysosomotropic agents in cultured fibroblasts
    • Ciftci K, Levy RJ. Enhanced plasmid DNA transfection with lysosomotropic agents in cultured fibroblasts. Int J Pharm 2001; 81-92.
    • (2001) Int J Pharm , pp. 81-92
    • Ciftci, K.1    Levy, R.J.2
  • 176
    • 2442670068 scopus 로고    scopus 로고
    • Endosome disruption enhances the functional nuclear delivery of Tat-fusion proteins
    • Caron NJ, Quenneville SP, Tremblay JP. Endosome disruption enhances the functional nuclear delivery of Tat-fusion proteins. Biochem Biophys Res Commun 2004; 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
  • 177
    • 77950521612 scopus 로고    scopus 로고
    • Enhancement of TAT cell membrane penetration efficiency by dimethyl sulphoxide
    • Wang H, Zhong CY, Wu JF, Huang YB, Liu CB. Enhancement of TAT cell membrane penetration efficiency by dimethyl sulphoxide. J Control Release 2010; 143:64-70.
    • (2010) J Control Release , vol.143 , pp. 64-70
    • Wang, H.1    Zhong, C.Y.2    Wu, J.F.3    Huang, Y.B.4    Liu, C.B.5
  • 179
    • 0033559618 scopus 로고    scopus 로고
    • Photochemical internalization: A novel technology for delivery of macromolecules into cytosol
    • Berg K, Selbo PK, Prasmickaite L, Tjelle TE, Sandvig K, Moan J, et al. Photochemical internalization: a novel technology for delivery of macromolecules into cytosol. Cancer Res 1999; 59:1180-3.
    • (1999) Cancer Res , vol.59 , pp. 1180-1183
    • Berg, K.1    Selbo, P.K.2    Prasmickaite, L.3    Tjelle, T.E.4    Sandvig, K.5    Moan, J.6
  • 180
    • 0005129736 scopus 로고
    • Interaction of influenza virus hemagglutinin with target membrane lipids is a key step in virus-induced hemolysis and fusion at pH 5.2
    • Maeda T, Kawasaki K, Ohnishi S. Interaction of influenza virus hemagglutinin with target membrane lipids is a key step in virus-induced hemolysis and fusion at pH 5.2. Proc Natl Acad Sci USA 1981; 78:4133-7.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 4133-4137
    • Maeda, T.1    Kawasaki, K.2    Ohnishi, S.3
  • 181
    • 0028023726 scopus 로고
    • Structure of influenza hemagglutinin at the Ph of membrane-fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC. Structure of influenza hemagglutinin at the Ph of membrane-fusion. Nature 1994; 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 182
    • 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
    • Michiue H, Tomizawa K, Wei FY, Matsushita M, Lu YF, Ichikawa T, et al. The NH2 terminus of influenza virus hemagglutinin-2 subunit peptides enhances the antitumor potency of polyarginine-mediated p53 protein transduction. J Biol Chem 2005; 280:8285-9.
    • (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
  • 183
    • 40649085520 scopus 로고    scopus 로고
    • An endosomolytic Tat peptide produced by incorporation of histidine and cysteine residues as a nonviral vector for DNA transfection
    • Lo SL, Wang S. An endosomolytic Tat peptide produced by incorporation of histidine and cysteine residues as a nonviral vector for DNA transfection. Biomaterials 2008; 29:2408-14.
    • (2008) Biomaterials , vol.29 , pp. 2408-2414
    • Lo, S.L.1    Wang, S.2
  • 184
    • 0346460957 scopus 로고    scopus 로고
    • Cell-penetrating peptides. A reevaluation of the mechanism of cellular uptake
    • Richard JP, Melikov K, Vives E, Ramos C, Verbeure B, Gait MJ, et al. Cell-penetrating peptides. A reevaluation of the mechanism of cellular uptake. J Biol Chem 2003; 278:585-90.
    • (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
  • 185
    • 34848892144 scopus 로고    scopus 로고
    • Cell penetrating peptides: Intracellular pathways and pharmaceutical perspectives
    • Patel LN, Zaro JL, Shen WC. Cell penetrating peptides: Intracellular pathways and pharmaceutical perspectives. Pharm Res 2007; 24:1977-92.
    • (2007) Pharm Res , vol.24 , pp. 1977-1992
    • Patel, L.N.1    Zaro, J.L.2    Shen, W.C.3
  • 186
    • 0042232110 scopus 로고    scopus 로고
    • Studies on the internalization mechanism of cationic cell-penetrating peptides
    • Drin G, Cottin S, Blanc E, Rees AR, Temsamani J. Studies on the internalization mechanism of cationic cell-penetrating peptides. J Biol Chem 2003; 278:31192-201.
    • (2003) J Biol Chem , vol.278 , pp. 31192-31201
    • Drin, G.1    Cottin, S.2    Blanc, E.3    Rees, A.R.4    Temsamani, J.5
  • 187
    • 67349211781 scopus 로고    scopus 로고
    • A novel method for monitoring the cytosolic delivery of peptide cargo
    • Cheung JC, Kim Chiaw P, Deber CM, Bear CE. A novel method for monitoring the cytosolic delivery of peptide cargo. J Control Release 2009; 137:2-7.
    • (2009) J Control Release , vol.137 , pp. 2-7
    • Cheung, J.C.1    Kim Chiaw, P.2    Deber, C.M.3    Bear, C.E.4
  • 188
    • 0021741835 scopus 로고
    • Biological approaches to the controlled delivery of drugs: A critical review
    • Poznansky MJ, Juliano RL. Biological approaches to the controlled delivery of drugs: A critical review. Pharmacol Rev 1984; 36:277-336.
    • (1984) Pharmacol Rev , vol.36 , pp. 277-336
    • Poznansky, M.J.1    Juliano, R.L.2
  • 189
    • 70349456654 scopus 로고    scopus 로고
    • Recent advances in the use of cell-penetrating peptides for medical and biological applications
    • Fonseca SB, Pereira MP, Kelley SO. Recent advances in the use of cell-penetrating peptides for medical and biological applications. Adv Drug Deliv Rev 2009; 61:953-64.
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 953-964
    • Fonseca, S.B.1    Pereira, M.P.2    Kelley, S.O.3
  • 190
    • 67649086303 scopus 로고    scopus 로고
    • TAT-based drug delivery system - New directions in protein delivery for new hopes?
    • Rapoport M, Lorberboum-Galski H. TAT-based drug delivery system - new directions in protein delivery for new hopes? Expert Opin Drug Deliv 2009; 6:453-63.
    • (2009) Expert Opin Drug Deliv , vol.6 , pp. 453-463
    • Rapoport, M.1    Lorberboum-Galski, H.2
  • 191
    • 24344448619 scopus 로고    scopus 로고
    • Cationic cell-penetrating peptides interfere with TNF signalling by induction of TNF receptor internalization
    • Fotin-Mleczek M, Welte S, Mader O, Duchardt F, Fischer R, Hufnagel H, et al. Cationic cell-penetrating peptides interfere with TNF signalling by induction of TNF receptor internalization. J Cell Sci 2005; 118:3339-51.
    • (2005) J Cell Sci , vol.118 , pp. 3339-3351
    • Fotin-Mleczek, M.1    Welte, S.2    Mader, O.3    Duchardt, F.4    Fischer, R.5    Hufnagel, H.6
  • 192
    • 33745157927 scopus 로고    scopus 로고
    • In vitro and in vivo nuclear factorkappaB inhibitory effects of the cell-penetrating penetratin peptide
    • Letoha T, Kusz E, Papai G, Szabolcs A, Kaszaki J, Varga I, et al. In vitro and in vivo nuclear factorkappaB inhibitory effects of the cell-penetrating penetratin peptide. Mol Pharmacol 2006; 69:2027-36.
    • (2006) Mol Pharmacol , vol.69 , pp. 2027-2036
    • Letoha, T.1    Kusz, E.2    Papai, G.3    Szabolcs, A.4    Kaszaki, J.5    Varga, I.6
  • 194
    • 58149099412 scopus 로고    scopus 로고
    • Comparison of cellular uptake using 22 CPPs in 4 different cell lines
    • Mueller J, Kretzschmar I, Volkmer R, Boisguerin P. Comparison of cellular uptake using 22 CPPs in 4 different cell lines. Bioconjug Chem 2008; 19:2363-74.
    • (2008) Bioconjug Chem , vol.19 , pp. 2363-2374
    • Mueller, J.1    Kretzschmar, I.2    Volkmer, R.3    Boisguerin, P.4
  • 198
    • 0035824862 scopus 로고    scopus 로고
    • Refined crystallographic structure of Pseudomonas aeruginosa exotoxin A and its implications for the molecular mechanism of toxicity
    • Wedekind JE, Trame CB, Dorywalska M, Koehl P, Raschke TM, McKee M, et al. Refined crystallographic structure of Pseudomonas aeruginosa exotoxin A and its implications for the molecular mechanism of toxicity. J Mol Biol 2001; 314:823-37.
    • (2001) J Mol Biol , vol.314 , pp. 823-837
    • Wedekind, J.E.1    Trame, C.B.2    Dorywalska, M.3    Koehl, P.4    Raschke, T.M.5    McKee, M.6
  • 199
    • 34548283134 scopus 로고    scopus 로고
    • Concerted protonation of key histidines triggers membrane interaction of the diphtheria toxin T domain
    • Perier A, Chassaing A, Raffestin S, Pichard S, Masella M, Menez A, et al. Concerted protonation of key histidines triggers membrane interaction of the diphtheria toxin T domain. J Biol Chem 2007; 282:24239-45.
    • (2007) J Biol Chem , vol.282 , pp. 24239-24245
    • Perier, A.1    Chassaing, A.2    Raffestin, S.3    Pichard, S.4    Masella, M.5    Menez, A.6
  • 200
    • 4344610200 scopus 로고    scopus 로고
    • Cytotoxic ribosome-inactivating lectins from plants
    • Hartley MR, Lord JM. Cytotoxic ribosome-inactivating lectins from plants. Biochim Biophys Acta 2004; 1701:1-14.
    • (2004) Biochim Biophys Acta , vol.1701 , pp. 1-14
    • Hartley, M.R.1    Lord, J.M.2
  • 201
    • 0035954402 scopus 로고    scopus 로고
    • Preparation of potent cytotoxic ribonucleases by cationization: Enhanced cellular uptake and decreased interaction with ribonuclease inhibitor by chemical modification of carboxyl groups
    • Futami J, Maeda T, Kitazoe M, Nukui E, Tada H, Seno M, et al. Preparation of potent cytotoxic ribonucleases by cationization: Enhanced cellular uptake and decreased interaction with ribonuclease inhibitor by chemical modification of carboxyl groups. Biochemistry 2001; 40:7518-24.
    • (2001) Biochemistry , vol.40 , pp. 7518-7524
    • Futami, J.1    Maeda, T.2    Kitazoe, M.3    Nukui, E.4    Tada, H.5    Seno, M.6
  • 202
    • 34249093093 scopus 로고    scopus 로고
    • Intracellular pathway of Onconase that enables its delivery to the cytosol
    • Rodriguez M, Torrent G, Bosch M, Rayne F, Dubremetz JF, Ribo M, et al. Intracellular pathway of Onconase that enables its delivery to the cytosol. J Cell Sci 2007; 120:1405-11.
    • (2007) J Cell Sci , vol.120 , pp. 1405-1411
    • Rodriguez, M.1    Torrent, G.2    Bosch, M.3    Rayne, F.4    Dubremetz, J.F.5    Ribo, M.6
  • 203
    • 0021194783 scopus 로고
    • Kinetics of cytotoxicity induced by immunotoxins. Enhancement by lysosomotropic amines and carboxylic ionophores
    • Casellas P, Bourrie BJ, Gros P, Jansen FK. Kinetics of cytotoxicity induced by immunotoxins. Enhancement by lysosomotropic amines and carboxylic ionophores. J Biol Chem 1984; 259:9359-64.
    • (1984) J Biol Chem , vol.259 , pp. 9359-9364
    • Casellas, P.1    Bourrie, B.J.2    Gros, P.3    Jansen, F.K.4
  • 204
    • 23744432460 scopus 로고    scopus 로고
    • Combined application of saponin and chimeric toxins drastically enhances the targeted cytotoxicity on tumor cells
    • Heisler I, Sutherland M, Bachran C, Hebestreit P, Schnitger A, Melzig MF, et al. Combined application of saponin and chimeric toxins drastically enhances the targeted cytotoxicity on tumor cells. J Control Release 2005; 106:123-37.
    • (2005) J Control Release , vol.106 , pp. 123-137
    • Heisler, I.1    Sutherland, M.2    Bachran, C.3    Hebestreit, P.4    Schnitger, A.5    Melzig, M.F.6
  • 205
    • 33645224029 scopus 로고    scopus 로고
    • The saponin-mediated enhanced uptake of targeted saporin-based drugs is strongly dependent on the saponin structure
    • Bachran C, Sutherland M, Heisler I, Hebestreit P, Melzig MF, Fuchs H. The saponin-mediated enhanced uptake of targeted saporin-based drugs is strongly dependent on the saponin structure. Exp Biol Med 2006; 231:412-20.
    • (2006) Exp Biol Med , vol.231 , pp. 412-420
    • Bachran, C.1    Sutherland, M.2    Heisler, I.3    Hebestreit, P.4    Melzig, M.F.5    Fuchs, H.6
  • 207
    • 33846865554 scopus 로고    scopus 로고
    • A cleavable molecular adapter reduces side effects and concomitantly enhances efficacy in tumor treatment by targeted toxins in mice
    • Fuchs H, Bachran C, Li T, Heisler I, Dürkop H, Sutherland M. A cleavable molecular adapter reduces side effects and concomitantly enhances efficacy in tumor treatment by targeted toxins in mice. J Control Release 2007; 117:342-50.
    • (2007) J Control Release , vol.117 , pp. 342-350
    • Fuchs, H.1    Bachran, C.2    Li, T.3    Heisler, I.4    Dürkop, H.5    Sutherland, M.6
  • 208
    • 42649116104 scopus 로고    scopus 로고
    • Small cleavable adapters enhance the specific cytotoxicity of a humanized immunotoxin directed against CD64-positive cells
    • Hetzel C, Bachran C, Fischer R, Fuchs H, Barth S, Stöcker M. Small cleavable adapters enhance the specific cytotoxicity of a humanized immunotoxin directed against CD64-positive cells. J Immunother 2008; 3:370-6.
    • (2008) J Immunother , vol.3 , pp. 370-376
    • Hetzel, C.1    Bachran, C.2    Fischer, R.3    Fuchs, H.4    Barth, S.5    Stöcker, M.6
  • 209
    • 67650457494 scopus 로고    scopus 로고
    • An engineered substance P variant for receptor-mediated delivery of synthetic antibodies into tumor cells
    • Rizk SS, Luchniak A, Uysal S, Brawley CM, Rock RS, Kossiakoff AA. An engineered substance P variant for receptor-mediated delivery of synthetic antibodies into tumor cells. Proc Natl Acad Sci USA 2009; 106:11011-5.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11011-11015
    • Rizk, S.S.1    Luchniak, A.2    Uysal, S.3    Brawley, C.M.4    Rock, R.S.5    Kossiakoff, A.A.6


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