메뉴 건너뛰기




Volumn 9, Issue 9, 2004, Pages 395-402

The use of cell-penetrating peptides as a tool for gene regulation

Author keywords

Biochemistry; Cell penetrating peptides; Cellular delivery; Chemical Biology; Drug Discovery; Gene regulation; Membrane translocation; Pharmaceutical Science; Transport

Indexed keywords

ADENOVIRUS VECTOR; ALANYLGLYCYLLYSYLLEUCYLLEUCYLGLYCYLLYSYLISOLEUCYLASPARAGINYLLEUCYLLYSYLA LAN YLLEUCYLALANYLALANYLLEUCYLALANYLLYSYLLYSYLISOLEUCYLLEUCINAMIDE; ANTISENSE OLIGONUCLEOTIDE; ARGINYLARGINYLARGINYLARGINYLARGINYLARGINYLARGININE; ARGINYLGLUTAMINYLISOLEUCYLLYSYLISOLEUCYLTRYPTOPHYLPHENYLALANYLGLUTAMINYL ASP ARAGINYLARGINYLARGINYLMETHIONYLLYSYLTRYPTOPHYLLYSYLLYSINE; CARRIER PROTEIN; CRE RECOMBINASE; DRUG CARRIER; GLYCYLALANYLLEUCYLPHENYLALANYLLEUCYLGLYCYLTRYPTOPHYLLEUCYLGLYCYLALANYLAL ANY LGLYCYLSERYLTHREONYLMETHIONYLGLYCYLALANYLPROLYLLYSYLLYSYLLYSYLARGINYLLYSYLVALINA MIDE; GLYCYLARGINYLLYSYLLYSYLARGINYLARGINYLGLUTAMINYLARGINYLARGINYLARGINYLPROL YLP ROLYLGLUTAMINE; LEUCYLLEUCYLISOLEUCYLISOLEUCYLLEUCYLARGINYLARGINYLISOLEUCYLARGINYLLYSYLG LUT AMINYLALANYLHISTIDYLALANYLHISTIDYLSERYLLYSINAMIDE; LYSYLLEUCYLALANYLLEUCYLLYSYLLEUCYLALANYLLEUCYLLYSYLALANYLLEUCYLLYSYLALAN YLA LANYLLEUCYLLYSYLLEUCYLALANINAMIDE; MYC PROTEIN; NEUROPROTECTIVE AGENT; PEPTIDE NUCLEIC ACID; POLYCATION; POLYETHYLENEIMINE; PROLYLLYSYLLYSYLLYSYLARGINYLLYSYLVALINE; STRESS ACTIVATED PROTEIN KINASE; SYNTHETIC PEPTIDE; THREONYLARGINYLSERYLSERYLARGINYLALANYLGLYCYLLEUCYLGLUTAMINYLPHENYLALANYL PRO LYLVALYLGLYCYLARGINYLVALYLHISTIDYLARGINYLLEUCYLLEUCYLARGINYLLYSINE; TRYPTOPHYLGLUTAMYLALANYLLYSYLLEUCYLALANYLLYSYLALANYLLEUCYLALANYLLEUCYLAL ANY LLEUCYLALANYLLYSYLHISTIDYLLEUCYLALANYLLYSYLALANYLLEUCYLALANYLLYSYLALANYLLEUCYLLY SYLALANYLCYSTEINYLGLUTAMYLGLUTAMYLALANINE; TYROSYLALANYLARGINYLALANYLALANYLALANYLARGINYLGLUTAMYLALANYLARGINYLALANIN E; UNCLASSIFIED DRUG; VIRUS VECTOR;

EID: 11144356131     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6446(04)03042-9     Document Type: Review
Times cited : (171)

References (68)
  • 1
    • 0003008343 scopus 로고    scopus 로고
    • Synthetic DNA delivery systems
    • Luo D., Saltzman W.M. Synthetic DNA delivery systems. Nat. Biotechnol. 18:2000;33-37.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 33-37
    • Luo, D.1    Saltzman, W.M.2
  • 3
    • 0038387344 scopus 로고    scopus 로고
    • TAT peptide internalization: Seeking the mechanism of entry
    • Vivés E., et al. TAT peptide internalization: seeking the mechanism of entry. Curr. Protein Pept. Sci. 4:2003;125-132.
    • (2003) Curr. Protein Pept. Sci. , vol.4 , pp. 125-132
    • Vivés, E.1
  • 4
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi D., et al. The third helix of the Antennapedia homeodomain translocates through biological membranes. J. Biol. Chem. 269:1994;10444-10450.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10444-10450
    • Derossi, D.1
  • 5
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • Vivés E., et al. A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 272:1997;16010-16017.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16010-16017
    • Vivés, E.1
  • 6
    • 2642680830 scopus 로고    scopus 로고
    • Cell penetration by transportan
    • Pooga M., et al. Cell penetration by transportan. FASEB J. 12:1998;67-77.
    • (1998) FASEB J. , vol.12 , pp. 67-77
    • Pooga, M.1
  • 7
    • 0042232110 scopus 로고    scopus 로고
    • Studies on the internalization mechanism of cationic cell-penetrating peptides
    • Drin G., et al. Studies on the internalization mechanism of cationic cell-penetrating peptides. J. Biol. Chem. 278:2003;31192-31201.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31192-31201
    • Drin, G.1
  • 8
    • 1842529513 scopus 로고    scopus 로고
    • A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides
    • [Epub ahead of print;
    • Fischer, R. et al. (2004) A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides. J. Biol. Chem. [Epub ahead of print; http://www.jbc.org/cgi/reprint/M311461200v2 ].
    • (2004) J. Biol. Chem.
    • Fischer, R.1
  • 9
    • 0029131395 scopus 로고
    • The retro-inverso form of a homeobox-derived short peptide is rapidly internalised by cultured neurones: A new basis for an efficient intracellular delivery system
    • Brugidou J., et al. The retro-inverso form of a homeobox-derived short peptide is rapidly internalised by cultured neurones: a new basis for an efficient intracellular delivery system. Biochem. Biophys. Res. Commun. 214:1995;685-693.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 685-693
    • Brugidou, J.1
  • 10
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters
    • Wender P.A., et al. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. Proc. Natl. Acad. Sci. U. S. A. 97:2000;13003-13008.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 13003-13008
    • Wender, P.A.1
  • 11
    • 0037169486 scopus 로고    scopus 로고
    • Possible existence of common internalization mechanisms among arginine-rich peptides
    • Suzuki T., et al. Possible existence of common internalization mechanisms among arginine-rich peptides. J. Biol. Chem. 277:2002;2437-2443.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2437-2443
    • Suzuki, T.1
  • 12
    • 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., et al. Antennapedia and HIV transactivator of transcription (TAT) 'protein transduction domains' promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans. J. Biol. Chem. 278:2003;35109-35114.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35109-35114
    • Console, S.1
  • 13
    • 0037206127 scopus 로고    scopus 로고
    • A quantitative validation of fluorophore-labelled cell-permeable peptide conjugates: Fluorophore and cargo dependence of import
    • Fischer R., et al. A quantitative validation of fluorophore-labelled cell-permeable peptide conjugates: fluorophore and cargo dependence of import. Biochim. Biophys. Acta. 1564:2002;365-374.
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 365-374
    • Fischer, R.1
  • 14
    • 0346460957 scopus 로고    scopus 로고
    • Cell-penetrating peptides. a reevaluation of the mechanism of cellular uptake
    • Richard J.P., et al. Cell-penetrating peptides. A reevaluation of the mechanism of cellular uptake. J. Biol. Chem. 278:2003;585-590.
    • (2003) J. Biol. Chem. , vol.278 , pp. 585-590
    • Richard, J.P.1
  • 15
    • 0032784061 scopus 로고    scopus 로고
    • Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis
    • Wang J., et al. Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis. Mol. Cell. Biol. 19:1999;6217-6228.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6217-6228
    • Wang, J.1
  • 16
    • 0034915150 scopus 로고    scopus 로고
    • The BH3 domain of BAD fused to the Antennapedia peptide induces apoptosis via its alpha helical structure and independent of Bcl-2
    • Schimmer A.D., et al. The BH3 domain of BAD fused to the Antennapedia peptide induces apoptosis via its alpha helical structure and independent of Bcl-2. Cell Death Differ. 8:2001;725-733.
    • (2001) Cell Death Differ. , vol.8 , pp. 725-733
    • Schimmer, A.D.1
  • 17
    • 17944392627 scopus 로고    scopus 로고
    • Inhibition of cancer cell growth and c-Myc transcriptional activity by a c-Myc helix 1-type peptide fused to an internalization sequence
    • Giorello L., et al. Inhibition of cancer cell growth and c-Myc transcriptional activity by a c-Myc helix 1-type peptide fused to an internalization sequence. Cancer Res. 58:1998;3654-3659.
    • (1998) Cancer Res. , vol.58 , pp. 3654-3659
    • Giorello, L.1
  • 18
    • 1842372659 scopus 로고    scopus 로고
    • Polo-like kinase, a novel marker for cellular proliferation
    • Yuan J., et al. Polo-like kinase, a novel marker for cellular proliferation. Am. J. Pathol. 150:1997;1165-1172.
    • (1997) Am. J. Pathol. , vol.150 , pp. 1165-1172
    • Yuan, J.1
  • 19
    • 0036682358 scopus 로고    scopus 로고
    • Efficient internalization of the polo-box of polo-like kinase 1 fused to an Antennapedia peptide results in inhibition of cancer cell proliferation
    • Yuan J., et al. Efficient internalization of the polo-box of polo-like kinase 1 fused to an Antennapedia peptide results in inhibition of cancer cell proliferation. Cancer Res. 62:2002;4186-4190.
    • (2002) Cancer Res. , vol.62 , pp. 4186-4190
    • Yuan, J.1
  • 20
    • 0141724805 scopus 로고    scopus 로고
    • A peptide inhibitor of c-Jun N-terminal kinase protects against excitotoxicity and cerebral ischemia
    • Borsello T., et al. A peptide inhibitor of c-Jun N-terminal kinase protects against excitotoxicity and cerebral ischemia. Nat. Med. 9:2003;1180-1186.
    • (2003) Nat. Med. , vol.9 , pp. 1180-1186
    • Borsello, T.1
  • 21
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman J.E. Mechanisms of intracellular protein transport. Nature. 372:1994;55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 22
    • 0028054797 scopus 로고
    • Tat-mediated delivery of heterologous proteins into cells
    • Fawell S., et al. Tat-mediated delivery of heterologous proteins into cells. Proc. Natl. Acad. Sci. U. S. A. 91:1994;664-668.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 664-668
    • Fawell, S.1
  • 23
    • 0034059140 scopus 로고    scopus 로고
    • Cre recombinase: The universal reagent for genome tailoring
    • Nagy A. Cre recombinase: the universal reagent for genome tailoring. Genesis. 26:2000;99-109.
    • (2000) Genesis , vol.26 , pp. 99-109
    • Nagy, A.1
  • 24
    • 0029155706 scopus 로고
    • Inducible gene targeting in mice
    • Kuhn R., et al. Inducible gene targeting in mice. Science. 269:1995;1427-1429.
    • (1995) Science , vol.269 , pp. 1427-1429
    • Kuhn, R.1
  • 25
    • 0028675511 scopus 로고
    • Cre-loxP-mediated gene replacement: A mouse strain producing humanized antibodies
    • Zou Y.R., et al. Cre-loxP-mediated gene replacement: a mouse strain producing humanized antibodies. Curr. Biol. 4:1994;1099-1103.
    • (1994) Curr. Biol. , vol.4 , pp. 1099-1103
    • Zou, Y.R.1
  • 26
    • 0025360095 scopus 로고
    • Targeted insertion of exogenous DNA into the eukaryotic genome by the Cre recombinase
    • Sauer B., Henderson N. Targeted insertion of exogenous DNA into the eukaryotic genome by the Cre recombinase. New Biol. 2:1990;441-449.
    • (1990) New Biol. , vol.2 , pp. 441-449
    • Sauer, B.1    Henderson, N.2
  • 27
    • 0026638820 scopus 로고
    • Targeted oncogene activation by site-specific recombination in transgenic mice
    • Lakso M., et al. Targeted oncogene activation by site-specific recombination in transgenic mice. Proc. Natl. Acad. Sci. U. S. A. 89:1992;6232-6236.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 6232-6236
    • Lakso, M.1
  • 28
    • 0037733977 scopus 로고    scopus 로고
    • Antisense technologies. Improvement through novel chemical modifications
    • Kurreck J. Antisense technologies. Improvement through novel chemical modifications. Eur. J. Biochem. 270:2003;1628-1644.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1628-1644
    • Kurreck, J.1
  • 29
    • 0030804766 scopus 로고    scopus 로고
    • A new peptide vector for efficient delivery of oligonucleotides into mammalian cells
    • Morris M.C., et al. A new peptide vector for efficient delivery of oligonucleotides into mammalian cells. Nucleic Acids Res. 25:1997;2730-2736.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2730-2736
    • Morris, M.C.1
  • 30
    • 0031754150 scopus 로고    scopus 로고
    • Cell penetrating PNA constructs regulate galanin receptor levels and modify pain transmission in vivo
    • Pooga M., et al. Cell penetrating PNA constructs regulate galanin receptor levels and modify pain transmission in vivo. Nat. Biotechnol. 16:1998;857-861.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 857-861
    • Pooga, M.1
  • 31
    • 0033799686 scopus 로고    scopus 로고
    • Preparation and applications of peptide-oligonucleotide conjugates
    • Tung C.H., Stein S. Preparation and applications of peptide- oligonucleotide conjugates. Bioconjug. Chem. 11:2000;605-618.
    • (2000) Bioconjug. Chem. , vol.11 , pp. 605-618
    • Tung, C.H.1    Stein, S.2
  • 32
    • 0035210628 scopus 로고    scopus 로고
    • Cellular delivery of impermeable effector molecules in the form of conjugates with peptides capable of mediating membrane translocation
    • Fischer P.M., et al. Cellular delivery of impermeable effector molecules in the form of conjugates with peptides capable of mediating membrane translocation. Bioconjug. Chem. 12:2001;825-841.
    • (2001) Bioconjug. Chem. , vol.12 , pp. 825-841
    • Fischer, P.M.1
  • 33
    • 0034061532 scopus 로고    scopus 로고
    • Effects in live cells of a c-myc anti-gene PNA linked to a nuclear localization signal
    • Cutrona G., et al. Effects in live cells of a c-myc anti-gene PNA linked to a nuclear localization signal. Nat. Biotechnol. 18:2000;300-303.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 300-303
    • Cutrona, G.1
  • 34
    • 0035575843 scopus 로고    scopus 로고
    • Cargo delivery kinetics of cell-penetrating peptides
    • Hällbrink M., et al. Cargo delivery kinetics of cell-penetrating peptides. Biochim. Biophys. Acta. 1515:2001;101-109.
    • (2001) Biochim. Biophys. Acta , vol.1515 , pp. 101-109
    • Hällbrink, M.1
  • 35
    • 0036859952 scopus 로고    scopus 로고
    • Radiometal-labeled peptide-PNA conjugates for targeting bcl-2 expression: Preparation, characterization, and in vitro mRNA binding
    • Lewis M.R., et al. Radiometal-labeled peptide-PNA conjugates for targeting bcl-2 expression: preparation, characterization, and in vitro mRNA binding. Bioconjug. Chem. 13:2002;1176-1180.
    • (2002) Bioconjug. Chem. , vol.13 , pp. 1176-1180
    • Lewis, M.R.1
  • 36
    • 0037592877 scopus 로고    scopus 로고
    • Insight into the mechanism of the peptide-based gene delivery system MPG: Implications for delivery of siRNA into mammalian cells
    • Simeoni F., et al. Insight into the mechanism of the peptide-based gene delivery system MPG: implications for delivery of siRNA into mammalian cells. Nucleic Acids Res. 31:2003;2717-2724.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2717-2724
    • Simeoni, F.1
  • 37
    • 0035135747 scopus 로고    scopus 로고
    • Viral vectors for gene therapy: The art of turning infectious agents into vehicles of therapeutics
    • Kay M.A., et al. Viral vectors for gene therapy: the art of turning infectious agents into vehicles of therapeutics. Nat. Med. 7:2001;33-40.
    • (2001) Nat. Med. , vol.7 , pp. 33-40
    • Kay, M.A.1
  • 38
    • 0037349932 scopus 로고    scopus 로고
    • Cell-permeable peptides improve cellular uptake and therapeutic gene delivery of replication-deficient viruses in cells and in vivo
    • Gratton J.P., et al. Cell-permeable peptides improve cellular uptake and therapeutic gene delivery of replication-deficient viruses in cells and in vivo. Nat. Med. 9:2003;357-362.
    • (2003) Nat. Med. , vol.9 , pp. 357-362
    • Gratton, J.P.1
  • 39
    • 0032859928 scopus 로고    scopus 로고
    • A peptide nucleic acid-nuclear localization signal fusion that mediates nuclear transport of DNA
    • Brandén L.J., et al. A peptide nucleic acid-nuclear localization signal fusion that mediates nuclear transport of DNA. Nat. Biotechnol. 17:1999;784-787.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 784-787
    • Brandén, L.J.1
  • 40
    • 0026806847 scopus 로고
    • A long synthetic peptide containing a nuclear localization signal and its flanking sequences of SV40 T-antigen directs the transport of IgM into the nucleus efficiently
    • Yoneda Y., et al. A long synthetic peptide containing a nuclear localization signal and its flanking sequences of SV40 T-antigen directs the transport of IgM into the nucleus efficiently. Exp. Cell Res. 201:1992;313-320.
    • (1992) Exp. Cell Res. , vol.201 , pp. 313-320
    • Yoneda, Y.1
  • 41
    • 0347926089 scopus 로고    scopus 로고
    • NLS bioconjugates for targeting therapeutic genes to the nucleus
    • Escriou V., et al. NLS bioconjugates for targeting therapeutic genes to the nucleus. Adv. Drug Deliv. Rev. 55:2003;295-306.
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 295-306
    • Escriou, V.1
  • 42
    • 0038176513 scopus 로고    scopus 로고
    • Oligomers of the arginine-rich motif of the HIV-1 TAT protein are capable of transferring plasmid DNA into cells
    • Rudolph C., et al. Oligomers of the arginine-rich motif of the HIV-1 TAT protein are capable of transferring plasmid DNA into cells. J. Biol. Chem. 278:2003;11411-11418.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11411-11418
    • Rudolph, C.1
  • 43
    • 0035210533 scopus 로고    scopus 로고
    • Stearylated arginine-rich peptides: A new class of transfection systems
    • Futaki S., et al. Stearylated arginine-rich peptides: a new class of transfection systems. Bioconjug. Chem. 12:2001;1005-1011.
    • (2001) Bioconjug. Chem. , vol.12 , pp. 1005-1011
    • Futaki, S.1
  • 44
    • 0036836978 scopus 로고    scopus 로고
    • Novel branching membrane translocational peptide as gene delivery vector
    • Tung C.H., et al. Novel branching membrane translocational peptide as gene delivery vector. Bioorg. Med. Chem. 10:2002;3609-3614.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3609-3614
    • Tung, C.H.1
  • 45
    • 0036169073 scopus 로고    scopus 로고
    • New basic membrane-destabilizing peptides for plasmid-based gene delivery in vitro and in vivo
    • Rittner K., et al. New basic membrane-destabilizing peptides for plasmid-based gene delivery in vitro and in vivo. Mol. Ther. 5:2002;104-114.
    • (2002) Mol. Ther. , vol.5 , pp. 104-114
    • Rittner, K.1
  • 46
    • 0042355298 scopus 로고    scopus 로고
    • Identification of a synovial fibroblast-specific protein transduction domain for delivery of apoptotic agents to hyperplastic synovium
    • Mi Z., et al. Identification of a synovial fibroblast-specific protein transduction domain for delivery of apoptotic agents to hyperplastic synovium. Mol. Ther. 8:2003;295-305.
    • (2003) Mol. Ther. , vol.8 , pp. 295-305
    • Mi, Z.1
  • 47
    • 0038726020 scopus 로고    scopus 로고
    • Uptake of analogs of penetratin, Tat(48-60) and oligoarginine in live cells
    • Thorén P.E., et al. Uptake of analogs of penetratin, Tat(48-60) and oligoarginine in live cells. Biochem. Biophys. Res. Commun. 307:2003;100-107.
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 100-107
    • Thorén, P.E.1
  • 48
    • 0037440187 scopus 로고    scopus 로고
    • Cellular uptake of Antennapedia Penetratin peptides is a two-step process in which phase transfer precedes a tryptophan-dependent translocation
    • Dom G., et al. Cellular uptake of Antennapedia Penetratin peptides is a two-step process in which phase transfer precedes a tryptophan-dependent translocation. Nucleic Acids Res. 31:2003;556-561.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 556-561
    • Dom, G.1
  • 49
    • 0036159271 scopus 로고    scopus 로고
    • Different mechanisms for cellular internalization of the HIV-1 Tat-derived cell penetrating peptide and recombinant proteins fused to tat
    • Silhol M., et al. Different mechanisms for cellular internalization of the HIV-1 Tat-derived cell penetrating peptide and recombinant proteins fused to tat. Eur. J. Biochem. 269:2002;494-501.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 494-501
    • Silhol, M.1
  • 50
    • 0032508926 scopus 로고    scopus 로고
    • Cellular uptake of an alpha-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically
    • Oehlke J., et al. Cellular uptake of an alpha-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically. Biochim. Biophys. Acta. 1414:1998;127-139.
    • (1998) Biochim. Biophys. Acta , vol.1414 , pp. 127-139
    • Oehlke, J.1
  • 51
    • 0034738525 scopus 로고    scopus 로고
    • Deletion analogues of transportan
    • Soomets U., et al. Deletion analogues of transportan. Biochim. Biophys. Acta. 1467:2000;165-176.
    • (2000) Biochim. Biophys. Acta , vol.1467 , pp. 165-176
    • Soomets, U.1
  • 52
    • 0033678653 scopus 로고    scopus 로고
    • Conjugation of arginine oligomers to cyclosporin a facilitates topical delivery and inhibition of inflammation
    • Rothbard J.B., et al. Conjugation of arginine oligomers to cyclosporin A facilitates topical delivery and inhibition of inflammation. Nat. Med. 6:2000;1253-1257.
    • (2000) Nat. Med. , vol.6 , pp. 1253-1257
    • Rothbard, J.B.1
  • 53
    • 0035478616 scopus 로고    scopus 로고
    • VE-cadherin-derived cell-penetrating peptide, pVEC, with carrier functions
    • Elmquist A., et al. VE-cadherin-derived cell-penetrating peptide, pVEC, with carrier functions. Exp. Cell Res. 269:2001;237-244.
    • (2001) Exp. Cell Res. , vol.269 , pp. 237-244
    • Elmquist, A.1
  • 54
    • 0030890748 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of a cationic peptide that binds to nucleic acids and permeabilizes bilayers
    • Wyman T.B., et al. Design, synthesis, and characterization of a cationic peptide that binds to nucleic acids and permeabilizes bilayers. Biochemistry. 36:1997;3008-3017.
    • (1997) Biochemistry , vol.36 , pp. 3008-3017
    • Wyman, T.B.1
  • 55
    • 0037428394 scopus 로고    scopus 로고
    • Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes
    • Takeshima K., et al. Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes. J. Biol. Chem. 278:2003;1310-1315.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1310-1315
    • Takeshima, K.1
  • 56
    • 0035940401 scopus 로고    scopus 로고
    • Peptides from the amino terminal mdm-2-binding domain of p53, designed from conformational analysis, are selectively cytotoxic to transformed cells
    • Kanovsky M., et al. Peptides from the amino terminal mdm-2-binding domain of p53, designed from conformational analysis, are selectively cytotoxic to transformed cells. Proc. Natl. Acad. Sci. U. S. A. 98:2001;12438-12443.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 12438-12443
    • Kanovsky, M.1
  • 57
    • 0033137321 scopus 로고    scopus 로고
    • Transduced p16INK4a peptides inhibit hypophosphorylation of the retinoblastoma protein and cell cycle progression prior to activation of Cdk2 complexes in late G1
    • Gius D.R., et al. Transduced p16INK4a peptides inhibit hypophosphorylation of the retinoblastoma protein and cell cycle progression prior to activation of Cdk2 complexes in late G1. Cancer Res. 59:1999;2577-2580.
    • (1999) Cancer Res. , vol.59 , pp. 2577-2580
    • Gius, D.R.1
  • 58
    • 0035839615 scopus 로고    scopus 로고
    • TAT fusion proteins containing tyrosine 42-deleted I(B( arrest osteoclastogenesis
    • Abu-Amer Y., et al. TAT fusion proteins containing tyrosine 42-deleted I(B( arrest osteoclastogenesis. J. Biol. Chem. 276:2001;30499-30503.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30499-30503
    • Abu-Amer, Y.1
  • 59
    • 0034948814 scopus 로고    scopus 로고
    • 1 cyclin-dependent kinase complexes in vivo
    • 1 cyclin-dependent kinase complexes in vivo. Mol. Cell. Biol. 21:2001;4773-4784.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4773-4784
    • Ezhevsky, S.A.1
  • 60
    • 0036531825 scopus 로고    scopus 로고
    • Antitumor effect of TAT-oxygen-dependent degradation-caspase-3 fusion protein specifically stabilized and activated in hypoxic tumor cells
    • Harada H., et al. Antitumor effect of TAT-oxygen-dependent degradation-caspase-3 fusion protein specifically stabilized and activated in hypoxic tumor cells. Cancer Res. 62:2002;2013-2018.
    • (2002) Cancer Res. , vol.62 , pp. 2013-2018
    • Harada, H.1
  • 61
    • 0034794191 scopus 로고    scopus 로고
    • Epigenetic regulation of gene structure and function with a cell-permeable Cre recombinase
    • Jo D., et al. Epigenetic regulation of gene structure and function with a cell-permeable Cre recombinase. Nat. Biotechnol. 19:2001;929-933.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 929-933
    • Jo, D.1
  • 62
    • 0034609864 scopus 로고    scopus 로고
    • A common E2F-1 and p73 pathway mediates cell death induced by TCR activation
    • Lissy N.A., et al. A common E2F-1 and p73 pathway mediates cell death induced by TCR activation. Nature. 407:2000;642-645.
    • (2000) Nature , vol.407 , pp. 642-645
    • Lissy, N.A.1
  • 63
    • 0034849664 scopus 로고    scopus 로고
    • 1 integrin: Unique and synergistic roles of the alpha(2) cytoplasmic domain
    • 1 integrin: unique and synergistic roles of the alpha(2) cytoplasmic domain. Am. J. Pathol. 159:2001;983-992.
    • (2001) Am. J. Pathol. , vol.159 , pp. 983-992
    • Klekotka, P.A.1
  • 64
    • 0036291286 scopus 로고    scopus 로고
    • Overexpression of protein-tyrosine phosphatase PTP sigma is linked to impaired glucose-induced insulin secretion in hereditary diabetic Goto-Kakizaki rats
    • Östenson C.G., et al. Overexpression of protein-tyrosine phosphatase PTP sigma is linked to impaired glucose-induced insulin secretion in hereditary diabetic Goto-Kakizaki rats. Biochem. Biophys. Res. Commun. 291:2002;945-950.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 945-950
    • Östenson, C.G.1
  • 65
    • 0034012647 scopus 로고    scopus 로고
    • Antisense inhibition of P-glycoprotein expression using peptide-oligonucleotide conjugates
    • Astriab-Fisher A., et al. Antisense inhibition of P-glycoprotein expression using peptide-oligonucleotide conjugates. Biochem. Pharmacol. 60:2000;83-90.
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 83-90
    • Astriab-Fisher, A.1
  • 66
    • 0037302448 scopus 로고    scopus 로고
    • HIV Tat peptide enhances cellular delivery of antisense morpholino oligomers
    • Moulton H.M., et al. HIV Tat peptide enhances cellular delivery of antisense morpholino oligomers. Antisense Nucleic Acid Drug Dev. 13:2003;31-43.
    • (2003) Antisense Nucleic Acid Drug Dev. , vol.13 , pp. 31-43
    • Moulton, H.M.1
  • 67
    • 0037122727 scopus 로고    scopus 로고
    • Designing peptide-based scaffolds as drug delivery vehicles
    • Brokx R.D., et al. Designing peptide-based scaffolds as drug delivery vehicles. J. Control. Release. 78:2002;115-123.
    • (2002) J. Control. Release , vol.78 , pp. 115-123
    • Brokx, R.D.1
  • 68
    • 0142149065 scopus 로고    scopus 로고
    • Complexes of plasmid DNA with basic domain 47-57 of the HIV-1 Tat protein are transferred to mammalian cells by endocytosis-mediated pathways
    • Ignatovich I.A., et al. Complexes of plasmid DNA with basic domain 47-57 of the HIV-1 Tat protein are transferred to mammalian cells by endocytosis-mediated pathways. J. Biol. Chem. 278:2003;42625-42636.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42625-42636
    • Ignatovich, I.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.