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Volumn 8, Issue 2, 2004, Pages 101-111

New transport peptides broaden the horizon of applications for peptidic pharmaceuticals

Author keywords

CPP; Erns; Protein transduction; PTD; Tat; Transport peptide

Indexed keywords

AMIDE; POLYPEPTIDE; RIBONUCLEASE;

EID: 3543039420     PISSN: 13811991     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:MODI.0000025653.26130.ce     Document Type: Article
Times cited : (22)

References (32)
  • 3
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • Derossi, D., Calvet, S., Trembleau, A., Brunissen, A., Chassaing, G. and Prochiantz, A., Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent, J. Biol. Chem., 271 (1996) 18188.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18188
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 4
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • Vives, E., Brodin, P. and Lebleu, B., 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
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 5
    • 0037085304 scopus 로고    scopus 로고
    • Translocation Activity of C-terminal Domain of Pestivirus Erns and Ribotoxin L3 Loop
    • Langedijk, J. P., Translocation Activity of C-terminal Domain of Pestivirus Erns and Ribotoxin L3 Loop, J. Biol. Chem., 277 (2002) 5308-5314.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5308-5314
    • Langedijk, J.P.1
  • 6
    • 0037119348 scopus 로고    scopus 로고
    • Efficiency of protein transduction is cell type-dependent and is enhanced by dextran sulfate
    • Mai, J. C., Shen, H. M., Watkins, S. C., Cheng, T. and Robbins, P. D., Efficiency of protein transduction is cell type-dependent and is enhanced by dextran sulfate, J. Biolog. Chem., 277 (2002) 30208-30218.
    • (2002) J. Biolog. Chem. , vol.277 , pp. 30208-30218
    • Mai, J.C.1    Shen, H.M.2    Watkins, S.C.3    Cheng, T.4    Robbins, P.D.5
  • 7
    • 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., 28 (2003) 145-151.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 145-151
    • Belting, M.1
  • 8
    • 0033948268 scopus 로고    scopus 로고
    • Messenger proteins: Homeoproteins, TAT and others
    • Prochiantz, A., Messenger proteins: Homeoproteins, TAT and others, Curr. Opinion Cell Biol., 12 (2000) 400-406.
    • (2000) Curr. Opinion Cell Biol. , vol.12 , pp. 400-406
    • Prochiantz, A.1
  • 9
    • 0034237577 scopus 로고    scopus 로고
    • Protein transduction: Unrestricted delivery into all cells?
    • Schwarze, S. R., Hruska, K. A. and Dowdy, S. F., Protein transduction: Unrestricted delivery into all cells?, Trends Cell Biol., 10 (2000) 290-295.
    • (2000) Trends Cell Biol. , vol.10 , pp. 290-295
    • Schwarze, S.R.1    Hruska, K.A.2    Dowdy, S.F.3
  • 11
    • 0036289650 scopus 로고    scopus 로고
    • Positively charged DNA-binding proteins cause apparent cell membrane translocation
    • Lundberg, M. and Johansson, M., Positively charged DNA-binding proteins cause apparent cell membrane translocation, Biochem. Biophys. Res. Commun., 291 (2002) 367-371.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 367-371
    • Lundberg, M.1    Johansson, M.2
  • 12
    • 0031024660 scopus 로고    scopus 로고
    • Analysis of bacteriophage N protein and peptide binding to boxB RNA using polyacrylamide gel coelectrophoresis (PACE)
    • Cilley, C. D. and Williamson, J. R., Analysis of bacteriophage N protein and peptide binding to boxB RNA using polyacrylamide gel coelectrophoresis (PACE), RNA, 3 (1997) 57-67.
    • (1997) RNA , vol.3 , pp. 57-67
    • Cilley, C.D.1    Williamson, J.R.2
  • 13
    • 0032798395 scopus 로고    scopus 로고
    • Identification of a linear heparin binding domain for human respiratory syncytial virus attachment glycoprotein G
    • Feldman, S. A., Hendry, R. M. and Beeler, J. A., Identification of a linear heparin binding domain for human respiratory syncytial virus attachment glycoprotein G, J. Virol., 73 (1999) 6610-6617.
    • (1999) J. Virol. , vol.73 , pp. 6610-6617
    • Feldman, S.A.1    Hendry, R.M.2    Beeler, J.A.3
  • 14
    • 0030973338 scopus 로고    scopus 로고
    • Heparin-dependent attachment of respiratory syncytial virus (RSV) to host cells
    • Krusat, T. and Streckert, H. J., Heparin-dependent attachment of respiratory syncytial virus (RSV) to host cells, Arch. Virol., 142 (1997) 1247-1254.
    • (1997) Arch. Virol. , vol.142 , pp. 1247-1254
    • Krusat, T.1    Streckert, H.J.2
  • 15
    • 0033598989 scopus 로고    scopus 로고
    • Transport of proteins and RNAs in and out of the nucleus
    • Nakielny, S. and Dreyfuss, G., Transport of proteins and RNAs in and out of the nucleus, Cell, 99 (1999) 677-690.
    • (1999) Cell , vol.99 , pp. 677-690
    • Nakielny, S.1    Dreyfuss, G.2
  • 16
    • 0035112563 scopus 로고    scopus 로고
    • Identification of a short amino acid sequence essential for efficient nuclear targeting of the Kaposi's sarcoma-associated herpesvirus/human herpesvirus-8 K8 protein
    • Portes-Sentis, S., Manet, E., Gourru, G., Sergeant, A. and Gruffat, H., Identification of a short amino acid sequence essential for efficient nuclear targeting of the Kaposi's sarcoma-associated herpesvirus/human herpesvirus-8 K8 protein, J. Gen. Virol., 82 (2001) 507-512.
    • (2001) J. Gen. Virol. , vol.82 , pp. 507-512
    • Portes-Sentis, S.1    Manet, E.2    Gourru, G.3    Sergeant, A.4    Gruffat, H.5
  • 17
    • 0027251792 scopus 로고
    • RNA recognition by an isolated alpha helix
    • Tan, R., Chen, L., Buettner, J. A., Hudson, D. and Frankel, A. D., RNA recognition by an isolated alpha helix, Cell, 73 (1993) 1031-1040.
    • (1993) Cell , vol.73 , pp. 1031-1040
    • Tan, R.1    Chen, L.2    Buettner, J.A.3    Hudson, D.4    Frankel, A.D.5
  • 19
  • 20
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II
    • Park, C. B., Yi, K.-S., Matsuzaki, K., Kim, M. S. and Kim, S. C., Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II, PNAS, 97 (2000) 8245-8250.
    • (2000) PNAS , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.-S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 22
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides - An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • Futaki, S., Suzuki, T., Ohashi, W., Yagami, T., Tanaka, S., Ueda, K. and Sugiura, Y., Arginine-rich peptides - An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery, J. Biolog. Chem., 276 (2001) 5836-5840.
    • (2001) J. Biolog. Chem. , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 23
    • 0037172801 scopus 로고    scopus 로고
    • Translocation of branched-chain arginine peptides through cell membranes: Flexibility in the spatial disposition of positive charges in membrane-permeable peptides
    • Futaki, S., Nakase, I., Suzuki, T., Zhang, Y. J. and Sugiura, Y., Translocation of branched-chain arginine peptides through cell membranes: Flexibility in the spatial disposition of positive charges in membrane-permeable peptides, Biochemistry, 41 (2002) 7925-7930.
    • (2002) Biochemistry , vol.41 , pp. 7925-7930
    • Futaki, S.1    Nakase, I.2    Suzuki, T.3    Zhang, Y.J.4    Sugiura, Y.5
  • 24
    • 0038725606 scopus 로고    scopus 로고
    • Guanidinium rich peptide transporters and drug delivery
    • Wright, L. R., Rothbard, J. B. and Wender, P. A., Guanidinium rich peptide transporters and drug delivery, Curr. Prot. Pept. Sci., 4 (2003) 105-124.
    • (2003) Curr. Prot. Pept. Sci. , vol.4 , pp. 105-124
    • Wright, L.R.1    Rothbard, J.B.2    Wender, P.A.3
  • 26
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters
    • Wender, P. A., Mitchell, D. J., Pattabiraman, K., Pelkey, E. T., Steinman, L. and Rothbard, J. B., The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters, Proc. Natl. Acad. Sci. USA, 97 (2000) 13003-13008.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13003-13008
    • Wender, P.A.1    Mitchell, D.J.2    Pattabiraman, K.3    Pelkey, E.T.4    Steinman, L.5    Rothbard, J.B.6
  • 27
    • 0037103242 scopus 로고    scopus 로고
    • Arginine-rich molecular transporters for drug deliveiy: Role of backbone spacing in cellular uptake
    • Rothbard, J. B., Kreider, E., Vandeusen, C. L., Wright, L., Wylie, B. L. and Wender, P. A., Arginine-rich molecular transporters for drug deliveiy: Role of backbone spacing in cellular uptake, J. Medicinal Chem., 45 (2002) 3612-3618.
    • (2002) J. Medicinal Chem. , vol.45 , pp. 3612-3618
    • Rothbard, J.B.1    Kreider, E.2    Vandeusen, C.L.3    Wright, L.4    Wylie, B.L.5    Wender, P.A.6
  • 28
    • 0037206127 scopus 로고    scopus 로고
    • A quantitative validation of fluorophore-labelled cell-permeable peptide conjugates: Fluorophore and cargo dependence of import
    • Fischer, R., Waizenegger, T., Kohler, K. and Brock, R., A quantitative validation of fluorophore-labelled cell-permeable peptide conjugates: Fluorophore and cargo dependence of import, Biochim. Biophys. Acta (BBA) - Biomembranes, 1564 (2002) 365-374.
    • (2002) Biochim. Biophys. Acta (BBA) - Biomembranes , vol.1564 , pp. 365-374
    • Fischer, R.1    Waizenegger, T.2    Kohler, K.3    Brock, R.4
  • 30
    • 0035078052 scopus 로고    scopus 로고
    • Physico-chemical requirements for cellular uptake of pAntp peptide. Role of lipid-binding affinity
    • Drin, G., Mazel, M., Clair, P., Mathieu, D., Kaczorek, M. and Temsamani, J., Physico-chemical requirements for cellular uptake of pAntp peptide. Role of lipid-binding affinity, Eur. J. Biochem., 268 (2001) 1304-1314.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1304-1314
    • Drin, G.1    Mazel, M.2    Clair, P.3    Mathieu, D.4    Kaczorek, M.5    Temsamani, J.6
  • 31
    • 0042199010 scopus 로고    scopus 로고
    • Cell surface adherence and endocytosis of protein transduction domains
    • Lundberg, M., Wikstrom, S. and Johansson, M., Cell surface adherence and endocytosis of protein transduction domains, Molecular Ther., 8 (2003) 143-150.
    • (2003) Molecular Ther. , vol.8 , pp. 143-150
    • Lundberg, M.1    Wikstrom, S.2    Johansson, M.3
  • 32
    • 0036792527 scopus 로고    scopus 로고
    • Peptide-mediated cell delivery: Application in protein target validation
    • Lindsay, M. A., Peptide-mediated cell delivery: Application in protein target validation, Curr. Opin. Pharmacol., 2 (2002) 587-594.
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 587-594
    • Lindsay, M.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.