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Volumn 298, Issue 2, 2005, Pages 305-309

Strategies for cytosolic delivery of liposomal macromolecules

Author keywords

Cell penetrating peptides; Cytosolic delivery; Endosomal escape; Liposomes; Photochemical internalization

Indexed keywords

HYBRID PROTEIN; IMMUNOTOXIN; LIPOSOME; PEPTIDE; PHOTOSENSITIZING AGENT; TRANSACTIVATOR PROTEIN;

EID: 21344450090     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2005.02.040     Document Type: Conference Paper
Times cited : (31)

References (24)
  • 2
    • 0021984076 scopus 로고
    • Membrane fusion activity of the influenza virus hemagglutinin. the low pH-induced conformational change
    • R.W. Doms, A. Helenius, and J. White Membrane fusion activity of the influenza virus hemagglutinin. The low pH-induced conformational change J. Biol. Chem. 260 1985 2973 2981
    • (1985) J. Biol. Chem. , vol.260 , pp. 2973-2981
    • Doms, R.W.1    Helenius, A.2    White, J.3
  • 4
    • 0024564217 scopus 로고
    • Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the "fusion peptide"
    • C. Harter, P. James, T. Bachi, G. Semenza, and J. Brunner Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the "fusion peptide" J. Biol. Chem. 264 1989 6459 6464
    • (1989) J. Biol. Chem. , vol.264 , pp. 6459-6464
    • Harter, C.1    James, P.2    Bachi, T.3    Semenza, G.4    Brunner, J.5
  • 7
    • 2442421428 scopus 로고    scopus 로고
    • Transferrin-modified liposomes equipped with a pH-sensitive fusogenic peptide: An artificial viral-like delivery system
    • T. Kakudo, S. Chaki, S. Futaki, I. Nakase, K. Akaji, T. Kawakami, K. Maruyama, H. Kamiya, and H. Harashima Transferrin-modified liposomes equipped with a pH-sensitive fusogenic peptide: an artificial viral-like delivery system Biochemistry 43 2004 5618 5628
    • (2004) Biochemistry , vol.43 , pp. 5618-5628
    • Kakudo, T.1    Chaki, S.2    Futaki, S.3    Nakase, I.4    Akaji, K.5    Kawakami, T.6    Maruyama, K.7    Kamiya, H.8    Harashima, H.9
  • 8
    • 0029961759 scopus 로고    scopus 로고
    • Delivering information-rich drugs - Prospects and challenges
    • B. Lebleu Delivering information-rich drugs - prospects and challenges Trends Biotechnol. 14 1996 109 110
    • (1996) Trends Biotechnol. , vol.14 , pp. 109-110
    • Lebleu, B.1
  • 10
    • 0036289650 scopus 로고    scopus 로고
    • Positively charged DNA-binding proteins cause apparent cell membrane translocation
    • M. Lundberg, and M. Johansson 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
  • 11
    • 0037071787 scopus 로고    scopus 로고
    • Listeriolysin O-liposome-mediated cytosolic delivery of macromolecule antigen in vivo: Enhancement of antigen-specific cytotoxic T lymphocyte frequency, activity, and tumor protection
    • M. Mandal, and K.D. Lee Listeriolysin O-liposome-mediated cytosolic delivery of macromolecule antigen in vivo: enhancement of antigen-specific cytotoxic T lymphocyte frequency, activity, and tumor protection Biochim. Biophys. Acta 1563 2002 7 17
    • (2002) Biochim. Biophys. Acta , vol.1563 , pp. 7-17
    • Mandal, M.1    Lee, K.D.2
  • 12
    • 0037178877 scopus 로고    scopus 로고
    • Functional characterization of an endosome-disruptive peptide and its application in cytosolic delivery of immunoliposome-entrapped proteins
    • E. Mastrobattista, G.A. Koning, L. Van Bloois, A.C. Filipe, W. Jiskoot, and G. Storm Functional characterization of an endosome-disruptive peptide and its application in cytosolic delivery of immunoliposome-entrapped proteins J. Biol. Chem. 277 2002 27135 27143
    • (2002) J. Biol. Chem. , vol.277 , pp. 27135-27143
    • Mastrobattista, E.1    Koning, G.A.2    Van Bloois, L.3    Filipe, A.C.4    Jiskoot, W.5    Storm, G.6
  • 13
    • 0034718170 scopus 로고    scopus 로고
    • Release of gelonin from endosomes and lysosomes to cytosol by photochemical internalization
    • P.K. Selbo, K. Sandvig, V. Kirveliene, and K. Berg Release of gelonin from endosomes and lysosomes to cytosol by photochemical internalization Biochim. Biophys. Acta 1475 2000 307 313
    • (2000) Biochim. Biophys. Acta , vol.1475 , pp. 307-313
    • Selbo, P.K.1    Sandvig, K.2    Kirveliene, V.3    Berg, K.4
  • 14
    • 0033844659 scopus 로고    scopus 로고
    • Photochemical internalisation increases the cytotoxic effect of the immunotoxin MOC31-gelonin
    • P.K. Selbo, G. Sivam, O. Fodstad, K. Sandvig, and K. Berg Photochemical internalisation increases the cytotoxic effect of the immunotoxin MOC31-gelonin Int. J. Cancer 87 2000 853 859
    • (2000) Int. J. Cancer , vol.87 , pp. 853-859
    • Selbo, P.K.1    Sivam, G.2    Fodstad, O.3    Sandvig, K.4    Berg, K.5
  • 15
    • 0035500592 scopus 로고    scopus 로고
    • On the mechanisms of internalization and intracellular delivery mediated by pH-sensitive liposomes
    • S. Simoes, V. Slepushkin, N. Duzgunes, and M.C. Pedroso de Lima On the mechanisms of internalization and intracellular delivery mediated by pH-sensitive liposomes Biochim. Biophys. Acta 1515 2001 23 37
    • (2001) Biochim. Biophys. Acta , vol.1515 , pp. 23-37
    • Simoes, S.1    Slepushkin, V.2    Duzgunes, N.3    Pedroso De Lima, M.C.4
  • 17
    • 0026062948 scopus 로고
    • The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion
    • T. Stegmann, J.M. Delfino, F.M. Richards, and A. Helenius The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion J. Biol. Chem. 266 1991 18404 18410
    • (1991) J. Biol. Chem. , vol.266 , pp. 18404-18410
    • Stegmann, T.1    Delfino, J.M.2    Richards, F.M.3    Helenius, A.4
  • 18
    • 0035902477 scopus 로고    scopus 로고
    • TAT peptide on the surface of liposomes affords their efficient intracellular delivery even at low temperature and in the presence of metabolic inhibitors
    • V.P. Torchilin, R. Rammohan, V. Weissig, and T.S. Levchenko TAT peptide on the surface of liposomes affords their efficient intracellular delivery even at low temperature and in the presence of metabolic inhibitors Proc. Natl. Acad. Sci. U.S.A. 98 2001 8786 8791
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8786-8791
    • Torchilin, V.P.1    Rammohan, R.2    Weissig, V.3    Levchenko, T.S.4
  • 19
    • 0036784335 scopus 로고    scopus 로고
    • Translocation of liposomes into cancer cells by cell-penetrating peptides penetratin and tat: A kinetic and efficacy study
    • Y.L. Tseng, J.J. Liu, and R.L. Hong Translocation of liposomes into cancer cells by cell-penetrating peptides penetratin and tat: a kinetic and efficacy study Mol. Pharmacol. 62 2002 864 872
    • (2002) Mol. Pharmacol. , vol.62 , pp. 864-872
    • Tseng, Y.L.1    Liu, J.J.2    Hong, R.L.3
  • 21
    • 0141907727 scopus 로고    scopus 로고
    • Cellular uptake [correction of utake] of the Tat peptide: An endocytosis mechanism following ionic interactions
    • E. Vives Cellular uptake [correction of utake] of the Tat peptide: an endocytosis mechanism following ionic interactions J. Mol. Recognit. 16 2003 265 271
    • (2003) J. Mol. Recognit. , vol.16 , pp. 265-271
    • Vives, E.1
  • 22
    • 0032764932 scopus 로고    scopus 로고
    • Application of membrane-active peptides for nonviral gene delivery
    • E. Wagner Application of membrane-active peptides for nonviral gene delivery Adv. Drug Deliv. Rev. 38 1999 279 289
    • (1999) Adv. Drug Deliv. Rev. , vol.38 , pp. 279-289
    • Wagner, E.1
  • 23
    • 0025276435 scopus 로고
    • Viral and cellular membrane fusion proteins
    • J.M. White Viral and cellular membrane fusion proteins Annu. Rev. Physiol. 52 1990 675 697
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 675-697
    • White, J.M.1
  • 24
    • 0034085963 scopus 로고    scopus 로고
    • Effects of physicochemical characteristics of poly(2-(dimethylamino)ethyl methacrylate)-based polyplexes on cellular association and internalisation
    • N.J. Zuidam, G. Posthuma, E.T. de Vries, D.J. Crommelin, W.E. Hennink, and G. Storm Effects of physicochemical characteristics of poly(2- (dimethylamino)ethyl methacrylate)-based polyplexes on cellular association and internalisation J. Drug Target. 8 2000 51 66
    • (2000) J. Drug Target. , vol.8 , pp. 51-66
    • Zuidam, N.J.1    Posthuma, G.2    De Vries, E.T.3    Crommelin, D.J.4    Hennink, W.E.5    Storm, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.