메뉴 건너뛰기




Volumn 307, Issue 1, 2003, Pages 100-107

Uptake of analogs of penetratin, Tat(48-60) and oligoarginine in live cells

Author keywords

Antennapedia homeodomain; ATP depletion; Endocytosis; Internalization; Membrane translocation; PC 12; Protein transduction domain; Rotenone; Tat; V79

Indexed keywords

FLUOROARGINYLGLUTAMINYLISOLEUCYLLYSYLISOLEUCYLTRYPTOPHYLPHENYLALANYLGLUT AMI NYLASPARAGINYLARGINYLARGINYLMETHIONYLLYSYLTRYPTOPHYLLYSYLLYSINAMIDE; ARGININE DERIVATIVE; PENETRATIN; PEPTIDE DERIVATIVE; TRANSACTIVATOR PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 0038726020     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)01135-5     Document Type: Article
Times cited : (281)

References (26)
  • 1
    • 0034141430 scopus 로고    scopus 로고
    • In vivo protein transduction: Intracellular delivery of biologically active proteins, compounds and DNA
    • Schwarze S.R., Dowdy S.F. In vivo protein transduction: intracellular delivery of biologically active proteins, compounds and DNA. Trends Pharmacol. Sci. 21:2000;45-48.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 45-48
    • Schwarze, S.R.1    Dowdy, S.F.2
  • 3
    • 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
    • Vivès E., Brodin P., 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
    • Vivès, E.1    Brodin, P.2    Lebleu, B.3
  • 4
    • 0001610172 scopus 로고    scopus 로고
    • Structure-activity relationship study of the plasma membrane translocating potential of a short peptide from HIV-1 Tat protein
    • Vivès E., Granier C., Prevot P., Lebleu B. Structure-activity relationship study of the plasma membrane translocating potential of a short peptide from HIV-1 Tat protein. Lett. Pept. Sci. 4:1997;429-436.
    • (1997) Lett. Pept. Sci. , vol.4 , pp. 429-436
    • Vivès, E.1    Granier, C.2    Prevot, P.3    Lebleu, B.4
  • 5
    • 0035863391 scopus 로고    scopus 로고
    • Synthetic protein transduction domains: Enhanced transduction potential in vitro and in vivo
    • Ho A., Schwarze S.R., Mermelstein S.J., Waksman G., Dowdy S.F. Synthetic protein transduction domains: enhanced transduction potential in vitro and in vivo. Cancer Res. 61:2001;474-477.
    • (2001) Cancer Res. , vol.61 , pp. 474-477
    • Ho, A.1    Schwarze, S.R.2    Mermelstein, S.J.3    Waksman, G.4    Dowdy, S.F.5
  • 6
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi D., Joliot A.H., Chassaing G., Prochiantz A. 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    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 7
    • 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., Prochiantz A. Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J. Biol. Chem. 271:1996;18188-18193.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 8
    • 0033973662 scopus 로고    scopus 로고
    • Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector penetratin
    • Fischer P.M., Zhelev N.Z., Wang S., Melville J.E., Fåhraeus R., Lane D.P. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector penetratin. J. Pept. Res. 55:2000;163-172.
    • (2000) J. Pept. Res. , vol.55 , pp. 163-172
    • Fischer, P.M.1    Zhelev, N.Z.2    Wang, S.3    Melville, J.E.4    Fåhraeus, R.5    Lane, D.P.6
  • 9
    • 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., Sugiura Y. Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276:2001;5836-5840.
    • (2001) J. Biol. 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
  • 10
    • 0037169486 scopus 로고    scopus 로고
    • Possible existence of common internalization mechanisms among arginine- rich peptides
    • Suzuki T., Futaki S., Niwa M., Tanaka S., Ueda K., Sugiura Y. 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    Futaki, S.2    Niwa, M.3    Tanaka, S.4    Ueda, K.5    Sugiura, Y.6
  • 13
    • 0036289650 scopus 로고    scopus 로고
    • Positively charged DNA-binding proteins cause apparent cell membrane translocation
    • Lundberg M., 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
  • 16
    • 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., Krausz E., Lane D.P. 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    Krausz, E.2    Lane, D.P.3
  • 17
    • 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
  • 18
    • 0033794501 scopus 로고    scopus 로고
    • Polyarginine enters cells more efficiently than other polycationic homopolymers
    • Mitchell D.J., Kim D.T., Steinman L., Fathman C.G., Rothbard J.B. Polyarginine enters cells more efficiently than other polycationic homopolymers. J. Pept. Res. 56:2000;318-325.
    • (2000) J. Pept. Res. , vol.56 , pp. 318-325
    • Mitchell, D.J.1    Kim, D.T.2    Steinman, L.3    Fathman, C.G.4    Rothbard, J.B.5
  • 19
    • 0034613057 scopus 로고    scopus 로고
    • The Antennapedia peptide penetratin translocates across lipid bilayers - The first direct observation
    • Thoren P.E.G., Persson D., Karlsson M., Norden B. The Antennapedia peptide penetratin translocates across lipid bilayers - the first direct observation. FEBS Lett. 482:2000;265-268.
    • (2000) FEBS Lett. , vol.482 , pp. 265-268
    • Thoren, P.E.G.1    Persson, D.2    Karlsson, M.3    Norden, B.4
  • 20
    • 0037457905 scopus 로고    scopus 로고
    • Application of a novel analysis to measure the binding of the membrane- translocating peptide penetratin to negatively charged liposomes
    • Persson D., Thoren P.E., Herner M., Lincoln P., Norden B. Application of a novel analysis to measure the binding of the membrane- translocating peptide penetratin to negatively charged liposomes. Biochemistry. 42:2003;421-429.
    • (2003) Biochemistry , vol.42 , pp. 421-429
    • Persson, D.1    Thoren, P.E.2    Herner, M.3    Lincoln, P.4    Norden, B.5
  • 21
    • 0030417483 scopus 로고    scopus 로고
    • Homeodomain-type DNA recognition
    • Billeter M. Homeodomain-type DNA recognition. Prog. Biophys. Mol. Biol. 66:1996;211-225.
    • (1996) Prog. Biophys. Mol. Biol. , vol.66 , pp. 211-225
    • Billeter, M.1
  • 22
    • 0038797932 scopus 로고    scopus 로고
    • Abiotic guanidinium containing receptors for anionic species
    • Best M.D., Tobey S.L., Anslyn E.V. Abiotic guanidinium containing receptors for anionic species. Coord. Chem. Rev. 240:2003;3-15.
    • (2003) Coord. Chem. Rev. , vol.240 , pp. 3-15
    • Best, M.D.1    Tobey, S.L.2    Anslyn, E.V.3
  • 23
    • 0036384267 scopus 로고    scopus 로고
    • Specific mode of interaction between components of model pulmonary surfactants using computer simulations
    • Kaznessis Y.N., Kim S., Larson R.G. Specific mode of interaction between components of model pulmonary surfactants using computer simulations. J. Mol. Biol. 322:2002;569-582.
    • (2002) J. Mol. Biol. , vol.322 , pp. 569-582
    • Kaznessis, Y.N.1    Kim, S.2    Larson, R.G.3
  • 24
    • 0025747497 scopus 로고
    • Alpha-2,8-Polysialic acid is the neuronal surface receptor of antennapedia homeobox peptide
    • Joliot A.H., Triller A., Volovitch M., Pernelle C., Prochiantz A. alpha-2,8-Polysialic acid is the neuronal surface receptor of antennapedia homeobox peptide. New Biol. 3:1991;1121-1134.
    • (1991) New Biol. , vol.3 , pp. 1121-1134
    • Joliot, A.H.1    Triller, A.2    Volovitch, M.3    Pernelle, C.4    Prochiantz, A.5
  • 25
    • 0034529953 scopus 로고    scopus 로고
    • Uptake of HIV-1 tat protein mediated by low-density lipoprotein receptor-related protein disrupts the neuronal metabolic balance of the receptor ligands
    • Liu Y., Jones M., Hingtgen C.M., Bu G., Laribee N., Tanzi R.E., Moir R.D., Nath A., He J.J. Uptake of HIV-1 tat protein mediated by low-density lipoprotein receptor-related protein disrupts the neuronal metabolic balance of the receptor ligands. Nat. Med. 6:2000;1380-1387.
    • (2000) Nat. Med. , vol.6 , pp. 1380-1387
    • Liu, Y.1    Jones, M.2    Hingtgen, C.M.3    Bu, G.4    Laribee, N.5    Tanzi, R.E.6    Moir, R.D.7    Nath, A.8    He, J.J.9
  • 26
    • 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. 276:2001;3254-3261.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3254-3261
    • Tyagi, M.1    Rusnati, M.2    Presta, M.3    Giacca, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.