메뉴 건너뛰기




Volumn 72, Issue 1, 2009, Pages 219-225

The cell-penetrating peptide octa-arginine is a potent inhibitor of proteasome activities

Author keywords

Cell penetrating peptides; HeLa cells; Inhibitor; Octa arginine; Proteasome; Ubiquitin conjugated proteins

Indexed keywords

CASPASE; CELL PENETRATING PEPTIDE; CHYMOTRYPSIN; OCTA ARGININE PEPTIDE; PROTEASOME; PROTEASOME INHIBITOR; UNCLASSIFIED DRUG;

EID: 62949248272     PISSN: 09396411     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejpb.2008.10.016     Document Type: Article
Times cited : (43)

References (54)
  • 1
    • 38349174536 scopus 로고    scopus 로고
    • On the biomedical promise of cell penetrating peptides: limits versus prospects
    • Foerg C., and Merkle H.P. On the biomedical promise of cell penetrating peptides: limits versus prospects. J. Pharm. Sci. 97 (2008) 144-162
    • (2008) J. Pharm. Sci. , vol.97 , pp. 144-162
    • Foerg, C.1    Merkle, H.P.2
  • 2
    • 34848892144 scopus 로고    scopus 로고
    • Cell penetrating peptides: intracellular pathways and pharmaceutical perspectives
    • Patel L.N., Zaro J.L., and Shen W.C. Cell penetrating peptides: intracellular pathways and pharmaceutical perspectives. Pharm Res. 24 (2007) 1977-1992
    • (2007) Pharm Res. , vol.24 , pp. 1977-1992
    • Patel, L.N.1    Zaro, J.L.2    Shen, W.C.3
  • 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
    • 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
    • 33846223900 scopus 로고    scopus 로고
    • Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis
    • Nakase I., Tadokoro A., Kawabata N., Takeuchi T., Katoh H., Hiramoto K., Negishi M., Nomizu M., Sugiura Y., and Futaki S. Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis. Biochemistry 46 (2007) 492-501
    • (2007) Biochemistry , vol.46 , pp. 492-501
    • Nakase, I.1    Tadokoro, A.2    Kawabata, N.3    Takeuchi, T.4    Katoh, H.5    Hiramoto, K.6    Negishi, M.7    Nomizu, M.8    Sugiura, Y.9    Futaki, S.10
  • 6
    • 0038352064 scopus 로고    scopus 로고
    • Quantitative comparison of membrane transduction and endocytosis of oligopeptides
    • Zaro J.L., and Shen W.C. Quantitative comparison of membrane transduction and endocytosis of oligopeptides. Biochem. Biophys. Res. Commun. 307 (2003) 241-247
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 241-247
    • Zaro, J.L.1    Shen, W.C.2
  • 7
    • 31544479580 scopus 로고    scopus 로고
    • Intracellular traffic and fate of protein transduction domains HIV-1 TAT peptide and octaarginine. Implications for their utilization as drug delivery vectors
    • Al-Taei S., Penning N.A., Simpson J.C., Futaki S., Takeuchi T., Nakase I., and Jones A.T. Intracellular traffic and fate of protein transduction domains HIV-1 TAT peptide and octaarginine. Implications for their utilization as drug delivery vectors. Bioconjugate Chem. 17 (2006) 90-100
    • (2006) Bioconjugate Chem. , vol.17 , pp. 90-100
    • Al-Taei, S.1    Penning, N.A.2    Simpson, J.C.3    Futaki, S.4    Takeuchi, T.5    Nakase, I.6    Jones, A.T.7
  • 8
    • 33646343733 scopus 로고    scopus 로고
    • Membrane transduction of oligoarginine in HeLa cells is not mediated by macropinocytosis
    • Zaro J.L., Rajapaksa T.E., Okamoto C.T., and Shen W.C. Membrane transduction of oligoarginine in HeLa cells is not mediated by macropinocytosis. Mol. Pharm. 3 (2006) 181-186
    • (2006) Mol. Pharm. , vol.3 , pp. 181-186
    • Zaro, J.L.1    Rajapaksa, T.E.2    Okamoto, C.T.3    Shen, W.C.4
  • 9
    • 19544370002 scopus 로고    scopus 로고
    • Evidence that membrane transduction of oligoarginine does not require vesicle formation
    • Zaro J.L., and Shen W.C. Evidence that membrane transduction of oligoarginine does not require vesicle formation. Exp. Cell Res. 307 (2005) 164-173
    • (2005) Exp. Cell Res. , vol.307 , pp. 164-173
    • Zaro, J.L.1    Shen, W.C.2
  • 12
    • 0034129207 scopus 로고    scopus 로고
    • Arginine-based structures are specific inhibitors of cathepsin C. Application of peptide combinatorial libraries
    • Horn M., Pavlik M., Doleckova L., Baudys M., and Mares M. Arginine-based structures are specific inhibitors of cathepsin C. Application of peptide combinatorial libraries. Eur. J. Biochem. 267 (2000) 3330-3336
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3330-3336
    • Horn, M.1    Pavlik, M.2    Doleckova, L.3    Baudys, M.4    Mares, M.5
  • 14
    • 10344260714 scopus 로고    scopus 로고
    • Polyarginine inhibits gp160 processing by furin and suppresses productive human immunodeficiency virus type 1 infection
    • Kibler K.V., Miyazato A., Yedavalli V.S., Dayton A.I., Jacobs B.L., Dapolito G., Kim S.J., and Jeang K.T. Polyarginine inhibits gp160 processing by furin and suppresses productive human immunodeficiency virus type 1 infection. J. Biol. Chem. 279 (2004) 49055-49063
    • (2004) J. Biol. Chem. , vol.279 , pp. 49055-49063
    • Kibler, K.V.1    Miyazato, A.2    Yedavalli, V.S.3    Dayton, A.I.4    Jacobs, B.L.5    Dapolito, G.6    Kim, S.J.7    Jeang, K.T.8
  • 15
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman M.H., and Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82 (2002) 373-428
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 16
    • 0035665515 scopus 로고    scopus 로고
    • PR-39 and PR-11 peptides inhibit ischemia-reperfusion injury by blocking proteasome-mediated I kappa B alpha degradation
    • Bao J., Sato K., Li M., Gao Y., Abid R., Aird W., Simons M., and Post M.J. PR-39 and PR-11 peptides inhibit ischemia-reperfusion injury by blocking proteasome-mediated I kappa B alpha degradation. Am. J. Physiol. Heart Circ. Physiol. 281 (2001) H2612-2618
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.281
    • Bao, J.1    Sato, K.2    Li, M.3    Gao, Y.4    Abid, R.5    Aird, W.6    Simons, M.7    Post, M.J.8
  • 18
    • 0028844134 scopus 로고
    • Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti M., Gennaro R., and Romeo D. Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett. 374 (1995) 1-5
    • (1995) FEBS Lett. , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 19
    • 0042848726 scopus 로고    scopus 로고
    • Proline- and arginine-rich peptides constitute a novel class of allosteric inhibitors of proteasome activity
    • Gaczynska M., Osmulski P.A., Gao Y., Post M.J., and Simons M. Proline- and arginine-rich peptides constitute a novel class of allosteric inhibitors of proteasome activity. Biochemistry 42 (2003) 8663-8670
    • (2003) Biochemistry , vol.42 , pp. 8663-8670
    • Gaczynska, M.1    Osmulski, P.A.2    Gao, Y.3    Post, M.J.4    Simons, M.5
  • 20
    • 0034634389 scopus 로고    scopus 로고
    • Different proteasome subtypes in a single tissue exhibit different enzymatic properties
    • Dahlmann B., Ruppert T., Kuehn L., Merforth S., and Kloetzel P.M. Different proteasome subtypes in a single tissue exhibit different enzymatic properties. J. Mol. Biol. 303 (2000) 643-653
    • (2000) J. Mol. Biol. , vol.303 , pp. 643-653
    • Dahlmann, B.1    Ruppert, T.2    Kuehn, L.3    Merforth, S.4    Kloetzel, P.M.5
  • 21
    • 0035955559 scopus 로고    scopus 로고
    • Reconstitution of hybrid proteasomes from purified PA700-20 S complexes and PA28alphabeta activator: ultrastructure and peptidase activities
    • Kopp F., Dahlmann B., and Kuehn L. Reconstitution of hybrid proteasomes from purified PA700-20 S complexes and PA28alphabeta activator: ultrastructure and peptidase activities. J. Mol. Biol. 313 (2001) 465-471
    • (2001) J. Mol. Biol. , vol.313 , pp. 465-471
    • Kopp, F.1    Dahlmann, B.2    Kuehn, L.3
  • 22
    • 0030607248 scopus 로고    scopus 로고
    • Reconstitution of proteasome activator PA28 from isolated subunits: optimal activity is associated with an alpha,beta-heteromultimer
    • Kuehn L., and Dahlmann B. Reconstitution of proteasome activator PA28 from isolated subunits: optimal activity is associated with an alpha,beta-heteromultimer. FEBS Lett. 394 (1996) 183-186
    • (1996) FEBS Lett. , vol.394 , pp. 183-186
    • Kuehn, L.1    Dahlmann, B.2
  • 23
    • 0029039632 scopus 로고
    • Studies on the activation by ATP of the 26 S proteasome complex from rat skeletal muscle
    • Dahlmann B., Kuehn L., and Reinauer H. Studies on the activation by ATP of the 26 S proteasome complex from rat skeletal muscle. Biochem. J. 309 (1995) 195-202
    • (1995) Biochem. J. , vol.309 , pp. 195-202
    • Dahlmann, B.1    Kuehn, L.2    Reinauer, H.3
  • 24
    • 0016167076 scopus 로고
    • The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters
    • Eisenthal R., and Cornish-Bowden A. The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters. Biochem. J. 139 (1974) 715-720
    • (1974) Biochem. J. , vol.139 , pp. 715-720
    • Eisenthal, R.1    Cornish-Bowden, A.2
  • 25
    • 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. 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
  • 26
    • 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., and 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
  • 27
    • 1842339868 scopus 로고    scopus 로고
    • Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles
    • Tawa Jr. N.E., Odessey R., and Goldberg A.L. Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles. J. Clin. Invest. 100 (1997) 197-203
    • (1997) J. Clin. Invest. , vol.100 , pp. 197-203
    • Tawa Jr., N.E.1    Odessey, R.2    Goldberg, A.L.3
  • 28
    • 0023370041 scopus 로고
    • Analysis of structural requirements for the absorption of drugs and macromolecules from the nasal cavity
    • McMartin C., Hutchinson L.E., Hyde R., and Peters G.E. Analysis of structural requirements for the absorption of drugs and macromolecules from the nasal cavity. J. Pharm. Sci. 76 (1987) 535-540
    • (1987) J. Pharm. Sci. , vol.76 , pp. 535-540
    • McMartin, C.1    Hutchinson, L.E.2    Hyde, R.3    Peters, G.E.4
  • 29
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • Frankel A.D., and Pabo C.O. Cellular uptake of the tat protein from human immunodeficiency virus. Cell 55 (1988) 1189-1193
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 30
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein
    • Green M., and Loewenstein P.M. Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein. Cell 55 (1988) 1179-1188
    • (1988) Cell , vol.55 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 31
    • 0034296675 scopus 로고    scopus 로고
    • Characterization of a class of cationic peptides able to facilitate efficient protein transduction in vitro and in vivo
    • Mi Z., Mai J., Lu X., and Robbins P.D. Characterization of a class of cationic peptides able to facilitate efficient protein transduction in vitro and in vivo. Mol. Ther. 2 (2000) 339-347
    • (2000) Mol. Ther. , vol.2 , pp. 339-347
    • Mi, Z.1    Mai, J.2    Lu, X.3    Robbins, P.D.4
  • 32
    • 0034962912 scopus 로고    scopus 로고
    • Improved nasal absorption of drugs using poly-l-arginine: effects of concentration and molecular weight of poly-l-arginine on the nasal absorption of fluorescein isothiocyanate-dextran in rats
    • Miyamoto M., Natsume H., Iwata S., Ohtake K., Yamaguchi M., Kobayashi D., Sugibayashi K., Yamashina M., and Morimoto Y. Improved nasal absorption of drugs using poly-l-arginine: effects of concentration and molecular weight of poly-l-arginine on the nasal absorption of fluorescein isothiocyanate-dextran in rats. Eur. J. Pharm. Biopharm. 52 (2001) 21-30
    • (2001) Eur. J. Pharm. Biopharm. , vol.52 , pp. 21-30
    • Miyamoto, M.1    Natsume, H.2    Iwata, S.3    Ohtake, K.4    Yamaguchi, M.5    Kobayashi, D.6    Sugibayashi, K.7    Yamashina, M.8    Morimoto, Y.9
  • 33
    • 34548180403 scopus 로고    scopus 로고
    • Applications of cell-penetrating peptides in regulation of gene expression
    • Jarver P., Langel K., El-Andaloussi S., and Langel U. Applications of cell-penetrating peptides in regulation of gene expression. Biochem. Soc. Trans. 35 (2007) 770-774
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 770-774
    • Jarver, P.1    Langel, K.2    El-Andaloussi, S.3    Langel, U.4
  • 34
    • 0037151122 scopus 로고    scopus 로고
    • Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20 S proteasomes. Evidence for peptide-induced channel opening in the alpha-rings
    • Kisselev A.F., Kaganovich D., and Goldberg A.L. Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20 S proteasomes. Evidence for peptide-induced channel opening in the alpha-rings. J. Biol. Chem. 277 (2002) 22260-22270
    • (2002) J. Biol. Chem. , vol.277 , pp. 22260-22270
    • Kisselev, A.F.1    Kaganovich, D.2    Goldberg, A.L.3
  • 35
    • 0037119348 scopus 로고    scopus 로고
    • Efficiency of protein transduction is cell type-dependent and is enhanced by dextran sulfate
    • Mai J.C., Shen H., Watkins S.C., Cheng T., and Robbins P.D. Efficiency of protein transduction is cell type-dependent and is enhanced by dextran sulfate. J. Biol. Chem. 277 (2002) 30208-30218
    • (2002) J. Biol. Chem. , vol.277 , pp. 30208-30218
    • Mai, J.C.1    Shen, H.2    Watkins, S.C.3    Cheng, T.4    Robbins, P.D.5
  • 36
    • 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., and 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
  • 39
    • 0037018938 scopus 로고    scopus 로고
    • Nanoenzymology of the 20S proteasome: proteasomal actions are controlled by the allosteric transition
    • Osmulski P.A., and Gaczynska M. Nanoenzymology of the 20S proteasome: proteasomal actions are controlled by the allosteric transition. Biochemistry 41 (2002) 7047-7053
    • (2002) Biochemistry , vol.41 , pp. 7047-7053
    • Osmulski, P.A.1    Gaczynska, M.2
  • 40
    • 0033197542 scopus 로고    scopus 로고
    • Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown
    • Kisselev A.F., Akopian T.N., Castillo V., and Goldberg A.L. Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol. Cell 4 (1999) 395-402
    • (1999) Mol. Cell , vol.4 , pp. 395-402
    • Kisselev, A.F.1    Akopian, T.N.2    Castillo, V.3    Goldberg, A.L.4
  • 41
    • 0035099055 scopus 로고    scopus 로고
    • Lack of proteasome active site allostery as revealed by subunit-specific inhibitors
    • Myung J., Kim K.B., Lindsten K., Dantuma N.P., and Crews C.M. Lack of proteasome active site allostery as revealed by subunit-specific inhibitors. Mol. Cell 7 (2001) 411-420
    • (2001) Mol. Cell , vol.7 , pp. 411-420
    • Myung, J.1    Kim, K.B.2    Lindsten, K.3    Dantuma, N.P.4    Crews, C.M.5
  • 42
    • 0036349006 scopus 로고    scopus 로고
    • Regulation of the 26S proteasome activities by peptides mimicking cleavage products
    • Papapostolou D., Coux O., and Reboud-Ravaux M. Regulation of the 26S proteasome activities by peptides mimicking cleavage products. Biochem. Biophys. Res. Commun. 295 (2002) 1090-1095
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 1090-1095
    • Papapostolou, D.1    Coux, O.2    Reboud-Ravaux, M.3
  • 43
    • 0141682702 scopus 로고    scopus 로고
    • Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits
    • Apcher G.S., Heink S., Zantopf D., Kloetzel P.M., Schmid H.P., Mayer R.J., and Kruger E. Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits. FEBS Lett. 553 (2003) 200-204
    • (2003) FEBS Lett. , vol.553 , pp. 200-204
    • Apcher, G.S.1    Heink, S.2    Zantopf, D.3    Kloetzel, P.M.4    Schmid, H.P.5    Mayer, R.J.6    Kruger, E.7
  • 44
    • 0036979090 scopus 로고    scopus 로고
    • The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing
    • Huang X., Seifert U., Salzmann U., Henklein P., Preissner R., Henke W., Sijts A.J., Kloetzel P.M., and Dubiel W. The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing. J. Mol. Biol. 323 (2002) 771-782
    • (2002) J. Mol. Biol. , vol.323 , pp. 771-782
    • Huang, X.1    Seifert, U.2    Salzmann, U.3    Henklein, P.4    Preissner, R.5    Henke, W.6    Sijts, A.J.7    Kloetzel, P.M.8    Dubiel, W.9
  • 45
    • 0030929321 scopus 로고    scopus 로고
    • HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation
    • Seeger M., Ferrell K., Frank R., and Dubiel W. HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. J. Biol. Chem. 272 (1997) 8145-8148
    • (1997) J. Biol. Chem. , vol.272 , pp. 8145-8148
    • Seeger, M.1    Ferrell, K.2    Frank, R.3    Dubiel, W.4
  • 46
    • 0034640520 scopus 로고    scopus 로고
    • Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis
    • Tanahashi N., Murakami Y., Minami Y., Shimbara N., Hendil K.B., and Tanaka K. Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. J. Biol. Chem. 275 (2000) 14336-14345
    • (2000) J. Biol. Chem. , vol.275 , pp. 14336-14345
    • Tanahashi, N.1    Murakami, Y.2    Minami, Y.3    Shimbara, N.4    Hendil, K.B.5    Tanaka, K.6
  • 47
    • 27644518292 scopus 로고    scopus 로고
    • Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates
    • Kisselev A.F., and Goldberg A.L. Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates. Methods Enzymol. 398 (2005) 364-378
    • (2005) Methods Enzymol. , vol.398 , pp. 364-378
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 48
    • 33748551023 scopus 로고    scopus 로고
    • A targeted protease substrate for a quantitative determination of protease activities in the endolysosomal pathway
    • Fischer R., Bachle D., Fotin-Mleczek M., Jung G., Kalbacher H., and Brock R. A targeted protease substrate for a quantitative determination of protease activities in the endolysosomal pathway. Chembiochem 7 (2006) 1428-1434
    • (2006) Chembiochem , vol.7 , pp. 1428-1434
    • Fischer, R.1    Bachle, D.2    Fotin-Mleczek, M.3    Jung, G.4    Kalbacher, H.5    Brock, R.6
  • 49
    • 33646236541 scopus 로고    scopus 로고
    • Oligoarginine vectors for intracellular delivery: design and cellular-uptake mechanisms
    • Futaki S. Oligoarginine vectors for intracellular delivery: design and cellular-uptake mechanisms. Biopolymers 84 (2006) 241-249
    • (2006) Biopolymers , vol.84 , pp. 241-249
    • Futaki, S.1
  • 51
    • 27744590845 scopus 로고    scopus 로고
    • Cytosolic delivery of a p16-peptide oligoarginine conjugate for inhibiting proliferation of MCF7 cells
    • Zaro J.L., and Shen W.C. Cytosolic delivery of a p16-peptide oligoarginine conjugate for inhibiting proliferation of MCF7 cells. J. Control Release 108 (2005) 409-417
    • (2005) J. Control Release , vol.108 , pp. 409-417
    • Zaro, J.L.1    Shen, W.C.2
  • 52
    • 35648941282 scopus 로고    scopus 로고
    • Cellular uptake mechanisms and potential therapeutic utility of peptidic cell delivery vectors: progress 2001-2006
    • Fischer P.M. Cellular uptake mechanisms and potential therapeutic utility of peptidic cell delivery vectors: progress 2001-2006. Med. Res. Rev. 27 (2007) 755-795
    • (2007) Med. Res. Rev. , vol.27 , pp. 755-795
    • Fischer, P.M.1
  • 54
    • 27244460815 scopus 로고    scopus 로고
    • Proteasome inhibition and its clinical prospects in the treatment of hematologic and solid malignancies
    • Ludwig H., Khayat D., Giaccone G., and Facon T. Proteasome inhibition and its clinical prospects in the treatment of hematologic and solid malignancies. Cancer 104 (2005) 1794-1807
    • (2005) Cancer , vol.104 , pp. 1794-1807
    • Ludwig, H.1    Khayat, D.2    Giaccone, G.3    Facon, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.