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Volumn 26, Issue 1, 2015, Pages 71-77

Dual peptide conjugation strategy for improved cellular uptake and mitochondria targeting

Author keywords

[No Author keywords available]

Indexed keywords

CYTOLOGY; DICHROISM; MOLECULES; PEPTIDES;

EID: 84921534709     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc500408p     Document Type: Article
Times cited : (75)

References (60)
  • 1
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer, G., Galluzzi, L., and Brenner, C. (2007) Mitochondrial membrane permeabilization in cell death. Physiol. Rev. 87, 99-163.
    • (2007) Physiol. Rev. , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 2
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin, M. T., and Beal, M. F. (2006) Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443, 787-795.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 5
    • 0035339611 scopus 로고    scopus 로고
    • Targeting peptide nucleic acid (PNA) oligomers to mitochondria within cells by conjugation to lipophilic cations: Implications for mitochondrial DNA replication, expression and disease
    • Muratovska, A., Lightowlers, R. N., Taylor, R. W., Turnbull, D. M., Smith, R. A. J., Wilce, J. A., Martin, S. W., and Murphy, M. P. (2001) Targeting peptide nucleic acid (PNA) oligomers to mitochondria within cells by conjugation to lipophilic cations: implications for mitochondrial DNA replication, expression and disease. Nucleic Acids Res. 29, 1852-1863.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1852-1863
    • Muratovska, A.1    Lightowlers, R.N.2    Taylor, R.W.3    Turnbull, D.M.4    Smith, R.A.J.5    Wilce, J.A.6    Martin, S.W.7    Murphy, M.P.8
  • 6
    • 0028796617 scopus 로고
    • Mitochondrial protein import - Reversible binding of the presequence at the trans side of the outer-membrane drives partial translocation and unfolding
    • Mayer, A., Neupert, W., and Lill, R. (1995) Mitochondrial protein import - reversible binding of the presequence at the trans side of the outer-membrane drives partial translocation and unfolding. Cell 80, 127-137.
    • (1995) Cell , vol.80 , pp. 127-137
    • Mayer, A.1    Neupert, W.2    Lill, R.3
  • 7
    • 0029774146 scopus 로고    scopus 로고
    • The protein import system of mitochondria
    • Schatz, G. (1996) The protein import system of mitochondria. J. Biol. Chem. 271, 31763-31766.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31763-31766
    • Schatz, G.1
  • 8
    • 0034237577 scopus 로고    scopus 로고
    • Protein transduction: Unrestricted delivery into all cells?
    • Schwarze, S. R., Hruska, K. A., and Dowdy, S. F. (2000) Protein transduction: unrestricted delivery into all cells? Trends Cell Biol. 10, 290-295.
    • (2000) Trends Cell Biol. , vol.10 , pp. 290-295
    • Schwarze, S.R.1    Hruska, K.A.2    Dowdy, S.F.3
  • 9
    • 0036804013 scopus 로고    scopus 로고
    • Arginine-rich peptides: Potential for intracellular delivery of macromolecules and the mystery of the translocation mechanisms
    • Futaki, S. (2002) Arginine-rich peptides: potential for intracellular delivery of macromolecules and the mystery of the translocation mechanisms. Int. J. Pharm. 245, 1-7.
    • (2002) Int. J. Pharm. , vol.245 , pp. 1-7
    • Futaki, S.1
  • 10
    • 0035839167 scopus 로고    scopus 로고
    • DQAsome/DNA complexes release DNA upon contact with isolated mouse liver mitochondria
    • Weissig, V., D 'Souza, G. G. M., and Torchilin, V. P. (2001) DQAsome/DNA complexes release DNA upon contact with isolated mouse liver mitochondria. J. Controlled Release 75, 401-408.
    • (2001) J. Controlled Release , vol.75 , pp. 401-408
    • Weissig, V.1    'Souza G G M, D.2    Torchilin, V.P.3
  • 11
    • 33847618832 scopus 로고    scopus 로고
    • Mitochondrial drug delivery and mitochondrial disease therapy - An approach to liposome-based delivery targeted to mitochondria
    • Yamada, Y., Akita, H., Kogure, K., Kamiya, H., and Harashima, H. (2007) Mitochondrial drug delivery and mitochondrial disease therapy - An approach to liposome-based delivery targeted to mitochondria. Mitochondrion 7, 63-71.
    • (2007) Mitochondrion , vol.7 , pp. 63-71
    • Yamada, Y.1    Akita, H.2    Kogure, K.3    Kamiya, H.4    Harashima, H.5
  • 13
    • 84856218021 scopus 로고    scopus 로고
    • Development of Novel Peptides for Mitochondrial Drug Delivery: Amino Acids Featuring Delocalized Lipophilic Cations
    • Kelley, S. O., Stewart, K. M., and Mourtada, R. (2011) Development of Novel Peptides for Mitochondrial Drug Delivery: Amino Acids Featuring Delocalized Lipophilic Cations. Pharm. Res. 28, 2808-2819.
    • (2011) Pharm. Res. , vol.28 , pp. 2808-2819
    • Kelley, S.O.1    Stewart, K.M.2    Mourtada, R.3
  • 14
    • 84883542016 scopus 로고    scopus 로고
    • Tuning the intracellular bacterial targeting of peptidic vectors
    • Lei, E. K., Pereira, M. P., and Kelley, S. O. (2013) Tuning the intracellular bacterial targeting of peptidic vectors. Angew. Chem., Int. Ed. 52, 9660-9663.
    • (2013) Angew. Chem., Int. Ed. , vol.52 , pp. 9660-9663
    • Lei, E.K.1    Pereira, M.P.2    Kelley, S.O.3
  • 16
  • 17
    • 0038365420 scopus 로고    scopus 로고
    • Targeted delivery of DNA to the mitochondrial compartment via import sequence-conjugated peptide nucleic acid
    • Flierl, A., Jackson, C., Cottrell, B., Murdock, D., Seibel, P., and Wallace, D. C. (2003) Targeted delivery of DNA to the mitochondrial compartment via import sequence-conjugated peptide nucleic acid. Mol. Ther. 7, 550-557.
    • (2003) Mol. Ther. , vol.7 , pp. 550-557
    • Flierl, A.1    Jackson, C.2    Cottrell, B.3    Murdock, D.4    Seibel, P.5    Wallace, D.C.6
  • 20
    • 33748126226 scopus 로고    scopus 로고
    • Recent approaches to intracellular delivery of drugs and DNA and organelle targeting
    • Torchilin, V. P. (2006) Recent approaches to intracellular delivery of drugs and DNA and organelle targeting. Annu. Rev. Biomed. Eng. 8, 343-375.
    • (2006) Annu. Rev. Biomed. Eng. , vol.8 , pp. 343-375
    • Torchilin, V.P.1
  • 21
    • 70349554126 scopus 로고    scopus 로고
    • Mitochondria-penetrating peptides: Sequence effects and model cargo transport
    • Yousif, L. F., Stewart, K. M., Horton, K. L., and Kelley, S. O. (2009) Mitochondria-penetrating peptides: sequence effects and model cargo transport. ChemBioChem 10, 2081-2088.
    • (2009) ChemBioChem , vol.10 , pp. 2081-2088
    • Yousif, L.F.1    Stewart, K.M.2    Horton, K.L.3    Kelley, S.O.4
  • 22
    • 0022731676 scopus 로고
    • Mitochondrial targeting sequences may form amphiphilic helices
    • Vonheijne, G. (1986) Mitochondrial targeting sequences may form amphiphilic helices. EMBO J. 5, 1335-1342.
    • (1986) EMBO J. , vol.5 , pp. 1335-1342
    • Vonheijne, G.1
  • 23
    • 0025077695 scopus 로고
    • 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle
    • Karslake, C., Piotto, M. E., Pak, Y. K., Weiner, H., and Gorenstein, D. G. (1990) 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle. Biochemistry 29, 9872-9878.
    • (1990) Biochemistry , vol.29 , pp. 9872-9878
    • Karslake, C.1    Piotto, M.E.2    Pak, Y.K.3    Weiner, H.4    Gorenstein, D.G.5
  • 24
    • 0025150997 scopus 로고
    • Import of chemically synthesized signal peptides into rat-liver mitochondria
    • Pak, Y. K., and Weiner, H. (1990) Import of chemically synthesized signal peptides into rat-liver mitochondria. J. Biol. Chem. 265, 14298-14307.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14298-14307
    • Pak, Y.K.1    Weiner, H.2
  • 25
    • 84889780429 scopus 로고    scopus 로고
    • Activation of cell-penetrating peptides by disulfide bridge formation of truncated precursors
    • Bode, S. A., Wallbrecher, R., Brock, R., van Hest, J. C. M., and Lowik, D. (2014) Activation of cell-penetrating peptides by disulfide bridge formation of truncated precursors. Chem. Commun. 50, 415-417.
    • (2014) Chem. Commun. , vol.50 , pp. 415-417
    • Bode, S.A.1    Wallbrecher, R.2    Brock, R.3    Van Hest, J.C.M.4    Lowik, D.5
  • 26
    • 84868546970 scopus 로고    scopus 로고
    • Constrained and UV-activatable cell-penetrating peptides for intracellular delivery of liposomes
    • Hansen, M. B., van Gaal, E., Minten, I., Storm, G., van Hest, J. C. M., and Lowik, D. (2012) Constrained and UV-activatable cell-penetrating peptides for intracellular delivery of liposomes. J. Controlled Release 164, 87-94.
    • (2012) J. Controlled Release , vol.164 , pp. 87-94
    • Hansen, M.B.1    Van Gaal, E.2    Minten, I.3    Storm, G.4    Van Hest, J.C.M.5    Lowik, D.6
  • 28
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • Frankel, A. D., and Pabo, C. O. (1988) Cellular uptake of the tat protein from human immunodeficiency virus. Cell 55, 1189-1193.
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 29
    • 84880789806 scopus 로고    scopus 로고
    • Self-assembled Tat nanofibers as effective drug carrier and transporter
    • Zhang, P. C., Cheetham, A. G., Lin, Y. A., and Cui, H. (2013) Self-assembled Tat nanofibers as effective drug carrier and transporter. ACS Nano 7, 5965-5977.
    • (2013) ACS Nano , vol.7 , pp. 5965-5977
    • Zhang, P.C.1    Cheetham, A.G.2    Lin, Y.A.3    Cui, H.4
  • 30
    • 84876485742 scopus 로고    scopus 로고
    • Cellular uptake and cytotoxicity of drug-peptide conjugates regulated by conjugation site
    • Zhang, P. C., Cheetham, A. G., Lock, L. L., and Cui, H. G. (2013) Cellular uptake and cytotoxicity of drug-peptide conjugates regulated by conjugation site. Bioconjugate Chem. 24, 604-613.
    • (2013) Bioconjugate Chem. , vol.24 , pp. 604-613
    • Zhang, P.C.1    Cheetham, A.G.2    Lock, L.L.3    Cui, H.G.4
  • 31
    • 84901743395 scopus 로고    scopus 로고
    • Enhanced cellular entry and efficacy of Tat conjugates by rational design of the auxiliary segment
    • Zhang, P. C., Lock, L. L., Cheetham, A. G., and Cui, H. G. (2014) Enhanced cellular entry and efficacy of Tat conjugates by rational design of the auxiliary segment. Mol. Pharmaceutics 11, 964-973.
    • (2014) Mol. Pharmaceutics , vol.11 , pp. 964-973
    • Zhang, P.C.1    Lock, L.L.2    Cheetham, A.G.3    Cui, H.G.4
  • 32
    • 52249093974 scopus 로고    scopus 로고
    • Shape effects of nanoparticles conjugated with cell-penetrating peptides (HIV Tat PTD) on CHO cell uptake
    • Zhang, K., Fang, H. F., Chen, Z. Y., Taylor, J. S. A., and Wooley, K. L. (2008) Shape effects of nanoparticles conjugated with cell-penetrating peptides (HIV Tat PTD) on CHO cell uptake. Bioconjugate Chem. 19, 1880-1887.
    • (2008) Bioconjugate Chem. , vol.19 , pp. 1880-1887
    • Zhang, K.1    Fang, H.F.2    Chen, Z.Y.3    Taylor, J.S.A.4    Wooley, K.L.5
  • 33
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: The penetratin system for intracellular delivery
    • Derossi, D., Chassaing, G., and Prochiantz, A. (1998) Trojan peptides: the penetratin system for intracellular delivery. Trends Cell Biol. 8, 84-87.
    • (1998) Trends Cell Biol. , vol.8 , pp. 84-87
    • Derossi, D.1    Chassaing, G.2    Prochiantz, A.3
  • 34
    • 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. (2000) Polyarginine enters cells more efficiently than other polycationic homopolymers. J. Pept. Res. 56, 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
  • 36
    • 84896914760 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Design, synthesis, and applications
    • Copolovici, D. M., Langel, K., Eriste, E., and Langel, U. (2014) Cell-penetrating peptides: design, synthesis, and applications. ACS Nano 8, 1972-1994.
    • (2014) ACS Nano , vol.8 , pp. 1972-1994
    • Copolovici, D.M.1    Langel, K.2    Eriste, E.3    Langel, U.4
  • 37
    • 0001408455 scopus 로고
    • Histones and basic polyamino acids stimulate the uptake of albumin by tumor cells in culture
    • Ryser, H. J., and Hancock, R. (1965) Histones and basic polyamino acids stimulate the uptake of albumin by tumor cells in culture. Science 150, 501-3.
    • (1965) Science , vol.150 , pp. 501-503
    • Ryser, H.J.1    Hancock, R.2
  • 38
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia, J. S., Stan, R. V., and Dowdy, S. F. (2004) Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat. Med. 10, 310-315.
    • (2004) Nat. Med. , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 39
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus Tat trans-activator protein
    • Green, M., and Loewenstein, P. M. (1988) Autonomous functional domains of chemically synthesized human immunodeficiency virus Tat trans-activator protein. Cell 55, 1179-1188.
    • (1988) Cell , vol.55 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 40
    • 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. (2001) Arginine-rich peptides - An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276, 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
  • 41
    • 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., Youjun, Z., and Sugiura, Y. (2002) Translocation of branched-chain arginine peptides through cell membranes: flexibility in the spatial disposition of positive charges in membrane-permeable peptides. Biochemistry 41, 7925-7930.
    • (2002) Biochemistry , vol.41 , pp. 7925-7930
    • Futaki, S.1    Nakase, I.2    Suzuki, T.3    Youjun, Z.4    Sugiura, Y.5
  • 42
    • 0027502921 scopus 로고
    • The presequence of rat-liver aldehyde dehydrogenase requires the presence of an alpha-helix at its N-terminal region which is stabilized by the helix at its C-termini
    • Wang, Y., and Weiner, H. (1993) The presequence of rat-liver aldehyde dehydrogenase requires the presence of an alpha-helix at its N-terminal region which is stabilized by the helix at its C-termini. J. Biol. Chem. 268, 4759-4765.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4759-4765
    • Wang, Y.1    Weiner, H.2
  • 43
    • 67749115965 scopus 로고    scopus 로고
    • Enhanced intracellular delivery using arginine-rich peptides by the addition of penetration accelerating sequences (Pas)
    • Takayama, K., Nakase, I., Michiue, H., Takeuchi, T., Tomizawa, K., Matsui, H., and Futaki, S. (2009) Enhanced intracellular delivery using arginine-rich peptides by the addition of penetration accelerating sequences (Pas). J. Controlled Release 138, 128-133.
    • (2009) J. Controlled Release , vol.138 , pp. 128-133
    • Takayama, K.1    Nakase, I.2    Michiue, H.3    Takeuchi, T.4    Tomizawa, K.5    Matsui, H.6    Futaki, S.7
  • 45
    • 0021281777 scopus 로고
    • Endosome pH measured in single cells by dual fluorescence flow-cytometry - Rapid acidification of insulin to pH-6
    • Murphy, R. F., Powers, S., and Cantor, C. R. (1984) Endosome pH measured in single cells by dual fluorescence flow-cytometry - rapid acidification of insulin to pH-6. J. Cell Biol. 98, 1757-1762.
    • (1984) J. Cell Biol. , vol.98 , pp. 1757-1762
    • Murphy, R.F.1    Powers, S.2    Cantor, C.R.3
  • 46
    • 56749104130 scopus 로고    scopus 로고
    • Fluorescent probes for super-resolution imaging in living cells
    • Fernandez-Suarez, M., and Ting, A. Y. (2008) Fluorescent probes for super-resolution imaging in living cells. Nat. Rev. Mol. Cell Biol. 9, 929-943.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 929-943
    • Fernandez-Suarez, M.1    Ting, A.Y.2
  • 47
    • 0021367562 scopus 로고
    • Effects of DEAE-dextran on infection and hemolysis by VSV. Evidence that nonspecific electrostatic interactions mediate effective binding of VSV to cells
    • Bailey, C. A., Miller, D. K., and Lenard, J. (1984) Effects of DEAE-dextran on infection and hemolysis by VSV. Evidence that nonspecific electrostatic interactions mediate effective binding of VSV to cells. Virology 133, 111-118.
    • (1984) Virology , vol.133 , pp. 111-118
    • Bailey, C.A.1    Miller, D.K.2    Lenard, J.3
  • 48
    • 84867402736 scopus 로고    scopus 로고
    • Dual-functional liposomes based on pH-responsive cell-penetrating peptide and hyaluronic acid for tumor-targeted anticancer drug delivery
    • Jiang, T. Y., Zhang, Z. H., Zhang, Y. L., Lv, H. X., Zhou, J. P., Li, C. C., Hou, L. L., and Zhang, Q. (2012) Dual-functional liposomes based on pH-responsive cell-penetrating peptide and hyaluronic acid for tumor-targeted anticancer drug delivery. Biomaterials 33, 9246-9258.
    • (2012) Biomaterials , vol.33 , pp. 9246-9258
    • Jiang, T.Y.1    Zhang, Z.H.2    Zhang, Y.L.3    Lv, H.X.4    Zhou, J.P.5    Li, C.C.6    Hou, L.L.7    Zhang, Q.8
  • 49
    • 84864402585 scopus 로고    scopus 로고
    • Arginine topology controls escape of minimally cationic proteins from early endosomes to the cytoplasm
    • Appelbaum, J. S., LaRochelle, J. R., Smith, B. A., Balkin, D. M., Holub, J. M., and Schepartz, A. (2012) Arginine topology controls escape of minimally cationic proteins from early endosomes to the cytoplasm. Chem. Biol. 19, 819-830.
    • (2012) Chem. Biol. , vol.19 , pp. 819-830
    • Appelbaum, J.S.1    LaRochelle, J.R.2    Smith, B.A.3    Balkin, D.M.4    Holub, J.M.5    Schepartz, A.6
  • 50
    • 0035853015 scopus 로고    scopus 로고
    • Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR
    • Lindberg, M., Jarvet, J., Langel, U., and Graslund, A. (2001) Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR. Biochemistry 40, 3141-3149.
    • (2001) Biochemistry , vol.40 , pp. 3141-3149
    • Lindberg, M.1    Jarvet, J.2    Langel, U.3    Graslund, A.4
  • 51
    • 0035795727 scopus 로고    scopus 로고
    • Interaction and structure induction of cell-penetrating peptides in the presence of phospholipid vesicles
    • Magzoub, M., Kilk, K., Eriksson, L. E. G., Langel, U., and Graslund, A. (2001) Interaction and structure induction of cell-penetrating peptides in the presence of phospholipid vesicles. Biochim. Biophys. Acta, Biomembr. 1512 , 77-89.
    • (2001) Biochim. Biophys. Acta, Biomembr. , vol.1512 , pp. 77-89
    • Magzoub, M.1    Kilk, K.2    Eriksson, L.E.G.3    Langel, U.4    Graslund, A.5
  • 52
    • 0037071786 scopus 로고    scopus 로고
    • Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: Effects of surface charge and peptide concentration
    • Magzoub, M., Eriksson, L. E. G., and Graslund, A. (2002) Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: effects of surface charge and peptide concentration. Biochim. Biophys. Acta, Biomembr. 1563, 53-63.
    • (2002) Biochim. Biophys. Acta, Biomembr. , vol.1563 , pp. 53-63
    • Magzoub, M.1    Eriksson, L.E.G.2    Graslund, A.3
  • 53
    • 77952580991 scopus 로고    scopus 로고
    • Secondary structure of cell-penetrating peptides controls membrane interaction and insertion
    • Eiriksdottir, E., Konate, K., Langel, U., Divita, G., and Deshayes, S. (2010) Secondary structure of cell-penetrating peptides controls membrane interaction and insertion. Biochim. Biophys. Acta, Biomembr. 1798, 1119-1128.
    • (2010) Biochim. Biophys. Acta, Biomembr. , vol.1798 , pp. 1119-1128
    • Eiriksdottir, E.1    Konate, K.2    Langel, U.3    Divita, G.4    Deshayes, S.5
  • 54
    • 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. (2000) 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. Proc. Natl. Acad. Sci. U.S.A. 97, 8245-8250.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 55
    • 34250835903 scopus 로고    scopus 로고
    • A comprehensive model for the cellular uptake of cationic cell-penetrating peptides
    • Duchardt, F., Fotin-Mleczek, M., Schwarz, H., Fischer, R., and Brock, R. (2007) A comprehensive model for the cellular uptake of cationic cell-penetrating peptides. Traffic 8, 848-866.
    • (2007) Traffic , vol.8 , pp. 848-866
    • Duchardt, F.1    Fotin-Mleczek, M.2    Schwarz, H.3    Fischer, R.4    Brock, R.5
  • 56
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert, W., and Herrmann, J. M. (2007) Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76, 723-749.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 57
    • 84867089289 scopus 로고    scopus 로고
    • Engineering of blended nanoparticle platform for delivery of mitochondria-acting therapeutics
    • Marrache, S., and Dhar, S. (2012) Engineering of blended nanoparticle platform for delivery of mitochondria-acting therapeutics. Proc. Natl. Acad. Sci. U.S.A. 109, 16288-16293.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 16288-16293
    • Marrache, S.1    Dhar, S.2
  • 58
    • 52049115848 scopus 로고    scopus 로고
    • Organelle-targeted nanocarriers: Specific delivery of liposomal ceramide to mitochondria enhances its cytotoxicity in vitro and in vivo
    • Boddapati, S. V., D'Souza, G. G. M., Erdogan, S., Torchilin, V. P., and Weissig, V. (2008) Organelle-targeted nanocarriers: Specific delivery of liposomal ceramide to mitochondria enhances its cytotoxicity in vitro and in vivo. Nano Lett. 8, 2559-2563.
    • (2008) Nano Lett. , vol.8 , pp. 2559-2563
    • Boddapati, S.V.1    D'Souza, G.G.M.2    Erdogan, S.3    Torchilin, V.P.4    Weissig, V.5
  • 60
    • 23044459574 scopus 로고    scopus 로고
    • Differences in subcellular distribution and toxicity of green and red emitting CdTe quantum dots
    • Lovric, J., Bazzi, H. S., Cuie, Y., Fortin, G. R. A., Winnik, F. M., and Maysinger, D. (2005) Differences in subcellular distribution and toxicity of green and red emitting CdTe quantum dots. J. Mol. Med. 83, 377-385.
    • (2005) J. Mol. Med. , vol.83 , pp. 377-385
    • Lovric, J.1    Bazzi, H.S.2    Cuie, Y.3    Fortin, G.R.A.4    Winnik, F.M.5    Maysinger, D.6


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