메뉴 건너뛰기




Volumn 62, Issue 15, 2010, Pages 1486-1496

Cell penetrating elastin-like polypeptides for therapeutic peptide delivery

Author keywords

C Myc; Cell penetrating peptide; Elastin like polypeptide; P21; Therapeutic peptide; Thermal targeting

Indexed keywords

C-MYC; CELL PENETRATING PEPTIDE; ELASTIN-LIKE POLYPEPTIDES; P21; THERAPEUTIC PEPTIDES; THERMAL TARGETING;

EID: 78649846843     PISSN: 0169409X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.addr.2010.05.003     Document Type: Review
Times cited : (94)

References (78)
  • 1
    • 34547653668 scopus 로고    scopus 로고
    • Enhanced permeability and retention of macromolecular drugs in solid tumors: a royal gate for targeted anticancer nanomedicines
    • Greish K. Enhanced permeability and retention of macromolecular drugs in solid tumors: a royal gate for targeted anticancer nanomedicines. J. Drug Target. 2007, 15(7-8):457-464.
    • (2007) J. Drug Target. , vol.15 , Issue.7-8 , pp. 457-464
    • Greish, K.1
  • 2
    • 33747762229 scopus 로고    scopus 로고
    • Exploiting the enhanced permeability and retention effect for tumor targeting
    • Iyer A.K., Khaled G., Fang J., Maeda H. Exploiting the enhanced permeability and retention effect for tumor targeting. Drug Discov. Today 2006, 11(17-18):812-818.
    • (2006) Drug Discov. Today , vol.11 , Issue.17-18 , pp. 812-818
    • Iyer, A.K.1    Khaled, G.2    Fang, J.3    Maeda, H.4
  • 3
    • 60749108001 scopus 로고    scopus 로고
    • Polymeric drugs for efficient tumor-targeted drug delivery based on EPR-effect
    • Maeda H., Bharate G.Y., Daruwalla J. Polymeric drugs for efficient tumor-targeted drug delivery based on EPR-effect. Eur. J. Pharm. Biopharm. 2009, 71(3):409-419.
    • (2009) Eur. J. Pharm. Biopharm. , vol.71 , Issue.3 , pp. 409-419
    • Maeda, H.1    Bharate, G.Y.2    Daruwalla, J.3
  • 5
    • 42649145864 scopus 로고    scopus 로고
    • Poly (amino acid) micelle nanocarriers in preclinical and clinical studies
    • Matsumura Y. Poly (amino acid) micelle nanocarriers in preclinical and clinical studies. Adv. Drug Deliv. Rev. 2008, 60(8):899-914.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , Issue.8 , pp. 899-914
    • Matsumura, Y.1
  • 6
    • 29544448116 scopus 로고    scopus 로고
    • Polymer conjugates: nanosized medicines for treating cancer
    • Vicent M.J., Duncan R. Polymer conjugates: nanosized medicines for treating cancer. Trends Biotechnol. 2006, 24(1):39-47.
    • (2006) Trends Biotechnol. , vol.24 , Issue.1 , pp. 39-47
    • Vicent, M.J.1    Duncan, R.2
  • 7
    • 70349386390 scopus 로고    scopus 로고
    • Biodegradable amphiphilic polymer-drug conjugate micelles
    • Hu X., Jing X. Biodegradable amphiphilic polymer-drug conjugate micelles. Expert Opin. Drug Deliv. 2009, 6(10):1079-1090.
    • (2009) Expert Opin. Drug Deliv. , vol.6 , Issue.10 , pp. 1079-1090
    • Hu, X.1    Jing, X.2
  • 10
    • 0022370012 scopus 로고
    • Phase-structure transitions of the elastin polypentapeptide-water system within the framework of composition-temperature studies
    • Urry D.W., Trapane T.L., Prasad K.U. Phase-structure transitions of the elastin polypentapeptide-water system within the framework of composition-temperature studies. Biopolymers 1985, 24(12):2345-2356.
    • (1985) Biopolymers , vol.24 , Issue.12 , pp. 2345-2356
    • Urry, D.W.1    Trapane, T.L.2    Prasad, K.U.3
  • 11
    • 0026468684 scopus 로고
    • Free energy transduction in polypeptides and proteins based on inverse temperature transitions
    • Urry D.W. Free energy transduction in polypeptides and proteins based on inverse temperature transitions. Prog. Biophys. Mol. Biol. 1992, 57(1):23-57.
    • (1992) Prog. Biophys. Mol. Biol. , vol.57 , Issue.1 , pp. 23-57
    • Urry, D.W.1
  • 12
    • 0035866357 scopus 로고    scopus 로고
    • Targeting a genetically engineered elastin-like polypeptide to solid tumors by local hyperthermia
    • Meyer D.E., Kong G.A., Dewhirst M.W., Zalutsky M.R., Chilkoti A. Targeting a genetically engineered elastin-like polypeptide to solid tumors by local hyperthermia. Cancer Res. 2001, 61(4):1548-1554.
    • (2001) Cancer Res. , vol.61 , Issue.4 , pp. 1548-1554
    • Meyer, D.E.1    Kong, G.A.2    Dewhirst, M.W.3    Zalutsky, M.R.4    Chilkoti, A.5
  • 13
    • 34249316870 scopus 로고    scopus 로고
    • Thermal cycling enhances the accumulation of a temperature-sensitive biopolymer in solid tumors
    • Dreher M.R., Liu W., Michelich C.R., Dewhirst M.W., Chilkoti A. Thermal cycling enhances the accumulation of a temperature-sensitive biopolymer in solid tumors. Cancer Res. 2007, 67(9):4418-4424.
    • (2007) Cancer Res. , vol.67 , Issue.9 , pp. 4418-4424
    • Dreher, M.R.1    Liu, W.2    Michelich, C.R.3    Dewhirst, M.W.4    Chilkoti, A.5
  • 15
    • 0029206160 scopus 로고
    • Regional hyperthermia combined with systemic chemotherapy of locally advanced sarcomas: preclinical aspects and clinical results
    • Issels R.D. Regional hyperthermia combined with systemic chemotherapy of locally advanced sarcomas: preclinical aspects and clinical results. Recent Results Cancer Res. 1995, 138:81-90.
    • (1995) Recent Results Cancer Res. , vol.138 , pp. 81-90
    • Issels, R.D.1
  • 16
    • 0030767539 scopus 로고    scopus 로고
    • Rationale and clinical status of local hyperthermia, radiation, and chemotherapy in locally advanced malignancies
    • Feyerabend T., Steeves R., Wiedemann G.J., Richter E., Robins H.I. Rationale and clinical status of local hyperthermia, radiation, and chemotherapy in locally advanced malignancies. Anticancer Res. 1997, 17(4B):2895-2897.
    • (1997) Anticancer Res. , vol.17 , Issue.4 B , pp. 2895-2897
    • Feyerabend, T.1    Steeves, R.2    Wiedemann, G.J.3    Richter, E.4    Robins, H.I.5
  • 18
    • 47249140485 scopus 로고    scopus 로고
    • Regional hyperthermia in high-risk soft tissue sarcomas
    • Issels R.D. Regional hyperthermia in high-risk soft tissue sarcomas. Curr. Opin. Oncol. 2008, 20(4):438-443.
    • (2008) Curr. Opin. Oncol. , vol.20 , Issue.4 , pp. 438-443
    • Issels, R.D.1
  • 21
    • 0036163396 scopus 로고    scopus 로고
    • Clinical application of hyperthermia combined with anticancer drugs for the treatment of solid tumors
    • Takahashi I., Emi Y., Hasuda S., Kakeji Y., Maehara Y., Sugimachi K. Clinical application of hyperthermia combined with anticancer drugs for the treatment of solid tumors. Surgery 2002, 131(1 Suppl):S78-84.
    • (2002) Surgery , vol.131 , Issue.1 SUPPL
    • Takahashi, I.1    Emi, Y.2    Hasuda, S.3    Kakeji, Y.4    Maehara, Y.5    Sugimachi, K.6
  • 22
    • 0033302303 scopus 로고    scopus 로고
    • Transport of molecules, particles, and cells in solid tumors
    • Jain R.K. Transport of molecules, particles, and cells in solid tumors. Annu. Rev. Biomed. Eng. 1999, 1:241-263.
    • (1999) Annu. Rev. Biomed. Eng. , vol.1 , pp. 241-263
    • Jain, R.K.1
  • 23
    • 0024505574 scopus 로고
    • Delivery of novel therapeutic agents in tumors: physiological barriers and strategies
    • Jain R.K. Delivery of novel therapeutic agents in tumors: physiological barriers and strategies. J. Natl Cancer Inst. 1989, 81(8):570-576.
    • (1989) J. Natl Cancer Inst. , vol.81 , Issue.8 , pp. 570-576
    • Jain, R.K.1
  • 24
    • 0023481357 scopus 로고
    • Transport of molecules across tumor vasculature
    • Jain R.K. Transport of molecules across tumor vasculature. Cancer Metastasis Rev. 1987, 6(4):559-593.
    • (1987) Cancer Metastasis Rev. , vol.6 , Issue.4 , pp. 559-593
    • Jain, R.K.1
  • 25
    • 13944258970 scopus 로고    scopus 로고
    • Intracellular targeting of polymer-bound drugs for cancer chemotherapy
    • Nori A., Kopecek J. Intracellular targeting of polymer-bound drugs for cancer chemotherapy. Adv. Drug Deliv. Rev. 2005, 57(4):609-636.
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , Issue.4 , pp. 609-636
    • Nori, A.1    Kopecek, J.2
  • 26
    • 1542721107 scopus 로고    scopus 로고
    • Cell penetrating peptides in drug delivery
    • Snyder E.L., Dowdy S.F. Cell penetrating peptides in drug delivery. Pharm. Res. 2004, 21(3):389-393.
    • (2004) Pharm. Res. , vol.21 , Issue.3 , pp. 389-393
    • Snyder, E.L.1    Dowdy, S.F.2
  • 27
    • 9644289511 scopus 로고    scopus 로고
    • The use of cell-penetrating peptides for drug delivery
    • Temsamani J., Vidal P. The use of cell-penetrating peptides for drug delivery. Drug Discov. Today 2004, 9(23):1012-1019.
    • (2004) Drug Discov. Today , vol.9 , Issue.23 , pp. 1012-1019
    • Temsamani, J.1    Vidal, P.2
  • 28
    • 13844298046 scopus 로고    scopus 로고
    • Intracellular delivery of large molecules and small particles by cell-penetrating proteins and peptides
    • Gupta B., Levchenko T.S., Torchilin V.P. Intracellular delivery of large molecules and small particles by cell-penetrating proteins and peptides. Adv. Drug Deliv. Rev. 2005, 57(4):637-651.
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , Issue.4 , pp. 637-651
    • Gupta, B.1    Levchenko, T.S.2    Torchilin, V.P.3
  • 29
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cell-penetrating peptides: from molecular mechanisms to therapeutics
    • Heitz F., Morris M.C., Divita G. Twenty years of cell-penetrating peptides: from molecular mechanisms to therapeutics. Br. J. Pharmacol. 2009, 157(2):195-206.
    • (2009) Br. J. Pharmacol. , vol.157 , Issue.2 , pp. 195-206
    • Heitz, F.1    Morris, M.C.2    Divita, G.3
  • 30
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: delivery of a biologically active protein into the mouse
    • Schwarze S.R., Ho A., Vocero-Akbani A., Dowdy S.F. In vivo protein transduction: delivery of a biologically active protein into the mouse. Science 1999, 285(5433):1569-1572.
    • (1999) Science , vol.285 , Issue.5433 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 31
    • 0034126420 scopus 로고    scopus 로고
    • New advances in the transport of doxorubicin through the blood-brain barrier by a peptide vector-mediated strategy
    • Rousselle C., Clair P., Lefauconnier J.M., Kaczorek M., Scherrmann J.M., Temsamani J. New advances in the transport of doxorubicin through the blood-brain barrier by a peptide vector-mediated strategy. Mol. Pharmacol. 2000, 57(4):679-686.
    • (2000) Mol. Pharmacol. , vol.57 , Issue.4 , pp. 679-686
    • Rousselle, C.1    Clair, P.2    Lefauconnier, J.M.3    Kaczorek, M.4    Scherrmann, J.M.5    Temsamani, J.6
  • 32
    • 85046914841 scopus 로고    scopus 로고
    • Peptide delivery to the brain via adsorptive-mediated endocytosis: advances with SynB vectors
    • Drin G., Rousselle C., Scherrmann J.M., Rees A.R., Temsamani J. Peptide delivery to the brain via adsorptive-mediated endocytosis: advances with SynB vectors. AAPS Pharm. Sci. 2002, 4(4):E26.
    • (2002) AAPS Pharm. Sci. , vol.4 , Issue.4
    • Drin, G.1    Rousselle, C.2    Scherrmann, J.M.3    Rees, A.R.4    Temsamani, J.5
  • 33
    • 33846434451 scopus 로고    scopus 로고
    • Applications of a blood-brain barrier technology platform to predict CNS penetration of various chemotherapeutic agents. 2. Cationic peptide vectors for brain delivery
    • Adenot M., Merida P., Lahana R. Applications of a blood-brain barrier technology platform to predict CNS penetration of various chemotherapeutic agents. 2. Cationic peptide vectors for brain delivery. Chemotherapy 2007, 53(1):73-76.
    • (2007) Chemotherapy , vol.53 , Issue.1 , pp. 73-76
    • Adenot, M.1    Merida, P.2    Lahana, R.3
  • 34
    • 56049093057 scopus 로고    scopus 로고
    • Cell-penetrating and cell-targeting peptides in drug delivery
    • Vives E., Schmidt J., Pelegrin A. Cell-penetrating and cell-targeting peptides in drug delivery. Biochim. Biophys. Acta 2008, 1786(2):126-138.
    • (2008) Biochim. Biophys. Acta , vol.1786 , Issue.2 , pp. 126-138
    • Vives, E.1    Schmidt, J.2    Pelegrin, A.3
  • 35
    • 23144442466 scopus 로고    scopus 로고
    • Application of thermally responsive polypeptides directed against c-Myc transcriptional function for cancer therapy
    • Bidwell G.L., Raucher D. Application of thermally responsive polypeptides directed against c-Myc transcriptional function for cancer therapy. Mol. Cancer Ther. 2005, 4(7):1076-1085.
    • (2005) Mol. Cancer Ther. , vol.4 , Issue.7 , pp. 1076-1085
    • Bidwell, G.L.1    Raucher, D.2
  • 36
    • 61649103094 scopus 로고    scopus 로고
    • Targeting a c-Myc inhibitory polypeptide to specific intracellular compartments using cell penetrating peptides
    • Bidwell G.L., Davis A.N., Raucher D. Targeting a c-Myc inhibitory polypeptide to specific intracellular compartments using cell penetrating peptides. J. Control. Release 2009, 135(1):2-10.
    • (2009) J. Control. Release , vol.135 , Issue.1 , pp. 2-10
    • Bidwell, G.L.1    Davis, A.N.2    Raucher, D.3
  • 37
    • 33846510441 scopus 로고    scopus 로고
    • Development of elastin-like polypeptide for thermally targeted delivery of doxorubicin
    • Bidwell G.L., Fokt I., Priebe W., Raucher D. Development of elastin-like polypeptide for thermally targeted delivery of doxorubicin. Biochem. Pharmacol. 2007, 73(5):620-631.
    • (2007) Biochem. Pharmacol. , vol.73 , Issue.5 , pp. 620-631
    • Bidwell, G.L.1    Fokt, I.2    Priebe, W.3    Raucher, D.4
  • 38
    • 27744525788 scopus 로고    scopus 로고
    • Evaluation of cell penetrating peptides fused to elastin-like polypeptide for drug delivery
    • Massodi I., Bidwell G.L., Raucher D. Evaluation of cell penetrating peptides fused to elastin-like polypeptide for drug delivery. J. Control. Release 2005, 108(2-3):396-408.
    • (2005) J. Control. Release , vol.108 , Issue.2-3 , pp. 396-408
    • Massodi, I.1    Bidwell, G.L.2    Raucher, D.3
  • 39
    • 70349388055 scopus 로고    scopus 로고
    • Therapeutic peptides for cancer therapy. Part I-peptide inhibitors of signal transduction cascades
    • Bidwell G.L., Raucher D. Therapeutic peptides for cancer therapy. Part I-peptide inhibitors of signal transduction cascades. Expert Opin. Drug Deliv. 2009, 6(10):1033-1047.
    • (2009) Expert Opin. Drug Deliv. , vol.6 , Issue.10 , pp. 1033-1047
    • Bidwell, G.L.1    Raucher, D.2
  • 40
    • 70349383205 scopus 로고    scopus 로고
    • Therapeutic peptides for cancer therapy. Part II-Cell cycle inhibitory peptides and apoptosis-inducing peptides
    • Raucher D., Moktan S., Massodi I., Bidwell G.L. Therapeutic peptides for cancer therapy. Part II-Cell cycle inhibitory peptides and apoptosis-inducing peptides. Expert Opin. Drug Deliv. 2009, 6(10):1049-1064.
    • (2009) Expert Opin. Drug Deliv. , vol.6 , Issue.10 , pp. 1049-1064
    • Raucher, D.1    Moktan, S.2    Massodi, I.3    Bidwell, G.L.4
  • 41
    • 0029885070 scopus 로고    scopus 로고
    • Transmembrane transport of peptide type compounds: prospects for oral delivery
    • Lipka E., Crison J., Amidon G.L. Transmembrane transport of peptide type compounds: prospects for oral delivery. J. Control. Release 1996, 39(2-3):121-129.
    • (1996) J. Control. Release , vol.39 , Issue.2-3 , pp. 121-129
    • Lipka, E.1    Crison, J.2    Amidon, G.L.3
  • 42
    • 0032494119 scopus 로고    scopus 로고
    • Pharmacodynamic aspects of peptide administration biological response modifiers
    • Talmadge J.E. Pharmacodynamic aspects of peptide administration biological response modifiers. Adv. Drug Deliv. Rev. 1998, 33(3):241-252.
    • (1998) Adv. Drug Deliv. Rev. , vol.33 , Issue.3 , pp. 241-252
    • Talmadge, J.E.1
  • 43
    • 0034601281 scopus 로고    scopus 로고
    • Biodegradable nanoparticles for oral delivery of peptides: is there a role for polymers to affect mucosal uptake?
    • Jung T., Kamm W., Breitenbach A., Kaiserling E., Xiao J.X., Kissel T. Biodegradable nanoparticles for oral delivery of peptides: is there a role for polymers to affect mucosal uptake?. Eur. J. Pharm. Biopharm. 2000, 50(1):147-160.
    • (2000) Eur. J. Pharm. Biopharm. , vol.50 , Issue.1 , pp. 147-160
    • Jung, T.1    Kamm, W.2    Breitenbach, A.3    Kaiserling, E.4    Xiao, J.X.5    Kissel, T.6
  • 44
    • 0038725603 scopus 로고    scopus 로고
    • TAT-liposomes: a novel intracellular drug carrier
    • Torchilin V.P., Levchenko T.S. TAT-liposomes: a novel intracellular drug carrier. Curr. Protein Pept. Sci. 2003, 4(2):133-140.
    • (2003) Curr. Protein Pept. Sci. , vol.4 , Issue.2 , pp. 133-140
    • Torchilin, V.P.1    Levchenko, T.S.2
  • 45
    • 70549101139 scopus 로고    scopus 로고
    • Self-assembling chimeric polypeptide-doxorubicin conjugate nanoparticles that abolish tumours after a single injection
    • MacKay J.A., Chen M., McDaniel J.R., Liu W., Simnick A.J., Chilkoti A. Self-assembling chimeric polypeptide-doxorubicin conjugate nanoparticles that abolish tumours after a single injection. Nat. Mater. 2009, 8(12):993-999.
    • (2009) Nat. Mater. , vol.8 , Issue.12 , pp. 993-999
    • MacKay, J.A.1    Chen, M.2    McDaniel, J.R.3    Liu, W.4    Simnick, A.J.5    Chilkoti, A.6
  • 47
    • 34250620539 scopus 로고    scopus 로고
    • A thermally targeted elastin-like polypeptide-doxorubicin conjugate overcomes drug resistance
    • Bidwell G.L., Davis A.N., Fokt I., Priebe W., Raucher D. A thermally targeted elastin-like polypeptide-doxorubicin conjugate overcomes drug resistance. Investig. New Drugs 2007, 25(4):313-326.
    • (2007) Investig. New Drugs , vol.25 , Issue.4 , pp. 313-326
    • Bidwell, G.L.1    Davis, A.N.2    Fokt, I.3    Priebe, W.4    Raucher, D.5
  • 48
    • 40549142439 scopus 로고    scopus 로고
    • Intelligent biosynthetic nanobiomaterials (IBNs) for hyperthermic gene delivery
    • Chen T.H., Bae Y., Furgeson D.Y. Intelligent biosynthetic nanobiomaterials (IBNs) for hyperthermic gene delivery. Pharm. Res. 2008, 25(3):683-691.
    • (2008) Pharm. Res. , vol.25 , Issue.3 , pp. 683-691
    • Chen, T.H.1    Bae, Y.2    Furgeson, D.Y.3
  • 49
    • 67649834226 scopus 로고    scopus 로고
    • Application of thermally responsive elastin-like polypeptide fused to a lactoferrin-derived peptide for treatment of pancreatic cancer
    • Massodi I., Thomas E., Raucher D. Application of thermally responsive elastin-like polypeptide fused to a lactoferrin-derived peptide for treatment of pancreatic cancer. Molecules 2009, 14(6):1999-2015.
    • (2009) Molecules , vol.14 , Issue.6 , pp. 1999-2015
    • Massodi, I.1    Thomas, E.2    Raucher, D.3
  • 50
    • 73549108720 scopus 로고    scopus 로고
    • Inhibition of ovarian cancer cell proliferation by a cell cycle inhibitory peptide fused to a thermally responsive polypeptide carrier
    • Massodi I., Moktan S., Rawat A., Bidwell G.L., Raucher D. Inhibition of ovarian cancer cell proliferation by a cell cycle inhibitory peptide fused to a thermally responsive polypeptide carrier. Int. J. Cancer 2010, 126(2):533-544.
    • (2010) Int. J. Cancer , vol.126 , Issue.2 , pp. 533-544
    • Massodi, I.1    Moktan, S.2    Rawat, A.3    Bidwell, G.L.4    Raucher, D.5
  • 52
    • 0036200174 scopus 로고    scopus 로고
    • Genetically encoded synthesis of protein-based polymers with precisely specified molecular weight and sequence by recursive directional ligation: examples from the elastin-like polypeptide system
    • Meyer D.E., Chilkoti A. Genetically encoded synthesis of protein-based polymers with precisely specified molecular weight and sequence by recursive directional ligation: examples from the elastin-like polypeptide system. Biomacromolecules 2002, 3(2):357-367.
    • (2002) Biomacromolecules , vol.3 , Issue.2 , pp. 357-367
    • Meyer, D.E.1    Chilkoti, A.2
  • 53
    • 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. 1994, 269(14):10444-10450.
    • (1994) J. Biol. Chem. , vol.269 , Issue.14 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 54
    • 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., 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. 1997, 272(25):16010-16017.
    • (1997) J. Biol. Chem. , vol.272 , Issue.25 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 55
    • 0029006149 scopus 로고
    • Inhibition of nuclear translocation of transcription factor NF-kappa B by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence
    • Lin Y.Z., Yao S.Y., Veach R.A., Torgerson T.R., Hawiger J. Inhibition of nuclear translocation of transcription factor NF-kappa B by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence. J. Biol. Chem. 1995, 270(24):14255-14258.
    • (1995) J. Biol. Chem. , vol.270 , Issue.24 , pp. 14255-14258
    • Lin, Y.Z.1    Yao, S.Y.2    Veach, R.A.3    Torgerson, T.R.4    Hawiger, J.5
  • 56
    • 0037016020 scopus 로고    scopus 로고
    • Translocating proline-rich peptides from the antimicrobial peptide bactenecin 7
    • Sadler K., Eom K.D., Yang J.L., Dimitrova Y., Tam J.P. Translocating proline-rich peptides from the antimicrobial peptide bactenecin 7. Biochemistry 2002, 41(48):14150-14157.
    • (2002) Biochemistry , vol.41 , Issue.48 , pp. 14150-14157
    • Sadler, K.1    Eom, K.D.2    Yang, J.L.3    Dimitrova, Y.4    Tam, J.P.5
  • 58
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: the penetratin system for intracellular delivery
    • Derossi D., Chassaing G., Prochiantz A. Trojan peptides: the penetratin system for intracellular delivery. Trends Cell. Biol. 1998, 8(2):84-87.
    • (1998) Trends Cell. Biol. , vol.8 , Issue.2 , pp. 84-87
    • Derossi, D.1    Chassaing, G.2    Prochiantz, A.3
  • 59
  • 60
    • 59849102702 scopus 로고    scopus 로고
    • Protein transduction revisited: novel insights into the mechanism underlying intracellular delivery of proteins
    • Edenhofer F. Protein transduction revisited: novel insights into the mechanism underlying intracellular delivery of proteins. Curr. Pharm. Des. 2008, 14(34):3628-3636.
    • (2008) Curr. Pharm. Des. , vol.14 , Issue.34 , pp. 3628-3636
    • Edenhofer, F.1
  • 61
    • 0024595608 scopus 로고
    • Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation
    • Heuser J.E., Anderson R.G. Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation. J. Cell. Biol. 1989, 108(2):389-400.
    • (1989) J. Cell. Biol. , vol.108 , Issue.2 , pp. 389-400
    • Heuser, J.E.1    Anderson, R.G.2
  • 62
    • 0036146652 scopus 로고    scopus 로고
    • Caveolae and cholesterol distribution in vascular smooth muscle cells of different phenotypes
    • Thyberg J. Caveolae and cholesterol distribution in vascular smooth muscle cells of different phenotypes. J. Histochem. Cytochem. 2002, 50(2):185-195.
    • (2002) J. Histochem. Cytochem. , vol.50 , Issue.2 , pp. 185-195
    • Thyberg, J.1
  • 63
    • 0036781812 scopus 로고    scopus 로고
    • C-MYC: more than just a matter of life and death
    • Pelengaris S., Khan M., Evan G. c-MYC: more than just a matter of life and death. Nat. Rev. Cancer 2002, 2(10):764-776.
    • (2002) Nat. Rev. Cancer , vol.2 , Issue.10 , pp. 764-776
    • Pelengaris, S.1    Khan, M.2    Evan, G.3
  • 64
    • 0028125659 scopus 로고
    • Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR
    • Draeger L.J., Mullen G.P. Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR. J. Biol. Chem. 1994, 269(3):1785-1793.
    • (1994) J. Biol. Chem. , vol.269 , Issue.3 , pp. 1785-1793
    • Draeger, L.J.1    Mullen, G.P.2
  • 66
    • 0035227317 scopus 로고    scopus 로고
    • A retro-inverso peptide homologous to helix 1 of c-Myc is a potent and specific inhibitor of proliferation in different cellular systems
    • Pescarolo M.P., Bagnasco L., Malacarne D., Melchiori A., Valente P., Millo E., Bruno S., Basso S., Parodi S. A retro-inverso peptide homologous to helix 1 of c-Myc is a potent and specific inhibitor of proliferation in different cellular systems. FASEB J. 2001, 15(1):31-33.
    • (2001) FASEB J. , vol.15 , Issue.1 , pp. 31-33
    • Pescarolo, M.P.1    Bagnasco, L.2    Malacarne, D.3    Melchiori, A.4    Valente, P.5    Millo, E.6    Bruno, S.7    Basso, S.8    Parodi, S.9
  • 67
    • 29144445979 scopus 로고    scopus 로고
    • Enhancing the antiproliferative effect of topoisomerase II inhibitors using a polypeptide inhibitor of c-Myc
    • Bidwell G.L., Raucher D. Enhancing the antiproliferative effect of topoisomerase II inhibitors using a polypeptide inhibitor of c-Myc. Biochem. Pharmacol. 2006, 71(3):248-256.
    • (2006) Biochem. Pharmacol. , vol.71 , Issue.3 , pp. 248-256
    • Bidwell, G.L.1    Raucher, D.2
  • 68
    • 0023606220 scopus 로고
    • Effect of polyamine depletion by alpha-difluoromethylornithine or (2R, 5R)-6-heptyne-2, 5-diamine on drug-induced topoisomerase II-mediated DNA cleavage and cytotoxicity in human and murine leukemia cells
    • Bakic M., Chan D., Freireich E.J., Marton L.J., Zwelling L.A. Effect of polyamine depletion by alpha-difluoromethylornithine or (2R, 5R)-6-heptyne-2, 5-diamine on drug-induced topoisomerase II-mediated DNA cleavage and cytotoxicity in human and murine leukemia cells. Cancer Res. 1987, 47(24 Pt 1):6437-6443.
    • (1987) Cancer Res. , vol.47 , Issue.24 PART 1 , pp. 6437-6443
    • Bakic, M.1    Chan, D.2    Freireich, E.J.3    Marton, L.J.4    Zwelling, L.A.5
  • 69
    • 0030895361 scopus 로고    scopus 로고
    • Treatment with inhibitors of polyamine biosynthesis, which selectively lower intracellular spermine, does not affect the activity of alkylating agents but antagonizes the cytotoxicity of DNA topoisomerase II inhibitors
    • Desiderio M.A., Bergamaschi D., Mascellani E., De Feudis P., Erba E., D'Incalci M. Treatment with inhibitors of polyamine biosynthesis, which selectively lower intracellular spermine, does not affect the activity of alkylating agents but antagonizes the cytotoxicity of DNA topoisomerase II inhibitors. Br. J. Cancer 1997, 75(7):1028-1034.
    • (1997) Br. J. Cancer , vol.75 , Issue.7 , pp. 1028-1034
    • Desiderio, M.A.1    Bergamaschi, D.2    Mascellani, E.3    De Feudis, P.4    Erba, E.5    D'Incalci, M.6
  • 71
    • 0020594001 scopus 로고
    • Depletion of intracellular polyamines may alter DNA conformation in 9L rat brain tumor cells
    • Hung D.T., Marton L.J., Deen D.F., Shafer R.H. Depletion of intracellular polyamines may alter DNA conformation in 9L rat brain tumor cells. Science 1983, 221(4608):368-370.
    • (1983) Science , vol.221 , Issue.4608 , pp. 368-370
    • Hung, D.T.1    Marton, L.J.2    Deen, D.F.3    Shafer, R.H.4
  • 72
    • 0029257341 scopus 로고
    • A small peptide inhibitor of DNA replication defines the site of interaction between the cyclin-dependent kinase inhibitor p21WAF1 and proliferating cell nuclear antigen
    • Warbrick E., Lane D.P., Glover D.M., Cox L.S. A small peptide inhibitor of DNA replication defines the site of interaction between the cyclin-dependent kinase inhibitor p21WAF1 and proliferating cell nuclear antigen. Curr. Biol. 1995, 5(3):275-282.
    • (1995) Curr. Biol. , vol.5 , Issue.3 , pp. 275-282
    • Warbrick, E.1    Lane, D.P.2    Glover, D.M.3    Cox, L.S.4
  • 74
  • 75
    • 0031025385 scopus 로고    scopus 로고
    • Cell-cycle arrest and inhibition of Cdk4 activity by small peptides based on the carboxy-terminal domain of p21WAF1
    • Ball K.L., Lain S., Fahraeus R., Smythe C., Lane D.P. Cell-cycle arrest and inhibition of Cdk4 activity by small peptides based on the carboxy-terminal domain of p21WAF1. Curr. Biol. 1997, 7(1):71-80.
    • (1997) Curr. Biol. , vol.7 , Issue.1 , pp. 71-80
    • Ball, K.L.1    Lain, S.2    Fahraeus, R.3    Smythe, C.4    Lane, D.P.5
  • 76
    • 0032556952 scopus 로고    scopus 로고
    • P21 binding to PCNA causes G1 and G2 cell cycle arrest in p53-deficient cells
    • Cayrol C., Knibiehler M., Ducommun B. p21 binding to PCNA causes G1 and G2 cell cycle arrest in p53-deficient cells. Oncogene 1998, 16(3):311-320.
    • (1998) Oncogene , vol.16 , Issue.3 , pp. 311-320
    • Cayrol, C.1    Knibiehler, M.2    Ducommun, B.3
  • 77
    • 0033565263 scopus 로고    scopus 로고
    • A p21(Waf1/Cip1)carboxyl-terminal peptide exhibited cyclin-dependent kinase-inhibitory activity and cytotoxicity when introduced into human cells
    • Mutoh M., Lung F.D., Long Y.Q., Roller P.P., Sikorski R.S., O'Connor P.M. A p21(Waf1/Cip1)carboxyl-terminal peptide exhibited cyclin-dependent kinase-inhibitory activity and cytotoxicity when introduced into human cells. Cancer Res. 1999, 59(14):3480-3488.
    • (1999) Cancer Res. , vol.59 , Issue.14 , pp. 3480-3488
    • Mutoh, M.1    Lung, F.D.2    Long, Y.Q.3    Roller, P.P.4    Sikorski, R.S.5    O'Connor, P.M.6
  • 78
    • 0035325262 scopus 로고    scopus 로고
    • Inhibition of cell proliferation by the PCNA-binding region of p21 expressed as a GFP miniprotein
    • Mattock H., Lane D.P., Warbrick E. Inhibition of cell proliferation by the PCNA-binding region of p21 expressed as a GFP miniprotein. Exp. Cell Res. 2001, 265(2):234-241.
    • (2001) Exp. Cell Res. , vol.265 , Issue.2 , pp. 234-241
    • Mattock, H.1    Lane, D.P.2    Warbrick, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.