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Volumn 6, Issue 10, 2009, Pages 1049-1064

Therapeutic peptides for cancer therapy. Part II - Cell cycle inhibitory peptides and apoptosis-inducing peptides

Author keywords

Bcl 2; Drug delivery; p16; p21; p27; Smac; Therapeutic peptide

Indexed keywords

ANTINEOPLASTIC AGENT; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; BAD BH3 FUSION PROTEIN; BAD BH3 PENETRATIN FUSION PROTEIN; BAK BH3 FUSION PROTEIN; BH3 PROTEIN; BID BH3 FUSION PROTEIN; BIM PROTEIN; C4 TAT FUSION PROTEIN; CASPASE 3; CASPASE 9; CPM 1285; CYCLIN A; CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE 2 INHIBITOR; CYCLIN DEPENDENT KINASE INHIBITOR; CYCLINE; HYBRID PROTEIN; PEN ELP P21 FUSION PROTEIN; PENETRATIN P16 FUSION PROTEIN; PEPTIDE DERIVATIVE; PROTEIN BAD; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN BID; PROTEIN KINASE B; R9 P16 FUSION PROTEIN; TAT BIM FUSION PROTEIN; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 70349383205     PISSN: 17425247     EISSN: None     Source Type: Journal    
DOI: 10.1517/17425240903158909     Document Type: Review
Times cited : (46)

References (106)
  • 1
    • 0029885070 scopus 로고    scopus 로고
    • Transmembrane transport of peptide type compounds: Prospects for oral delivery
    • DOI 10.1016/0168-3659(95)00145-X
    • Lipka E, Crison J, Amidon GL. Transmembrane transport of peptide type compounds: prospects for oral delivery. J Control Release 1996;39(2-3):121-129 (Pubitemid 26194211)
    • (1996) Journal of Controlled Release , vol.39 , Issue.2-3 , pp. 121-129
    • Lipka, E.1    Crison, J.2    Amidon, G.L.3
  • 2
    • 0032494119 scopus 로고    scopus 로고
    • Pharmacodynamic aspects of peptide administration biological response modifiers
    • Talmadge JE. 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
  • 3
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi D, Joliot AH, Chassaing G, et al. The third helix of the Antennapedia homeodomain translocates through biological membranes. J Biol Chem 1994;269(14):10444-10450 (Pubitemid 24198241)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.14 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 4
    • 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
    • DOI 10.1074/jbc.272.25.16010
    • 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 (Pubitemid 27265584)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 5
    • 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 YZ, Yao SY, Veach RA, etal. 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
  • 6
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: The penetratin system for intracellular delivery
    • DOI 10.1016/S0962-8924(97)01214-2
    • Derossi D, Chassaing G, Prochiantz A. Trojan peptides: the penetratin system for intracellular delivery. Trends Cell Biol 1998;8(2):84-87 (Pubitemid 28056816)
    • (1998) Trends in Cell Biology , vol.8 , Issue.2 , pp. 84-87
    • Derossi, D.1    Chassaing, G.2    Prochiantz, A.3
  • 7
    • 0141942113 scopus 로고    scopus 로고
    • A brief introduction to cell-penetrating peptides
    • Lundberg P, Langel U. A brief introduction to cell-penetrating peptides. J Mol Recognit 2003;16(5):227-233
    • (2003) J Mol Recognit , vol.16 , Issue.5 , pp. 227-233
    • Lundberg, P.1    Langel, U.2
  • 8
    • 13844298046 scopus 로고    scopus 로고
    • Intracellular delivery of large molecules and small particles by cell-penetrating proteins and peptides
    • DOI 10.1016/j.addr.2004.10.007, PII S0169409X04002716
    • Gupta B, Levchenko TS, Torchilin VP. Intracellular delivery of large molecules and small particles by cell-penetrating proteins and peptides. Adv Drug Deliv Rev 2005;57(4):637-651 (Pubitemid 40255564)
    • (2005) Advanced Drug Delivery Reviews , vol.57 , Issue.4 SPEC.ISS , pp. 637-651
    • Gupta, B.1    Levchenko, T.S.2    Torchilin, V.P.3
  • 9
    • 3042737827 scopus 로고    scopus 로고
    • Membrane disrupting lytic peptides for cancer treatments
    • DOI 10.2174/1381612043383971
    • Leuschner C, Hansel W. Membrane disrupting lytic peptides for cancer treatments. Curr Pharm Des 2004;10(19):2299-2310 (Pubitemid 38855038)
    • (2004) Current Pharmaceutical Design , vol.10 , Issue.19 , pp. 2299-2310
    • Leuschner, C.1    Hansel, W.2
  • 10
    • 0033760789 scopus 로고    scopus 로고
    • Inhibitors of cyclin-dependent kinases as anti-cancer therapeutics
    • Fischer PM, Lane DP. Inhibitors of cyclin-dependent kinases as anti-cancer therapeutics. Curr Med Chem 2000;7(12):1213-1245 (Pubitemid 30822349)
    • (2000) Current Medicinal Chemistry , vol.7 , Issue.12 , pp. 1213-1245
    • Fischer, P.M.1    Lane, D.P.2
  • 11
    • 0029063745 scopus 로고
    • Cell-cycle inhibition by independent CDK and PCNA binding domains in p21Cip1
    • This paper first identified domains of p21 capable of inhibiting cell proliferation, and determined which regions interacted with the cyclin/Cdk and which interacted with PCNA
    • Luo Y, Hurwitz J, Massague J. Cell-cycle inhibition by independent CDK and PCNA binding domains in p21Cip1. Nature 1995;375(6527):159-161 •• This paper first identified domains of p21 capable of inhibiting cell proliferation, and determined which regions interacted with the cyclin/Cdk and which interacted with PCNA.
    • (1995) Nature , vol.375 , Issue.6527 , pp. 159-161
    • Luo, Y.1    Hurwitz, J.2    Massague, J.3
  • 13
    • 0030615324 scopus 로고    scopus 로고
    • P21(WAF1)-derived peptides linked to an internalization peptide inhibit human cancer cell growth
    • Bonfanti M, Taverna S, Salmona M, et al. p21WAF1-derived peptides linked to an internalization peptide inhibit human cancer cell growth. Cancer Res 1997;57(8):1442-1446 (Pubitemid 27175558)
    • (1997) Cancer Research , vol.57 , Issue.8 , pp. 1442-1446
    • Bonfanti, M.1    Taverna, S.2    Salmona, M.3    D'Incalci, M.4    Broggini, M.5
  • 14
    • 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 DP, Glover DM, etal. 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
  • 15
    • 0029102829 scopus 로고
    • Inhibition of nucleotide excision repair by the cyclin-dependent kinase inhibitor p21
    • Pan ZQ, Reardon JT, Li L, etal. Inhibition of nucleotide excision repair by the cyclin-dependent kinase inhibitor p21. J Biol Chem 1995;270(37):22008- 22016
    • (1995) J Biol Chem , vol.270 , Issue.37 , pp. 22008-22016
    • Pan, Z.Q.1    Reardon, J.T.2    Li, L.3
  • 16
    • 0031025385 scopus 로고    scopus 로고
    • Cell-cycle arrest and inhibition of Cdk4 activity by small peptides based on the carboxy-terminal domain of p21(WAF1)
    • Ball KL, Lain S, Fahraeus R, et al. 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 (Pubitemid 27058942)
    • (1997) Current Biology , vol.7 , Issue.1 , pp. 71-80
    • Ball, K.L.1    Lain, S.2    Fahraeus, R.3    Smythe, C.4    Lane, D.P.5
  • 17
    • 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 (Pubitemid 28052285)
    • (1998) Oncogene , vol.16 , Issue.3 , pp. 311-320
    • Cayrol, C.1    Knibiehler, M.2    Ducommun, B.3
  • 18
    • 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 FD, Long YQ, et al. 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 (Pubitemid 29334512)
    • (1999) Cancer Research , vol.59 , Issue.14 , pp. 3480-3488
    • Mutoh, M.1    Lung, F.-D.T.2    Long, Y.-Q.3    Roller, P.P.4    Sikorski, R.S.5    O'Connor, P.M.6
  • 19
    • 0035325262 scopus 로고    scopus 로고
    • Inhibition of cell proliferation by the PCNA-binding region of p21 expressed as a GFP miniprotein
    • DOI 10.1006/excr.2001.5160
    • Mattock H, Lane DP, 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 • This paper demonstrates the utility of attaching a peptide to a larger protein carrier to increase its stability. (Pubitemid 32980211)
    • (2001) Experimental Cell Research , vol.265 , Issue.2 , pp. 234-241
    • Mattock, H.1    Lane, D.P.2    Warbrick, E.3
  • 20
    • 84984621304 scopus 로고
    • Temperature of polypeptide inverse temperature transition depends on mean residue hydrophobicity
    • Urry DW, Luan C-H, Parker TM, et al. Temperature of polypeptide inverse temperature transition depends on mean residue hydrophobicity. J Am Chem Soc 1991;113:4346-4348
    • (1991) J Am Chem Soc , vol.113 , pp. 4346-4348
    • Urry, D.W.1    Luan, C.-H.2    Parker, T.M.3
  • 21
    • 33747875376 scopus 로고    scopus 로고
    • Tracking the in vivo fate of recombinant polypeptides by isotopic labeling
    • DOI 10.1016/j.jconrel.2006.06.001, PII S0168365906002562, Third International Nanomedicine and Drug Delivery Symposium
    • Liu W, Dreher MR, Chow DC, et al. Tracking the invivo fate of recombinant polypeptides by isotopic labeling. J Control Release 2006;114(2):184-192 (Pubitemid 44291852)
    • (2006) Journal of Controlled Release , vol.114 , Issue.2 , pp. 184-192
    • Liu, W.1    Dreher, M.R.2    Chow, D.C.3    Zalutsky, M.R.4    Chilkoti, A.5
  • 22
    • 0035866357 scopus 로고    scopus 로고
    • Targeting a genetically engineered elastin like polypeptide to solid tumors by local hyperthermia
    • Meyer DE, Kong GA, Dewhirst MW, et al. 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
  • 23
    • 33845223376 scopus 로고    scopus 로고
    • Tumor accumulation, degradation and pharmacokinetics of elastin-like polypeptides in nude mice
    • Liu W, Dreher MR, Furgeson DY, et al. Tumor accumulation, degradation and pharmacokinetics of elastin-like polypeptides in nude mice.J Control Release 2006;116(2):170-178
    • (2006) J Control Release , vol.116 , Issue.2 , pp. 170-178
    • Liu, W.1    Dreher, M.R.2    Furgeson, D.Y.3
  • 24
    • 34249316870 scopus 로고    scopus 로고
    • Thermal cycling enhances the accumulation of a temperature-sensitive biopolymer in solid tumors
    • DOI 10.1158/0008-5472.CAN-06-4444
    • Dreher MR, Liu W, Michelich CR, et al. Thermal cycling enhances the accumulation of a temperature-sensitive biopolymer in solid tumors. Cancer Res 2007;67(9):4418-4424 (Pubitemid 46815091)
    • (2007) Cancer Research , 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
  • 25
    • 27744525788 scopus 로고    scopus 로고
    • Evaluation of cell penetrating peptides fused to elastin-like polypeptide for drug delivery
    • DOI 10.1016/j.jconrel.2005.08.007, PII S0168365905003627
    • Massodi I, Bidwell GL 3rd, Raucher D. Evaluation of cell penetrating peptides fused to elastin-like polypeptide for drug delivery. J Control Release 2005;108(2-3):396-408 • This paper describes a thermally responsive carrier for TPs. (Pubitemid 41608671)
    • (2005) Journal of Controlled Release , vol.108 , Issue.2-3 , pp. 396-408
    • Massodi, I.1    Bidwell III, G.L.2    Raucher, D.3
  • 26
    • 0037016020 scopus 로고    scopus 로고
    • Translocating proline-rich peptides from the antimicrobial peptide bactenecin 7
    • DOI 10.1021/bi026661l
    • Sadler K, Eom KD, Yang JL, et al. Translocating proline-rich peptides from the antimicrobial peptide bactenecin 7. Biochemistry 2002;41(48):14150- 14157 (Pubitemid 35403333)
    • (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
  • 27
    • 70349378909 scopus 로고    scopus 로고
    • Inhibition of ovarian cancer cell proliferation by a cell cycle inhibitory peptide fused to a thermally responsive elastin like polypeptide carrier
    • In press This paper describes a thermally responsive carrier for a p21 peptide.
    • Massodi I, Moktan S, Rawat A, et al. Inhibition of ovarian cancer cell proliferation by a cell cycle inhibitory peptide fused to a thermally responsive elastin like polypeptide carrier. Int J Cancer 2009. In press • This paper describes a thermally responsive carrier for a p21 peptide.
    • (2009) Int J Cancer
    • Massodi, I.1    Moktan, S.2    Rawat, A.3
  • 28
    • 0029177397 scopus 로고    scopus 로고
    • Inhibition of pRb phosphorylation and cell-cycle progression by a 20-residue peptide derived from p16CDKN2/INK4A
    • This paper describes a p16 mimetic peptide
    • Fåhraeus R, Paramio JM, Ball KL, et al. Inhibition of pRb phosphorylation and cell-cycle progression by a 20-residue peptide derived from p16CDKN2/INK4A. Curr Biol 1996;6(1):84-91 • This paper describes a p16 mimetic peptide.
    • (1996) Curr Biol , vol.6 , Issue.1 , pp. 84-91
    • Fåhraeus, R.1    Paramio, J.M.2    Ball, K.L.3
  • 29
    • 0032485025 scopus 로고    scopus 로고
    • Characterization of the cyclin-dependent kinase inhibitory domain of the INK4 family as a model for a synthetic tumour suppressor molecule
    • Fahraeus R, Lain S, Ball KL, et al. Characterization of the cyclin-dependent kinase inhibitory domain of the INK4 family as a model for a synthetic tumour suppressor molecule. Oncogene 1998;16(5):587-596 (Pubitemid 28062338)
    • (1998) Oncogene , vol.16 , Issue.5 , pp. 587-596
    • Fahraeus, R.1    Lain, S.2    Ball, K.L.3    Lane, D.P.4
  • 30
    • 0034739710 scopus 로고    scopus 로고
    • Inhibition of pRb phosphorylation and cell cycle progression by an antennapedia-p16(INK4A) fusion peptide in pancreatic cancer cells
    • Fujimoto K, Hosotani R, Miyamoto Y, et al. Inhibition of pRb phosphorylation and cell cycle progression by an antennapedia-p16(INK4A) fusion peptide in pancreatic cancer cells. Cancer Lett 2000;159(2):151-158
    • (2000) Cancer Lett , vol.159 , Issue.2 , pp. 151-158
    • Fujimoto, K.1    Hosotani, R.2    Miyamoto, Y.3
  • 31
    • 0036554868 scopus 로고    scopus 로고
    • Trojan p16 peptide suppresses pancreatic cancer growth and prolongs survival in mice
    • Hosotani R, Miyamoto Y, Fujimoto K, et al. Trojan p16 peptide suppresses pancreatic cancer growth and prolongs survival in mice. Clin Cancer Res 2002;8(4):1271-6 •• This paper describes the application of the p16 peptide in vivo in a mouse model of pancreatic cancer. (Pubitemid 35177384)
    • (2002) Clinical Cancer Research , vol.8 , Issue.4 , pp. 1271-1276
    • Hosotani, R.1    Miyamoto, Y.2    Fujimoto, K.3    Doi, R.4    Otaka, A.5    Fujii, N.6    Imamura, M.7
  • 32
    • 12344326814 scopus 로고    scopus 로고
    • Highly efficient delivery of p16 antitumor peptide into aggressive leukemia/lymphoma cells using a novel transporter system
    • Kondo E, Seto M, Yoshikawa K, et al. Highly efficient delivery of p16 antitumor peptide into aggressive leukemia/lymphoma cells using a novel transporter system. Mol Cancer Ther 2004;3(12):1623-1630 (Pubitemid 40136718)
    • (2004) Molecular Cancer Therapeutics , vol.3 , Issue.12 , pp. 1623-1630
    • Kondo, E.1    Seto, M.2    Yoshikawa, K.3    Yoshino, T.4
  • 33
    • 0034603897 scopus 로고    scopus 로고
    • An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination invitro and can activate p53 invivo
    • Midgley CA, Desterro JM, Saville MK, et al. An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination invitro and can activate p53 invivo. Oncogene 2000;19(19):2312-2323
    • (2000) Oncogene , vol.19 , Issue.19 , pp. 2312-2323
    • Midgley, C.A.1    Desterro, J.M.2    Saville, M.K.3
  • 34
    • 49849085428 scopus 로고    scopus 로고
    • Potent synergy of dual antitumor peptides for growth suppression of human glioblastoma cell lines
    • Kondo E, Tanaka T, Miyake T, et al. Potent synergy of dual antitumor peptides for growth suppression of human glioblastoma cell lines. Mol Cancer Ther 2008;7(6):1461-1471
    • (2008) Mol Cancer Ther , vol.7 , Issue.6 , pp. 1461-1471
    • Kondo, E.1    Tanaka, T.2    Miyake, T.3
  • 35
    • 0033561310 scopus 로고    scopus 로고
    • The p16(INK4a) tumour suppressor protein inhibits alphavbeta3 integrin-mediated cell spreading on vitronectin by blocking PKC-dependent localization of alphavbeta3 to focal contacts
    • This paper describes a promising alternative use for the p16 peptide as an anti-metastatic agent
    • Fåhraeus R, Lane DP. The p16(INK4a) tumour suppressor protein inhibits alphavbeta3 integrin-mediated cell spreading on vitronectin by blocking PKC-dependent localization of alphavbeta3 to focal contacts. EMBO J 1999;18(8):2106-18 • This paper describes a promising alternative use for the p16 peptide as an anti-metastatic agent.
    • (1999) EMBO J , vol.18 , Issue.8 , pp. 2106-2118
    • Fåhraeus, R.1    Lane, D.P.2
  • 36
    • 33748945325 scopus 로고    scopus 로고
    • Changes in motility, gene expression and actin dynamics: Cdk6-induced cytoskeletal changes associated with differentiation in mouse astrocytes
    • DOI 10.1002/jcb.20966
    • Slomiany P, Baker T, Elliott ER, et al. Changes in motility, gene expression and actin dynamics: Cdk6-induced cytoskeletal changes associated with differentiation in mouse astrocytes. J Cell Biochem 2006;99(2):635-646 (Pubitemid 44435579)
    • (2006) Journal of Cellular Biochemistry , vol.99 , Issue.2 , pp. 635-646
    • Slomiany, P.1    Baker, T.2    Elliott, E.R.3    Grossel, M.J.4
  • 38
    • 6344240541 scopus 로고    scopus 로고
    • Design, synthesis, biological activity and structural analysis of cyclic peptide inhibitors targeting the substrate recruitment site of cyclin-dependent kinase complexes
    • Andrews MJ, McInnes C, Kontopidis G, et al. Design, synthesis, biological activity and structural analysis of cyclic peptide inhibitors targeting the substrate recruitment site of cyclin-dependent kinase complexes. Org Biomol Chem 2004;2(19):2735-2741
    • (2004) Org Biomol Chem , vol.2 , Issue.19 , pp. 2735-2741
    • Andrews, M.J.1    McInnes, C.2    Kontopidis, G.3
  • 40
    • 0029973557 scopus 로고    scopus 로고
    • Identification of a cyclin-cdk2 recognition motif present in substrates and p21-like cyclin-dependent kinase inhibitors
    • Adams PD, Sellers WR, Sharma SK, et al. Identification of a cyclin-cdk2 recognition motif present in substrates and p21-like cyclin-dependent kinase inhibitors. Mol Cell Biol 1996;16(12):6623-6633
    • (1996) Mol Cell Biol , vol.16 , Issue.12 , pp. 6623-6633
    • Adams, P.D.1    Sellers, W.R.2    Sharma, S.K.3
  • 41
    • 0033551066 scopus 로고    scopus 로고
    • Selective killing of transformed cells by cyclin/cyclin-dependent kinase 2 antagonists
    • Chen YN, Sharma SK, Ramsey TM, et al. Selective killing of transformed cells by cyclin/cyclin-dependent kinase 2 antagonists. Proc Natl Acad Sci USA 1999;96(8):4325-4329
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.8 , pp. 4325-4329
    • Chen, Y.N.1    Sharma, S.K.2    Ramsey, T.M.3
  • 43
    • 0001582482 scopus 로고
    • Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: Amplification of AKT1 in a primary human gastric adenocarcinoma
    • Staal SP. Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma. Proc Natl Acad Sci USA 1987;84(14):5034-5037
    • (1987) Proc Natl Acad Sci USA , vol.84 , Issue.14 , pp. 5034-5037
    • Staal, S.P.1
  • 44
    • 0026095665 scopus 로고
    • A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region
    • Bellacosa A, Testa JR, Staal SP, et al. A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region. Science 1991;254(5029):274-277 (Pubitemid 21917339)
    • (1991) Science , vol.254 , Issue.5029 , pp. 274-277
    • Bellacosa, A.1    Testa, J.R.2    Staal, S.P.3    Tsichlis, P.N.4
  • 45
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • Franke TF, Kaplan DR, Cantley LC, et al. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science 1997;275(5300):665-668
    • (1997) Science , vol.275 , Issue.5300 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3
  • 46
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • DOI 10.1126/science.278.5338.687
    • del Peso L, Gonzalez-Garcia M, Page C, et al. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 1997;278(5338):687-689 (Pubitemid 27464966)
    • (1997) Science , vol.278 , Issue.5338 , pp. 687-689
    • Del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 47
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta SR, Dudek H, Tao X, etal. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 1997;91(2):231-241
    • (1997) Cell , vol.91 , Issue.2 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3
  • 49
    • 0033596127 scopus 로고    scopus 로고
    • Control of apoptosis by Rel/NF-kappaB transcription factors
    • Barkett M, Gilmore TD. Control of apoptosis by Rel/NF-kappaB transcription factors. Oncogene 1999;18(49):6910-6924
    • (1999) Oncogene , vol.18 , Issue.49 , pp. 6910-6924
    • Barkett, M.1    Gilmore, T.D.2
  • 50
    • 0033965412 scopus 로고    scopus 로고
    • Role of the BH3 (Bcl-2 homology 3) domain in the regulation of apoptosis and Bcl-2-related proteins
    • Lutz RJ. Role of the BH3 (Bcl-2 homology 3) domain in the regulation of apoptosis and Bcl-2-related proteins. Biochem Soc Trans 2000;28(2):51-56
    • (2000) Biochem Soc Trans , vol.28 , Issue.2 , pp. 51-56
    • Lutz, R.J.1
  • 51
    • 0033636528 scopus 로고    scopus 로고
    • The protooncogene TCL1 is an Akt kinase coactivator
    • Laine J, Kunstle G, Obata T, etal. The protooncogene TCL1 is an Akt kinase coactivator. Mol Cell 2000;6(2):395-407
    • (2000) Mol Cell , vol.6 , Issue.2 , pp. 395-407
    • Laine, J.1    Kunstle, G.2    Obata, T.3
  • 52
    • 11144222174 scopus 로고    scopus 로고
    • Inhibition of Akt kinase activity by a peptide spanning the betaA strand of the proto-oncogene TCL1
    • DOI 10.1074/jbc.M403775200
    • Hiromura M, Okada F, Obata T, et al. Inhibition of Akt kinase activity by a peptide spanning the betaA strand of the proto-oncogene TCL1. J Biol Chem 2004;279(51):53407-53418 • This paper demonstrates that a peptide from TCL1 can inhibit Akt activity. (Pubitemid 40051845)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53407-53418
    • Hiromura, M.1    Okada, F.2    Obata, T.3    Auguin, D.4    Shibata, T.5    Roumestand, C.6    Noguchi, M.7
  • 54
    • 0029097470 scopus 로고
    • Multiple Bcl-2 family members demonstrate selective dimerizations with Bax
    • Sedlak TW, Oltvai ZN, Yang E, et al. Multiple Bcl-2 family members demonstrate selective dimerizations with Bax. Proc Natl Acad Sci USA 1995;92(17):7834-7838
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.17 , pp. 7834-7838
    • Sedlak, T.W.1    Oltvai, Z.N.2    Yang, E.3
  • 58
    • 0033531926 scopus 로고    scopus 로고
    • L function and induce apoptosis through cytochrome c-independent activation of caspases
    • Holinger EP, Chittenden T, Lutz RJ. Bak BH3 peptides antagonize Bcl-xL function and induce apoptosis through cytochrome c-independent activation of caspases. J Biol Chem 1999;274(19):13298-13304 (Pubitemid 129518538)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.19 , pp. 13298-13304
    • Holinger, E.P.1    Chittenden, T.2    Lutz, R.J.3
  • 59
    • 0042330448 scopus 로고    scopus 로고
    • L binding region within the ATPase domain of Apaf-1
    • DOI 10.1016/j.bbrc.2003.08.030
    • Yajima H, Suzuki F. Identification of a Bcl-XL binding region within the ATPase domain of Apaf-1. Biochem Biophys Res Commun 2003;309(3):520-527 (Pubitemid 37083282)
    • (2003) Biochemical and Biophysical Research Communications , vol.309 , Issue.3 , pp. 520-527
    • Yajima, H.1    Suzuki, F.2
  • 60
    • 0033774569 scopus 로고    scopus 로고
    • Failure of Bcl-2 family members to interact with Apaf-1 in normal and apoptotic cells
    • Conus S, Rosse T, Borner C. Failure of Bcl-2 family members to interact with Apaf-1 in normal and apoptotic cells. Cell Death Differ 2000;7(10):947-954
    • (2000) Cell Death Differ , vol.7 , Issue.10 , pp. 947-954
    • Conus, S.1    Rosse, T.2    Borner, C.3
  • 61
    • 0035816232 scopus 로고    scopus 로고
    • Induction of apoptosis in prostate carcinoma cells by BH3 peptides which inhibit Bak/Bcl-2 interactions
    • DOI 10.1054/bjoc.2001.1850
    • Finnegan NM, Curtin JF, Prevost G, et al. Induction of apoptosis in prostate carcinoma cells by BH3 peptides which inhibit Bak/Bcl-2 interactions. Br J Cancer 2001;85(1):115-121 (Pubitemid 32695726)
    • (2001) British Journal of Cancer , vol.85 , Issue.1 , pp. 115-121
    • Finnegan, N.M.1    Curtin, J.F.2    Prevost, G.3    Morgan, B.4    Cotter, T.G.5
  • 62
    • 0036565880 scopus 로고    scopus 로고
    • Erythrocyte survival is promoted by plasma and suppressed by a Bak-derived BH3 peptide that interacts with membrane-associated Bcl-X(L)
    • Walsh M, Lutz RJ, Cotter TG, et al. Erythrocyte survival is promoted by plasma and suppressed by a Bak-derived BH3 peptide that interacts with membrane-associated Bcl-X(L). Blood 2002;99(9):3439-3448
    • (2002) Blood , vol.99 , Issue.9 , pp. 3439-3448
    • Walsh, M.1    Lutz, R.J.2    Cotter, T.G.3
  • 63
    • 0037303782 scopus 로고    scopus 로고
    • Particle assembly incorporating a VP22-BH3 fusion protein, facilitating intracellular delivery, regulated release, and apoptosis
    • DOI 10.1016/S1525-0016(02)00054-0
    • Brewis ND, Phelan A, Normand N, et al. Particle assembly incorporating a VP22-BH3 fusion protein, facilitating intracellular delivery, regulated release, and apoptosis. Mol Ther 2003;7(2):262-270 • This paper describes generation of a vectosome delivery system for a BH3 peptide. (Pubitemid 36395362)
    • (2003) Molecular Therapy , vol.7 , Issue.2 , pp. 262-270
    • Brewis, N.D.1    Phelan, A.2    Normand, N.3    Choolun, E.4    O'Hare, P.5
  • 64
    • 20044389500 scopus 로고    scopus 로고
    • Intracellular delivery of Bak BH3 peptide by microbubble-enhanced ultrasound
    • DOI 10.1007/s11095-005-2586-7
    • Kinoshita M, Hynynen K. Intracellular delivery of Bak BH3 peptide by microbubble-enhanced ultrasound. Pharm Res 2005;22(5):716-720 (Pubitemid 40768582)
    • (2005) Pharmaceutical Research , vol.22 , Issue.5 , pp. 716-720
    • Kinoshita, M.1    Hynynen, K.2
  • 65
    • 0038015452 scopus 로고    scopus 로고
    • Targeted proapoptotic LHRH-BH3 peptide
    • Dharap SS, Minko T. Targeted proapoptotic LHRH-BH3 peptide. Pharm Res 2003;20(6):889-896
    • (2003) Pharm Res , vol.20 , Issue.6 , pp. 889-896
    • Dharap, S.S.1    Minko, T.2
  • 66
    • 0141886989 scopus 로고    scopus 로고
    • Molecular targeting of drug delivery systems to ovarian cancer by BH3 and LHRH peptides
    • DOI 10.1016/S0168-3659(03)00209-8
    • Dharap SS, Qiu B, Williams GC, et al. Molecular targeting of drug delivery systems to ovarian cancer by BH3 and LHRH peptides. J Control Release 2003;91(1-2):61-73 (Pubitemid 37288877)
    • (2003) Journal of Controlled Release , vol.91 , Issue.1-2 , pp. 61-73
    • Dharap, S.S.1    Qiu, B.2    Williams, G.C.3    Sinko, P.4    Stein, S.5    Minko, T.6
  • 68
    • 35448930178 scopus 로고    scopus 로고
    • Targeting antiapoptotic Bcl-2 family members with cell-permeable BH3 peptides induces apoptosis signaling and death in head and neck squamous cell carcinoma cells
    • DOI 10.1593/neo.07394
    • Li R, Boehm AL, Miranda MB, et al. Targeting antiapoptotic Bcl-2 family members with cell-permeable BH3 peptides induces apoptosis signaling and death in head and neck squamous cell carcinoma cells. Neoplasia 2007;9(10):801-811 (Pubitemid 47623420)
    • (2007) Neoplasia , vol.9 , Issue.10 , pp. 801-811
    • Li, R.1    Boehm, A.L.2    Miranda, M.B.3    Shangary, S.4    Grandis, J.R.5    Johnson, D.E.6
  • 69
    • 52249106626 scopus 로고    scopus 로고
    • Anti-apoptotic Bcl-XL protein in complex with BH3 peptides of pro-apoptotic Bak, Bad, and Bim proteins: Comparative molecular dynamics simulations
    • Lama D, Sankararamakrishnan R. Anti-apoptotic Bcl-XL protein in complex with BH3 peptides of pro-apoptotic Bak, Bad, and Bim proteins: comparative molecular dynamics simulations. Proteins 2008;73(2):492-514
    • (2008) Proteins , vol.73 , Issue.2 , pp. 492-514
    • Lama, D.1    Sankararamakrishnan, R.2
  • 70
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M, Shimizu S, Ito T, etal. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc Natl Acad Sci USA 1998;95(25):14681-14686
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.25 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3
  • 71
    • 0035851110 scopus 로고    scopus 로고
    • BH3 Death Domain Peptide Induces Cell Type-selective Mitochondrial Outer Membrane Permeability
    • Polster BM, Kinnally KW, Fiskum G. BH3 death domain peptide induces cell type-selective mitochondrial outer membrane permeability. J Biol Chem 2001;276(41):37887-37894 (Pubitemid 37384036)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.41 , pp. 37887-37894
    • Polster, B.M.1    Kinnally, K.W.2    Fiskum, G.3
  • 74
    • 0030695837 scopus 로고    scopus 로고
    • Bad is a BH3 domain-containing protein that forms an inactivating dimer with Bcl-XL
    • Kelekar A, Chang BS, Harlan JE, etal. Bad is a BH3 domain-containing protein that forms an inactivating dimer with Bcl-XL. Mol Cell Biol 1997;17(12):7040-7046
    • (1997) Mol Cell Biol , vol.17 , Issue.12 , pp. 7040-7046
    • Kelekar, A.1    Chang, B.S.2    Harlan, J.E.3
  • 76
    • 0034654522 scopus 로고    scopus 로고
    • Cell permeable Bcl-2 binding peptides: A chemical approach to apoptosis induction in tumor cells
    • Wang JL, Zhang ZJ, Choksi S, etal. Cell permeable Bcl-2 binding peptides: a chemical approach to apoptosis induction in tumor cells. Cancer Res 2000;60(6):1498-1502
    • (2000) Cancer Res , vol.60 , Issue.6 , pp. 1498-1502
    • Wang, J.L.1    Zhang, Z.J.2    Choksi, S.3
  • 78
    • 33746843081 scopus 로고    scopus 로고
    • BH3 peptidomimetics potently activate apoptosis and demonstrate single agent efficacy in neuroblastoma
    • Goldsmith KC, Liu X, Dam V, etal. BH3 peptidomimetics potently activate apoptosis and demonstrate single agent efficacy in neuroblastoma. Oncogene 2006;25(33):4525-4533
    • (2006) Oncogene , vol.25 , Issue.33 , pp. 4525-4533
    • Goldsmith, K.C.1    Liu, X.2    Dam, V.3
  • 79
    • 33947637591 scopus 로고    scopus 로고
    • TAT-Bim induces extensive apoptosis in cancer cells
    • Kashiwagi H, McDunn JE, Goedegebuure PS, etal. TAT-Bim induces extensive apoptosis in cancer cells. Ann Surg Oncol 2007;14(5):1763-1771
    • (2007) Ann Surg Oncol , vol.14 , Issue.5 , pp. 1763-1771
    • Kashiwagi, H.1    McDunn, J.E.2    Goedegebuure, P.S.3
  • 80
    • 4444291734 scopus 로고    scopus 로고
    • Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix
    • DOI 10.1126/science.1099191
    • Walensky LD, Kung AL, Escher I, et al. Activation of apoptosis invivo by a hydrocarbon-stapled BH3 helix. Science 2004;305(5689):1466-1470 • This paper describes hydrocarbon stapling as a method to stabilize the structure of a BH3 peptide and increase its protease resistance. (Pubitemid 39167667)
    • (2004) Science , vol.305 , Issue.5689 , pp. 1466-1470
    • Walensky, L.D.1    Kung, A.L.2    Escher, I.3    Malia, T.J.4    Barbuto, S.5    Wright, R.D.6    Wagner, G.7    Verdine, G.L.8    Korsmeyer, S.J.9
  • 83
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/DIABLO
    • This work describes the mechanism of apoptosis induction by Smac/DIABLO
    • Chai J, Du C, Wu JW, etal. Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature 2000;406(6798):855-862 •• This work describes the mechanism of apoptosis induction by Smac/DIABLO.
    • (2000) Nature , vol.406 , Issue.6798 , pp. 855-862
    • Chai, J.1    Du, C.2    Wu, J.W.3
  • 84
    • 0034700491 scopus 로고    scopus 로고
    • Structural basis of IAP recognition by Smac/DIABLO
    • Wu G, Chai J, Suber TL, etal. Structural basis of IAP recognition by Smac/DIABLO. Nature 2000;408(6815):1008-1012
    • (2000) Nature , vol.408 , Issue.6815 , pp. 1008-1012
    • Wu, G.1    Chai, J.2    Suber, T.L.3
  • 85
    • 0036341291 scopus 로고    scopus 로고
    • Smac agonists sensitize for Apo2L/TRAIL- Or anticancer drug-induced apoptosis and induce regression of malignant glioma in vivo
    • Fulda S, Wick W, Weller M, etal. Smac agonists sensitize for Apo2L/TRAIL- or anticancer drug-induced apoptosis and induce regression of malignant glioma in vivo. Nat Med 2002;8(8):808-815
    • (2002) Nat Med , vol.8 , Issue.8 , pp. 808-815
    • Fulda, S.1    Wick, W.2    Weller, M.3
  • 86
    • 0347895102 scopus 로고    scopus 로고
    • Synthetic Smac/DIABLO peptides enhance the effects of chemotherapeutic agents by binding XIAP and cIAP1 in situ
    • Arnt CR, Chiorean MV, Heldebrant MP, et al. Synthetic Smac/DIABLO peptides enhance the effects of chemotherapeutic agents by binding XIAP and cIAP1 in situ. J Biol Chem 2002;277(46):44236-44243
    • (2002) J Biol Chem , vol.277 , Issue.46 , pp. 44236-44243
    • Arnt, C.R.1    Chiorean, M.V.2    Heldebrant, M.P.3
  • 87
    • 0037442965 scopus 로고    scopus 로고
    • Predominant suppression of apoptosome by inhibitor of apoptosis protein in non-small cell lung cancer H460 cells: Therapeutic effect of a novel polyarginine-conjugated Smac peptide
    • Yang L, Mashima T, Sato S, et al. Predominant suppression of apoptosome by inhibitor of apoptosis protein in non-small cell lung cancer H460 cells: therapeutic effect of a novel polyarginine-conjugated Smac peptide. Cancer Res 2003;63(4):831-837 (Pubitemid 36231984)
    • (2003) Cancer Research , vol.63 , Issue.4 , pp. 831-837
    • Yang, L.1    Mashima, T.2    Sato, S.3    Mochizuki, M.4    Sakamoto, H.5    Yamori, T.6    Oh-hara, T.7    Tsuruo, T.8
  • 88
    • 50049134643 scopus 로고    scopus 로고
    • A novel polyarginine containing Smac peptide conjugate that mediates cell death in tumor and healthy cells
    • Heckl S, Sturzu A, Regenbogen M, et al. A novel polyarginine containing Smac peptide conjugate that mediates cell death in tumor and healthy cells. Med Chem 2008;4(4):348-354
    • (2008) Med Chem , vol.4 , Issue.4 , pp. 348-354
    • Heckl, S.1    Sturzu, A.2    Regenbogen, M.3
  • 89
    • 4444243683 scopus 로고    scopus 로고
    • A small molecule Smac mimic potentiates TRAIL- and TNFalpha-mediated cell death
    • Li L, Thomas RM, Suzuki H, etal. A small molecule Smac mimic potentiates TRAIL- and TNFalpha-mediated cell death. Science 2004;305(5689):1471-1474
    • (2004) Science , vol.305 , Issue.5689 , pp. 1471-1474
    • Li, L.1    Thomas, R.M.2    Suzuki, H.3
  • 91
    • 34247611460 scopus 로고    scopus 로고
    • Smac-mediated sensitization of human B-lymphoma cells to staurosporine- And lactacystin-triggered apoptosis is apoptosome-dependent
    • DOI 10.1038/sj.leu.2404660, PII 2404660
    • Sun Y, Ottosson A, Pervaiz S, et al. Smac-mediated sensitization of human B-lymphoma cells to staurosporine- and lactacystin-triggered apoptosis is apoptosome-dependent. Leukemia 2007;21(5):1035-1043 (Pubitemid 46672081)
    • (2007) Leukemia , vol.21 , Issue.5 , pp. 1035-1043
    • Sun, Y.1    Ottosson, A.2    Pervaiz, S.3    Fadeel, B.4
  • 92
    • 48249140223 scopus 로고    scopus 로고
    • Smac/DIABLO enhances the therapeutic potential of chemotherapeutic drugs and irradiation, and sensitizes TRAIL-resistant breast cancer cells
    • Fandy TE, Shankar S, Srivastava RK. Smac/DIABLO enhances the therapeutic potential of chemotherapeutic drugs and irradiation, and sensitizes TRAIL-resistant breast cancer cells. Mol Cancer 2008;7:60
    • (2008) Mol Cancer , vol.7 , pp. 60
    • Fandy, T.E.1    Shankar, S.2    Srivastava, R.K.3
  • 94
    • 33646489207 scopus 로고    scopus 로고
    • Cytoplasmic transduction peptide (CTP): New approach for the delivery of biomolecules into cytoplasm invitro and in vivo
    • Kim D, Jeon C, Kim JH, et al. Cytoplasmic transduction peptide (CTP): new approach for the delivery of biomolecules into cytoplasm invitro and in vivo. Exp Cell Res 2006;312(8):1277-1288
    • (2006) Exp Cell Res , vol.312 , Issue.8 , pp. 1277-1288
    • Kim, D.1    Jeon, C.2    Kim, J.H.3
  • 95
    • 35648961848 scopus 로고    scopus 로고
    • A dimeric Smac/Diablo peptide directly relieves caspase-3 inhibition by XIAP: Dynamic and cooperative regulation of XIAP by Smac/Diablo
    • DOI 10.1074/jbc.M705258200
    • Gao Z, Tian Y, Wang J, etal. A dimeric Smac/diablo peptide directly relieves caspase-3 inhibition by XIAP. Dynamic and cooperative regulation of XIAP by Smac/Diablo. J Biol Chem 2007;282(42):30718-30727 (Pubitemid 350035215)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.42 , pp. 30718-30727
    • Gao, Z.1    Tian, Y.2    Wang, J.3    Yin, Q.4    Wu, H.5    Li, Y.-M.6    Jiang, X.7
  • 96
    • 47849083565 scopus 로고    scopus 로고
    • A mechanistic insight into SMAC peptide interference with XIAP-Bir2 inhibition of executioner caspases
    • Abhari BA, Davoodi J. A mechanistic insight into SMAC peptide interference with XIAP-Bir2 inhibition of executioner caspases. J Mol Biol 2008;381(3):645-654
    • (2008) J Mol Biol , vol.381 , Issue.3 , pp. 645-654
    • Abhari, B.A.1    Davoodi, J.2
  • 97
    • 38349131701 scopus 로고    scopus 로고
    • Design and characterization of bivalent Smac-based peptides as antagonists of XIAP and development and validation of a fluorescence polarization assay for XIAP containing both BIR2 and BIR3 domains
    • Nikolovska-Coleska Z, Meagher JL, Jiang S, etal. Design and characterization of bivalent Smac-based peptides as antagonists of XIAP and development and validation of a fluorescence polarization assay for XIAP containing both BIR2 and BIR3 domains. Anal Biochem 2008;374(1):87-98
    • (2008) Anal Biochem , vol.374 , Issue.1 , pp. 87-98
    • Nikolovska-Coleska, Z.1    Meagher, J.L.2    Jiang, S.3
  • 98
    • 33751520245 scopus 로고    scopus 로고
    • Thermo- And pH-responsive polymers in drug delivery
    • DOI 10.1016/j.addr.2006.09.020, PII S0169409X06001839
    • Schmaljohann D. Thermo- and pH-responsive polymers in drug delivery. Adv Drug Deliv Rev 2006;58(15):1655-1670 (Pubitemid 44830149)
    • (2006) Advanced Drug Delivery Reviews , vol.58 , Issue.15 , pp. 1655-1670
    • Schmaljohann, D.1
  • 99
    • 41449116221 scopus 로고    scopus 로고
    • Thermally targeted delivery of chemotherapeutics and anti-cancer peptides by elastin-like polypeptide
    • Raucher D, Massodi I, Bidwell GL. Thermally targeted delivery of chemotherapeutics and anti-cancer peptides by elastin-like polypeptide. Expert Opin Drug Deliv 2008;5(3):353-369
    • (2008) Expert Opin Drug Deliv , vol.5 , Issue.3 , pp. 353-369
    • Raucher, D.1    Massodi, I.2    Bidwell, G.L.3
  • 101
    • 0343882023 scopus 로고    scopus 로고
    • Targeted drug delivery via the folate receptor
    • DOI 10.1016/S0169-409X(99)00062-9, PII S0169409X99000629
    • Sudimack J, Lee RJ. Targeted drug delivery via the folate receptor. Adv Drug Deliv Rev 2000;41(2):147-162 (Pubitemid 30122955)
    • (2000) Advanced Drug Delivery Reviews , vol.41 , Issue.2 , pp. 147-162
    • Sudimack, J.1    Lee, R.J.2
  • 103
    • 59849110112 scopus 로고    scopus 로고
    • Targeting of albumin-embedded paclitaxel nanoparticles to tumors
    • Karmali PP, Kotamraju VR, Kastantin M, et al. Targeting of albumin-embedded paclitaxel nanoparticles to tumors. Nanomedicine 2009;5(1):73-82
    • (2009) Nanomedicine , vol.5 , Issue.1 , pp. 73-82
    • Karmali, P.P.1    Kotamraju, V.R.2    Kastantin, M.3
  • 104
    • 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
  • 105
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cell-penetrating peptides: From molecular mechanisms to therapeutics
    • Heitz F, Morris MC, 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
  • 106
    • 0033520487 scopus 로고    scopus 로고
    • Invivo protein transduction: Delivery of a biologically active protein into the mouse
    • Schwarze SR, Ho A, Vocero-Akbani A, etal. Invivo 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


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