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Volumn , Issue , 2013, Pages 576-581

In vitro characterization and in vivo application of a dual functional peptide

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; CANCER-TARGETING; CATIONIC PROTEINS; FUNCTIONAL PEPTIDES; HEPARIN-BINDING REGIONS; MAGNETIC NANO-PARTICLES; QUANTITATIVE ASSAY; SULFATED GLYCOSAMINOGLYCANS;

EID: 84885232154     PISSN: None     EISSN: None     Source Type: Conference Proceeding    
DOI: 10.1109/CISIS.2013.104     Document Type: Conference Paper
Times cited : (1)

References (47)
  • 1
    • 56649100319 scopus 로고    scopus 로고
    • The structure of glycosaminoglycans and their interactions with proteins
    • Gandhi, N.S. and R.L. Mancera, The structure of glycosaminoglycans and their interactions with proteins. Chem Biol Drug Des, 2008. 72(6): p. 455-82.
    • (2008) Chem Biol Drug des , vol.72 , Issue.6 , pp. 455-82
    • Gandhi, N.S.1    Mancera, R.L.2
  • 2
    • 77950833141 scopus 로고    scopus 로고
    • Chemical tumor biology of heparan sulfate proteoglycans
    • Raman, K. and B. Kuberan, Chemical Tumor Biology of Heparan Sulfate Proteoglycans. Curr Chem Biol, 2010. 4(1): p. 20-31.
    • (2010) Curr Chem Biol , vol.4 , Issue.1 , pp. 20-31
    • Raman, K.1    Kuberan, B.2
  • 3
    • 0035879011 scopus 로고    scopus 로고
    • Glypican-1 is overexpressed in human breast cancer and modulates the mitogenic effects of multiple heparin-binding growth factors in breast cancer cells
    • Matsuda, K., et al., Glypican-1 is overexpressed in human breast cancer and modulates the mitogenic effects of multiple heparin-binding growth factors in breast cancer cells. Cancer Res, 2001. 61(14): p. 5562-9.
    • (2001) Cancer Res , vol.61 , Issue.14 , pp. 5562-9
    • Matsuda, K.1
  • 4
    • 0034904048 scopus 로고    scopus 로고
    • Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis
    • Vlodavsky, I. and Y. Friedmann, Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis. J Clin Invest, 2001. 108(3): p. 341-7.
    • (2001) J Clin Invest , vol.108 , Issue.3 , pp. 341-7
    • Vlodavsky, I.1    Friedmann, Y.2
  • 5
    • 79251500680 scopus 로고    scopus 로고
    • Syndecan-1 in breast cancer stroma fibroblasts regulates extracellular matrix fiber organization and carcinoma cell motility
    • Yang, N., et al., Syndecan-1 in breast cancer stroma fibroblasts regulates extracellular matrix fiber organization and carcinoma cell motility. Am J Pathol, 2011. 178(1): p. 325-35.
    • (2011) Am J Pathol , vol.178 , Issue.1 , pp. 325-35
    • Yang, N.1
  • 6
    • 20444477205 scopus 로고    scopus 로고
    • Breast pathology: Rationale for adopting the ductal intraepithelial neoplasia (DIN) classification
    • Tavassoli, F.A., Breast pathology: rationale for adopting the ductal intraepithelial neoplasia (DIN) classification. Nat Clin Pract Oncol, 2005. 2(3): p. 116-7.
    • (2005) Nat Clin Pract Oncol , vol.2 , Issue.3 , pp. 116-7
    • Tavassoli, F.A.1
  • 7
    • 34548150237 scopus 로고    scopus 로고
    • Cell-penetrating-peptide-based delivery of oligonucleotides: An overview
    • Abes, R., et al., Cell-penetrating-peptide-based delivery of oligonucleotides: an overview. Biochem Soc Trans, 2007. 35(Pt 4): p. 775-9.
    • (2007) Biochem Soc Trans , vol.35 , Issue.PART 4 , pp. 775-9
    • Abes, R.1
  • 8
    • 72149099569 scopus 로고    scopus 로고
    • The systemic delivery of siRNAs by a cell penetrating peptide, low molecular weight protamine
    • Choi, Y.S., et al., The systemic delivery of siRNAs by a cell penetrating peptide, low molecular weight protamine. Biomaterials, 2010. 31(6): p. 1429-43.
    • (2010) Biomaterials , vol.31 , Issue.6 , pp. 1429-43
    • Choi, Y.S.1
  • 9
    • 56049093057 scopus 로고    scopus 로고
    • Cell-penetrating and celltargeting peptides in drug delivery
    • Vives, E., J. Schmidt, and A. Pelegrin, Cell-penetrating and celltargeting peptides in drug delivery. Biochim Biophys Acta, 2008. 1786(2): p. 126-38.
    • (2008) Biochim Biophys Acta , vol.1786 , Issue.2 , pp. 126-38
    • Vives, E.1    Schmidt, J.2    Pelegrin, A.3
  • 10
    • 38949116621 scopus 로고    scopus 로고
    • Thermodynamic studies and binding mechanisms of cellpenetrating peptides with lipids and glycosaminoglycans
    • Ziegler, A., Thermodynamic studies and binding mechanisms of cellpenetrating peptides with lipids and glycosaminoglycans. Adv Drug Deliv Rev, 2008. 60(4-5): p. 580-97.
    • (2008) Adv Drug Deliv Rev , vol.60 , Issue.4-5 , pp. 580-97
    • Ziegler, A.1
  • 11
    • 77949741829 scopus 로고    scopus 로고
    • Intracellular transduction using cellpenetrating peptides
    • Sawant, R. and V. Torchilin, Intracellular transduction using cellpenetrating peptides. Mol Biosyst, 2010. 6(4): p. 628-40.
    • (2010) Mol Biosyst , vol.6 , Issue.4 , pp. 628-40
    • Sawant, R.1    Torchilin, V.2
  • 12
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cell-penetrating peptides: From molecular mechanisms to therapeutics
    • Heitz, F., M.C. Morris, and G. Divita, Twenty years of cell-penetrating peptides: from molecular mechanisms to therapeutics. Br J Pharmacol, 2009. 157(2): p. 195-206.
    • (2009) Br J Pharmacol , vol.157 , Issue.2 , pp. 195-206
    • Heitz, F.1    Morris, M.C.2    Divita, G.3
  • 13
    • 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., P. Brodin, and B. Lebleu, 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): p. 16010-7.
    • (1997) J Biol Chem , vol.272 , Issue.25 , pp. 16010-7
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 14
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia, J.S., R.V. Stan, and S.F. Dowdy, Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat Med, 2004. 10(3): p. 310-5.
    • (2004) Nat Med , vol.10 , Issue.3 , pp. 310-5
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 15
    • 0031471203 scopus 로고    scopus 로고
    • Intercellular trafficking and protein delivery by a herpesvirus structural protein
    • Elliott, G. and P. O'Hare, Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell, 1997. 88(2): p. 223-33.
    • (1997) Cell , vol.88 , Issue.2 , pp. 223-33
    • Elliott, G.1    O'Hare, P.2
  • 16
    • 40949160615 scopus 로고    scopus 로고
    • Comparative study on transduction and toxicity of protein transduction domains
    • Sugita, T., et al., Comparative study on transduction and toxicity of protein transduction domains. Br J Pharmacol, 2008. 153(6): p. 1143-52.
    • (2008) Br J Pharmacol , vol.153 , Issue.6 , pp. 1143-52
    • Sugita, T.1
  • 17
    • 76749166383 scopus 로고    scopus 로고
    • Assessing the uptake kinetics and internalization mechanisms of cell-penetrating peptides using a quenched fluorescence assay
    • Mager, I., et al., Assessing the uptake kinetics and internalization mechanisms of cell-penetrating peptides using a quenched fluorescence assay. Biochim Biophys Acta, 2010. 1798(3): p. 338-43.
    • (2010) Biochim Biophys Acta , vol.1798 , Issue.3 , pp. 338-43
    • Mager, I.1
  • 18
    • 35048856889 scopus 로고    scopus 로고
    • Cargo-dependent cytotoxicity and delivery efficacy of cell-penetrating peptides: A comparative study
    • El-Andaloussi, S., et al., Cargo-dependent cytotoxicity and delivery efficacy of cell-penetrating peptides: a comparative study. Biochem J, 2007. 407(2): p. 285-92.
    • (2007) Biochem J , vol.407 , Issue.2 , pp. 285-92
    • El-Andaloussi, S.1
  • 19
    • 0034738525 scopus 로고    scopus 로고
    • Deletion analogues of transportan
    • Soomets, U., et al., Deletion analogues of transportan. Biochim Biophys Acta, 2000. 1467(1): p. 165-76.
    • (2000) Biochim Biophys Acta , vol.1467 , Issue.1 , pp. 165-76
    • Soomets, U.1
  • 20
    • 0019820017 scopus 로고
    • Morphological studies on the killing of schistosomula of Schistosoma mansoni by human eosinophil and neutrophil cationic proteins in vitro
    • McLaren, D.J., et al., Morphological studies on the killing of schistosomula of Schistosoma mansoni by human eosinophil and neutrophil cationic proteins in vitro. Parasite Immunol, 1981. 3(4): p. 359-73.
    • (1981) Parasite Immunol , vol.3 , Issue.4 , pp. 359-73
    • McLaren, D.J.1
  • 21
    • 0022403203 scopus 로고
    • Comparative toxicity of purified human eosinophil granule cationic proteins for schistosomula of Schistosoma mansoni
    • Ackerman, S.J., et al., Comparative toxicity of purified human eosinophil granule cationic proteins for schistosomula of Schistosoma mansoni. Am J Trop Med Hyg, 1985. 34(4): p. 735-45.
    • (1985) Am J Trop Med Hyg , vol.34 , Issue.4 , pp. 735-45
    • Ackerman, S.J.1
  • 22
    • 0036156089 scopus 로고    scopus 로고
    • Growth inhibition of mammalian cells by eosinophil cationic protein
    • Maeda, T., et al., Growth inhibition of mammalian cells by eosinophil cationic protein. Eur J Biochem, 2002. 269(1): p. 307-16.
    • (2002) Eur J Biochem , vol.269 , Issue.1 , pp. 307-16
    • Maeda, T.1
  • 23
    • 0024500320 scopus 로고
    • Toxicity of eosinophil cationic proteins for guinea pig tracheal epithelium in vitro
    • Motojima, S., et al., Toxicity of eosinophil cationic proteins for guinea pig tracheal epithelium in vitro. Am Rev Respir Dis, 1989. 139(3): p. 801-5.
    • (1989) Am Rev Respir Dis , vol.139 , Issue.3 , pp. 801-5
    • Motojima, S.1
  • 24
    • 20944447573 scopus 로고    scopus 로고
    • Surface-exposed amino acids of eosinophil cationic protein play a critical role in the inhibition of mammalian cell proliferation
    • Carreras, E., et al., Surface-exposed amino acids of eosinophil cationic protein play a critical role in the inhibition of mammalian cell proliferation. Mol Cell Biochem, 2005. 272(1-2): p. 1-7.
    • (2005) Mol Cell Biochem , vol.272 , Issue.1-2 , pp. 1-7
    • Carreras, E.1
  • 25
    • 0033022636 scopus 로고    scopus 로고
    • Kinetic and product distribution analysis of human eosinophil cationic protein indicates a subsite arrangement that favors exonuclease-type activity
    • Boix, E., et al., Kinetic and product distribution analysis of human eosinophil cationic protein indicates a subsite arrangement that favors exonuclease-type activity. J Biol Chem, 1999. 274(22): p. 15605-14.
    • (1999) J Biol Chem , vol.274 , Issue.22 , pp. 15605-14
    • Boix, E.1
  • 26
    • 0024584913 scopus 로고
    • Molecular modeling of protein-glycosaminoglycan interactions
    • Cardin, A.D. and H.J. Weintraub, Molecular modeling of protein-glycosaminoglycan interactions. Arteriosclerosis, 1989. 9(1): p. 21-32.
    • (1989) Arteriosclerosis , vol.9 , Issue.1 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.2
  • 27
    • 84874620927 scopus 로고    scopus 로고
    • In silico prediction and in vitro characterization of multifunctional human RNase3
    • Lien, P.-C., et al., In Silico Prediction and In Vitro Characterization of Multifunctional Human RNase3. BioMed Research International, 2013. 2013: p. 12.
    • (2013) BioMed Research International , vol.2013 , pp. 12
    • Lien, P.-C.1
  • 28
    • 84874641140 scopus 로고    scopus 로고
    • A novel cell-penetrating Peptide derived from human eosinophil cationic protein
    • Fang, S.L., et al., A novel cell-penetrating Peptide derived from human eosinophil cationic protein. PLoS One, 2013. 8(3): p. e57318.
    • (2013) PLoS One , vol.8 , Issue.3
    • Fang, S.L.1
  • 29
    • 84865260947 scopus 로고    scopus 로고
    • A novel quantitative immunomagnetic reduction assay for Nervous necrosis virus
    • Yang, S.Y., et al., A novel quantitative immunomagnetic reduction assay for Nervous necrosis virus. J Vet Diagn Invest, 2012. 24(5): p. 911-7.
    • (2012) J Vet Diagn Invest , vol.24 , Issue.5 , pp. 911-7
    • Yang, S.Y.1
  • 30
    • 38149078879 scopus 로고    scopus 로고
    • Hyper-high-sensitivity wash-free magnetoreduction assay on biomolecules using high-T(c) superconducting quantum interference devices
    • Chieh, J.J., et al., Hyper-high-sensitivity wash-free magnetoreduction assay on biomolecules using high-T(c) superconducting quantum interference devices. Journal of Applied Physics, 2008. 103(1).
    • (2008) Journal of Applied Physics , vol.103 , Issue.1
    • Chieh, J.J.1
  • 31
    • 79451473831 scopus 로고    scopus 로고
    • Nanoparticles as contrast agents for in-vivo bioimaging: Current status and future perspectives
    • Hahn, M.A., et al., Nanoparticles as contrast agents for in-vivo bioimaging: current status and future perspectives. Anal Bioanal Chem, 2011. 399(1): p. 3-27.
    • (2011) Anal Bioanal Chem , vol.399 , Issue.1 , pp. 3-27
    • Hahn, M.A.1
  • 32
    • 33947598165 scopus 로고    scopus 로고
    • Inhibition of human pancreatic ribonuclease by the human ribonuclease inhibitor protein
    • Johnson, R.J., et al., Inhibition of human pancreatic ribonuclease by the human ribonuclease inhibitor protein. J Mol Biol, 2007. 368(2): p. 434-49.
    • (2007) J Mol Biol , vol.368 , Issue.2 , pp. 434-49
    • Johnson, R.J.1
  • 33
    • 0001633426 scopus 로고
    • Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: Homology with ribonuclease
    • Gleich, G.J., et al., Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease. Proc Natl Acad Sci U S A, 1986. 83(10): p. 3146-50.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , Issue.10 , pp. 3146-50
    • Gleich, G.J.1
  • 34
    • 0009464172 scopus 로고
    • Antibiotic proteins of human polymorphonuclear leukocytes
    • Gabay, J.E., et al., Antibiotic proteins of human polymorphonuclear leukocytes. Proc Natl Acad Sci U S A, 1989. 86(14): p. 5610-4.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , Issue.14 , pp. 5610-4
    • Gabay, J.E.1
  • 35
    • 8444222667 scopus 로고    scopus 로고
    • Human ribonuclease A superfamily members, eosinophil-derived neurotoxin and pancreatic ribonuclease, induce dendritic cell maturation and activation
    • Yang, D., et al., Human ribonuclease A superfamily members, eosinophil-derived neurotoxin and pancreatic ribonuclease, induce dendritic cell maturation and activation. J Immunol, 2004. 173(10): p. 6134-42.
    • (2004) J Immunol , vol.173 , Issue.10 , pp. 6134-42
    • Yang, D.1
  • 36
    • 0028955199 scopus 로고
    • Molecular cloning and expression of human ribonuclease 4 cDNA
    • Seno, M., et al., Molecular cloning and expression of human ribonuclease 4 cDNA. Biochim Biophys Acta, 1995. 1261(3): p. 424-6.
    • (1995) Biochim Biophys Acta , vol.1261 , Issue.3 , pp. 424-6
    • Seno, M.1
  • 37
    • 76149093190 scopus 로고    scopus 로고
    • In vitro biological activity of bovine milk ribonuclease-4
    • Di Liddo, R., et al., In vitro biological activity of bovine milk ribonuclease-4. Mol Med Report, 2010. 3(1): p. 127-32.
    • (2010) Mol Med Report , vol.3 , Issue.1 , pp. 127-32
    • Di Liddo, R.1
  • 38
    • 0026794004 scopus 로고
    • Angiogenin is a cytotoxic, tRNA-specific ribonuclease in the RNase A superfamily
    • Saxena, S.K., et al., Angiogenin is a cytotoxic, tRNA-specific ribonuclease in the RNase A superfamily. J Biol Chem, 1992. 267(30): p. 21982-6.
    • (1992) J Biol Chem , vol.267 , Issue.30 , pp. 21982-6
    • Saxena, S.K.1
  • 39
    • 84866627376 scopus 로고    scopus 로고
    • Role of platelet-derived growth factor-AB in tumour growth and angiogenesis in relation with other angiogenic cytokines in multiple myeloma
    • Tsirakis, G., et al., Role of platelet-derived growth factor-AB in tumour growth and angiogenesis in relation with other angiogenic cytokines in multiple myeloma. Hematol Oncol, 2011.
    • (2011) Hematol Oncol
    • Tsirakis, G.1
  • 40
    • 0033256881 scopus 로고    scopus 로고
    • Following angiogenin during angiogenesis: A journey from the cell surface to the nucleolus
    • Wiedlocha, A., Following angiogenin during angiogenesis: a journey from the cell surface to the nucleolus. Arch Immunol Ther Exp (Warsz), 1999. 47(5): p. 299-305.
    • (1999) Arch Immunol Ther Exp (Warsz) , vol.47 , Issue.5 , pp. 299-305
    • Wiedlocha, A.1
  • 41
    • 0029792027 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel human ribonuclease (RNase k6): Increasing diversity in the enlarging ribonuclease gene family
    • Rosenberg, H.F. and K.D. Dyer, Molecular cloning and characterization of a novel human ribonuclease (RNase k6): increasing diversity in the enlarging ribonuclease gene family. Nucleic Acids Res, 1996. 24(18): p. 3507-13.
    • (1996) Nucleic Acids Res , vol.24 , Issue.18 , pp. 3507-13
    • Rosenberg, H.F.1    Dyer, K.D.2
  • 42
    • 65249140613 scopus 로고    scopus 로고
    • Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ECP and RNase 7
    • Torrent, M., et al., Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ECP and RNase 7. Biochim Biophys Acta, 2009. 1788(5): p. 1116-25.
    • (2009) Biochim Biophys Acta , vol.1788 , Issue.5 , pp. 1116-25
    • Torrent, M.1
  • 43
    • 33947513637 scopus 로고    scopus 로고
    • The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity
    • Huang, Y.C., et al., The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity. J Biol Chem, 2007. 282(7): p. 4626-33.
    • (2007) J Biol Chem , vol.282 , Issue.7 , pp. 4626-33
    • Huang, Y.C.1
  • 44
    • 0036493226 scopus 로고    scopus 로고
    • RNase 8, a novel RNase A superfamily ribonuclease expressed uniquely in placenta
    • Zhang, J., K.D. Dyer, and H.F. Rosenberg, RNase 8, a novel RNase A superfamily ribonuclease expressed uniquely in placenta. Nucleic Acids Res, 2002. 30(5): p. 1169-75.
    • (2002) Nucleic Acids Res , vol.30 , Issue.5 , pp. 1169-75
    • Zhang, J.1    Dyer, K.D.2    Rosenberg, H.F.3
  • 45
    • 77955813859 scopus 로고    scopus 로고
    • Cloning, expression and location of RNase9 in human epididymis
    • Liu, J., et al., Cloning, expression and location of RNase9 in human epididymis. BMC Res Notes, 2008. 1: p. 111.
    • (2008) BMC Res Notes , vol.1 , pp. 111
    • Liu, J.1
  • 46
    • 69249203872 scopus 로고    scopus 로고
    • Human ribonuclease 9, a member of ribonuclease A superfamily, specifically expressed in epididymis, is a novel spermbinding protein
    • Cheng, G.Z., et al., Human ribonuclease 9, a member of ribonuclease A superfamily, specifically expressed in epididymis, is a novel spermbinding protein. Asian J Androl, 2009. 11(2): p. 240-51.
    • (2009) Asian J Androl , vol.11 , Issue.2 , pp. 240-51
    • Cheng, G.Z.1
  • 47
    • 84864839075 scopus 로고    scopus 로고
    • Tumour lineage-homing cell-penetrating peptides as anticancer molecular delivery systems
    • Kondo, E., et al., Tumour lineage-homing cell-penetrating peptides as anticancer molecular delivery systems. Nat Commun, 2012. 3: p. 951.
    • (2012) Nat Commun , vol.3 , pp. 951
    • Kondo, E.1


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