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Volumn 7, Issue 9, 2012, Pages

Antitumor and Angiostatic Activities of the Antimicrobial Peptide Dermaseptin B2

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; DERMASEPTIN; DERMASEPTIN B2; LACTATE DEHYDROGENASE; PACLITAXEL; UNCLASSIFIED DRUG;

EID: 84866645181     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0044351     Document Type: Article
Times cited : (62)

References (78)
  • 1
    • 0036176510 scopus 로고    scopus 로고
    • Mechanisms of cancer drug resistance
    • Gottesman MM, (2002) Mechanisms of cancer drug resistance. Annu Rev Med 53: 615-627.
    • (2002) Annu Rev Med , vol.53 , pp. 615-627
    • Gottesman, M.M.1
  • 2
    • 20544437870 scopus 로고    scopus 로고
    • Overview of tumor cell chemoresistance mechanisms
    • Gatti L, Zunino F, (2005) Overview of tumor cell chemoresistance mechanisms. Methods Mol Med 111: 127-148.
    • (2005) Methods Mol Med , vol.111 , pp. 127-148
    • Gatti, L.1    Zunino, F.2
  • 3
    • 0029051685 scopus 로고
    • Defensins and other endogenous peptide antibiotics of vertebrates
    • Martin E, Ganz T, Lehrer RI, (1995) Defensins and other endogenous peptide antibiotics of vertebrates. J Leukoc Biol 58: 128-136.
    • (1995) J Leukoc Biol , vol.58 , pp. 128-136
    • Martin, E.1    Ganz, T.2    Lehrer, R.I.3
  • 4
    • 0347755460 scopus 로고    scopus 로고
    • APD: the Antimicrobial Peptide Database
    • Wang Z, Wang G, (2004) APD: the Antimicrobial Peptide Database. Nucleic Acids Res 32: D590-592.
    • (2004) Nucleic Acids Res , vol.32
    • Wang, Z.1    Wang, G.2
  • 5
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman HG, (1995) Peptide antibiotics and their role in innate immunity. Annu Rev Immunol 13: 61-92.
    • (1995) Annu Rev Immunol , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 6
    • 0032005344 scopus 로고    scopus 로고
    • Antimicrobial peptides of vertebrates
    • Ganz T, Lehrer RI, (1998) Antimicrobial peptides of vertebrates. Curr Opin Immunol 10: 41-44.
    • (1998) Curr Opin Immunol , vol.10 , pp. 41-44
    • Ganz, T.1    Lehrer, R.I.2
  • 7
    • 0032444189 scopus 로고    scopus 로고
    • Antimicrobial peptides from amphibian skin: what do they tell us?
    • Simmaco M, Mignogna G, Barra D, (1998) Antimicrobial peptides from amphibian skin: what do they tell us? Biopolymers 47: 435-450.
    • (1998) Biopolymers , vol.47 , pp. 435-450
    • Simmaco, M.1    Mignogna, G.2    Barra, D.3
  • 8
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M, (2002) Antimicrobial peptides of multicellular organisms. Nature 415: 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 9
    • 0028829183 scopus 로고
    • Peptides as weapons against microorganisms in the chemical defense system of vertebrates
    • Nicolas P, Mor A, (1995) Peptides as weapons against microorganisms in the chemical defense system of vertebrates. Annu Rev Microbiol 49: 277-304.
    • (1995) Annu Rev Microbiol , vol.49 , pp. 277-304
    • Nicolas, P.1    Mor, A.2
  • 10
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defences
    • Hancock RE, Diamond G, (2000) The role of cationic antimicrobial peptides in innate host defences. Trends Microbiol 8: 402-410.
    • (2000) Trends Microbiol , vol.8 , pp. 402-410
    • Hancock, R.E.1    Diamond, G.2
  • 11
    • 33645063190 scopus 로고    scopus 로고
    • Modelling the anti-herpes simplex virus activity of small cationic peptides using amino acid descriptors
    • Jenssen H, Gutteberg TJ, Lejon T, (2005) Modelling the anti-herpes simplex virus activity of small cationic peptides using amino acid descriptors. J Pept Res 66Suppl 1: 48-56.
    • (2005) J Pept Res , vol.66 , pp. 48-56
    • Jenssen, H.1    Gutteberg, T.J.2    Lejon, T.3
  • 12
    • 38349009178 scopus 로고    scopus 로고
    • Studies on anticancer activities of antimicrobial peptides
    • Hoskin DW, Ramamoorthy A, (2008) Studies on anticancer activities of antimicrobial peptides. Biochim Biophys Acta 1778: 357-375.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 357-375
    • Hoskin, D.W.1    Ramamoorthy, A.2
  • 13
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: a new source of antibiotics
    • Hancock RE, Lehrer R, (1998) Cationic peptides: a new source of antibiotics. Trends Biotechnol 16: 82-88.
    • (1998) Trends Biotechnol , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 14
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman MR, Yount NY, (2003) Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 55: 27-55.
    • (2003) Pharmacol Rev , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 15
    • 18544366816 scopus 로고    scopus 로고
    • Host defense peptides as new weapons in cancer treatment
    • Papo N, Shai Y, (2005) Host defense peptides as new weapons in cancer treatment. Cell Mol Life Sci 62: 784-790.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 784-790
    • Papo, N.1    Shai, Y.2
  • 16
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H, Hultmark D, Engstrom A, Bennich H, Boman HG, (1981) Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292: 246-248.
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 17
    • 0030746525 scopus 로고    scopus 로고
    • Effects of the anti-bacterial peptide cecropin B and its analogs, cecropins B-1 and B-2, on liposomes, bacteria, and cancer cells
    • Chen HM, Wang W, Smith D, Chan SC, (1997) Effects of the anti-bacterial peptide cecropin B and its analogs, cecropins B-1 and B-2, on liposomes, bacteria, and cancer cells. Biochim Biophys Acta 1336: 171-179.
    • (1997) Biochim Biophys Acta , vol.1336 , pp. 171-179
    • Chen, H.M.1    Wang, W.2    Smith, D.3    Chan, S.C.4
  • 18
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff M, (1987) Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc Natl Acad Sci U S A 84: 5449-5453.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 19
    • 0025860280 scopus 로고
    • Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation
    • Cruciani RA, Barker JL, Zasloff M, Chen HC, Colamonici O, (1991) Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation. Proc Natl Acad Sci U S A 88: 3792-3796.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3792-3796
    • Cruciani, R.A.1    Barker, J.L.2    Zasloff, M.3    Chen, H.C.4    Colamonici, O.5
  • 20
    • 0027166016 scopus 로고
    • Anticancer efficacy of Magainin2 and analogue peptides
    • Baker MA, Maloy WL, Zasloff M, Jacob LS, (1993) Anticancer efficacy of Magainin2 and analogue peptides. Cancer Res 53: 3052-3057.
    • (1993) Cancer Res , vol.53 , pp. 3052-3057
    • Baker, M.A.1    Maloy, W.L.2    Zasloff, M.3    Jacob, L.S.4
  • 21
    • 0013849093 scopus 로고
    • [On the biochemistry of bee venom peptides, melittin and apamin]
    • Habermann E, Reiz KG, (1965) [On the biochemistry of bee venom peptides, melittin and apamin]. Biochem Z 343: 192-203.
    • (1965) Biochem Z , vol.343 , pp. 192-203
    • Habermann, E.1    Reiz, K.G.2
  • 22
    • 0035503496 scopus 로고    scopus 로고
    • A proapoptotic peptide for the treatment of solid tumors
    • Mai JC, Mi Z, Kim SH, Ng B, Robbins PD, (2001) A proapoptotic peptide for the treatment of solid tumors. Cancer Res 61: 7709-7712.
    • (2001) Cancer Res , vol.61 , pp. 7709-7712
    • Mai, J.C.1    Mi, Z.2    Kim, S.H.3    Ng, B.4    Robbins, P.D.5
  • 23
    • 0022886732 scopus 로고
    • In vitro tumor cell cytolysis mediated by peptide defensins of human and rabbit granulocytes
    • Lichtenstein A, Ganz T, Selsted ME, Lehrer RI, (1986) In vitro tumor cell cytolysis mediated by peptide defensins of human and rabbit granulocytes. Blood 68: 1407-1410.
    • (1986) Blood , vol.68 , pp. 1407-1410
    • Lichtenstein, A.1    Ganz, T.2    Selsted, M.E.3    Lehrer, R.I.4
  • 24
    • 0032488904 scopus 로고    scopus 로고
    • Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37
    • Johansson J, Gudmundsson GH, Rottenberg ME, Berndt KD, Agerberth B, (1998) Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. J Biol Chem 273: 3718-3724.
    • (1998) J Biol Chem , vol.273 , pp. 3718-3724
    • Johansson, J.1    Gudmundsson, G.H.2    Rottenberg, M.E.3    Berndt, K.D.4    Agerberth, B.5
  • 25
    • 1042267410 scopus 로고    scopus 로고
    • Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes?
    • Papo N, Shai Y, (2003) Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes? Peptides 24: 1693-1703.
    • (2003) Peptides , vol.24 , pp. 1693-1703
    • Papo, N.1    Shai, Y.2
  • 26
    • 0042573730 scopus 로고    scopus 로고
    • New lytic peptides based on the D,L-amphipathic helix motif preferentially kill tumor cells compared to normal cells
    • Papo N, Shai Y, (2003) New lytic peptides based on the D,L-amphipathic helix motif preferentially kill tumor cells compared to normal cells. Biochemistry 42: 9346-9354.
    • (2003) Biochemistry , vol.42 , pp. 9346-9354
    • Papo, N.1    Shai, Y.2
  • 27
    • 0034618590 scopus 로고    scopus 로고
    • CRAMP analogues having potent antibiotic activity against bacterial, fungal, and tumor cells without hemolytic activity
    • Shin SY, Kang SW, Lee DG, Eom SH, Song WK, et al. (2000) CRAMP analogues having potent antibiotic activity against bacterial, fungal, and tumor cells without hemolytic activity. Biochem Biophys Res Commun 275: 904-909.
    • (2000) Biochem Biophys Res Commun , vol.275 , pp. 904-909
    • Shin, S.Y.1    Kang, S.W.2    Lee, D.G.3    Eom, S.H.4    Song, W.K.5
  • 29
    • 0032511047 scopus 로고    scopus 로고
    • Structure, synthesis, and molecular cloning of dermaseptins B, a family of skin peptide antibiotics
    • Charpentier S, Amiche M, Mester J, Vouille V, Le Caer JP, et al. (1998) Structure, synthesis, and molecular cloning of dermaseptins B, a family of skin peptide antibiotics. J Biol Chem 273: 14690-14697.
    • (1998) J Biol Chem , vol.273 , pp. 14690-14697
    • Charpentier, S.1    Amiche, M.2    Mester, J.3    Vouille, V.4    Le Caer, J.P.5
  • 30
    • 59849092098 scopus 로고    scopus 로고
    • Mechanism of antibacterial action of dermaseptin B2: interplay between helix-hinge-helix structure and membrane curvature strain
    • Galanth C, Abbassi F, Lequin O, Ayala-Sanmartin J, Ladram A, et al. (2009) Mechanism of antibacterial action of dermaseptin B2: interplay between helix-hinge-helix structure and membrane curvature strain. Biochemistry 48: 313-327.
    • (2009) Biochemistry , vol.48 , pp. 313-327
    • Galanth, C.1    Abbassi, F.2    Lequin, O.3    Ayala-Sanmartin, J.4    Ladram, A.5
  • 31
    • 0028240042 scopus 로고
    • Structure, synthesis, and activity of dermaseptin b, a novel vertebrate defensive peptide from frog skin: relationship with adenoregulin
    • Mor A, Amiche M, Nicolas P, (1994) Structure, synthesis, and activity of dermaseptin b, a novel vertebrate defensive peptide from frog skin: relationship with adenoregulin. Biochemistry 33: 6642-6650.
    • (1994) Biochemistry , vol.33 , pp. 6642-6650
    • Mor, A.1    Amiche, M.2    Nicolas, P.3
  • 32
    • 67649262194 scopus 로고    scopus 로고
    • The dermaseptin superfamily: a gene-based combinatorial library of antimicrobial peptides
    • Nicolas P, El Amri C, (2009) The dermaseptin superfamily: a gene-based combinatorial library of antimicrobial peptides. Biochim Biophys Acta 1788: 1537-1550.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1537-1550
    • Nicolas, P.1    El Amri, C.2
  • 33
    • 0027204174 scopus 로고
    • Molecular cloning of a cDNA encoding the precursor of adenoregulin from frog skin. Relationships with the vertebrate defensive peptides, dermaseptins
    • Amiche M, Ducancel F, Lajeunesse E, Boulain JC, Menez A, et al. (1993) Molecular cloning of a cDNA encoding the precursor of adenoregulin from frog skin. Relationships with the vertebrate defensive peptides, dermaseptins. Biochem Biophys Res Commun 191: 983-990.
    • (1993) Biochem Biophys Res Commun , vol.191 , pp. 983-990
    • Amiche, M.1    Ducancel, F.2    Lajeunesse, E.3    Boulain, J.C.4    Menez, A.5
  • 34
    • 0028225882 scopus 로고
    • Precursors of vertebrate peptide antibiotics dermaseptin b and adenoregulin have extensive sequence identities with precursors of opioid peptides dermorphin, dermenkephalin, and deltorphins
    • Amiche M, Ducancel F, Mor A, Boulain JC, Menez A, et al. (1994) Precursors of vertebrate peptide antibiotics dermaseptin b and adenoregulin have extensive sequence identities with precursors of opioid peptides dermorphin, dermenkephalin, and deltorphins. J Biol Chem 269: 17847-17852.
    • (1994) J Biol Chem , vol.269 , pp. 17847-17852
    • Amiche, M.1    Ducancel, F.2    Mor, A.3    Boulain, J.C.4    Menez, A.5
  • 36
    • 0026493568 scopus 로고
    • Frog secretions and hunting magic in the upper Amazon: identification of a peptide that interacts with an adenosine receptor
    • Daly JW, Caceres J, Moni RW, Gusovsky F, Moos M Jr, et al. (1992) Frog secretions and hunting magic in the upper Amazon: identification of a peptide that interacts with an adenosine receptor. Proc Natl Acad Sci U S A 89: 10960-10963.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 10960-10963
    • Daly, J.W.1    Caceres, J.2    Moni, R.W.3    Gusovsky, F.4    Moos Jr., M.5
  • 37
    • 0033083310 scopus 로고    scopus 로고
    • Elevation of mitochondrial transmembrane potential and reactive oxygen intermediate levels are early events and occur independently from activation of caspases in Fas signaling
    • Banki K, Hutter E, Gonchoroff NJ, Perl A, (1999) Elevation of mitochondrial transmembrane potential and reactive oxygen intermediate levels are early events and occur independently from activation of caspases in Fas signaling. J Immunol 162: 1466-1479.
    • (1999) J Immunol , vol.162 , pp. 1466-1479
    • Banki, K.1    Hutter, E.2    Gonchoroff, N.J.3    Perl, A.4
  • 38
    • 80052827055 scopus 로고    scopus 로고
    • EMMPRIN modulates epithelial barrier function through a MMP-mediated occludin cleavage: implications in dry eye disease
    • Huet E, Vallee B, Delbe J, Mourah S, Pruliere-Escabasse V, et al. (2011) EMMPRIN modulates epithelial barrier function through a MMP-mediated occludin cleavage: implications in dry eye disease. Am J Pathol 179: 1278-1286.
    • (2011) Am J Pathol , vol.179 , pp. 1278-1286
    • Huet, E.1    Vallee, B.2    Delbe, J.3    Mourah, S.4    Pruliere-Escabasse, V.5
  • 39
    • 34548461166 scopus 로고    scopus 로고
    • Peptides with differential cytolytic activity from skin secretions of the lemur leaf frog Hylomantis lemur (Hylidae: Phyllomedusinae)
    • Conlon JM, Woodhams DC, Raza H, Coquet L, Leprince J, et al. (2007) Peptides with differential cytolytic activity from skin secretions of the lemur leaf frog Hylomantis lemur (Hylidae: Phyllomedusinae). Toxicon 50: 498-506.
    • (2007) Toxicon , vol.50 , pp. 498-506
    • Conlon, J.M.1    Woodhams, D.C.2    Raza, H.3    Coquet, L.4    Leprince, J.5
  • 40
    • 84875090987 scopus 로고    scopus 로고
    • APD (website) (Antimicrobial Peptide Database). Available: http://apsunmcedu/AP Accessed: 2012 August 26.
  • 41
    • 0037742621 scopus 로고    scopus 로고
    • A novel lytic peptide composed of DL-amino acids selectively kills cancer cells in culture and in mice
    • Papo N, Shahar M, Eisenbach L, Shai Y, (2003) A novel lytic peptide composed of DL-amino acids selectively kills cancer cells in culture and in mice. J Biol Chem 278: 21018-21023.
    • (2003) J Biol Chem , vol.278 , pp. 21018-21023
    • Papo, N.1    Shahar, M.2    Eisenbach, L.3    Shai, Y.4
  • 42
    • 0030940982 scopus 로고    scopus 로고
    • Bovine lactoferrin and lactoferricin, a peptide derived from bovine lactoferrin, inhibit tumor metastasis in mice
    • Yoo YC, Watanabe S, Watanabe R, Hata K, Shimazaki K, et al. (1997) Bovine lactoferrin and lactoferricin, a peptide derived from bovine lactoferrin, inhibit tumor metastasis in mice. Jpn J Cancer Res 88: 184-190.
    • (1997) Jpn J Cancer Res , vol.88 , pp. 184-190
    • Yoo, Y.C.1    Watanabe, S.2    Watanabe, R.3    Hata, K.4    Shimazaki, K.5
  • 43
    • 18044397724 scopus 로고    scopus 로고
    • Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines
    • Mader JS, Salsman J, Conrad DM, Hoskin DW, (2005) Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines. Mol Cancer Ther 4: 612-624.
    • (2005) Mol Cancer Ther , vol.4 , pp. 612-624
    • Mader, J.S.1    Salsman, J.2    Conrad, D.M.3    Hoskin, D.W.4
  • 44
    • 33745441169 scopus 로고    scopus 로고
    • The antimicrobial peptide, lactoferricin B, is cytotoxic to neuroblastoma cells in vitro and inhibits xenograft growth in vivo
    • Eliassen LT, Berge G, Leknessund A, Wikman M, Lindin I, et al. (2006) The antimicrobial peptide, lactoferricin B, is cytotoxic to neuroblastoma cells in vitro and inhibits xenograft growth in vivo. Int J Cancer 119: 493-500.
    • (2006) Int J Cancer , vol.119 , pp. 493-500
    • Eliassen, L.T.1    Berge, G.2    Leknessund, A.3    Wikman, M.4    Lindin, I.5
  • 46
    • 0033067113 scopus 로고    scopus 로고
    • Peptide-bilayer interactions: simulations of dermaseptin B, an antimicrobial peptide
    • La Rocca P, Shai Y, Sansom MS, (1999) Peptide-bilayer interactions: simulations of dermaseptin B, an antimicrobial peptide. Biophys Chem 76: 145-159.
    • (1999) Biophys Chem , vol.76 , pp. 145-159
    • La Rocca, P.1    Shai, Y.2    Sansom, M.S.3
  • 47
    • 0028174888 scopus 로고
    • The NH2-terminal alpha-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity
    • Mor A, Nicolas P, (1994) The NH2-terminal alpha-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity. J Biol Chem 269: 1934-1939.
    • (1994) J Biol Chem , vol.269 , pp. 1934-1939
    • Mor, A.1    Nicolas, P.2
  • 48
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Pouny Y, Rapaport D, Mor A, Nicolas P, Shai Y, (1992) Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry 31: 12416-12423.
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 49
    • 50349083103 scopus 로고    scopus 로고
    • Synthesis and antimicrobial activity of dermaseptin S1 analogues
    • Savoia D, Guerrini R, Marzola E, Salvadori S, (2008) Synthesis and antimicrobial activity of dermaseptin S1 analogues. Bioorg Med Chem 16: 8205-8209.
    • (2008) Bioorg Med Chem , vol.16 , pp. 8205-8209
    • Savoia, D.1    Guerrini, R.2    Marzola, E.3    Salvadori, S.4
  • 50
    • 0028101288 scopus 로고
    • Spectrum of antimicrobial activity and assembly of dermaseptin-b and its precursor form in phospholipid membranes
    • Strahilevitz J, Mor A, Nicolas P, Shai Y, (1994) Spectrum of antimicrobial activity and assembly of dermaseptin-b and its precursor form in phospholipid membranes. Biochemistry 33: 10951-10960.
    • (1994) Biochemistry , vol.33 , pp. 10951-10960
    • Strahilevitz, J.1    Mor, A.2    Nicolas, P.3    Shai, Y.4
  • 51
    • 79960444560 scopus 로고    scopus 로고
    • Dermaseptins as models for the elucidation of membrane-acting helical amphipathic antimicrobial peptides
    • Amiche M, Galanth C, (2011) Dermaseptins as models for the elucidation of membrane-acting helical amphipathic antimicrobial peptides. Curr Pharm Biotechnol 12: 1184-1193.
    • (2011) Curr Pharm Biotechnol , vol.12 , pp. 1184-1193
    • Amiche, M.1    Galanth, C.2
  • 52
    • 0034630167 scopus 로고    scopus 로고
    • Induction of apoptosis by cancer chemotherapy
    • Kaufmann SH, Earnshaw WC, (2000) Induction of apoptosis by cancer chemotherapy. Exp Cell Res 256: 42-49.
    • (2000) Exp Cell Res , vol.256 , pp. 42-49
    • Kaufmann, S.H.1    Earnshaw, W.C.2
  • 53
    • 0033773114 scopus 로고    scopus 로고
    • Apoptosis in cancer: cause and cure
    • Kaufmann SH, Gores GJ, (2000) Apoptosis in cancer: cause and cure. Bioessays 22: 1007-1017.
    • (2000) Bioessays , vol.22 , pp. 1007-1017
    • Kaufmann, S.H.1    Gores, G.J.2
  • 54
  • 55
    • 0038481271 scopus 로고    scopus 로고
    • Mitochondrial regulation of apoptosis
    • Mayer B, Oberbauer R, (2003) Mitochondrial regulation of apoptosis. News Physiol Sci 18: 89-94.
    • (2003) News Physiol Sci , vol.18 , pp. 89-94
    • Mayer, B.1    Oberbauer, R.2
  • 56
    • 33847400593 scopus 로고    scopus 로고
    • Metabolic catastrophe as a means to cancer cell death
    • Jin S, DiPaola RS, Mathew R, White E, (2007) Metabolic catastrophe as a means to cancer cell death. J Cell Sci 120: 379-383.
    • (2007) J Cell Sci , vol.120 , pp. 379-383
    • Jin, S.1    DiPaola, R.S.2    Mathew, R.3    White, E.4
  • 57
    • 0033600733 scopus 로고    scopus 로고
    • The mode of action of taxol: apoptosis at low concentration and necrosis at high concentration
    • Yeung TK, Germond C, Chen X, Wang Z, (1999) The mode of action of taxol: apoptosis at low concentration and necrosis at high concentration. Biochem Biophys Res Commun 263: 398-404.
    • (1999) Biochem Biophys Res Commun , vol.263 , pp. 398-404
    • Yeung, T.K.1    Germond, C.2    Chen, X.3    Wang, Z.4
  • 58
    • 0034949453 scopus 로고    scopus 로고
    • Anticancer drugs induce necrosis of human endothelial cells involving both oncosis and apoptosis
    • Mailloux A, Grenet K, Bruneel A, Beneteau-Burnat B, Vaubourdolle M, et al. (2001) Anticancer drugs induce necrosis of human endothelial cells involving both oncosis and apoptosis. Eur J Cell Biol 80: 442-449.
    • (2001) Eur J Cell Biol , vol.80 , pp. 442-449
    • Mailloux, A.1    Grenet, K.2    Bruneel, A.3    Beneteau-Burnat, B.4    Vaubourdolle, M.5
  • 59
    • 12844274352 scopus 로고    scopus 로고
    • Cell cycle specific induction of apoptosis and necrosis by paclitaxel in the leukemic U937 cells
    • Liao PC, Lieu CH, (2005) Cell cycle specific induction of apoptosis and necrosis by paclitaxel in the leukemic U937 cells. Life Sci 76: 1623-1639.
    • (2005) Life Sci , vol.76 , pp. 1623-1639
    • Liao, P.C.1    Lieu, C.H.2
  • 60
    • 7044262888 scopus 로고    scopus 로고
    • Effect of defensin peptides on eukaryotic cells: primary epithelial cells, fibroblasts and squamous cell carcinoma cell lines
    • Nishimura M, Abiko Y, Kurashige Y, Takeshima M, Yamazaki M, et al. (2004) Effect of defensin peptides on eukaryotic cells: primary epithelial cells, fibroblasts and squamous cell carcinoma cell lines. J Dermatol Sci 36: 87-95.
    • (2004) J Dermatol Sci , vol.36 , pp. 87-95
    • Nishimura, M.1    Abiko, Y.2    Kurashige, Y.3    Takeshima, M.4    Yamazaki, M.5
  • 61
    • 0028243313 scopus 로고
    • Mitogenic and in vitro angiogenic activity of human recombinant heparin affin regulatory peptide
    • Laaroubi K, Delbe J, Vacherot F, Desgranges P, Tardieu M, et al. (1994) Mitogenic and in vitro angiogenic activity of human recombinant heparin affin regulatory peptide. Growth Factors 10: 89-98.
    • (1994) Growth Factors , vol.10 , pp. 89-98
    • Laaroubi, K.1    Delbe, J.2    Vacherot, F.3    Desgranges, P.4    Tardieu, M.5
  • 62
    • 0024333838 scopus 로고
    • Modulation of mitogenic activity and cellular binding of basic fibroblast growth factor by basic proteins
    • Dauchel MC, Courty J, Mereau A, Barritault D, (1989) Modulation of mitogenic activity and cellular binding of basic fibroblast growth factor by basic proteins. J Cell Biochem 39: 411-420.
    • (1989) J Cell Biochem , vol.39 , pp. 411-420
    • Dauchel, M.C.1    Courty, J.2    Mereau, A.3    Barritault, D.4
  • 63
    • 36849053590 scopus 로고    scopus 로고
    • Inhibition of the mitogenic, angiogenic and tumorigenic activities of pleiotrophin by a synthetic peptide corresponding to its C-thrombospondin repeat-I domain
    • Hamma-Kourbali Y, Bernard-Pierrot I, Heroult M, Dalle S, Caruelle D, et al. (2008) Inhibition of the mitogenic, angiogenic and tumorigenic activities of pleiotrophin by a synthetic peptide corresponding to its C-thrombospondin repeat-I domain. J Cell Physiol 214: 250-259.
    • (2008) J Cell Physiol , vol.214 , pp. 250-259
    • Hamma-Kourbali, Y.1    Bernard-Pierrot, I.2    Heroult, M.3    Dalle, S.4    Caruelle, D.5
  • 64
    • 0032894996 scopus 로고    scopus 로고
    • Involvement of heparin affin regulatory peptide in human prostate cancer
    • Vacherot F, Caruelle D, Chopin D, Gil-Diez S, Barritault D, et al. (1999) Involvement of heparin affin regulatory peptide in human prostate cancer. Prostate 38: 126-136.
    • (1999) Prostate , vol.38 , pp. 126-136
    • Vacherot, F.1    Caruelle, D.2    Chopin, D.3    Gil-Diez, S.4    Barritault, D.5
  • 65
    • 55349145994 scopus 로고    scopus 로고
    • Pleiotrophin induces expression of inflammatory cytokines in peripheral blood mononuclear cells
    • Achour A, M'Bika J P, Baudouin F, Caruelle D, Courty J, (2008) Pleiotrophin induces expression of inflammatory cytokines in peripheral blood mononuclear cells. Biochimie 90: 1791-1795.
    • (2008) Biochimie , vol.90 , pp. 1791-1795
    • Achour, A.1    M'Bika, J.P.2    Baudouin, F.3    Caruelle, D.4    Courty, J.5
  • 66
    • 0032842569 scopus 로고    scopus 로고
    • Transforming growth factor(beta)-mediated corneal myofibroblast differentiation requires actin and fibronectin assembly
    • Jester JV, Huang J, Barry-Lane PA, Kao WW, Petroll WM, et al. (1999) Transforming growth factor(beta)-mediated corneal myofibroblast differentiation requires actin and fibronectin assembly. Invest Ophthalmol Vis Sci 40: 1959-1967.
    • (1999) Invest Ophthalmol Vis Sci , vol.40 , pp. 1959-1967
    • Jester, J.V.1    Huang, J.2    Barry-Lane, P.A.3    Kao, W.W.4    Petroll, W.M.5
  • 67
    • 0021041091 scopus 로고
    • Bovine brain and pituitary fibroblast growth factors: comparison of their abilities to support the proliferation of human and bovine vascular endothelial cells
    • Gospodarowicz D, Cheng J, Lirette M, (1983) Bovine brain and pituitary fibroblast growth factors: comparison of their abilities to support the proliferation of human and bovine vascular endothelial cells. J Cell Biol 97: 1677-1685.
    • (1983) J Cell Biol , vol.97 , pp. 1677-1685
    • Gospodarowicz, D.1    Cheng, J.2    Lirette, M.3
  • 68
    • 0022880936 scopus 로고
    • Determination of cell number in monolayer cultures
    • Gillies RJ, Didier N, Denton M, (1986) Determination of cell number in monolayer cultures. Anal Biochem 159: 109-113.
    • (1986) Anal Biochem , vol.159 , pp. 109-113
    • Gillies, R.J.1    Didier, N.2    Denton, M.3
  • 69
    • 0041935939 scopus 로고    scopus 로고
    • Rasband WS (1997-2011) ImageJ website, U. S. National Institutes of Health, Bethesda, Maryland, USA. Available: http://imagejnihgov/ij/ Accessed 2012 August 26.
    • (1997) ImageJ
    • Rasband, W.S.1
  • 70
    • 0030837243 scopus 로고    scopus 로고
    • Adaptive color segmentation - a comparison of neural and statistical methods
    • Littmann E, Ritter H, (1997) Adaptive color segmentation- a comparison of neural and statistical methods. IEEE Trans Neural Netw 8: 175-185.
    • (1997) IEEE Trans Neural Netw , vol.8 , pp. 175-185
    • Littmann, E.1    Ritter, H.2
  • 71
    • 84875100505 scopus 로고    scopus 로고
    • A plugin that does gaussian filtering in Fourier space
    • website Available
    • Walter J (2001) A plugin that does gaussian filtering in Fourier space. Research Services Branch, Image J website Available: http://rsbinfonihgov/ij/plugins/fft-filterhtml Accessed 2012 August 26.
    • (2001) Image J
    • Walter, J.1
  • 73
    • 0018004847 scopus 로고
    • Picture Thresholding Using an Iterative Selection Method, IEEE transactions on Systems
    • Ridler T, Calvard S, (1978) Picture Thresholding Using an Iterative Selection Method, IEEE transactions on Systems. Man and Cybernetics.
    • (1978) Man and Cybernetics
    • Ridler, T.1    Calvard, S.2
  • 74
    • 84875102984 scopus 로고    scopus 로고
    • Macros that demonstrate how to do curve fitting and how to calculate and plot first and second derivatives
    • website Available
    • Carpentier G (2009) Macros that demonstrate how to do curve fitting and how to calculate and plot first and second derivatives. Research Services Branch, Image J website Available: http://rsbinfonihgov/ij/macros/examples/PlotSigmoidDerivativestxt Accessed 2012 August 26.
    • (2009) Image J
    • Carpentier, G.1
  • 75
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 76
    • 84875120641 scopus 로고    scopus 로고
    • Zoom in Images and Stacks
    • website Available
    • Carpentier G (2010) Zoom in Images and Stacks. Research Services Branch, Image J website Available: http://rsbinfonihgov/ij/macros/tools/Zoom_in_Images_and_Stackstxt Accessed 2012 August 26.
    • (2010) Image J
    • Carpentier, G.1
  • 77
    • 80051474736 scopus 로고    scopus 로고
    • "Comparison of Deconvolution Software in 3D Microscopy. A User Point of View" Part I and Part II
    • Griffa A, Garin N, Sage D, (2010) "Comparison of Deconvolution Software in 3D Microscopy. A User Point of View" Part I and Part II. GIT Imaging & Microscopy 1: 43-45.
    • (2010) GIT Imaging & Microscopy , vol.1 , pp. 43-45
    • Griffa, A.1    Garin, N.2    Sage, D.3
  • 78
    • 41849087358 scopus 로고    scopus 로고
    • A fast thresholded landweber algorithm for wavelet-regularized multidimensional deconvolution
    • Vonesch C, Unser M, (2008) A fast thresholded landweber algorithm for wavelet-regularized multidimensional deconvolution. IEEE Trans Image Process 17: 539-549.
    • (2008) IEEE Trans Image Process , vol.17 , pp. 539-549
    • Vonesch, C.1    Unser, M.2


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