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Volumn 35, Issue 11, 2014, Pages 3627-3640

The mechanisms by which pardaxin, a natural cationic antimicrobial peptide, targets the endoplasmic reticulum and induces c-FOS

Author keywords

C FOS; Calcium; Cationic antimicrobial peptide; Endoplasmic reticulum; Pardaxin

Indexed keywords

C-FOS; CALCIUM; CATIONIC ANTIMICROBIAL PEPTIDE; ENDOPLASMIC RETICULUM; PARDAXIN;

EID: 84894934931     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2014.01.032     Document Type: Article
Times cited : (60)

References (58)
  • 1
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002, 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 2
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti M. Cathelicidins, multifunctional peptides of the innate immunity. JLeukoc Biol 2004, 75:39-48.
    • (2004) JLeukoc Biol , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 3
    • 28044469064 scopus 로고    scopus 로고
    • Function and therapeutic potential of host defence peptides
    • McPhee J.B., Hancock R.E. Function and therapeutic potential of host defence peptides. JPept Sci 2005, 11:677-687.
    • (2005) JPept Sci , vol.11 , pp. 677-687
    • McPhee, J.B.1    Hancock, R.E.2
  • 4
    • 33749006591 scopus 로고    scopus 로고
    • The human beta-defensin-3, an antibacterial peptide with multiple biological functions
    • Dhople V., Krukemeyer A., Ramamoorthy A. The human beta-defensin-3, an antibacterial peptide with multiple biological functions. Biochim Biophys Acta 2006, 1758:1499-1512.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1499-1512
    • Dhople, V.1    Krukemeyer, A.2    Ramamoorthy, A.3
  • 5
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • Durr U.H., Sudheendra U.S., Ramamoorthy A. LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim Biophys Acta 2006, 1758:1408-1425.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1408-1425
    • Durr, U.H.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 6
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers J.P., Hancock R.E. The relationship between peptide structure and antibacterial activity. Peptides 2003, 24:1681-1691.
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.2
  • 7
    • 0037742621 scopus 로고    scopus 로고
    • Anovel lytic peptide composed of DL-amino acids selectively kills cancer cells in culture and in mice
    • Papo N., Shahar M., Eisenbach L., Shai Y. Anovel lytic peptide composed of DL-amino acids selectively kills cancer cells in culture and in mice. JBiol Chem 2003, 278:21018-21023.
    • (2003) JBiol Chem , vol.278 , pp. 21018-21023
    • Papo, N.1    Shahar, M.2    Eisenbach, L.3    Shai, Y.4
  • 8
    • 80054881646 scopus 로고    scopus 로고
    • Pardaxin, an antimicrobial peptide, triggers caspase-dependent and ROS-mediated apoptosis in HT-1080 cells
    • Huang T.C., Lee J.F., Chen J.Y. Pardaxin, an antimicrobial peptide, triggers caspase-dependent and ROS-mediated apoptosis in HT-1080 cells. Mar Drugs 2011, 9:1995-2009.
    • (2011) Mar Drugs , vol.9 , pp. 1995-2009
    • Huang, T.C.1    Lee, J.F.2    Chen, J.Y.3
  • 9
    • 38349009178 scopus 로고    scopus 로고
    • Studies on anticancer activities of antimicrobial peptides
    • Hoskin D.W., Ramamoorthy A. Studies on anticancer activities of antimicrobial peptides. Biochim Biophys Acta 2008, 1778:357-375.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 357-375
    • Hoskin, D.W.1    Ramamoorthy, A.2
  • 10
    • 67649262183 scopus 로고    scopus 로고
    • Structure, membrane orientation, mechanism, and function of pexiganan-a highly potent antimicrobial peptide designed from magainin
    • Gottler L.M., Ramamoorthy A. Structure, membrane orientation, mechanism, and function of pexiganan-a highly potent antimicrobial peptide designed from magainin. Biochim Biophys Acta 2009, 1788:1680-1686.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1680-1686
    • Gottler, L.M.1    Ramamoorthy, A.2
  • 11
    • 67349241519 scopus 로고    scopus 로고
    • Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights
    • Ramamoorthy A. Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights. Solid State Nucl Magn Reson 2009, 35:201-207.
    • (2009) Solid State Nucl Magn Reson , vol.35 , pp. 201-207
    • Ramamoorthy, A.1
  • 12
    • 74249106455 scopus 로고    scopus 로고
    • Cholesterol reduces pardaxin's dynamics-a barrel-stave mechanism of membrane disruption investigated by solid-state NMR
    • Ramamoorthy A., Lee D.K., Narasimhaswamy T., Nanga R.P. Cholesterol reduces pardaxin's dynamics-a barrel-stave mechanism of membrane disruption investigated by solid-state NMR. Biochim Biophys Acta 2010, 1798:223-227.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 223-227
    • Ramamoorthy, A.1    Lee, D.K.2    Narasimhaswamy, T.3    Nanga, R.P.4
  • 13
    • 0035997051 scopus 로고    scopus 로고
    • Membrane composition determines pardaxin's mechanism of lipid bilayer disruption
    • Hallock K.J., Lee D.K., Omnaas J., Mosberg H.I., Ramamoorthy A. Membrane composition determines pardaxin's mechanism of lipid bilayer disruption. Biophys J 2002, 83:1004-1013.
    • (2002) Biophys J , vol.83 , pp. 1004-1013
    • Hallock, K.J.1    Lee, D.K.2    Omnaas, J.3    Mosberg, H.I.4    Ramamoorthy, A.5
  • 14
    • 7744229375 scopus 로고    scopus 로고
    • Structure and orientation of pardaxin determined by NMR experiments in model membranes
    • Porcelli F., Buck B., Lee D.K., Hallock K.J., Ramamoorthy A., Veglia G. Structure and orientation of pardaxin determined by NMR experiments in model membranes. JBiol Chem 2004, 279:45815-45823.
    • (2004) JBiol Chem , vol.279 , pp. 45815-45823
    • Porcelli, F.1    Buck, B.2    Lee, D.K.3    Hallock, K.J.4    Ramamoorthy, A.5    Veglia, G.6
  • 15
    • 33645737243 scopus 로고    scopus 로고
    • Membrane lipid composition and the interaction of pardaxin: the role of cholesterol
    • Epand R.F., Ramamoorthy A., Epand R.M. Membrane lipid composition and the interaction of pardaxin: the role of cholesterol. Protein Pept Lett 2006, 13:1-5.
    • (2006) Protein Pept Lett , vol.13 , pp. 1-5
    • Epand, R.F.1    Ramamoorthy, A.2    Epand, R.M.3
  • 16
    • 0001613365 scopus 로고
    • Melittin-like peptides from the shark-repelling defense secretion of the sole Pardachirus pavoninus
    • Thompson S.A., Tachibana K., Nakanishi K., Kubota I. Melittin-like peptides from the shark-repelling defense secretion of the sole Pardachirus pavoninus. Science 1986, 233:341-343.
    • (1986) Science , vol.233 , pp. 341-343
    • Thompson, S.A.1    Tachibana, K.2    Nakanishi, K.3    Kubota, I.4
  • 17
    • 0019785158 scopus 로고
    • Pardaxin, a hydrophobic toxin of the Red Sea flatfish, disassembles the intact membrane of vesicular stomatitis virus
    • Pal R., Barenholz Y., Wagner R.R. Pardaxin, a hydrophobic toxin of the Red Sea flatfish, disassembles the intact membrane of vesicular stomatitis virus. JBiol Chem 1981, 256:10209-10212.
    • (1981) JBiol Chem , vol.256 , pp. 10209-10212
    • Pal, R.1    Barenholz, Y.2    Wagner, R.R.3
  • 18
    • 0030474868 scopus 로고    scopus 로고
    • Specific antimicrobial and hemolytic activities of 18-residue peptides derived from the amino terminal region of the toxin pardaxin
    • Thennarasu S., Nagaraj R. Specific antimicrobial and hemolytic activities of 18-residue peptides derived from the amino terminal region of the toxin pardaxin. Protein Eng 1996, 9:1219-1224.
    • (1996) Protein Eng , vol.9 , pp. 1219-1224
    • Thennarasu, S.1    Nagaraj, R.2
  • 19
    • 84885370518 scopus 로고    scopus 로고
    • Acancer vaccine based on the marine antimicrobial peptide pardaxin (GE33) for control of bladder-associated tumors
    • Huang H.N., Rajanbabu V., Pan C.Y., Chan Y.L., Wu C.J., Chen J.Y. Acancer vaccine based on the marine antimicrobial peptide pardaxin (GE33) for control of bladder-associated tumors. Biomaterials 2013, 34:10151-10159.
    • (2013) Biomaterials , vol.34 , pp. 10151-10159
    • Huang, H.N.1    Rajanbabu, V.2    Pan, C.Y.3    Chan, Y.L.4    Wu, C.J.5    Chen, J.Y.6
  • 20
    • 84881533679 scopus 로고    scopus 로고
    • Proteomic analysis reveals that pardaxin triggers apoptotic signaling pathways in human cervical carcinoma HeLa cells: cross talk among the UPR, c-Jun and ROS
    • Huang T.C., Chen J.Y. Proteomic analysis reveals that pardaxin triggers apoptotic signaling pathways in human cervical carcinoma HeLa cells: cross talk among the UPR, c-Jun and ROS. Carcinogenesis 2013, 34:1833-1842.
    • (2013) Carcinogenesis , vol.34 , pp. 1833-1842
    • Huang, T.C.1    Chen, J.Y.2
  • 21
    • 84865963859 scopus 로고    scopus 로고
    • Pardaxin, a fish antimicrobial peptide, exhibits antitumor activity toward murine fibrosarcoma invitro and invivo
    • Wu S.P., Huang T.C., Lin C.C., Hui C.F., Lin C.H., Chen J.Y. Pardaxin, a fish antimicrobial peptide, exhibits antitumor activity toward murine fibrosarcoma invitro and invivo. Mar Drugs 2012, 10:1852-1872.
    • (2012) Mar Drugs , vol.10 , pp. 1852-1872
    • Wu, S.P.1    Huang, T.C.2    Lin, C.C.3    Hui, C.F.4    Lin, C.H.5    Chen, J.Y.6
  • 22
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • Shaulian E., Karin M. AP-1 as a regulator of cell life and death. Nat Cell Biol 2002, 4:E131-E136.
    • (2002) Nat Cell Biol , vol.4
    • Shaulian, E.1    Karin, M.2
  • 23
    • 0242691046 scopus 로고    scopus 로고
    • AP-1: a double-edged sword in tumorigenesis
    • Eferl R., Wagner E.F. AP-1: a double-edged sword in tumorigenesis. Nat Rev Cancer 2003, 3:859-868.
    • (2003) Nat Rev Cancer , vol.3 , pp. 859-868
    • Eferl, R.1    Wagner, E.F.2
  • 24
    • 12344252237 scopus 로고    scopus 로고
    • AP-1 subunits: quarrel and harmony among siblings
    • Hess J., Angel P., Schorpp-Kistner M. AP-1 subunits: quarrel and harmony among siblings. JCell Sci 2004, 117:5965-5973.
    • (2004) JCell Sci , vol.117 , pp. 5965-5973
    • Hess, J.1    Angel, P.2    Schorpp-Kistner, M.3
  • 25
    • 0027236534 scopus 로고
    • Osteoblasts are target cells for transformation in c-fos transgenic mice
    • Grigoriadis A.E., Schellander K., Wang Z.Q., Wagner E.F. Osteoblasts are target cells for transformation in c-fos transgenic mice. JCell Biol 1993, 122:685-701.
    • (1993) JCell Biol , vol.122 , pp. 685-701
    • Grigoriadis, A.E.1    Schellander, K.2    Wang, Z.Q.3    Wagner, E.F.4
  • 26
    • 53849101060 scopus 로고    scopus 로고
    • C-Fos expression is a molecular predictor of progression and survival in epithelial ovarian carcinoma
    • Mahner S., Baasch C., Schwarz J., Hein S., Wolber L., Janicke F., et al. C-Fos expression is a molecular predictor of progression and survival in epithelial ovarian carcinoma. Br J Cancer 2008, 99:1269-1275.
    • (2008) Br J Cancer , vol.99 , pp. 1269-1275
    • Mahner, S.1    Baasch, C.2    Schwarz, J.3    Hein, S.4    Wolber, L.5    Janicke, F.6
  • 27
    • 0034885470 scopus 로고    scopus 로고
    • Expression pattern of the AP-1 family in endometrial cancer: correlations with cell cycle regulators
    • Bamberger A.M., Milde-Langosch K., Rossing E., Goemann C., Loning T. Expression pattern of the AP-1 family in endometrial cancer: correlations with cell cycle regulators. JCancer Res Clin Oncol 2001, 127:545-550.
    • (2001) JCancer Res Clin Oncol , vol.127 , pp. 545-550
    • Bamberger, A.M.1    Milde-Langosch, K.2    Rossing, E.3    Goemann, C.4    Loning, T.5
  • 28
    • 84873579368 scopus 로고    scopus 로고
    • Sodium vanadate combined with L-ascorbic acid delays disease progression, enhances motor performance, and ameliorates muscle atrophy and weakness in mice with spinal muscular atrophy
    • Liu H.C., Ting C.H., Wen H.L., Tsai L.K., Hsieh-Li H.M., Li H., et al. Sodium vanadate combined with L-ascorbic acid delays disease progression, enhances motor performance, and ameliorates muscle atrophy and weakness in mice with spinal muscular atrophy. BMC Med 2013, 11:38.
    • (2013) BMC Med , vol.11 , pp. 38
    • Liu, H.C.1    Ting, C.H.2    Wen, H.L.3    Tsai, L.K.4    Hsieh-Li, H.M.5    Li, H.6
  • 29
    • 77950515754 scopus 로고    scopus 로고
    • NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide micelles: mechanism of outer membrane permeabilization
    • Bhunia A., Domadia P.N., Torres J., Hallock K.J., Ramamoorthy A., Bhattacharjya S. NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide micelles: mechanism of outer membrane permeabilization. JBiol Chem 2010, 285:3883-3895.
    • (2010) JBiol Chem , vol.285 , pp. 3883-3895
    • Bhunia, A.1    Domadia, P.N.2    Torres, J.3    Hallock, K.J.4    Ramamoorthy, A.5    Bhattacharjya, S.6
  • 30
    • 0036329140 scopus 로고    scopus 로고
    • 2-aminoethoxydiphenyl borate (2-APB) is a reliable blocker of store-operated Ca2+ entry but an inconsistent inhibitor of InsP3-induced Ca2+ release
    • Bootman M.D., Collins T.J., Mackenzie L., Roderick H.L., Berridge M.J., Peppiatt C.M. 2-aminoethoxydiphenyl borate (2-APB) is a reliable blocker of store-operated Ca2+ entry but an inconsistent inhibitor of InsP3-induced Ca2+ release. FASEB J 2002, 16:1145-1150.
    • (2002) FASEB J , vol.16 , pp. 1145-1150
    • Bootman, M.D.1    Collins, T.J.2    Mackenzie, L.3    Roderick, H.L.4    Berridge, M.J.5    Peppiatt, C.M.6
  • 31
    • 0025331522 scopus 로고
    • Inhibition of growth factor-dependent inositol phosphate Ca2+ signaling by antitumor ether lipid analogues
    • Seewald M.J., Olsen R.A., Sehgal I., Melder D.C., Modest E.J., Powis G. Inhibition of growth factor-dependent inositol phosphate Ca2+ signaling by antitumor ether lipid analogues. Cancer Res 1990, 50:4458-4463.
    • (1990) Cancer Res , vol.50 , pp. 4458-4463
    • Seewald, M.J.1    Olsen, R.A.2    Sehgal, I.3    Melder, D.C.4    Modest, E.J.5    Powis, G.6
  • 32
    • 0031039206 scopus 로고    scopus 로고
    • Variations in Jun and Fos protein expression and AP-1 activity in cycling, resting and stimulated fibroblasts
    • Lallemand D., Spyrou G., Yaniv M., Pfarr C.M. Variations in Jun and Fos protein expression and AP-1 activity in cycling, resting and stimulated fibroblasts. Oncogene 1997, 14:819-830.
    • (1997) Oncogene , vol.14 , pp. 819-830
    • Lallemand, D.1    Spyrou, G.2    Yaniv, M.3    Pfarr, C.M.4
  • 33
    • 84895044237 scopus 로고    scopus 로고
    • C-Fos regulation by the MAPK and PKC pathways in intervertebral disc cells
    • Yokoyama K., Hiyama A., Arai F., Nukaga T., Sakai D., Mochida J. C-Fos regulation by the MAPK and PKC pathways in intervertebral disc cells. PloS One 2013, 8:e73210.
    • (2013) PloS One , vol.8
    • Yokoyama, K.1    Hiyama, A.2    Arai, F.3    Nukaga, T.4    Sakai, D.5    Mochida, J.6
  • 34
    • 0041854253 scopus 로고    scopus 로고
    • The role of JNK and p38 MAPK activities in UVA-induced signaling pathways leading to AP-1 activation and c-Fos expression
    • Silvers A.L., Bachelor M.A., Bowden G.T. The role of JNK and p38 MAPK activities in UVA-induced signaling pathways leading to AP-1 activation and c-Fos expression. Neoplasia 2003, 5:319-329.
    • (2003) Neoplasia , vol.5 , pp. 319-329
    • Silvers, A.L.1    Bachelor, M.A.2    Bowden, G.T.3
  • 35
    • 0033521651 scopus 로고    scopus 로고
    • C-Jun regulates cell cycle progression and apoptosis by distinct mechanisms
    • Wisdom R., Johnson R.S., Moore C. c-Jun regulates cell cycle progression and apoptosis by distinct mechanisms. EMBO J 1999, 18:188-197.
    • (1999) EMBO J , vol.18 , pp. 188-197
    • Wisdom, R.1    Johnson, R.S.2    Moore, C.3
  • 36
    • 61849085224 scopus 로고    scopus 로고
    • C-Fos overexpression increases the proliferation of human hepatocytes by stabilizing nuclear cyclin D1
    • Guller M., Toualbi-Abed K., Legrand A., Michel L., Mauviel A., Bernuau D., et al. c-Fos overexpression increases the proliferation of human hepatocytes by stabilizing nuclear cyclin D1. World J Gastroenterol 2008, 14:6339-6346.
    • (2008) World J Gastroenterol , vol.14 , pp. 6339-6346
    • Guller, M.1    Toualbi-Abed, K.2    Legrand, A.3    Michel, L.4    Mauviel, A.5    Bernuau, D.6
  • 38
    • 0023091227 scopus 로고
    • Deregulated c-fos expression interferes with normal bone development in transgenic mice
    • Ruther U., Garber C., Komitowski D., Muller R., Wagner E.F. Deregulated c-fos expression interferes with normal bone development in transgenic mice. Nature 1987, 325:412-416.
    • (1987) Nature , vol.325 , pp. 412-416
    • Ruther, U.1    Garber, C.2    Komitowski, D.3    Muller, R.4    Wagner, E.F.5
  • 39
    • 0026486816 scopus 로고
    • Pleiotropic effects of a null mutation in the c-fos proto-oncogene
    • Johnson R.S., Spiegelman B.M., Papaioannou V. Pleiotropic effects of a null mutation in the c-fos proto-oncogene. Cell 1992, 71:577-586.
    • (1992) Cell , vol.71 , pp. 577-586
    • Johnson, R.S.1    Spiegelman, B.M.2    Papaioannou, V.3
  • 41
    • 0023245615 scopus 로고
    • Kindling stimulation induces c-fos protein(s) in granule cells of the rat dentate gyrus
    • Dragunow M., Robertson H.A. Kindling stimulation induces c-fos protein(s) in granule cells of the rat dentate gyrus. Nature 1987, 329:441-442.
    • (1987) Nature , vol.329 , pp. 441-442
    • Dragunow, M.1    Robertson, H.A.2
  • 42
    • 0023193514 scopus 로고
    • Mapping patterns of c-fos expression in the central nervous system after seizure
    • Morgan J.I., Cohen D.R., Hempstead J.L., Curran T. Mapping patterns of c-fos expression in the central nervous system after seizure. Science 1987, 237:192-197.
    • (1987) Science , vol.237 , pp. 192-197
    • Morgan, J.I.1    Cohen, D.R.2    Hempstead, J.L.3    Curran, T.4
  • 43
    • 0025270328 scopus 로고
    • Membrane depolarization and calcium induce c-fos transcription via phosphorylation of transcription factor CREB
    • Sheng M., McFadden G., Greenberg M.E. Membrane depolarization and calcium induce c-fos transcription via phosphorylation of transcription factor CREB. Neuron 1990, 4:571-582.
    • (1990) Neuron , vol.4 , pp. 571-582
    • Sheng, M.1    McFadden, G.2    Greenberg, M.E.3
  • 44
    • 0026812207 scopus 로고
    • Role of [Ca2+]i in induction of c-fos, c-jun, and c-myc mRNA in rat PTE after oxidative stress
    • Maki A., Berezesky I.K., Fargnoli J., Holbrook N.J., Trump B.F. Role of [Ca2+]i in induction of c-fos, c-jun, and c-myc mRNA in rat PTE after oxidative stress. FASEB J 1992, 6:919-924.
    • (1992) FASEB J , vol.6 , pp. 919-924
    • Maki, A.1    Berezesky, I.K.2    Fargnoli, J.3    Holbrook, N.J.4    Trump, B.F.5
  • 45
    • 0024507195 scopus 로고
    • Glucocorticoids activate a suicide process in thymocytes through an elevation of cytosolic Ca2+ concentration
    • McConkey D.J., Nicotera P., Hartzell P., Bellomo G., Wyllie A.H., Orrenius S. Glucocorticoids activate a suicide process in thymocytes through an elevation of cytosolic Ca2+ concentration. Arch Biochem Biophys 1989, 269:365-370.
    • (1989) Arch Biochem Biophys , vol.269 , pp. 365-370
    • McConkey, D.J.1    Nicotera, P.2    Hartzell, P.3    Bellomo, G.4    Wyllie, A.H.5    Orrenius, S.6
  • 46
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri K.F., Kroemer G. Organelle-specific initiation of cell death pathways. Nat Cell Biol 2001, 3:E255-E263.
    • (2001) Nat Cell Biol , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 47
    • 0027340729 scopus 로고
    • Microdomains with high Ca2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria
    • Rizzuto R., Brini M., Murgia M., Pozzan T. Microdomains with high Ca2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria. Science 1993, 262:744-747.
    • (1993) Science , vol.262 , pp. 744-747
    • Rizzuto, R.1    Brini, M.2    Murgia, M.3    Pozzan, T.4
  • 48
    • 0033214784 scopus 로고    scopus 로고
    • Thapsigargin directly induces the mitochondrial permeability transition
    • Korge P., Weiss J.N. Thapsigargin directly induces the mitochondrial permeability transition. Eur J Biochem 1999, 265:273-280.
    • (1999) Eur J Biochem , vol.265 , pp. 273-280
    • Korge, P.1    Weiss, J.N.2
  • 49
    • 0037155258 scopus 로고    scopus 로고
    • Paclitaxel affects cytosolic calcium signals by opening the mitochondrial permeability transition pore
    • Kidd J.F., Pilkington M.F., Schell M.J., Fogarty K.E., Skepper J.N., Taylor C.W., et al. Paclitaxel affects cytosolic calcium signals by opening the mitochondrial permeability transition pore. JBiol Chem 2002, 277:6504-6510.
    • (2002) JBiol Chem , vol.277 , pp. 6504-6510
    • Kidd, J.F.1    Pilkington, M.F.2    Schell, M.J.3    Fogarty, K.E.4    Skepper, J.N.5    Taylor, C.W.6
  • 50
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • Park C.B., Kim H.S., Kim S.C. Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem Biophys Res Commun 1998, 244:253-257.
    • (1998) Biochem Biophys Res Commun , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 51
    • 11144348648 scopus 로고    scopus 로고
    • Interaction and cellular localization of the human host defense peptide LL-37 with lung epithelial cells
    • Lau Y.E., Rozek A., Scott M.G., Goosney D.L., Davidson D.J., Hancock R.E. Interaction and cellular localization of the human host defense peptide LL-37 with lung epithelial cells. Infect Immun 2005, 73:583-591.
    • (2005) Infect Immun , vol.73 , pp. 583-591
    • Lau, Y.E.1    Rozek, A.2    Scott, M.G.3    Goosney, D.L.4    Davidson, D.J.5    Hancock, R.E.6
  • 52
    • 28244489607 scopus 로고    scopus 로고
    • Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes
    • Powers J.P., Tan A., Ramamoorthy A., Hancock R.E. Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes. Biochemistry 2005, 44:15504-15513.
    • (2005) Biochemistry , vol.44 , pp. 15504-15513
    • Powers, J.P.1    Tan, A.2    Ramamoorthy, A.3    Hancock, R.E.4
  • 53
    • 0027528472 scopus 로고
    • Functional and chemical characterization of Hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera)
    • Casteels P., Ampe C., Jacobs F., Tempst P. Functional and chemical characterization of Hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera). JBiol Chem 1993, 268:7044-7054.
    • (1993) JBiol Chem , vol.268 , pp. 7044-7054
    • Casteels, P.1    Ampe, C.2    Jacobs, F.3    Tempst, P.4
  • 54
    • 0025245504 scopus 로고
    • Channel formation properties of synthetic pardaxin and analogues
    • Shai Y., Bach D., Yanovsky A. Channel formation properties of synthetic pardaxin and analogues. JBiol Chem 1990, 265:20202-20209.
    • (1990) JBiol Chem , vol.265 , pp. 20202-20209
    • Shai, Y.1    Bach, D.2    Yanovsky, A.3
  • 55
    • 0024292077 scopus 로고
    • Sequencing and synthesis of pardaxin, a polypeptide from the Red Sea moses sole with ionophore activity
    • Shai Y., Fox J., Caratsch C., Shih Y.L., Edwards C., Lazarovici P. Sequencing and synthesis of pardaxin, a polypeptide from the Red Sea moses sole with ionophore activity. FEBS Lett 1988, 242:161-166.
    • (1988) FEBS Lett , vol.242 , pp. 161-166
    • Shai, Y.1    Fox, J.2    Caratsch, C.3    Shih, Y.L.4    Edwards, C.5    Lazarovici, P.6
  • 57
    • 0016668191 scopus 로고
    • Lipid composition of the golgi apparatus of rat kidney and liver in comparison with other subcellular organelles
    • Zambrano F., Fleischer S., Fleischer B. Lipid composition of the golgi apparatus of rat kidney and liver in comparison with other subcellular organelles. Biochim Biophys Acta 1975, 380:357-369.
    • (1975) Biochim Biophys Acta , vol.380 , pp. 357-369
    • Zambrano, F.1    Fleischer, S.2    Fleischer, B.3
  • 58
    • 0024381901 scopus 로고
    • Interactions between a new class of eukaryotic antimicrobial agents and isolated rat liver mitochondria
    • Westerhoff H.V., Hendler R.W., Zasloff M., Juretic D. Interactions between a new class of eukaryotic antimicrobial agents and isolated rat liver mitochondria. Biochim Biophys Acta 1989, 975:361-369.
    • (1989) Biochim Biophys Acta , vol.975 , pp. 361-369
    • Westerhoff, H.V.1    Hendler, R.W.2    Zasloff, M.3    Juretic, D.4


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