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Volumn , Issue , 2011, Pages 153-176

Mechanisms by which pathogens hijack and utilize membrane domains to mediate cytotoxicity

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EID: 84901486014     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (1)

References (181)
  • 1
    • 0033523767 scopus 로고    scopus 로고
    • Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin
    • Abrami, L. and F. van Der Goot. 1999. Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin. J Cell Biol. 147:175-184
    • (1999) J Cell Biol , vol.147 , pp. 175-184
    • Abrami, L.1    van Der Goot, F.2
  • 2
    • 15244349709 scopus 로고    scopus 로고
    • Melittin-induced bilayer leakage depends on lipid material properties: Evidence for toroidal pores
    • Allende, D., S.A. Simon, and T.J. McIntosh. 2005. Melittin-induced bilayer leakage depends on lipid material properties: Evidence for toroidal pores. Biophys J. 88:1828-1837
    • (2005) Biophys J , vol.88 , pp. 1828-1837
    • Allende, D.1    Simon, S.A.2    McIntosh, T.J.3
  • 3
    • 0034700264 scopus 로고    scopus 로고
    • Lipids favoring inverted phase enhance the ability of aerolysin to permeabilize liposome bilayers
    • Alonso, A., F.M. Goni, and J.T. Buckley. 2000. Lipids favoring inverted phase enhance the ability of aerolysin to permeabilize liposome bilayers. Biochemistry. 39:14019-14024
    • (2000) Biochemistry , vol.39 , pp. 14019-14024
    • Alonso, A.1    Goni, F.M.2    Buckley, J.T.3
  • 4
    • 0242664967 scopus 로고    scopus 로고
    • Pore formation by Equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures
    • Anderluh, G., M.D. Serra, G. Viero, G. Guella, P. Macek, and G. Menestrina. 2003. Pore formation by Equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures. J Biol Chem. 278:45216-45233
    • (2003) J Biol Chem , vol.278 , pp. 45216-45233
    • Anderluh, G.1    Serra, M.D.2    Viero, G.3    Guella, G.4    Macek, P.5    Menestrina, G.6
  • 5
    • 34347262391 scopus 로고    scopus 로고
    • Bilayer thickness and membrane protein function: An energetic perspective
    • Andersen, O.S. and R.E. Koeppe II. 2007. Bilayer thickness and membrane protein function: An energetic perspective. Ann Rev Biophys Biomol Struct. 36:107-130
    • (2007) Ann Rev Biophys Biomol Struct , vol.36 , pp. 107-130
    • Andersen, O.S.1    Koeppe, R.E.2
  • 6
    • 36749035394 scopus 로고    scopus 로고
    • Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion
    • Atanasiu, D., J.C. Whitbeck, T.M. Cairns, B. Reilly, G.H. Cohen, and R.J. Eisenberg. 2007. Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion. Proc Natl Acad Sci USA. 104:18718-18723
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 18718-18723
    • Atanasiu, D.1    Whitbeck, J.C.2    Cairns, T.M.3    Reilly, B.4    Cohen, G.H.5    Eisenberg, R.J.6
  • 7
    • 34848849474 scopus 로고    scopus 로고
    • Mannheimia haemolytica Leukotoxin binds to lipid rafts in bovine lymphoblastoid cells and is internalized in a dynamin-2-and clathrin-dependent manner
    • Atapattu, D.N. and C.J. Czuprynski. 2007. Mannheimia haemolytica Leukotoxin binds to lipid rafts in bovine lymphoblastoid cells and is internalized in a dynamin-2-and clathrin-dependent manner. Infect Immun. 75:4719-4727
    • (2007) Infect Immun , vol.75 , pp. 4719-4727
    • Atapattu, D.N.1    Czuprynski, C.J.2
  • 8
    • 35148879065 scopus 로고    scopus 로고
    • Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein
    • Avitabile, E., C. Forghieri, and G. Campadelli-Fiume. 2007. Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein. J Virol. 81:11532-11537
    • (2007) J Virol , vol.81 , pp. 11532-11537
    • Avitabile, E.1    Forghieri, C.2    Campadelli-Fiume, G.3
  • 9
    • 64549129051 scopus 로고    scopus 로고
    • Class III viral membrane fusion proteins
    • Backovic, M. and T.S. Jardetzky. 2009. Class III viral membrane fusion proteins. Curr Opin Struct Biol. 19:189-196
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 189-196
    • Backovic, M.1    Jardetzky, T.S.2
  • 10
    • 0037021456 scopus 로고    scopus 로고
    • Interaction of hagfish cathelicidin antimicrobial peptides with model lipid membranes
    • Basanez, G., A.E. Shinnar, and J. Zimmerberg. 2002. Interaction of hagfish cathelicidin antimicrobial peptides with model lipid membranes. FEBS Lett. 532:115-120
    • (2002) FEBS Lett , vol.532 , pp. 115-120
    • Basanez, G.1    Shinnar, A.E.2    Zimmerberg, J.3
  • 11
    • 0029859138 scopus 로고    scopus 로고
    • Association of RTX toxins with erythrocytes
    • Bauer, M.E. and R.A. Welch. 1996. Association of RTX toxins with erythrocytes. Infect Immun. 64:4665-4672
    • (1996) Infect Immun , vol.64 , pp. 4665-4672
    • Bauer, M.E.1    Welch, R.A.2
  • 12
    • 0042890360 scopus 로고    scopus 로고
    • Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry
    • Bender, F., J. Whitbeck, M. Ponce de Leon, H. Lou, R. Eisenberg, and G. Cohen. 2003. Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry. J Virol. 77:9542-9552
    • (2003) J Virol , vol.77 , pp. 9542-9552
    • Bender, F.1    Whitbeck, J.2    Ponce de Leon, M.3    Lou, H.4    Eisenberg, R.5    Cohen, G.6
  • 13
    • 0024505102 scopus 로고
    • Pore formation by the Escherichia coli hemolysin: Evidence for an association-dissociation equilibrium of the pore-forming aggregates
    • Benz, R., A. Schmid, W. Wagner, and W. Goebel. 1989. Pore formation by the Escherichia coli hemolysin: Evidence for an association-dissociation equilibrium of the pore-forming aggregates. Infect Immun. 57:887-895
    • (1989) Infect Immun , vol.57 , pp. 887-895
    • Benz, R.1    Schmid, A.2    Wagner, W.3    Goebel, W.4
  • 14
    • 0024535720 scopus 로고
    • Potent leukocidal action of Escherichia coli hemolysin mediated by permeabilization of target cell membranes
    • Bhakdi, S., S. Greulich, M. Muhly, B. Eberspacher, H. Becker, A. Thiele, and F. Hugo. 1989. Potent leukocidal action of Escherichia coli hemolysin mediated by permeabilization of target cell membranes. J Exp Med. 169:737-754
    • (1989) J Exp Med , vol.169 , pp. 737-754
    • Bhakdi, S.1    Greulich, S.2    Muhly, M.3    Eberspacher, B.4    Becker, H.5    Thiele, A.6    Hugo, F.7
  • 15
    • 0022654450 scopus 로고
    • Escherichia coli hemolysin may damage target cell membranes by generating transmembrane pores
    • Bhakdi, S., N. Mackman, J.-M. Nicaud, and I.B. Holland. 1986. Escherichia coli hemolysin may damage target cell membranes by generating transmembrane pores. Infect Immun. 52:63-69
    • (1986) Infect Immun , vol.52 , pp. 63-69
    • Bhakdi, S.1    Mackman, N.2    Nicaud, J.-M.3    Holland, I.B.4
  • 16
    • 0027183815 scopus 로고
    • A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes
    • Bhakdi, S., U. Weller, I. Walev, E. Martin, D. Jonas, and M. Palmer. 1993. A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes. Med Microbiol Immunol. 182:167-175
    • (1993) Med Microbiol Immunol , vol.182 , pp. 167-175
    • Bhakdi, S.1    Weller, U.2    Walev, I.3    Martin, E.4    Jonas, D.5    Palmer, M.6
  • 17
    • 0025288364 scopus 로고
    • Domains of Escherichia coli hemolysin (HlyA) involved in binding of calcium and erythrocyte membranes
    • Boehm, D.F., R.A. Welch, and I.S. Snyder. 1990. Domains of Escherichia coli hemolysin (HlyA) involved in binding of calcium and erythrocyte membranes. Infect Immun. 58:1959-1964
    • (1990) Infect Immun , vol.58 , pp. 1959-1964
    • Boehm, D.F.1    Welch, R.A.2    Snyder, I.S.3
  • 18
    • 33645539767 scopus 로고    scopus 로고
    • Cholestrol-rich membrane microdomains mediate cell cycle arrast induced by Actinobacillus actinomycetemcomitans cytolethal distending toxin
    • Boesze-Battaglia, K., D. Besack, T.L. McKay, A. Zekavat, L. Otis, K. Jordan-Sciutto, and B.J. Shenker, 2006. Cholestrol-rich membrane microdomains mediate cell cycle arrast induced by Actinobacillus actinomycetemcomitans cytolethal distending toxin. Cell Microbiol. 8:823-836
    • (2006) Cell Microbiol , vol.8 , pp. 823-836
    • Boesze-Battaglia, K.1    Besack, D.2    McKay, T.L.3    Zekavat, A.4    Otis, L.5    Jordan-Sciutto, K.6    Shenker, B.J.7
  • 19
    • 67449090254 scopus 로고    scopus 로고
    • Cytolethal distending toxin-induced cell cycle arrest of lymphocytes is dependent upon recognition and binding to cholesterol
    • Boesze-Battaglia, K., A. Brown, L. Walker, D. Besack, A. Zekavat, S. Wrenn, C. Krummenacher, and B.J. Shenker. 2009. Cytolethal distending toxin-induced cell cycle arrest of lymphocytes is dependent upon recognition and binding to cholesterol. J Biol Chem. 284:10650-10658
    • (2009) J Biol Chem , vol.284 , pp. 10650-10658
    • Boesze-Battaglia, K.1    Brown, A.2    Walker, L.3    Besack, D.4    Zekavat, A.5    Wrenn, S.6    Krummenacher, C.7    Shenker, B.J.8
  • 20
    • 0026541137 scopus 로고
    • Circulating integrins: Alpha 5 beta 1, alpha 6 beta 4 and Mac-1, but not alpha 3 beta 1, alpha 4 beta 1 or LFA-1
    • Bretscher, M.S. 1992. Circulating integrins: Alpha 5 beta 1, alpha 6 beta 4 and Mac-1, but not alpha 3 beta 1, alpha 4 beta 1 or LFA-1. EMBO J. 11:405-410
    • (1992) EMBO J , vol.11 , pp. 405-410
    • Bretscher, M.S.1
  • 21
    • 67849131060 scopus 로고    scopus 로고
    • The role of glycoprotein H in herpesvirus membrane fusion
    • Browne, H.M. 2009. The role of glycoprotein H in herpesvirus membrane fusion. Protein Pept Lett. 16:760-765
    • (2009) Protein Pept Lett , vol.16 , pp. 760-765
    • Browne, H.M.1
  • 22
    • 0026654267 scopus 로고
    • Molecular characterization of an RTX toxin determinant from Actinobacillus suis
    • Burrows, L.L. and R.Y. Lo. 1992. Molecular characterization of an RTX toxin determinant from Actinobacillus suis. Infect Immun. 60:2166-2173
    • (1992) Infect Immun , vol.60 , pp. 2166-2173
    • Burrows, L.L.1    Lo, R.Y.2
  • 23
    • 0023705653 scopus 로고
    • Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion
    • Cai, W., B. Gu, and S. Person. 1988. Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion. J Virol. 62:2596-2604
    • (1988) J Virol , vol.62 , pp. 2596-2604
    • Cai, W.1    Gu, B.2    Person, S.3
  • 25
    • 0030586161 scopus 로고    scopus 로고
    • Non-bilayer lipids and biological fusion intermediates
    • Chernomordik, L.V. 1996. Non-bilayer lipids and biological fusion intermediates. Chem Phys Lipids. 81:203-213
    • (1996) Chem Phys Lipids , vol.81 , pp. 203-213
    • Chernomordik, L.V.1
  • 27
    • 0024544823 scopus 로고
    • Transmembrane pore size and role of swelling in cytotoxicity caused by Pasteurella haemolytica leukotoxin
    • Clinkenbeard, K.D., P.A. Mosier, and A.W. Confer. 1989. Transmembrane pore size and role of swelling in cytotoxicity caused by Pasteurella haemolytica leukotoxin. Infect Immun. 57:420-425
    • (1989) Infect Immun , vol.57 , pp. 420-425
    • Clinkenbeard, K.D.1    Mosier, P.A.2    Confer, A.W.3
  • 28
    • 0030775355 scopus 로고    scopus 로고
    • Escherichia coli cytolethal distending toxin blocks the HeLa cell cycle at the G2-M transition by preventing cdc2 protein kinase dephosphorylation and activation
    • Comayras, C., C. Tasca, S.Y. Peres, B. Ducommun, E. Oswald, and J. DeRycke. 1997. Escherichia coli cytolethal distending toxin blocks the HeLa cell cycle at the G2-M transition by preventing cdc2 protein kinase dephosphorylation and activation. Infect Immun. 65:5088-5095
    • (1997) Infect Immun , vol.65 , pp. 5088-5095
    • Comayras, C.1    Tasca, C.2    Peres, S.Y.3    Ducommun, B.4    Oswald, E.5    DeRycke, J.6
  • 30
    • 0034441256 scopus 로고    scopus 로고
    • Cellualr internalization of cytolethal distending toxin from Haemophilus ducreyi
    • Cortes-Bratti, X., E. Chaves-Olarte, T. Lagergard, and M. Thelastam. 2000. Cellualr internalization of cytolethal distending toxin from Haemophilus ducreyi. Infect. Immun. 68:6903-6911
    • (2000) Infect. Immun , vol.68 , pp. 6903-6911
    • Cortes-Bratti, X.1    Chaves-Olarte, E.2    Lagergard, T.3    Thelastam, M.4
  • 31
    • 0002103170 scopus 로고
    • Structural properties and functional roles of phospholipids in biological membranes
    • J.F. Kuo (Ed.). CRC Press, Boca Raton, FL
    • Cullis, P.R., M.J. Hope, B. de Kruijff, A.J. Verkleij, and C.P.S. Tilcock. 1985. Structural properties and functional roles of phospholipids in biological membranes. In Phospholipids and Cellular Regulations. Vol. 1. J.F. Kuo (Ed.). CRC Press, Boca Raton, FL
    • (1985) Phospholipids and Cellular Regulations , vol.1
    • Cullis, P.R.1    Hope, M.J.2    de Kruijff, B.3    Verkleij, A.J.4    Tilcock, C.P.S.5
  • 32
    • 0028811427 scopus 로고
    • Biological effects of RTX toxins: The possible role of lipopolysaccharide
    • Czuprynski, C.J. and R.A. Welch. 1995. Biological effects of RTX toxins: The possible role of lipopolysaccharide. Trends Microbiol. 3:480-483
    • (1995) Trends Microbiol , vol.3 , pp. 480-483
    • Czuprynski, C.J.1    Welch, R.A.2
  • 33
  • 34
    • 0035949444 scopus 로고    scopus 로고
    • Cytolethal distending toxin (CDT): A bacterial weapon to control host cell proliferation
    • De Rycke, J. and Oswald, E. 2001. Cytolethal distending toxin (CDT): A bacterial weapon to control host cell proliferation. FEMS Microbiol Lett. 203:141-148
    • (2001) FEMS Microbiol Lett , vol.203 , pp. 141-148
    • De Rycke, J.1    Oswald, E.2
  • 35
    • 33846520001 scopus 로고    scopus 로고
    • Nectin-2-mediated entry of a syncytial strain of herpes simplex virus via pH-independent fusion with the plasma membrane of Chinese hamster ovary cells
    • Delboy, M.G., J.L. Patterson, A.M. Hollander, and A.V. Nicola. 2006. Nectin-2-mediated entry of a syncytial strain of herpes simplex virus via pH-independent fusion with the plasma membrane of Chinese hamster ovary cells. Virol J. 3:105
    • (2006) Virol J , vol.3 , pp. 105
    • Delboy, M.G.1    Patterson, J.L.2    Hollander, A.M.3    Nicola, A.V.4
  • 38
    • 0035058434 scopus 로고    scopus 로고
    • Escherichia coli CdtB mediates cytolethal distending toxin cell cycle arrest
    • Elwell, C.A., K. Chao, K. Patel, and L.A. Dreyfus. 2001. Escherichia coli CdtB mediates cytolethal distending toxin cell cycle arrest. Infect Immun. 69:3418-3422
    • (2001) Infect Immun , vol.69 , pp. 3418-3422
    • Elwell, C.A.1    Chao, K.2    Patel, K.3    Dreyfus, L.A.4
  • 39
    • 0033854239 scopus 로고    scopus 로고
    • Dnase I homologous residues in CdtB are critical for cytolethal distending toxin-mediated cell cycle arrest
    • Elwell, C.A. and Dreyfus, L.A. 2000. Dnase I homologous residues in CdtB are critical for cytolethal distending toxin-mediated cell cycle arrest. Mol Microbiol. 37:952-963
    • (2000) Mol Microbiol , vol.37 , pp. 952-963
    • Elwell, C.A.1    Dreyfus, L.A.2
  • 40
    • 0031795752 scopus 로고    scopus 로고
    • Lipid polymorphism and protein-lipid interactions
    • Epand, R.M. 1998. Lipid polymorphism and protein-lipid interactions. Biochim Biophys Acta. 1376:353-368
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 353-368
    • Epand, R.M.1
  • 41
    • 33744512299 scopus 로고    scopus 로고
    • Cholesterol and the interaction of proteins with membrane domains
    • Epand, R.M. 2006. Cholesterol and the interaction of proteins with membrane domains. Prog Lipid Res. 45:279-294
    • (2006) Prog Lipid Res , vol.45 , pp. 279-294
    • Epand, R.M.1
  • 42
    • 0025892516 scopus 로고
    • Evidence for the regulation of the activity of protein kinase C through changes in membrane properties
    • Epand, R.M., R.F. Epand, B.T.-C. Leon, F.M. Menger, and J.F. Kuo. 1991. Evidence for the regulation of the activity of protein kinase C through changes in membrane properties. Biosci Rep. 11:59-64
    • (1991) Biosci Rep , vol.11 , pp. 59-64
    • Epand, R.M.1    Epand, R.F.2    Leon, B.T.-C.3    Menger, F.M.4    Kuo, J.F.5
  • 43
    • 9644281567 scopus 로고    scopus 로고
    • Caveolin scaffolding region and cholesterol-rich domains in membranes
    • Epand, R., B. Sayer, and R. Epand. 2005. Caveolin scaffolding region and cholesterol-rich domains in membranes. J Mol Biol. 345:339-350
    • (2005) J Mol Biol , vol.345 , pp. 339-350
    • Epand, R.1    Sayer, B.2    Epand, R.3
  • 44
    • 34547232297 scopus 로고    scopus 로고
    • Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane
    • Farnsworth, A., T.W. Wisner, M. Webb, R. Roller, G. Cohen, R. Eisenberg, and D.C. Johnson. 2007. Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane. Proc Natl Acad Sci USA. 104:10187-10192
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 10187-10192
    • Farnsworth, A.1    Wisner, T.W.2    Webb, M.3    Roller, R.4    Cohen, G.5    Eisenberg, R.6    Johnson, D.C.7
  • 47
    • 0026556674 scopus 로고
    • Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted
    • Forrester, A., H. Farrell, G. Wilkinson, J. Kaye, N. Davis-Poynter, and T. Minson. 1992. Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted. J Virol. 66:341-348
    • (1992) J Virol , vol.66 , pp. 341-348
    • Forrester, A.1    Farrell, H.2    Wilkinson, G.3    Kaye, J.4    Davis-Poynter, N.5    Minson, T.6
  • 48
    • 0034953016 scopus 로고    scopus 로고
    • The role of different protein components from the Haemophilus ducreyi cytolethal distending toxin in the generation of cell toxicity
    • Frisk, A., M. Lebens, C. Johansson, H. Ahmed, L. Svensson, K. Ahlman, and T. Lagergard. 2001. The role of different protein components from the Haemophilus ducreyi cytolethal distending toxin in the generation of cell toxicity. Microb Pathog. 30:313-324
    • (2001) Microb Pathog , vol.30 , pp. 313-324
    • Frisk, A.1    Lebens, M.2    Johansson, C.3    Ahmed, H.4    Svensson, L.5    Ahlman, K.6    Lagergard, T.7
  • 50
    • 0035811836 scopus 로고    scopus 로고
    • Use of chimeric nectin-1(HveC)-related receptors to demonstrate that ability to bind alphaherpesvirus gD is not necessarily sufficient for viral entry
    • Geraghty, R.J., A. Fridberg, C. Krummenacher, G.H. Cohen, R.J. Eisenberg, and P.G. Spear. 2001. Use of chimeric nectin-1(HveC)-related receptors to demonstrate that ability to bind alphaherpesvirus gD is not necessarily sufficient for viral entry. Virology. 285:366-375
    • (2001) Virology , vol.285 , pp. 366-375
    • Geraghty, R.J.1    Fridberg, A.2    Krummenacher, C.3    Cohen, G.H.4    Eisenberg, R.J.5    Spear, P.G.6
  • 51
    • 0032486317 scopus 로고    scopus 로고
    • Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor
    • Geraghty, R.J., C. Krummenacher, G.H. Cohen, R.J. Eisenberg, and P.G. Spear. 1998. Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. Science. 280:1618-1620
    • (1998) Science , vol.280 , pp. 1618-1620
    • Geraghty, R.J.1    Krummenacher, C.2    Cohen, G.H.3    Eisenberg, R.J.4    Spear, P.G.5
  • 52
    • 33749259227 scopus 로고    scopus 로고
    • The herpesvirus glycoproteins B and H.L are sequentially recruited to the receptor-bound gD to effect membrane fusion at virus entry
    • Gianni, T., C. Forghieri, and G. Campadelli-Fiume. 2006. The herpesvirus glycoproteins B and H.L are sequentially recruited to the receptor-bound gD to effect membrane fusion at virus entry. Proc Natl Acad Sci USA. 103:14572-14577
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 14572-14577
    • Gianni, T.1    Forghieri, C.2    Campadelli-Fiume, G.3
  • 53
    • 13944263161 scopus 로고    scopus 로고
    • The ectodomain of herpes simplex virus glycoprotein H contains a membrane alpha-helix with attributes of an internal fusion peptide, positionally conserved in the herpesviridae family
    • Gianni, T., P.L. Martelli, R. Casadio, and G. Campadelli-Fiume. 2005. The ectodomain of herpes simplex virus glycoprotein H contains a membrane alpha-helix with attributes of an internal fusion peptide, positionally conserved in the herpesviridae family. J Virol. 79:2931-2940
    • (2005) J Virol , vol.79 , pp. 2931-2940
    • Gianni, T.1    Martelli, P.L.2    Casadio, R.3    Campadelli-Fiume, G.4
  • 54
    • 0024195829 scopus 로고
    • Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis
    • Glaser, P., H. Sakamoto, J. Bellalou, A. Ullmann, and A. Danchin. 1988. Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis. EMBO J. 7:3997-4004
    • (1988) EMBO J , vol.7 , pp. 3997-4004
    • Glaser, P.1    Sakamoto, H.2    Bellalou, J.3    Ullmann, A.4    Danchin, A.5
  • 56
    • 0022080948 scopus 로고
    • Intrinsic curvature hypothesis for biomembrane lipid composition: A role for nonbilayer lipids
    • Gruner, S.M. 1985. Intrinsic curvature hypothesis for biomembrane lipid composition: A role for nonbilayer lipids. Proc Natl Acad Sci. 82:3665-3669
    • (1985) Proc Natl Acad Sci , vol.82 , pp. 3665-3669
    • Gruner, S.M.1
  • 57
    • 77949296102 scopus 로고    scopus 로고
    • Nonlamellar lipid phases
    • P.L. Yeagle (Ed.). CRC Press, Boca Raton, FL
    • Gruner, S.M. 2005. Nonlamellar lipid phases. In The Structure of Biological Membranes. P.L. Yeagle (Ed.). CRC Press, Boca Raton, FL
    • (2005) The Structure of Biological Membranes
    • Gruner, S.M.1
  • 60
    • 0028519151 scopus 로고
    • Internal lysine palmitoylation in adenylate cyclase toxin from Bordetella pertussis
    • Hackett, M., L. Guo, J. Shabanowitz, D.F. Hunt, and E.L. Hewlett. 1994. Internal lysine palmitoylation in adenylate cyclase toxin from Bordetella pertussis. Science. 266:433-435
    • (1994) Science , vol.266 , pp. 433-435
    • Hackett, M.1    Guo, L.2    Shabanowitz, J.3    Hunt, D.F.4    Hewlett, E.L.5
  • 61
    • 71649106004 scopus 로고    scopus 로고
    • Induction of non-lamellar lipid phases by antimicrobial peptides: A potential link to mode of action
    • Haney, E.F., S. Nathoo, H.J. Vogel, and E.J. Prenner. 2010. Induction of non-lamellar lipid phases by antimicrobial peptides: A potential link to mode of action. Chem Phys Lipids. 163:82-93
    • (2010) Chem Phys Lipids , vol.163 , pp. 82-93
    • Haney, E.F.1    Nathoo, S.2    Vogel, H.J.3    Prenner, E.J.4
  • 64
    • 0037025377 scopus 로고    scopus 로고
    • Associations of B-and C-Raf with cholesterol, phosphatidylserine, and lipid second messengers: Preferential binding of Raf to artificial lipid rafts
    • Hekman, M., H. Hamm, A. Villar, B. Bader, J. Kuhlmann, J. Nickel, and U. Rapp. 2002. Associations of B-and C-Raf with cholesterol, phosphatidylserine, and lipid second messengers: Preferential binding of Raf to artificial lipid rafts. J Biol Chem. 277:24090-24102
    • (2002) J Biol Chem , vol.277 , pp. 24090-24102
    • Hekman, M.1    Hamm, H.2    Villar, A.3    Bader, B.4    Kuhlmann, J.5    Nickel, J.6    Rapp, U.7
  • 65
    • 44749091723 scopus 로고    scopus 로고
    • Entry of herpesviruses into mammalian cells
    • Heldwein, E.E. and C. Krummenacher. 2008. Entry of herpesviruses into mammalian cells. Cell Mol Life Sci. 65:1653-1668
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1653-1668
    • Heldwein, E.E.1    Krummenacher, C.2
  • 67
    • 33751414583 scopus 로고    scopus 로고
    • Early herpes simplex virus type 1 infection is dependent on regulated Rac1/Cdc42 signalling in epithelial MDCKII cells
    • Hoppe, S., M. Schelhaas, V. Jaeger, T. Liebig, P. Petermann, and D. Knebel-Morsdorf. 2006. Early herpes simplex virus type 1 infection is dependent on regulated Rac1/Cdc42 signalling in epithelial MDCKII cells. J Gen Virol. 87:3483-3494
    • (2006) J Gen Virol , vol.87 , pp. 3483-3494
    • Hoppe, S.1    Schelhaas, M.2    Jaeger, V.3    Liebig, T.4    Petermann, P.5    Knebel-Morsdorf, D.6
  • 68
    • 8844258034 scopus 로고    scopus 로고
    • Restoration of SHIP activity in a human leukemia cell line downregualtes constitutively activated phosphatidylinositol 3-kinase/Akt/BSK-3b signaling and leads to an increased transit time through the G1 phase of the cell cycle
    • Horn, S., E. Endl, B. Fehse, M. Weck, G. Mayr, and M. Jucker. 2004. Restoration of SHIP activity in a human leukemia cell line downregualtes constitutively activated phosphatidylinositol 3-kinase/Akt/BSK-3b signaling and leads to an increased transit time through the G1 phase of the cell cycle. Leukemia. 18:1839-1849
    • (2004) Leukemia , vol.18 , pp. 1839-1849
    • Horn, S.1    Endl, E.2    Fehse, B.3    Weck, M.4    Mayr, G.5    Jucker, M.6
  • 71
    • 0000502524 scopus 로고
    • Non-bilayer-forming lipids: Why are they necessary in biomembranes?
    • Hui, S.W. 1987. Non-bilayer-forming lipids: Why are they necessary in biomembranes? Comments Mol Cell Biophys. 4:233-248
    • (1987) Comments Mol Cell Biophys , vol.4 , pp. 233-248
    • Hui, S.W.1
  • 72
    • 0036054348 scopus 로고    scopus 로고
    • Expression and roles of herpesvirus entry mediators A and C in cells of oral origin
    • Hung, S.L., Y.Y. Cheng, Y.H. Wang, K.W. Chang, and Y.T. Chen. 2002. Expression and roles of herpesvirus entry mediators A and C in cells of oral origin. Oral Microbiol Immunol. 17:215-223
    • (2002) Oral Microbiol Immunol , vol.17 , pp. 215-223
    • Hung, S.L.1    Cheng, Y.Y.2    Wang, Y.H.3    Chang, K.W.4    Chen, Y.T.5
  • 73
    • 0035423556 scopus 로고    scopus 로고
    • Roles of lipid rafts in membrane transport
    • Ikonen, E. 2001. Roles of lipid rafts in membrane transport. Curr Opin Cell Biol. 13:470-477
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 470-477
    • Ikonen, E.1
  • 74
    • 0026432638 scopus 로고
    • Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation
    • Issartel, J.-P., V. Koronakis, and C. Hughes. 1991. Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation. Nature. 351:759-761
    • (1991) Nature , vol.351 , pp. 759-761
    • Issartel, J.-P.1    Koronakis, V.2    Hughes, C.3
  • 75
    • 75449089945 scopus 로고    scopus 로고
    • Insertion mutations in herpes simplex virus 1 glycoprotein H reduce cell surface expression, slow the rate of cell fusion or abrogate function in cell fusion and viral entry
    • Jackson, J.O., E. Lin, P.G. Spear, and R. Longnecker. 2009. Insertion mutations in herpes simplex virus 1 glycoprotein H reduce cell surface expression, slow the rate of cell fusion or abrogate function in cell fusion and viral entry. J Virol. 84:2038-2046
    • (2009) J Virol , vol.84 , pp. 2038-2046
    • Jackson, J.O.1    Lin, E.2    Spear, P.G.3    Longnecker, R.4
  • 78
    • 53549088587 scopus 로고    scopus 로고
    • The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
    • Kadlec, J., S. Loureiro, N.G. Abrescia, D.I. Stuart, and I.M. Jones. 2008. The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines. Nat Struct Mol Biol. 15:1024-1030
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1024-1030
    • Kadlec, J.1    Loureiro, S.2    Abrescia, N.G.3    Stuart, D.I.4    Jones, I.M.5
  • 79
    • 45749112586 scopus 로고    scopus 로고
    • Glycoproteins required for entry are not necessary for egress of pseudorabies virus
    • Klupp, B., J. Altenschmidt, H. Granzow, W. Fuchs, and T.C. Mettenleiter. 2008. Glycoproteins required for entry are not necessary for egress of pseudorabies virus. J Virol. 82:6299-6309
    • (2008) J Virol , vol.82 , pp. 6299-6309
    • Klupp, B.1    Altenschmidt, J.2    Granzow, H.3    Fuchs, W.4    Mettenleiter, T.C.5
  • 80
    • 34249844954 scopus 로고    scopus 로고
    • Vesicle formation from the nuclear membrane is induced by coexpression of two conserved herpesvirus proteins
    • Klupp, B.G., H. Granzow, W. Fuchs, G.M. Keil, S. Finke, and T.C. Mettenleiter. 2007. Vesicle formation from the nuclear membrane is induced by coexpression of two conserved herpesvirus proteins. Proc Natl Acad Sci USA. 104:7241-7246
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7241-7246
    • Klupp, B.G.1    Granzow, H.2    Fuchs, W.3    Keil, G.M.4    Finke, S.5    Mettenleiter, T.C.6
  • 81
    • 0023238044 scopus 로고
    • The secreted hemolysins of Proteus mirabilis, Proteus vulgaris, and Morganella morganii are genetically related to each other and to the alpha-hemolysin of Escherichia coli
    • Koronakis, V., M. Cross, B. Senior, E. Koronakis, and C. Hughes. 1987. The secreted hemolysins of Proteus mirabilis, Proteus vulgaris, and Morganella morganii are genetically related to each other and to the alpha-hemolysin of Escherichia coli. J Bacteriol. 169:1509-1515
    • (1987) J Bacteriol , vol.169 , pp. 1509-1515
    • Koronakis, V.1    Cross, M.2    Senior, B.3    Koronakis, E.4    Hughes, C.5
  • 82
    • 1942521177 scopus 로고    scopus 로고
    • Comparative usage of herpesvirus entry mediator A and nectin-1 by laboratory strains and clinical isolates of herpes simplex virus
    • Krummenacher, C., F. Baribaud, M. Ponce de Leon, I. Baribaud, J.C. Whitbeck, R. Xu, G.H. Cohen, and R.J. Eisenberg. 2004. Comparative usage of herpesvirus entry mediator A and nectin-1 by laboratory strains and clinical isolates of herpes simplex virus. Virology. 322:286-299
    • (2004) Virology , vol.322 , pp. 286-299
    • Krummenacher, C.1    Baribaud, F.2    Ponce de Leon, M.3    Baribaud, I.4    Whitbeck, J.C.5    Xu, R.6    Cohen, G.H.7    Eisenberg, R.J.8
  • 83
    • 34247092027 scopus 로고    scopus 로고
    • Entry of herpesviruses into cells: The Enigma variations
    • S. Pohlmann and G. Simmons (Eds.). Landes Bioscience, Georgetown, TX
    • Krummenacher, C., A. Carfi, R.J. Eisenberg, and G.H. Cohen. 2007. Entry of herpesviruses into cells: The Enigma variations. In Viral Entry into Host Cells. S. Pohlmann and G. Simmons (Eds.). Landes Bioscience, Georgetown, TX. http://www.eurekah.com/chapter/3035
    • (2007) Viral Entry into Host Cells
    • Krummenacher, C.1    Carfi, A.2    Eisenberg, R.J.3    Cohen, G.H.4
  • 85
    • 0033804532 scopus 로고    scopus 로고
    • Lipid phosphatases in the immune system
    • Krystal, G. 2000. Lipid phosphatases in the immune system. Semin Immunol. 12:397-403
    • (2000) Semin Immunol , vol.12 , pp. 397-403
    • Krystal, G.1
  • 86
    • 0024423256 scopus 로고
    • Analysis of the Actinobacillus actinomycetemcomitans leukotoxin gene. Delineation of unique features and comparison to homologous toxins
    • Lally, E.T., E.E. Golub, I.R. Kieba, N.S. Taichman, J. Rosenbloom, J.C. Rosenbloom, C.W. Gibson, and D.R. Demuth. 1989. Analysis of the Actinobacillus actinomycetemcomitans leukotoxin gene. Delineation of unique features and comparison to homologous toxins. J Biol Chem. 264:15451-15456
    • (1989) J Biol Chem , vol.264 , pp. 15451-15456
    • Lally, E.T.1    Golub, E.E.2    Kieba, I.R.3    Taichman, N.S.4    Rosenbloom, J.5    Rosenbloom, J.C.6    Gibson, C.W.7    Demuth, D.R.8
  • 89
    • 0034644631 scopus 로고    scopus 로고
    • A bacterial toxin that controls cell cycle progression as a deoxribonuclease I-like proteins
    • Lara-Tejero, M. and J.E. Galan. 2000. A bacterial toxin that controls cell cycle progression as a deoxribonuclease I-like proteins. Science. 290:354-357
    • (2000) Science , vol.290 , pp. 354-357
    • Lara-Tejero, M.1    Galan, J.E.2
  • 90
    • 0034967972 scopus 로고    scopus 로고
    • CdtA, CdtB, and CdtC form a tripartite complex that is required for cytolethal distending toxin activity
    • Lara-Tejero, M. and J.E. Galan, 2001. CdtA, CdtB, and CdtC form a tripartite complex that is required for cytolethal distending toxin activity. Infect Immun. 69:4358-4365
    • (2001) Infect Immun , vol.69 , pp. 4358-4365
    • Lara-Tejero, M.1    Galan, J.E.2
  • 91
    • 37849035957 scopus 로고    scopus 로고
    • Engineered disulfide bonds in herpes simplex virus type 1 gD separate receptor binding from fusion initiation and viral entry
    • Lazear, E., A. Carfi, J.C. Whitbeck, T.M. Cairns, C. Krummenacher, G.H. Cohen, and R.J. Eisenberg. 2008. Engineered disulfide bonds in herpes simplex virus type 1 gD separate receptor binding from fusion initiation and viral entry. J Virol. 82:700-709
    • (2008) J Virol , vol.82 , pp. 700-709
    • Lazear, E.1    Carfi, A.2    Whitbeck, J.C.3    Cairns, T.M.4    Krummenacher, C.5    Cohen, G.H.6    Eisenberg, R.J.7
  • 92
    • 0031755752 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern
    • Li, H. and V. Papadopoulos. 1998. Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern. Endocrinology. 139:4991-4997
    • (1998) Endocrinology , vol.139 , pp. 4991-4997
    • Li, H.1    Papadopoulos, V.2
  • 93
    • 0023906081 scopus 로고
    • A herpes simplex virus mutant in which glycoprotein D sequences are replaced by b-galactosidase sequences binds to but is unable to penetrate into cells
    • Ligas, M.W. and D.C. Johnson. 1988. A herpes simplex virus mutant in which glycoprotein D sequences are replaced by b-galactosidase sequences binds to but is unable to penetrate into cells. J Virol. 62:1486-1494
    • (1988) J Virol , vol.62 , pp. 1486-1494
    • Ligas, M.W.1    Johnson, D.C.2
  • 94
    • 50149119228 scopus 로고    scopus 로고
    • Comprehensive characterization of extracellular herpes simplex virus type 1 virions
    • Loret, S., G. Guay, and R. Lippe. 2008. Comprehensive characterization of extracellular herpes simplex virus type 1 virions. J Virol. 82:8605-8618
    • (2008) J Virol , vol.82 , pp. 8605-8618
    • Loret, S.1    Guay, G.2    Lippe, R.3
  • 96
    • 0029812094 scopus 로고    scopus 로고
    • Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli
    • Ludwig, A., F. Garcia, S. Bauer, T. Jarchau, R. Benz, J. Hoppe, and W. Goebel. 1996. Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli. J Bacteriol. 178:5422-5430
    • (1996) J Bacteriol , vol.178 , pp. 5422-5430
    • Ludwig, A.1    Garcia, F.2    Bauer, S.3    Jarchau, T.4    Benz, R.5    Hoppe, J.6    Goebel, W.7
  • 97
    • 0002846942 scopus 로고    scopus 로고
    • The family of the multigenic encoded RTX toxins
    • J.E. Alouf and J.H. Freer (Eds.). Academic Press, San Diego, CA
    • Ludwig, A. and W. Goebel. 1999. The family of the multigenic encoded RTX toxins. In The Comprehensive Sourcebook of Bacterial Protein Toxins. J.E. Alouf and J.H. Freer (Eds.). Academic Press, San Diego, CA, pp. 330-348
    • (1999) The Comprehensive Sourcebook of Bacterial Protein Toxins , pp. 330-348
    • Ludwig, A.1    Goebel, W.2
  • 98
    • 0015529164 scopus 로고
    • Molecular sieving of red cell membranes during gradual osmotic hemolysis
    • MacGregor II, R.D. and C.A. Tobias. 1972. Molecular sieving of red cell membranes during gradual osmotic hemolysis. J Membr Biol. 10:345-356
    • (1972) J Membr Biol , vol.10 , pp. 345-356
    • MacGregor, R.D.1    Tobias, C.A.2
  • 99
    • 0033574526 scopus 로고    scopus 로고
    • The role of phosphatases in inositol signaling reactions
    • Majerus, P., M. Kisseleva, and F. Norris. 1999. The role of phosphatases in inositol signaling reactions. J Biol Chem. 274:10669-10672
    • (1999) J Biol Chem , vol.274 , pp. 10669-10672
    • Majerus, P.1    Kisseleva, M.2    Norris, F.3
  • 101
    • 0036196812 scopus 로고    scopus 로고
    • Regulation of the immune response by SHIP
    • March, M. and K. Ravichandran. 2002. Regulation of the immune response by SHIP. Semin Immunol. 14:37-47
    • (2002) Semin Immunol , vol.14 , pp. 37-47
    • March, M.1    Ravichandran, K.2
  • 102
    • 2942522547 scopus 로고    scopus 로고
    • Membrane restructuring by Bordetella pertussis adenylate cyclase toxin, a member of the RTX toxin family
    • Martin, C., M.-A. Requero, J. Masin, I. Konopásek, F.M. Goni, P. Sebo, and H. Ostolaza. 2004. Membrane restructuring by Bordetella pertussis adenylate cyclase toxin, a member of the RTX toxin family. J Bacteriol. 186:3760-3765
    • (2004) J Bacteriol , vol.186 , pp. 3760-3765
    • Martin, C.1    Requero, M.-A.2    Masin, J.3    Konopásek, I.4    Goni, F.M.5    Sebo, P.6    Ostolaza, H.7
  • 104
    • 0030790179 scopus 로고    scopus 로고
    • Pore formation and translocation of melittin
    • Matsuzaki, K., S. Yoneyama, and K. Miyajima. 1997. Pore formation and translocation of melittin. Biophys J. 73:831-838
    • (1997) Biophys J , vol.73 , pp. 831-838
    • Matsuzaki, K.1    Yoneyama, S.2    Miyajima, K.3
  • 106
    • 48749114826 scopus 로고    scopus 로고
    • Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry
    • Maurer, U.E., B. Sodeik, and K. Grunewald. 2008. Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry. Proc Natl Acad Sci USA. 105:10559-10564
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10559-10564
    • Maurer, U.E.1    Sodeik, B.2    Grunewald, K.3
  • 107
    • 0033009746 scopus 로고    scopus 로고
    • Identification of a cytolethal distending toxin gene locus and features of a virulence-associated region in Actinobacillus actinomycetemcomitans
    • Mayer, M., L. Bueno, E. Hansen, and J.M. DiRienzo. 1999. Identification of a cytolethal distending toxin gene locus and features of a virulence-associated region in Actinobacillus actinomycetemcomitans. Infect Immun. 67:1227-1237
    • (1999) Infect Immun , vol.67 , pp. 1227-1237
    • Mayer, M.1    Bueno, L.2    Hansen, E.3    DiRienzo, J.M.4
  • 108
    • 1842840103 scopus 로고    scopus 로고
    • Nuclear localization of the Escherichia coli cytolethal distending toxin CdtB subunit
    • McSweeney, L. and L. Dreyfus. 2004. Nuclear localization of the Escherichia coli cytolethal distending toxin CdtB subunit. Cell Microbiol. 6:447-458
    • (2004) Cell Microbiol , vol.6 , pp. 447-458
    • McSweeney, L.1    Dreyfus, L.2
  • 109
    • 16244386487 scopus 로고    scopus 로고
    • Carbohydrate-binding specificity of the Escherichia coli cytolethal distending toxin CdtA-II and CdtC-II subunits
    • McSweeney, L. and L. Dreyfus. 2005. Carbohydrate-binding specificity of the Escherichia coli cytolethal distending toxin CdtA-II and CdtC-II subunits. Infect Immun. 73:2051-2060
    • (2005) Infect Immun , vol.73 , pp. 2051-2060
    • McSweeney, L.1    Dreyfus, L.2
  • 110
    • 0028281989 scopus 로고
    • Pore-formation by Escherichia coli hemolysin (HlyA) and other members of the RTX toxins family
    • Menestrina, G., C. Moser, S. Pellet, and R.A. Welch. 1994. Pore-formation by Escherichia coli hemolysin (HlyA) and other members of the RTX toxins family. Toxicology. 87:249-267
    • (1994) Toxicology , vol.87 , pp. 249-267
    • Menestrina, G.1    Moser, C.2    Pellet, S.3    Welch, R.A.4
  • 111
    • 0036148284 scopus 로고    scopus 로고
    • Herpesvirus assembly and egress
    • Mettenleiter, T.C. 2002. Herpesvirus assembly and egress. J Virol. 76:1537-1547
    • (2002) J Virol , vol.76 , pp. 1537-1547
    • Mettenleiter, T.C.1
  • 112
    • 18744382150 scopus 로고    scopus 로고
    • Glycoprotein D receptor-dependent, low-pH-independent endocytic entry of herpes simplex virus type 1
    • Milne, R.S., A.V. Nicola, J.C. Whitbeck, R.J. Eisenberg, and G.H. Cohen. 2005. Glycoprotein D receptor-dependent, low-pH-independent endocytic entry of herpes simplex virus type 1. J Virol. 79:6655-6663
    • (2005) J Virol , vol.79 , pp. 6655-6663
    • Milne, R.S.1    Nicola, A.V.2    Whitbeck, J.C.3    Eisenberg, R.J.4    Cohen, G.H.5
  • 113
    • 0029989370 scopus 로고    scopus 로고
    • Regulation of second messengers by the inositol polyphosphate 5-phosphatases
    • Mitchell, C., S. Brown, J. Campbell, A. Munday, and C. Speed. 1996. Regulation of second messengers by the inositol polyphosphate 5-phosphatases. Biochem Soc Trans. 24:994-1000
    • (1996) Biochem Soc Trans , vol.24 , pp. 994-1000
    • Mitchell, C.1    Brown, S.2    Campbell, J.3    Munday, A.4    Speed, C.5
  • 114
    • 0030298375 scopus 로고    scopus 로고
    • Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family
    • Montgomery, R.I., M.S. Warner, B.J. Lum, and P.G. Spear. 1996. Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. Cell. 87:427-436
    • (1996) Cell , vol.87 , pp. 427-436
    • Montgomery, R.I.1    Warner, M.S.2    Lum, B.J.3    Spear, P.G.4
  • 115
    • 0141703462 scopus 로고    scopus 로고
    • Biological activities and pore formation of Clostridium perfringens beta toxin in HL 60 cells
    • Nagahama, M., S. Hayashi, S. Morimitsu, and J. Sakurai. 2003. Biological activities and pore formation of Clostridium perfringens beta toxin in HL 60 cells. J Biol Chem. 278:36934-36941
    • (2003) J Biol Chem , vol.278 , pp. 36934-36941
    • Nagahama, M.1    Hayashi, S.2    Morimitsu, S.3    Sakurai, J.4
  • 116
    • 2642550772 scopus 로고    scopus 로고
    • Assembly and function of a bacterial genotoxin
    • Nesic, D., Y. Hsu, and C.E. Stebbins. 2004. Assembly and function of a bacterial genotoxin. Nature. 429:429-433
    • (2004) Nature , vol.429 , pp. 429-433
    • Nesic, D.1    Hsu, Y.2    Stebbins, C.E.3
  • 117
    • 19944423114 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway
    • Nicola, A.V., J. Hou, E.O. Major, and S.E. Straus. 2005. Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway. J Virol. 79:7609-7616
    • (2005) J Virol , vol.79 , pp. 7609-7616
    • Nicola, A.V.1    Hou, J.2    Major, E.O.3    Straus, S.E.4
  • 118
    • 0037404499 scopus 로고    scopus 로고
    • Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells
    • Nicola, A.V., A.M. McEvoy, and S.E. Straus. 2003. Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells. J Virol. 77:5324-5332
    • (2003) J Virol , vol.77 , pp. 5324-5332
    • Nicola, A.V.1    McEvoy, A.M.2    Straus, S.E.3
  • 119
    • 3142719117 scopus 로고    scopus 로고
    • Cellular and viral requirements for rapid endocytic entry of herpes simplex virus
    • Nicola, A.V. and S.E. Straus. 2004. Cellular and viral requirements for rapid endocytic entry of herpes simplex virus. J Virol. 78:7508-7517
    • (2004) J Virol , vol.78 , pp. 7508-7517
    • Nicola, A.V.1    Straus, S.E.2
  • 120
    • 75749100159 scopus 로고    scopus 로고
    • Expanding the role of 3-O sulfated heparan sulfate in herpes simplex virus type-1 entry
    • O'Donnell, C.D., M. Kovacs, J. Akhtar, T. Valyi-Nagy, and D. Shukla. 2009. Expanding the role of 3-O sulfated heparan sulfate in herpes simplex virus type-1 entry. Virology. 397:389-398
    • (2009) Virology , vol.397 , pp. 389-398
    • O'Donnell, C.D.1    Kovacs, M.2    Akhtar, J.3    Valyi-Nagy, T.4    Shukla, D.5
  • 121
    • 58049209246 scopus 로고    scopus 로고
    • The importance of heparan sulfate in herpesvirus infection
    • O'Donnell, C.D. and D. Shukla. 2008. The importance of heparan sulfate in herpesvirus infection. Virol Sin. 23:383-393
    • (2008) Virol Sin , vol.23 , pp. 383-393
    • O'Donnell, C.D.1    Shukla, D.2
  • 122
    • 0031036624 scopus 로고    scopus 로고
    • Examination of diarrheagenicity of cytolethal distending toxin: Suckling mouse response to the products of the cdtABC genes of Shigella dysenteriae
    • Okuda, J., M. Fukumoto, Y. Takeda, and M. Nishibuchi. 1997. Examination of diarrheagenicity of cytolethal distending toxin: Suckling mouse response to the products of the cdtABC genes of Shigella dysenteriae. Infect Immun. 65:428-433
    • (1997) Infect Immun , vol.65 , pp. 428-433
    • Okuda, J.1    Fukumoto, M.2    Takeda, Y.3    Nishibuchi, M.4
  • 123
    • 0029008918 scopus 로고
    • Distribution of the cytolethal distending toxin A gene (cdtA) among species of Shigella dn Vibrio, and cloning and sequencing of the cdt gene from Shigella dysenteriae
    • Okuda, J., H. Kurazono, and Y. Takeda. 1995. Distribution of the cytolethal distending toxin A gene (cdtA) among species of Shigella dn Vibrio, and cloning and sequencing of the cdt gene from Shigella dysenteriae. Microb Pathog. 18:167-172
    • (1995) Microb Pathog , vol.18 , pp. 167-172
    • Okuda, J.1    Kurazono, H.2    Takeda, Y.3
  • 124
    • 70350322311 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 production requires a functional ESCRT-III complex but is independent of TSG101 and ALIX expression
    • Pawliczek, T. and C.M. Crump. 2009. Herpes simplex virus type 1 production requires a functional ESCRT-III complex but is independent of TSG101 and ALIX expression. J Virol. 83:11254-11264
    • (2009) J Virol , vol.83 , pp. 11254-11264
    • Pawliczek, T.1    Crump, C.M.2
  • 125
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips, R., T. Ursell, P. Wiggins, and P. Sens. 2009. Emerging roles for lipids in shaping membrane-protein function. Nature. 459:379-385
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 126
    • 0028045039 scopus 로고
    • Cloning, sequencing, and expression of the Escherichia coli cytolethal distending toxin genes
    • Pickett, C.L., D.L. Cottle, E.C. Pesci, and G. Bikah. 1994. Cloning, sequencing, and expression of the Escherichia coli cytolethal distending toxin genes. Infect Immun. 62:1227-1237
    • (1994) Infect Immun , vol.62 , pp. 1227-1237
    • Pickett, C.L.1    Cottle, D.L.2    Pesci, E.C.3    Bikah, G.4
  • 127
    • 0033167976 scopus 로고    scopus 로고
    • The cytolethal distending toxin family
    • Pickett, C.L. and C.A. Whitehouse. 1999. The cytolethal distending toxin family. Trends Microbiol. 7:292-297
    • (1999) Trends Microbiol , vol.7 , pp. 292-297
    • Pickett, C.L.1    Whitehouse, C.A.2
  • 128
    • 3042818271 scopus 로고    scopus 로고
    • Kinetics of dye efflux and lipid flip-flop induced by d-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, a-helical peptides
    • Pokorny, A. and P.F.F. Almeida. 2004. Kinetics of dye efflux and lipid flip-flop induced by d-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, a-helical peptides. Biochemistry. 43:8846-8857
    • (2004) Biochemistry , vol.43 , pp. 8846-8857
    • Pokorny, A.1    Almeida, P.F.F.2
  • 129
    • 0036712127 scopus 로고    scopus 로고
    • Mechanism and kinetics of d-lysin interaction with phospholipid vesicles
    • Pokorny, A., T.H. Birkbeck, and P.F.F. Almeida. 2002. Mechanism and kinetics of d-lysin interaction with phospholipid vesicles. Biochemistry. 41:11044-11056
    • (2002) Biochemistry , vol.41 , pp. 11044-11056
    • Pokorny, A.1    Birkbeck, T.H.2    Almeida, P.F.F.3
  • 130
    • 28244489607 scopus 로고    scopus 로고
    • Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes
    • Powers, J.-P.S., A. Tan, A. Ramamoorthy, and R.E.W. Hancock. 2005. Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes. Biochemistry. 44:15504-15513
    • (2005) Biochemistry , vol.44 , pp. 15504-15513
    • Powers, J.-P.S.1    Tan, A.2    Ramamoorthy, A.3    Hancock, R.E.W.4
  • 132
    • 2442697760 scopus 로고    scopus 로고
    • Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes U(L)31 and U(L)34
    • Reynolds, A.E., L. Liang, and J.D. Baines. 2004. Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes U(L)31 and U(L)34. J Virol. 78:5564-5575
    • (2004) J Virol , vol.78 , pp. 5564-5575
    • Reynolds, A.E.1    Liang, L.2    Baines, J.D.3
  • 133
    • 0028785891 scopus 로고
    • Non-bilayer lipids are required for efficient protein transport across the plasma membrane of Escherichia coli
    • Rietveld, A.G., M.C. Koorengevel, and B. De Kruijff. 1995. Non-bilayer lipids are required for efficient protein transport across the plasma membrane of Escherichia coli. EMBO J. 14:5506-5513
    • (1995) EMBO J , vol.14 , pp. 5506-5513
    • Rietveld, A.G.1    Koorengevel, M.C.2    De Kruijff, B.3
  • 134
    • 44749085794 scopus 로고    scopus 로고
    • Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited
    • Roche, S., A.A. Albertini, J. Lepault, S. Bressanelli, and Y. Gaudin. 2008. Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited. Cell Mol Life Sci. 65:1716-1728
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1716-1728
    • Roche, S.1    Albertini, A.A.2    Lepault, J.3    Bressanelli, S.4    Gaudin, Y.5
  • 135
    • 33745974537 scopus 로고    scopus 로고
    • Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G
    • Roche, S., S. Bressanelli, F.A. Rey, and Y. Gaudin. 2006. Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G. Science. 313:187-191
    • (2006) Science , vol.313 , pp. 187-191
    • Roche, S.1    Bressanelli, S.2    Rey, F.A.3    Gaudin, Y.4
  • 136
    • 0027502727 scopus 로고
    • A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells, and its particles lack glycoprotein H
    • Roop, C., L. Hutchinson, and D.C. Johnson. 1993. A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells, and its particles lack glycoprotein H. J Virol. 67:2285-2297
    • (1993) J Virol , vol.67 , pp. 2285-2297
    • Roop, C.1    Hutchinson, L.2    Johnson, D.C.3
  • 137
    • 40749106962 scopus 로고    scopus 로고
    • PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B
    • Satoh, T., J. Arii, T. Suenaga, J. Wang, A. Kogure, J. Uehori, N. Arase et al. 2008. PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B. Cell. 132:935-944
    • (2008) Cell , vol.132 , pp. 935-944
    • Satoh, T.1    Arii, J.2    Suenaga, T.3    Wang, J.4    Kogure, A.5    Uehori, J.6    Arase, N.7
  • 138
    • 0037564493 scopus 로고    scopus 로고
    • Lipid phosphatases in the regulation of T cell activiation: Living up to their PTEN-tial
    • Seminario, M. and R. Wange. 2003a. Lipid phosphatases in the regulation of T cell activiation: Living up to their PTEN-tial. Immunol Cell Biol. 192:80-97
    • (2003) Immunol Cell Biol , vol.192 , pp. 80-97
    • Seminario, M.1    Wange, R.2
  • 139
    • 0345687901 scopus 로고    scopus 로고
    • PTEN expression in PTEN-null leukeamic T cells lines leads to reduced proliferation via slowed cell cycle progression
    • Seminario, M., P. Precht, R. Wersto, M. Gorospe, and R. Wange. 2003b. PTEN expression in PTEN-null leukeamic T cells lines leads to reduced proliferation via slowed cell cycle progression. Oncogene. 22:8195-8204
    • (2003) Oncogene , vol.22 , pp. 8195-8204
    • Seminario, M.1    Precht, P.2    Wersto, R.3    Gorospe, M.4    Wange, R.5
  • 140
    • 0027179178 scopus 로고
    • Role of membrane defects in the regulation of the activity of protein kinase C
    • Senisterra, G. and R.M. Epand. 1993. Role of membrane defects in the regulation of the activity of protein kinase C. Arch Biochem Biophys. 300:378-383
    • (1993) Arch Biochem Biophys , vol.300 , pp. 378-383
    • Senisterra, G.1    Epand, R.M.2
  • 141
    • 0017141468 scopus 로고
    • Enrichment of PHA transformed lymphocytes in samples containing mixed populations
    • Shenker, B. and I. Gray. 1976. Enrichment of PHA transformed lymphocytes in samples containing mixed populations. J Immunol Methods. 13:161-166
    • (1976) J Immunol Methods , vol.13 , pp. 161-166
    • Shenker, B.1    Gray, I.2
  • 142
    • 13544272029 scopus 로고    scopus 로고
    • Induction of cell cycle arrest in lymphocytes by Actinobacillus actinomycetemcomitans cytolethal distending toxin requires three subunits for maximum activity
    • Shenker, B.J., D. Besack, T.L. McKay, L. Pankoski, A. Zekavat, and D.R. Demuth. 2005. Induction of cell cycle arrest in lymphocytes by Actinobacillus actinomycetemcomitans cytolethal distending toxin requires three subunits for maximum activity. J Immunol. 174:2228-2234
    • (2005) J Immunol , vol.174 , pp. 2228-2234
    • Shenker, B.J.1    Besack, D.2    McKay, T.L.3    Pankoski, L.4    Zekavat, A.5    Demuth, D.R.6
  • 143
    • 34247148624 scopus 로고    scopus 로고
    • A novel mode of action for a microbial-derived immunotoxin: the cytolethal distending toxin subunit B exhibits phosphatidylinositol 3,4,5-triphosphate phosphatase activity
    • Shenker, B.J., M. Dlakic, L.P. Walker, D. Besack, E. Jaffe, E. LaBelle, and K. Boesze-Battaglia. 2007. A novel mode of action for a microbial-derived immunotoxin: the cytolethal distending toxin subunit B exhibits phosphatidylinositol 3,4,5-triphosphate phosphatase activity. J Immunol. 178:5099-5108
    • (2007) J Immunol , vol.178 , pp. 5099-5108
    • Shenker, B.J.1    Dlakic, M.2    Walker, L.P.3    Besack, D.4    Jaffe, E.5    LaBelle, E.6    Boesze-Battaglia, K.7
  • 144
    • 0034283934 scopus 로고    scopus 로고
    • Expression of the cytolethal distending toxin (Cdt) operon in Actinobacillus actinomycetemcomitans: Evidence that the CdtB protein is responsible for G2 arrest of the cell cycle in human T-cells
    • Shenker, B.J., R.H. Hoffmaster, T.L. McKay, and D.R. Demuth. 2000. Expression of the cytolethal distending toxin (Cdt) operon in Actinobacillus actinomycetemcomitans: Evidence that the CdtB protein is responsible for G2 arrest of the cell cycle in human T-cells. J Immunol. 165:2612-2618
    • (2000) J Immunol , vol.165 , pp. 2612-2618
    • Shenker, B.J.1    Hoffmaster, R.H.2    McKay, T.L.3    Demuth, D.R.4
  • 145
    • 0035399760 scopus 로고    scopus 로고
    • Induction of apoptosis in human T cells by Actinobacillus actinomycetemcomitans cytolethal distending toxin is a consequence of G2 arrest of the cell cycle
    • Shenker, B.J., R.H. Hoffmaster, A. Zekavat, N. Yamguchi, E.T. Lally, and D.R. Demuth. 2001. Induction of apoptosis in human T cells by Actinobacillus actinomycetemcomitans cytolethal distending toxin is a consequence of G2 arrest of the cell cycle. J Immunol. 167:435-441
    • (2001) J Immunol , vol.167 , pp. 435-441
    • Shenker, B.J.1    Hoffmaster, R.H.2    Zekavat, A.3    Yamguchi, N.4    Lally, E.T.5    Demuth, D.R.6
  • 146
    • 0033561543 scopus 로고    scopus 로고
    • Actinobacillus actinomycetemcmitans immunosuppressive protein is a member of the family of cytolethal distending toxins capable of causing a G2 arrest in human T cells
    • Shenker, B.J., T.L. McKay, S. Datar, M. Miller, R. Chowhan, and D.R. Demuth. 1999. Actinobacillus actinomycetemcmitans immunosuppressive protein is a member of the family of cytolethal distending toxins capable of causing a G2 arrest in human T cells. J Immunol. 162:4773-4780
    • (1999) J Immunol , vol.162 , pp. 4773-4780
    • Shenker, B.J.1    McKay, T.L.2    Datar, S.3    Miller, M.4    Chowhan, R.5    Demuth, D.R.6
  • 148
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K. and E. Ikonen. 1997. Functional rafts in cell membranes. Nature. 387:569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 149
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons, K. and D. Toomre. 2000. Lipid rafts and signal transduction. Nat Rev Cell Mol Biol. 1:31-39
    • (2000) Nat Rev Cell Mol Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 150
  • 151
    • 1842850945 scopus 로고    scopus 로고
    • Herpes simplex virus: Receptors and ligands for cell entry
    • Spear, P.G. 2004. Herpes simplex virus: Receptors and ligands for cell entry. Cell Microbiol. 6:401-410
    • (2004) Cell Microbiol , vol.6 , pp. 401-410
    • Spear, P.G.1
  • 152
    • 29144441087 scopus 로고    scopus 로고
    • Different receptors binding to distinct interfaces on herpes simplex virus gD can trigger events leading to cell fusion and viral entry
    • Spear, P.G., S. Manoj, M. Yoon, C.R. Jogger, A. Zago, and D. Myscofski. 2006. Different receptors binding to distinct interfaces on herpes simplex virus gD can trigger events leading to cell fusion and viral entry. Virology. 344:17-24
    • (2006) Virology , vol.344 , pp. 17-24
    • Spear, P.G.1    Manoj, S.2    Yoon, M.3    Jogger, C.R.4    Zago, A.5    Myscofski, D.6
  • 153
  • 154
    • 77049108867 scopus 로고    scopus 로고
    • Glycoprotein D actively induces rapid internalization of two nectin-1 isoforms during herpes simplex virus entry
    • Stiles, K.M. and C. Krummenacher. 2010. Glycoprotein D actively induces rapid internalization of two nectin-1 isoforms during herpes simplex virus entry. Virology. 399:109-119
    • (2010) Virology , vol.399 , pp. 109-119
    • Stiles, K.M.1    Krummenacher, C.2
  • 155
    • 40649105829 scopus 로고    scopus 로고
    • The herpes simplex virus receptor nectin-1 is down-regulated after trans-interaction with glycoprotein D
    • Stiles, K.M., R.S. Milne, G.H. Cohen, R.J. Eisenberg, and C. Krummenacher. 2008. The herpes simplex virus receptor nectin-1 is down-regulated after trans-interaction with glycoprotein D. Virology. 373:98-111
    • (2008) Virology , vol.373 , pp. 98-111
    • Stiles, K.M.1    Milne, R.S.2    Cohen, G.H.3    Eisenberg, R.J.4    Krummenacher, C.5
  • 156
    • 0023513629 scopus 로고
    • Extensive homology between the leukotoxin of Pasteurella haemolytica A1 and the alpha-hemolysin of Escherichia coli
    • Strathdee, C.A. and R.Y. Lo. 1987. Extensive homology between the leukotoxin of Pasteurella haemolytica A1 and the alpha-hemolysin of Escherichia coli. Infect Immun. 55:3233-3236
    • (1987) Infect Immun , vol.55 , pp. 3233-3236
    • Strathdee, C.A.1    Lo, R.Y.2
  • 157
    • 33847295240 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B
    • Subramanian, R.P. and R.J. Geraghty. 2007. Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B. Proc Natl Acad Sci USA. 104:2903-2908
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2903-2908
    • Subramanian, R.P.1    Geraghty, R.J.2
  • 158
    • 72749092609 scopus 로고    scopus 로고
    • A FRET-based method for probing the conformational behavior of an intrinsically disordered repeat domain from Bordatella pertussis adenylate cyclase
    • Szilvay, G.R., M.A. Blenner, O. Shur, D.M. Cropek, and S. Banta. 2009. A FRET-based method for probing the conformational behavior of an intrinsically disordered repeat domain from Bordatella pertussis adenylate cyclase. Biochemistry. 48:11273-11282
    • (2009) Biochemistry , vol.48 , pp. 11273-11282
    • Szilvay, G.R.1    Blenner, M.A.2    Shur, O.3    Cropek, D.M.4    Banta, S.5
  • 159
    • 0018827360 scopus 로고
    • Biochemical and morphological characterization of the killing of human monocytes by a leukotoxin derived from Actinobacillus actinomycetemcomitans
    • Taichman, N.S., R.T. Dean, and C.J. Sanderson. 1980. Biochemical and morphological characterization of the killing of human monocytes by a leukotoxin derived from Actinobacillus actinomycetemcomitans. Infect Immun. 28:258-268
    • (1980) Infect Immun , vol.28 , pp. 258-268
    • Taichman, N.S.1    Dean, R.T.2    Sanderson, C.J.3
  • 162
    • 26444445063 scopus 로고    scopus 로고
    • A role for herpesvirus entry mediator as the receptor for herpes simplex virus 1 entry into primary human trabecular meshwork cells
    • Tiwari, V., C. Clement, P.M. Scanlan, D. Kowlessur, B.Y. Yue, and D. Shukla. 2005. A role for herpesvirus entry mediator as the receptor for herpes simplex virus 1 entry into primary human trabecular meshwork cells. J Virol. 79:13173-13179
    • (2005) J Virol , vol.79 , pp. 13173-13179
    • Tiwari, V.1    Clement, C.2    Scanlan, P.M.3    Kowlessur, D.4    Yue, B.Y.5    Shukla, D.6
  • 163
    • 53849128530 scopus 로고    scopus 로고
    • Role for nectin-1 in herpes simplex virus 1 entry and spread in human retinal pigment epithelial cells
    • Tiwari, V., M.J. Oh, M. Kovacs, S.Y. Shukla, T. Valyi-Nagy, and D. Shukla. 2008. Role for nectin-1 in herpes simplex virus 1 entry and spread in human retinal pigment epithelial cells. FEBS J. 275:5272-5285
    • (2008) FEBS J , vol.275 , pp. 5272-5285
    • Tiwari, V.1    Oh, M.J.2    Kovacs, M.3    Shukla, S.Y.4    Valyi-Nagy, T.5    Shukla, D.6
  • 164
    • 0035805064 scopus 로고    scopus 로고
    • Specificity determinants in phosphoinoitide dephosphorylation: crystal structure of an archetypalinositol polyphosphate 5-phosphatase
    • Tsujishita, Y., S. Guo, L. Stolz, J. York, and H. Hurley. 2001. Specificity determinants in phosphoinoitide dephosphorylation: crystal structure of an archetypalinositol polyphosphate 5-phosphatase. Cell. 105:379-389
    • (2001) Cell , vol.105 , pp. 379-389
    • Tsujishita, Y.1    Guo, S.2    Stolz, L.3    York, J.4    Hurley, H.5
  • 166
    • 0035004910 scopus 로고    scopus 로고
    • Effects of lipid composition on membrane permeabilization by Sticholysin I and II, two cytolysins of the sea anemone Stichodactyla helanthus
    • Valcarcel, C.A., M.D. Serra, C. Potrich, I. Bernhart, M. Tejuca, D. Martinez, F. Pazos, M.E. Lanio, and G. Menestrina. 2001. Effects of lipid composition on membrane permeabilization by Sticholysin I and II, two cytolysins of the sea anemone Stichodactyla helanthus. Biophys J. 80:2761-2774
    • (2001) Biophys J , vol.80 , pp. 2761-2774
    • Valcarcel, C.A.1    Serra, M.D.2    Potrich, C.3    Bernhart, I.4    Tejuca, M.5    Martinez, D.6    Pazos, F.7    Lanio, M.E.8    Menestrina, G.9
  • 167
    • 0034193232 scopus 로고    scopus 로고
    • Role of lipids in the translocation of proteins across membranes
    • van Voorst, F. and B. De Kruijff. 2000. Role of lipids in the translocation of proteins across membranes. Biochem J. 347:601-612
    • (2000) Biochem J , vol.347 , pp. 601-612
    • van Voorst, F.1    De Kruijff, B.2
  • 170
    • 0023269886 scopus 로고
    • Identification of two different hemolysin determinants in uropathogenic Proteus isolates
    • Welch, R.A. 1987. Identification of two different hemolysin determinants in uropathogenic Proteus isolates. Infect Immun. 55:2183-2190
    • (1987) Infect Immun , vol.55 , pp. 2183-2190
    • Welch, R.A.1
  • 171
    • 0026080402 scopus 로고
    • Pore-forming cytolysins of gram-negative bacteria
    • Welch, R.A. 1991. Pore-forming cytolysins of gram-negative bacteria. Mol Microbiol. 5:521-528
    • (1991) Mol Microbiol , vol.5 , pp. 521-528
    • Welch, R.A.1
  • 172
    • 0030793175 scopus 로고    scopus 로고
    • Glycoprotein D of herpes simplex virus (HSV) binds directly to HVEM, a member of the TNFR superfamily and a mediator of HSV entry
    • Whitbeck, J.C., C. Peng, H. Lou, R. Xu, S.H. Willis, M. Ponce de Leon, T. Peng et al. 1997. Glycoprotein D of herpes simplex virus (HSV) binds directly to HVEM, a member of the TNFR superfamily and a mediator of HSV entry. J Virol. 71:6083-6093
    • (1997) J Virol , vol.71 , pp. 6083-6093
    • Whitbeck, J.C.1    Peng, C.2    Lou, H.3    Xu, R.4    Willis, S.H.5    Ponce de Leon, M.6    Peng, T.7
  • 173
    • 33645791673 scopus 로고    scopus 로고
    • Stable association of herpes simplex virus with target membranes is triggered by low pH in the presence of the gD receptor, HVEM
    • Whitbeck, J.C., Y. Zuo, R.S. Milne, G.H. Cohen, and R.J. Eisenberg. 2006. Stable association of herpes simplex virus with target membranes is triggered by low pH in the presence of the gD receptor, HVEM. J Virol. 80:3773-3780
    • (2006) J Virol , vol.80 , pp. 3773-3780
    • Whitbeck, J.C.1    Zuo, Y.2    Milne, R.S.3    Cohen, G.H.4    Eisenberg, R.J.5
  • 174
    • 0035849323 scopus 로고    scopus 로고
    • Herpes simplex virus infections
    • Whitley, R.J. and B. Roizman. 2001. Herpes simplex virus infections. Lancet. 357:1513-8
    • (2001) Lancet , vol.357 , pp. 1513-1518
    • Whitley, R.J.1    Roizman, B.2
  • 175
    • 65349186030 scopus 로고    scopus 로고
    • The U(L)31 and U(L)34 gene products of herpes simplex virus 1 are required for optimal localization of viral glycoproteins D and M to the inner nuclear membranes of infected cells
    • Wills, E., F. Mou, and J.D. Baines. 2009. The U(L)31 and U(L)34 gene products of herpes simplex virus 1 are required for optimal localization of viral glycoproteins D and M to the inner nuclear membranes of infected cells. J Virol. 83:4800-4809
    • (2009) J Virol , vol.83 , pp. 4800-4809
    • Wills, E.1    Mou, F.2    Baines, J.D.3
  • 176
    • 63149111461 scopus 로고    scopus 로고
    • Herpesvirus gB-induced fusion between the virion envelope and outer nuclear membrane during virus egress is regulated by the viral US3 kinase
    • Wisner, T.W., C.C. Wright, A. Kato, Y. Kawaguchi, F. Mou, J.D. Baines, R.J. Roller, and D.C. Johnson. 2009. Herpesvirus gB-induced fusion between the virion envelope and outer nuclear membrane during virus egress is regulated by the viral US3 kinase. J Virol. 83:3115-3126
    • (2009) J Virol , vol.83 , pp. 3115-3126
    • Wisner, T.W.1    Wright, C.C.2    Kato, A.3    Kawaguchi, Y.4    Mou, F.5    Baines, J.D.6    Roller, R.J.7    Johnson, D.C.8
  • 177
    • 0030663666 scopus 로고    scopus 로고
    • Inositol lipid 5-phosphatases-Traffic signals and signal traffic
    • Woscholski, R. and P. Parker. 1997. Inositol lipid 5-phosphatases-Traffic signals and signal traffic. Trends Biochem Sci. 22:427-431
    • (1997) Trends Biochem Sci , vol.22 , pp. 427-431
    • Woscholski, R.1    Parker, P.2
  • 179
    • 31344440038 scopus 로고    scopus 로고
    • Varation of loop sequence alters stability of cytolethal distending toxin 9CDT): crystal structure of CDT from Actinobacillus actinomycetemcomitans
    • Yamada, T., J. Komoto, K. Saiki, K. Konishi, and F. Takusagawa. 2006. Varation of loop sequence alters stability of cytolethal distending toxin 9CDT): crystal structure of CDT from Actinobacillus actinomycetemcomitans. Protein Sci. 15:362-372
    • (2006) Protein Sci , vol.15 , pp. 362-372
    • Yamada, T.1    Komoto, J.2    Saiki, K.3    Konishi, K.4    Takusagawa, F.5
  • 180
    • 0037134485 scopus 로고    scopus 로고
    • Heliothis virescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation
    • Zhuang, M., D.I. Oltean, I. Gomez, A.K. Pullikuth, M. Soberon, A. Bravo, and S.S. Gill. 2002. Heliothis virescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation. J Biol Chem. 277:13863-13872
    • (2002) J Biol Chem , vol.277 , pp. 13863-13872
    • Zhuang, M.1    Oltean, D.I.2    Gomez, I.3    Pullikuth, A.K.4    Soberon, M.5    Bravo, A.6    Gill, S.S.7
  • 181
    • 0035805608 scopus 로고    scopus 로고
    • Coupling of cholesterol and cone-shaped lipids in bilayers augments membrane permeabilization by the cholesterol-specific toxins streptolysin O and vibrio cholerae cytolysin
    • Zitzer, A., R. Bittman, C.A. Verbicky, R.K. Erukulla, S. Bhakdi, S. Weis, A. Valveva, and M. Palmer. 2001. Coupling of cholesterol and cone-shaped lipids in bilayers augments membrane permeabilization by the cholesterol-specific toxins streptolysin O and vibrio cholerae cytolysin. J Biol Chem. 276:14628-14633
    • (2001) J Biol Chem , vol.276 , pp. 14628-14633
    • Zitzer, A.1    Bittman, R.2    Verbicky, C.A.3    Erukulla, R.K.4    Bhakdi, S.5    Weis, S.6    Valveva, A.7    Palmer, M.8


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