메뉴 건너뛰기




Volumn 70, Issue 12, 2013, Pages 2083-2098

Effects of MACPF/CDC proteins on lipid membranes

Author keywords

Cholesterol dependent cytolysins; MACPF domain; Membrane damage; Membrane interactions; Pore

Indexed keywords

CHOLESTEROL DEPENDENT CYTOLYSIN; GRANZYME B; MEMBRANE ATTACK COMPLEX PERFORIN; MEMBRANE PROTEIN; MONOMER; PERFORIN; UNCLASSIFIED DRUG;

EID: 84878546568     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-012-1153-8     Document Type: Review
Times cited : (67)

References (127)
  • 1
    • 0022466507 scopus 로고
    • Structural/functional similarity between proteins involved in complement- and cytotoxic T-lymphocyte-mediated cytolysis
    • 2427956 1:CAS:528:DyaL2sXhtVSmsLs%3D 10.1038/322831a0
    • Tschopp J, Masson D, Stanley KK (1986) Structural/functional similarity between proteins involved in complement- and cytotoxic T-lymphocyte-mediated cytolysis. Nature 322:831-834
    • (1986) Nature , vol.322 , pp. 831-834
    • Tschopp, J.1    Masson, D.2    Stanley, K.K.3
  • 3
    • 34548670476 scopus 로고    scopus 로고
    • Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense
    • 17872444 1:CAS:528:DC%2BD2sXhtVejt7%2FN 10.1126/science.1147103
    • Hadders MA, Beringer DX, Gros P (2007) Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense. Science 317:1552-1554
    • (2007) Science , vol.317 , pp. 1552-1554
    • Hadders, M.A.1    Beringer, D.X.2    Gros, P.3
  • 4
    • 43049094015 scopus 로고    scopus 로고
    • Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunit
    • 18440555 1:CAS:528:DC%2BD1cXlslWlur8%3D 10.1016/j.jmb.2008.03.061
    • Slade DJ, Lovelace LL, Chruszcz M, Minor W, Lebioda L, Sodetz JM (2008) Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunit. J Mol Biol 379:331-342
    • (2008) J Mol Biol , vol.379 , pp. 331-342
    • Slade, D.J.1    Lovelace, L.L.2    Chruszcz, M.3    Minor, W.4    Lebioda, L.5    Sodetz, J.M.6
  • 6
    • 23444457403 scopus 로고    scopus 로고
    • Inactivation and activity of cholesterol-dependent cytolysins: What structural studies tell us
    • 16084382 1:CAS:528:DC%2BD2MXntVOiu7s%3D 10.1016/j.str.2005.04.019
    • Gilbert RJ (2005) Inactivation and activity of cholesterol-dependent cytolysins: what structural studies tell us. Structure 13:1097-1106
    • (2005) Structure , vol.13 , pp. 1097-1106
    • Gilbert, R.J.1
  • 7
    • 84857650341 scopus 로고    scopus 로고
    • Membrane assembly of the cholesterol-dependent cytolysin pore complex
    • 21835159 1:CAS:528:DC%2BC38XjtlOltLY%3D 10.1016/j.bbamem.2011.07.036
    • Hotze EM, Tweten RK (2012) Membrane assembly of the cholesterol-dependent cytolysin pore complex. Biochim Biophys Acta 1818:1028-1038
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1028-1038
    • Hotze, E.M.1    Tweten, R.K.2
  • 8
    • 77749292162 scopus 로고    scopus 로고
    • Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface
    • 20145114 1:CAS:528:DC%2BC3cXjsFWiurk%3D 10.1073/pnas.0911581107
    • Farrand AJ, LaChapelle S, Hotze EM, Johnson AE, Tweten RK (2010) Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface. Proc Natl Acad Sci USA 107:4341-4346
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4341-4346
    • Farrand, A.J.1    Lachapelle, S.2    Hotze, E.M.3    Johnson, A.E.4    Tweten, R.K.5
  • 9
    • 16544370492 scopus 로고    scopus 로고
    • Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin
    • 15543155 1:CAS:528:DC%2BD2cXhtVens7jP 10.1038/nsmb862
    • Giddings KS, Zhao J, Sims PJ, Tweten RK (2004) Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin. Nat Struct Mol Biol 11:1173-1178
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1173-1178
    • Giddings, K.S.1    Zhao, J.2    Sims, P.J.3    Tweten, R.K.4
  • 10
    • 0033612389 scopus 로고    scopus 로고
    • Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae
    • 10367893 1:CAS:528:DyaK1MXjs1yqtbc%3D 10.1016/S0092-8674(00)80775-8
    • Gilbert RJ, Jimenez JL, Chen S, Tickle IJ, Rossjohn J, Parker M, Andrew PW, Saibil HR (1999) Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae. Cell 97:647-655
    • (1999) Cell , vol.97 , pp. 647-655
    • Gilbert, R.J.1    Jimenez, J.L.2    Chen, S.3    Tickle, I.J.4    Rossjohn, J.5    Parker, M.6    Andrew, P.W.7    Saibil, H.R.8
  • 11
    • 17444405610 scopus 로고    scopus 로고
    • Structural basis of pore formation by the bacterial toxin pneumolysin
    • 15851031 1:CAS:528:DC%2BD2MXjvV2jtb0%3D 10.1016/j.cell.2005.02.033
    • Tilley SJ, Orlova EV, Gilbert RJ, Andrew PW, Saibil HR (2005) Structural basis of pore formation by the bacterial toxin pneumolysin. Cell 121:247-256
    • (2005) Cell , vol.121 , pp. 247-256
    • Tilley, S.J.1    Orlova, E.V.2    Gilbert, R.J.3    Andrew, P.W.4    Saibil, H.R.5
  • 12
    • 46949109372 scopus 로고    scopus 로고
    • Characterization of a streptococcal cholesterol-dependent cytolysin with a Lewis y and b specific lectin domain
    • 18553932 1:CAS:528:DC%2BD1cXnt1Clsbc%3D 10.1021/bi8005835
    • Farrand S, Hotze E, Friese P, Hollingshead SK, Smith DF, Cummings RD, Dale GL, Tweten RK (2008) Characterization of a streptococcal cholesterol-dependent cytolysin with a Lewis y and b specific lectin domain. Biochemistry 47:7097-7107
    • (2008) Biochemistry , vol.47 , pp. 7097-7107
    • Farrand, S.1    Hotze, E.2    Friese, P.3    Hollingshead, S.K.4    Smith, D.F.5    Cummings, R.D.6    Dale, G.L.7    Tweten, R.K.8
  • 13
    • 84858967104 scopus 로고    scopus 로고
    • Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC)
    • 22267737 1:CAS:528:DC%2BC38XktlKrsro%3D 10.1074/jbc.M111.327809
    • Aleshin AE, Schraufstatter IU, Stec B, Bankston LA, Liddington RC, DiScipio RG (2012) Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC). J Biol Chem 287:10210-10222
    • (2012) J Biol Chem , vol.287 , pp. 10210-10222
    • Aleshin, A.E.1    Schraufstatter, I.U.2    Stec, B.3    Bankston, L.A.4    Liddington, R.C.5    Discipio, R.G.6
  • 17
    • 0033576666 scopus 로고    scopus 로고
    • Chlamydial homologues of the MACPF (MAC/perforin) domain
    • 10608922 1:CAS:528:DC%2BD3cXhtFOqsg%3D%3D 10.1016/S0960-9822(00)80102-5
    • Ponting CP (1999) Chlamydial homologues of the MACPF (MAC/perforin) domain. Curr Biol 9:R911-R913
    • (1999) Curr Biol , vol.9
    • Ponting, C.P.1
  • 19
    • 33845199637 scopus 로고    scopus 로고
    • Perforin-mediated target-cell death and immune homeostasis
    • 17124515 1:CAS:528:DC%2BD28Xht1Clsr7F 10.1038/nri1983
    • Voskoboinik I, Smyth MJ, Trapani JA (2006) Perforin-mediated target-cell death and immune homeostasis. Nat Rev Immunol 6:940-952
    • (2006) Nat Rev Immunol , vol.6 , pp. 940-952
    • Voskoboinik, I.1    Smyth, M.J.2    Trapani, J.A.3
  • 20
    • 84934434219 scopus 로고    scopus 로고
    • Pore formers of the immune system
    • 17892222 10.1007/978-0-387-71767-8-23
    • Podack ER, Deyev V, Shiratsuchi M (2007) Pore formers of the immune system. Adv Exp Med Biol 598:325-341
    • (2007) Adv Exp Med Biol , vol.598 , pp. 325-341
    • Podack, E.R.1    Deyev, V.2    Shiratsuchi, M.3
  • 21
    • 1442286390 scopus 로고    scopus 로고
    • A new membrane-attack complex/perforin (MACPF) domain lethal toxin from the nematocyst venom of the Okinawan sea anemone Actineria villosa
    • 15019483 1:CAS:528:DC%2BD2cXhs1Crs7g%3D 10.1016/j.toxicon.2003.11.017
    • Oshiro N, Kobayashi C, Iwanaga S, Nozaki M, Namikoshi M, Spring J, Nagai H (2004) A new membrane-attack complex/perforin (MACPF) domain lethal toxin from the nematocyst venom of the Okinawan sea anemone Actineria villosa. Toxicon 43:225-228
    • (2004) Toxicon , vol.43 , pp. 225-228
    • Oshiro, N.1    Kobayashi, C.2    Iwanaga, S.3    Nozaki, M.4    Namikoshi, M.5    Spring, J.6    Nagai, H.7
  • 22
    • 23044492638 scopus 로고    scopus 로고
    • Innate immune defense of the sponge Suberites domuncula against bacteria involves a MyD88-dependent signaling pathway. Induction of a perforin-like molecule
    • 15923643 1:CAS:528:DC%2BD2MXmsVyqu78%3D 10.1074/jbc.M504049200
    • Wiens M, Korzhev M, Krasko A, Thakur NL, Perovic-Ottstadt S, Breter HJ, Ushijima H, Diehl-Seifert B, Muller IM, Muller WE (2005) Innate immune defense of the sponge Suberites domuncula against bacteria involves a MyD88-dependent signaling pathway. Induction of a perforin-like molecule. J Biol Chem 280:27949-27959
    • (2005) J Biol Chem , vol.280 , pp. 27949-27959
    • Wiens, M.1    Korzhev, M.2    Krasko, A.3    Thakur, N.L.4    Perovic-Ottstadt, S.5    Breter, H.J.6    Ushijima, H.7    Diehl-Seifert, B.8    Muller, I.M.9    Muller, W.E.10
  • 23
    • 0025194986 scopus 로고
    • Localized requirement for torso-like expression in follicle cells for development of terminal anlagen of the Drosophila embryo
    • 2385293 1:STN:280:DyaK3czkvV2ltQ%3D%3D 10.1038/346660a0
    • Stevens LM, Frohnhofer HG, Klingler M, Nusslein-Volhard C (1990) Localized requirement for torso-like expression in follicle cells for development of terminal anlagen of the Drosophila embryo. Nature 346:660-663
    • (1990) Nature , vol.346 , pp. 660-663
    • Stevens, L.M.1    Frohnhofer, H.G.2    Klingler, M.3    Nusslein-Volhard, C.4
  • 24
    • 0036336931 scopus 로고    scopus 로고
    • Mice that lack astrotactin have slowed neuronal migration
    • 11861479 1:CAS:528:DC%2BD38XitFygtrw%3D
    • Adams NC, Tomoda T, Cooper M, Dietz G, Hatten ME (2002) Mice that lack astrotactin have slowed neuronal migration. Development 129:965-972
    • (2002) Development , vol.129 , pp. 965-972
    • Adams, N.C.1    Tomoda, T.2    Cooper, M.3    Dietz, G.4    Hatten, M.E.5
  • 25
    • 0029947209 scopus 로고    scopus 로고
    • CNS gene encoding astrotactin, which supports neuronal migration along glial fibers
    • 8602532 1:CAS:528:DyaK28XisVegsro%3D 10.1126/science.272.5260.417
    • Zheng C, Heintz N, Hatten ME (1996) CNS gene encoding astrotactin, which supports neuronal migration along glial fibers. Science 272:417-419
    • (1996) Science , vol.272 , pp. 417-419
    • Zheng, C.1    Heintz, N.2    Hatten, M.E.3
  • 26
    • 77952845030 scopus 로고    scopus 로고
    • Apicomplexan perforin-like proteins
    • 20539776 10.4161/cib.3.1.9794
    • Kafsack BF, Carruthers VB (2010) Apicomplexan perforin-like proteins. Commun Integr Biol 3:18-23
    • (2010) Commun Integr Biol , vol.3 , pp. 18-23
    • Kafsack, B.F.1    Carruthers, V.B.2
  • 28
    • 38749123992 scopus 로고    scopus 로고
    • Friend or foe: The same fold for attack and defense
    • 18248850 1:CAS:528:DC%2BD1cXhslGit7c%3D 10.1016/j.it.2007.11.003
    • Lukoyanova N, Saibil HR (2008) Friend or foe: the same fold for attack and defense. Trends Immunol 29:51-53
    • (2008) Trends Immunol , vol.29 , pp. 51-53
    • Lukoyanova, N.1    Saibil, H.R.2
  • 29
    • 52949087550 scopus 로고    scopus 로고
    • Disparate proteins use similar architectures to damage membranes
    • 18778941 1:CAS:528:DC%2BD1cXhtFyqu7nI 10.1016/j.tibs.2008.07.004
    • Anderluh G, Lakey JH (2008) Disparate proteins use similar architectures to damage membranes. Trends Biochem Sci 33:482-490
    • (2008) Trends Biochem Sci , vol.33 , pp. 482-490
    • Anderluh, G.1    Lakey, J.H.2
  • 32
    • 14844321553 scopus 로고    scopus 로고
    • Calcium-dependent plasma membrane binding and cell lysis by perforin are mediated through its C2 domain: A critical role for aspartate residues 429, 435, 483, and 485 but not 491
    • 15576364 1:CAS:528:DC%2BD2MXhs1yhs7g%3D 10.1074/jbc.M413303200
    • Voskoboinik I, Thia MC, Fletcher J, Ciccone A, Browne K, Smyth MJ, Trapani JA (2005) Calcium-dependent plasma membrane binding and cell lysis by perforin are mediated through its C2 domain: a critical role for aspartate residues 429, 435, 483, and 485 but not 491. J Biol Chem 280:8426-8434
    • (2005) J Biol Chem , vol.280 , pp. 8426-8434
    • Voskoboinik, I.1    Thia, M.C.2    Fletcher, J.3    Ciccone, A.4    Browne, K.5    Smyth, M.J.6    Trapani, J.A.7
  • 33
    • 84861721290 scopus 로고    scopus 로고
    • Crystal structure of C5b-6 suggests a structural basis for priming the assembly of the membrane attack complex (MAC)
    • 22500023 1:CAS:528:DC%2BC38XnvVSqtLg%3D 10.1074/jbc.M112.361121
    • Aleshin AE, Discipio RG, Stec B, Liddington RC (2012) Crystal structure of C5b-6 suggests a structural basis for priming the assembly of the membrane attack complex (MAC). J Biol Chem 287:19642-19652
    • (2012) J Biol Chem , vol.287 , pp. 19642-19652
    • Aleshin, A.E.1    Discipio, R.G.2    Stec, B.3    Liddington, R.C.4
  • 35
    • 79955953166 scopus 로고    scopus 로고
    • Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement
    • 21454577 1:CAS:528:DC%2BC3MXmtVGjtrc%3D 10.1074/jbc.M111.219766
    • Lovelace LL, Cooper CL, Sodetz JM, Lebioda L (2011) Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement. J Biol Chem 286:17585-17592
    • (2011) J Biol Chem , vol.286 , pp. 17585-17592
    • Lovelace, L.L.1    Cooper, C.L.2    Sodetz, J.M.3    Lebioda, L.4
  • 36
    • 3042555480 scopus 로고    scopus 로고
    • Pleurotolysin, a novel sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus, assembles into a transmembrane pore complex
    • 15084605 1:CAS:528:DC%2BD2cXkvFGnsrg%3D 10.1074/jbc.M402676200
    • Tomita T, Noguchi K, Mimuro H, Ukaji F, Ito K, Sugawara-Tomita N, Hashimoto Y (2004) Pleurotolysin, a novel sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus, assembles into a transmembrane pore complex. J Biol Chem 279:26975-26982
    • (2004) J Biol Chem , vol.279 , pp. 26975-26982
    • Tomita, T.1    Noguchi, K.2    Mimuro, H.3    Ukaji, F.4    Ito, K.5    Sugawara-Tomita, N.6    Hashimoto, Y.7
  • 39
    • 0034682457 scopus 로고    scopus 로고
    • Interpreting the universal phylogenetic tree
    • 10900003 1:CAS:528:DC%2BD3cXlt1Ggtbc%3D 10.1073/pnas.97.15.8392
    • Woese CR (2000) Interpreting the universal phylogenetic tree. Proc Natl Acad Sci USA 97:8392-8396
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8392-8396
    • Woese, C.R.1
  • 40
    • 1842859044 scopus 로고    scopus 로고
    • Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins
    • 12467570 1:CAS:528:DC%2BD38XptlWls7w%3D 10.1016/S0969-2126(02)00896-1
    • Riffel N, Harlos K, Iourin O, Rao Z, Kingsman A, Stuart D, Fry E (2002) Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins. Structure 10:1627-1636
    • (2002) Structure , vol.10 , pp. 1627-1636
    • Riffel, N.1    Harlos, K.2    Iourin, O.3    Rao, Z.4    Kingsman, A.5    Stuart, D.6    Fry, E.7
  • 41
    • 27944491964 scopus 로고    scopus 로고
    • What does structure tell us about virus evolution?
    • 16271469 1:CAS:528:DC%2BD2MXht1Gnsr%2FF 10.1016/j.sbi.2005.10.012
    • Bamford DH, Grimes JM, Stuart DI (2005) What does structure tell us about virus evolution? Curr Opin Struct Biol 15:655-663
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 655-663
    • Bamford, D.H.1    Grimes, J.M.2    Stuart, D.I.3
  • 43
    • 79960194345 scopus 로고    scopus 로고
    • Insights into the evolution of a complex virus from the crystal structure of vaccinia virus D13
    • 21742267 1:CAS:528:DC%2BC3MXoslWhs74%3D 10.1016/j.str.2011.03.023
    • Bahar MW, Graham SC, Stuart DI, Grimes JM (2011) Insights into the evolution of a complex virus from the crystal structure of vaccinia virus D13. Structure 19:1011-1020
    • (2011) Structure , vol.19 , pp. 1011-1020
    • Bahar, M.W.1    Graham, S.C.2    Stuart, D.I.3    Grimes, J.M.4
  • 44
    • 75049083128 scopus 로고    scopus 로고
    • How baculovirus polyhedra fit square pegs into round holes to robustly package viruses
    • 19959989 1:CAS:528:DC%2BD1MXhsVylsLjP 10.1038/emboj.2009.352
    • Ji X, Sutton G, Evans G, Axford D, Owen R, Stuart DI (2010) How baculovirus polyhedra fit square pegs into round holes to robustly package viruses. EMBO J 29:505-514
    • (2010) EMBO J , vol.29 , pp. 505-514
    • Ji, X.1    Sutton, G.2    Evans, G.3    Axford, D.4    Owen, R.5    Stuart, D.I.6
  • 45
    • 84862605391 scopus 로고    scopus 로고
    • Packing a punch: The mechanism of pore formation by cholesterol-dependent cytolysins and membrane attack complex/perforin-like proteins
    • 22658510 1:CAS:528:DC%2BC38XotVaqu78%3D 10.1016/j.sbi.2012.04.008
    • Dunstone MA, Tweten RK (2012) Packing a punch: the mechanism of pore formation by cholesterol-dependent cytolysins and membrane attack complex/perforin-like proteins. Curr Opin Struct Biol 22:342-349
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 342-349
    • Dunstone, M.A.1    Tweten, R.K.2
  • 46
    • 23144463785 scopus 로고    scopus 로고
    • Mechanisms of cell membrane electropermeabilization: A minireview of our present (lack of ?) knowledge
    • 15951114 1:CAS:528:DC%2BD2MXntVGjt7c%3D 10.1016/j.bbagen.2005.05.006
    • Teissie J, Golzio M, Rols MP (2005) Mechanisms of cell membrane electropermeabilization: a minireview of our present (lack of ?) knowledge. Biochim Biophys Acta 1724:270-280
    • (2005) Biochim Biophys Acta , vol.1724 , pp. 270-280
    • Teissie, J.1    Golzio, M.2    Rols, M.P.3
  • 47
    • 0035252074 scopus 로고    scopus 로고
    • Fusion needs more than SNAREs
    • 11214300 1:CAS:528:DC%2BD3MXhtVygs7g%3D 10.1038/35054637
    • Almers W (2001) Fusion needs more than SNAREs. Nature 409:567-568
    • (2001) Nature , vol.409 , pp. 567-568
    • Almers, W.1
  • 48
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • 16357862 1:CAS:528:DC%2BD2MXhtlSqu7nN 10.1038/nrmicro1326
    • Kielian M, Rey FA (2006) Virus membrane-fusion proteins: more than one way to make a hairpin. Nat Rev Microbiol 4:67-76
    • (2006) Nat Rev Microbiol , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 49
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
    • 8943190 1:CAS:528:DyaK28XnsFGis7w%3D 10.1126/science.274.5294.1859
    • Song L, Hobaugh MR, Shustak C, Cheley S, Bayley H, Gouaux JE (1996) Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 274:1859-1866
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 50
    • 0037147239 scopus 로고    scopus 로고
    • Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature
    • 12381734 1:CAS:528:DC%2BD38XpsFaksrw%3D 10.1074/jbc.M206069200
    • Basanez G, Sharpe JC, Galanis J, Brandt TB, Hardwick JM, Zimmerberg J (2002) Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature. J Biol Chem 277:49360-49365
    • (2002) J Biol Chem , vol.277 , pp. 49360-49365
    • Basanez, G.1    Sharpe, J.C.2    Galanis, J.3    Brandt, T.B.4    Hardwick, J.M.5    Zimmerberg, J.6
  • 51
    • 56249132688 scopus 로고    scopus 로고
    • Structure of transmembrane pore induced by Bax-derived peptide: Evidence for lipidic pores
    • 18987313 1:CAS:528:DC%2BD1cXhsVWns73E 10.1073/pnas.0807764105
    • Qian S, Wang W, Yang L, Huang HW (2008) Structure of transmembrane pore induced by Bax-derived peptide: evidence for lipidic pores. Proc Natl Acad Sci USA 105:17379-17383
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 17379-17383
    • Qian, S.1    Wang, W.2    Yang, L.3    Huang, H.W.4
  • 53
    • 0028062876 scopus 로고
    • Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form
    • 7929224 1:CAS:528:DyaK2cXlvFyitrk%3D
    • Morgan PJ, Hyman SC, Byron O, Andrew PW, Mitchell TJ, Rowe AJ (1994) Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form. J Biol Chem 269:25315-25320
    • (1994) J Biol Chem , vol.269 , pp. 25315-25320
    • Morgan, P.J.1    Hyman, S.C.2    Byron, O.3    Andrew, P.W.4    Mitchell, T.J.5    Rowe, A.J.6
  • 54
    • 0027526035 scopus 로고
    • The projection structure of Perfringolysin O (Clostridium perfringens [theta]-toxin)
    • 8454043 1:CAS:528:DyaK3sXit1Oqs74%3D 10.1016/0014-5793(93)80050-5
    • Olofsson A, Hebert H, Thelestam M (1993) The projection structure of Perfringolysin O (Clostridium perfringens [theta]-toxin). FEBS Lett 319:125-127
    • (1993) FEBS Lett , vol.319 , pp. 125-127
    • Olofsson, A.1    Hebert, H.2    Thelestam, M.3
  • 55
    • 66649132042 scopus 로고    scopus 로고
    • The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism
    • 19421192 1:CAS:528:DC%2BD1MXlsVKksb4%3D 10.1038/nature08026
    • Mueller M, Grauschopf U, Maier T, Glockshuber R, Ban N (2009) The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism. Nature 459:726-730
    • (2009) Nature , vol.459 , pp. 726-730
    • Mueller, M.1    Grauschopf, U.2    Maier, T.3    Glockshuber, R.4    Ban, N.5
  • 56
    • 0030741317 scopus 로고    scopus 로고
    • The heptameric prepore of a staphylococcal alpha-hemolysin mutant in lipid bilayers imaged by atomic force microscopy
    • 9235997 1:CAS:528:DyaK2sXkslelurs%3D 10.1021/bi970600j
    • Fang Y, Cheley S, Bayley H, Yang J (1997) The heptameric prepore of a staphylococcal alpha-hemolysin mutant in lipid bilayers imaged by atomic force microscopy. Biochemistry 36:9518-9522
    • (1997) Biochemistry , vol.36 , pp. 9518-9522
    • Fang, Y.1    Cheley, S.2    Bayley, H.3    Yang, J.4
  • 57
    • 0032228375 scopus 로고    scopus 로고
    • Structure-based prediction of the conductance properties of ion channels
    • 10822609 1:CAS:528:DyaK1MXisVajtbc%3D 10.1039/a806771f
    • Smart OS, Coates GM, Sansom MS, Alder GM, Bashford CL (1998) Structure-based prediction of the conductance properties of ion channels. Faraday Discuss 111:185-199
    • (1998) Faraday Discuss , vol.111 , pp. 185-199
    • Smart, O.S.1    Coates, G.M.2    Sansom, M.S.3    Alder, G.M.4    Bashford, C.L.5
  • 58
    • 80054794259 scopus 로고    scopus 로고
    • Crystal structure of the octameric pore of staphylococcal gamma-hemolysin reveals the beta-barrel pore formation mechanism by two components
    • 21969538 1:CAS:528:DC%2BC3MXhsVShtr7O 10.1073/pnas.1110402108
    • Yamashita K, Kawai Y, Tanaka Y, Hirano N, Kaneko J, Tomita N, Ohta M, Kamio Y, Yao M, Tanaka I (2011) Crystal structure of the octameric pore of staphylococcal gamma-hemolysin reveals the beta-barrel pore formation mechanism by two components. Proc Natl Acad Sci USA 108:17314-17319
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 17314-17319
    • Yamashita, K.1    Kawai, Y.2    Tanaka, Y.3    Hirano, N.4    Kaneko, J.5    Tomita, N.6    Ohta, M.7    Kamio, Y.8    Yao, M.9    Tanaka, I.10
  • 59
    • 0036015641 scopus 로고    scopus 로고
    • Protein engineering modulates the transport properties and ion selectivity of the pores formed by staphylococcal gamma-haemolysins in lipid membranes
    • 12068809 1:CAS:528:DC%2BD38XksFGqur0%3D 10.1046/j.1365-2958.2002.02943.x
    • Comai M, Dalla Serra M, Coraiola M, Werner S, Colin DA, Monteil H, Prevost G, Menestrina G (2002) Protein engineering modulates the transport properties and ion selectivity of the pores formed by staphylococcal gamma-haemolysins in lipid membranes. Mol Microbiol 44:1251-1267
    • (2002) Mol Microbiol , vol.44 , pp. 1251-1267
    • Comai, M.1    Dalla Serra, M.2    Coraiola, M.3    Werner, S.4    Colin, D.A.5    Monteil, H.6    Prevost, G.7    Menestrina, G.8
  • 60
    • 0036716731 scopus 로고    scopus 로고
    • Stochastic assembly of two-component staphylococcal gamma-hemolysin into heteroheptameric transmembrane pores with alternate subunit arrangements in ratios of 3:4 and 4:3
    • 12169599 1:CAS:528:DC%2BD38Xmt12gu7o%3D 10.1128/JB.184.17.4747-4756.2002
    • Sugawara-Tomita N, Tomita T, Kamio Y (2002) Stochastic assembly of two-component staphylococcal gamma-hemolysin into heteroheptameric transmembrane pores with alternate subunit arrangements in ratios of 3:4 and 4:3. J Bacteriol 184:4747-4756
    • (2002) J Bacteriol , vol.184 , pp. 4747-4756
    • Sugawara-Tomita, N.1    Tomita, T.2    Kamio, Y.3
  • 61
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
    • 10555145 1:CAS:528:DyaK1MXnt1Gqs70%3D 10.1016/S0092-8674(00)81660-8
    • Shatursky O, Heuck AP, Shepard LA, Rossjohn J, Parker MW, Johnson AE, Tweten RK (1999) The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins. Cell 99:293-299
    • (1999) Cell , vol.99 , pp. 293-299
    • Shatursky, O.1    Heuck, A.P.2    Shepard, L.A.3    Rossjohn, J.4    Parker, M.W.5    Johnson, A.E.6    Tweten, R.K.7
  • 62
    • 0035896507 scopus 로고    scopus 로고
    • Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate
    • 11102453 1:CAS:528:DC%2BD3MXitFKgsbg%3D 10.1074/jbc.M009865200
    • Hotze EM, Wilson-Kubalek EM, Rossjohn J, Parker MW, Johnson AE, Tweten RK (2001) Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate. J Biol Chem 276:8261-8268
    • (2001) J Biol Chem , vol.276 , pp. 8261-8268
    • Hotze, E.M.1    Wilson-Kubalek, E.M.2    Rossjohn, J.3    Parker, M.W.4    Johnson, A.E.5    Tweten, R.K.6
  • 63
    • 4444291857 scopus 로고    scopus 로고
    • Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane
    • 15297878 1:CAS:528:DC%2BD2cXmslWhtb4%3D 10.1038/sj.emboj.7600350
    • Czajkowsky DM, Hotze EM, Shao Z, Tweten RK (2004) Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane. EMBO J 23:3206-3215
    • (2004) EMBO J , vol.23 , pp. 3206-3215
    • Czajkowsky, D.M.1    Hotze, E.M.2    Shao, Z.3    Tweten, R.K.4
  • 64
    • 0025739648 scopus 로고
    • Kinetic aspects of the aggregation of Clostridium perfringens theta- toxin on erythrocyte membranes. A fluorescence energy transfer study
    • 2016307 1:CAS:528:DyaK3MXkt1Cjuro%3D
    • Harris RW, Sims PJ, Tweten RK (1991) Kinetic aspects of the aggregation of Clostridium perfringens theta- toxin on erythrocyte membranes. A fluorescence energy transfer study. J Biol Chem 266:6936-6941
    • (1991) J Biol Chem , vol.266 , pp. 6936-6941
    • Harris, R.W.1    Sims, P.J.2    Tweten, R.K.3
  • 65
    • 0021971199 scopus 로고
    • Mechanism of membrane damage by streptolysin-O
    • 3880730 1:CAS:528:DyaL2MXhtVOrt7w%3D
    • Bhakdi S, Tranum-Jensen J, Sziegoleit A (1985) Mechanism of membrane damage by streptolysin-O. Infect Immun 47:52-60
    • (1985) Infect Immun , vol.47 , pp. 52-60
    • Bhakdi, S.1    Tranum-Jensen, J.2    Sziegoleit, A.3
  • 66
    • 0032536856 scopus 로고    scopus 로고
    • Assembly mechanism of the oligomeric streptolysin O pore: The early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization
    • 9501081 1:CAS:528:DyaK1cXit1Gitrw%3D 10.1093/emboj/17.6.1598
    • Palmer M, Harris R, Freytag C, Kehoe M, Tranum-Jensen J, Bhakdi S (1998) Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization. EMBO J 17:1598-1605
    • (1998) EMBO J , vol.17 , pp. 1598-1605
    • Palmer, M.1    Harris, R.2    Freytag, C.3    Kehoe, M.4    Tranum-Jensen, J.5    Bhakdi, S.6
  • 67
    • 0018331380 scopus 로고
    • Comparison of metridiolysin from the sea anemone with thiol-activated cytolysins from bacteria
    • 33471 1:CAS:528:DyaE1MXhsVKksbY%3D 10.1016/0041-0101(79)90257-5
    • Bernheimer AW, Avigad LS, Kim K (1979) Comparison of metridiolysin from the sea anemone with thiol-activated cytolysins from bacteria. Toxicon 17:69-75
    • (1979) Toxicon , vol.17 , pp. 69-75
    • Bernheimer, A.W.1    Avigad, L.S.2    Kim, K.3
  • 68
    • 0031927661 scopus 로고    scopus 로고
    • Cholesterol-streptolysin O interaction: An em study of wild-type and mutant streptolysin O
    • 9705878 1:CAS:528:DyaK1cXls1aitL8%3D 10.1006/jsbi.1998.3989
    • Harris JR, Adrian M, Bhakdi S, Palmer M (1998) Cholesterol-streptolysin O interaction: an EM study of wild-type and mutant streptolysin O. J Struct Biol 121:343-355
    • (1998) J Struct Biol , vol.121 , pp. 343-355
    • Harris, J.R.1    Adrian, M.2    Bhakdi, S.3    Palmer, M.4
  • 69
    • 78649908803 scopus 로고    scopus 로고
    • Cholesterol microcrystals and cochleate cylinders: Attachment of pyolysin oligomers and domain 4
    • 20682347 1:CAS:528:DC%2BC3cXhsFCqur%2FF 10.1016/j.jsb.2010.07.010
    • Harris JR, Lewis RJ, Baik C, Pokrajac L, Billington SJ, Palmer M (2011) Cholesterol microcrystals and cochleate cylinders: attachment of pyolysin oligomers and domain 4. J Struct Biol 173:38-45
    • (2011) J Struct Biol , vol.173 , pp. 38-45
    • Harris, J.R.1    Lewis, R.J.2    Baik, C.3    Pokrajac, L.4    Billington, S.J.5    Palmer, M.6
  • 70
    • 0022497854 scopus 로고
    • Purification and characterization of a cytolytic pore-forming protein from granules of cloned lymphocytes with natural killer activity
    • 2420467 1:CAS:528:DyaL28XitVGgt7o%3D 10.1016/0092-8674(86)90007-3
    • Young JD, Hengartner H, Podack ER, Cohn ZA (1986) Purification and characterization of a cytolytic pore-forming protein from granules of cloned lymphocytes with natural killer activity. Cell 44:849-859
    • (1986) Cell , vol.44 , pp. 849-859
    • Young, J.D.1    Hengartner, H.2    Podack, E.R.3    Cohn, Z.A.4
  • 71
    • 0020679842 scopus 로고
    • Assembly of two types of tubules with putative cytolytic function by cloned natural killer cells
    • 6835377 1:STN:280:DyaL3s7mslCqug%3D%3D 10.1038/302442a0
    • Podack ER, Dennert G (1983) Assembly of two types of tubules with putative cytolytic function by cloned natural killer cells. Nature 302:442-445
    • (1983) Nature , vol.302 , pp. 442-445
    • Podack, E.R.1    Dennert, G.2
  • 72
    • 0025077187 scopus 로고
    • Perforin-mediated myocardial damage in acute myocarditis
    • 1699101 1:STN:280:DyaK3M%2FhsVeksA%3D%3D 10.1016/0140-6736(90)92486-2
    • Young LH, Joag SV, Zheng LM, Lee CP, Lee YS, Young JD (1990) Perforin-mediated myocardial damage in acute myocarditis. Lancet 336:1019-1021
    • (1990) Lancet , vol.336 , pp. 1019-1021
    • Young, L.H.1    Joag, S.V.2    Zheng, L.M.3    Lee, C.P.4    Lee, Y.S.5    Young, J.D.6
  • 73
    • 0021160732 scopus 로고
    • On the cause and nature of C9-related heterogeneity of terminal complement complexes generated on target erythrocytes through the action of whole serum
    • 6747293 1:CAS:528:DyaL2cXlsV2msro%3D
    • Bhakdi S, Tranum-Jensen J (1984) On the cause and nature of C9-related heterogeneity of terminal complement complexes generated on target erythrocytes through the action of whole serum. J Immunol 133:1453-1463
    • (1984) J Immunol , vol.133 , pp. 1453-1463
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 74
    • 0022624819 scopus 로고
    • C5b-9 assembly: Average binding of one C9 molecule to C5b-8 without poly-C9 formation generates a stable transmembrane pore
    • 3958488 1:CAS:528:DyaL28Xit1eiu7w%3D
    • Bhakdi S, Tranum-Jensen J (1986) C5b-9 assembly: average binding of one C9 molecule to C5b-8 without poly-C9 formation generates a stable transmembrane pore. J Immunol 136:2999-3005
    • (1986) J Immunol , vol.136 , pp. 2999-3005
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 75
    • 0025376488 scopus 로고
    • Comparison of channels formed by poly C9, C5b-8 and the membrane attack complex of complement
    • 1696352 1:CAS:528:DyaK3cXlslSjtLk%3D 10.1016/0161-5890(90)90072-8
    • Zalman LS, Muller-Eberhard HJ (1990) Comparison of channels formed by poly C9, C5b-8 and the membrane attack complex of complement. Mol Immunol 27:533-537
    • (1990) Mol Immunol , vol.27 , pp. 533-537
    • Zalman, L.S.1    Muller-Eberhard, H.J.2
  • 76
    • 47849083269 scopus 로고    scopus 로고
    • Demonstration of a cholesterol-dependent cytolysin in a noninsecticidal Bacillus sphaericus strain and evidence for widespread distribution of the toxin within the species
    • 18616599 1:CAS:528:DC%2BD1cXhtVGqtb7P 10.1111/j.1574-6968.2008.01256.x
    • From C, Granum PE, Hardy SP (2008) Demonstration of a cholesterol-dependent cytolysin in a noninsecticidal Bacillus sphaericus strain and evidence for widespread distribution of the toxin within the species. FEMS Microbiol Lett 286:85-92
    • (2008) FEMS Microbiol Lett , vol.286 , pp. 85-92
    • From, C.1    Granum, P.E.2    Hardy, S.P.3
  • 77
    • 0026695462 scopus 로고
    • Differential sensitivity of pneumolysin-induced channels to gating by divalent cations
    • 1379644 1:CAS:528:DyaK38XkvVGgurc%3D
    • Korchev YE, Bashford CL, Pasternak CA (1992) Differential sensitivity of pneumolysin-induced channels to gating by divalent cations. J Membr Biol 127:195-203
    • (1992) J Membr Biol , vol.127 , pp. 195-203
    • Korchev, Y.E.1    Bashford, C.L.2    Pasternak, C.A.3
  • 78
    • 39749125475 scopus 로고    scopus 로고
    • Pneumolysin generates multiple conductance pores in the membrane of nucleated cells
    • 18261465 1:CAS:528:DC%2BD1cXislahtro%3D 10.1016/j.bbrc.2008.01.151
    • El-Rachkidy RG, Davies NW, Andrew PW (2008) Pneumolysin generates multiple conductance pores in the membrane of nucleated cells. Biochem Biophys Res Commun 368:786-792
    • (2008) Biochem Biophys Res Commun , vol.368 , pp. 786-792
    • El-Rachkidy, R.G.1    Davies, N.W.2    Andrew, P.W.3
  • 79
    • 83655192826 scopus 로고    scopus 로고
    • PH dependence of listeriolysin O aggregation and pore-forming ability
    • 22023160 10.1111/j.1742-4658.2011.08405.x 1:CAS:528: DC%2BC38Xit1SmsQ%3D%3D
    • Bavdek A, Kostanjšek R, Antonini V, Lakey JH, Dalla Serra M, Gilbert RJ, Anderluh G (2011) pH dependence of listeriolysin O aggregation and pore-forming ability. FEBS J 279:126-141
    • (2011) FEBS J , vol.279 , pp. 126-141
    • Bavdek, A.1    Kostanjšek, R.2    Antonini, V.3    Lakey, J.H.4    Dalla Serra, M.5    Gilbert, R.J.6    Anderluh, G.7
  • 80
    • 0023689857 scopus 로고
    • Cell damage by cytolysin. Spontaneous recovery and reversible inhibition by divalent cations
    • 2846697 1:CAS:528:DyaL1MXit1WjsA%3D%3D
    • Bashford CL, Menestrina G, Henkart PA, Pasternak CA (1988) Cell damage by cytolysin. Spontaneous recovery and reversible inhibition by divalent cations. J Immunol 141:3965-3974
    • (1988) J Immunol , vol.141 , pp. 3965-3974
    • Bashford, C.L.1    Menestrina, G.2    Henkart, P.A.3    Pasternak, C.A.4
  • 81
    • 0001041396 scopus 로고
    • Isolation and biochemical and functional characterization of perforin 1 from cytolytic T-cell granules
    • 2417226 1:CAS:528:DyaL28XhtVOmsLs%3D 10.1073/pnas.82.24.8629
    • Podack ER, Young JD, Cohn ZA (1985) Isolation and biochemical and functional characterization of perforin 1 from cytolytic T-cell granules. Proc Natl Acad Sci USA 82:8629-8633
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8629-8633
    • Podack, E.R.1    Young, J.D.2    Cohn, Z.A.3
  • 82
    • 0022570037 scopus 로고
    • Functional channel formation associated with cytotoxic T-cell granules
    • 2417234 1:CAS:528:DyaL28XhtVOksb0%3D 10.1073/pnas.83.1.150
    • Young JD, Nathan CF, Podack ER, Palladino MA, Cohn ZA (1986) Functional channel formation associated with cytotoxic T-cell granules. Proc Natl Acad Sci USA 83:150-154
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 150-154
    • Young, J.D.1    Nathan, C.F.2    Podack, E.R.3    Palladino, M.A.4    Cohn, Z.A.5
  • 83
    • 0022494081 scopus 로고
    • Properties of a purified pore-forming protein (perforin 1) isolated from H-2-restricted cytotoxic T cell granules
    • 2425027 1:CAS:528:DyaL28XksF2gtrY%3D 10.1084/jem.164.1.144
    • Young JD, Podack ER, Cohn ZA (1986) Properties of a purified pore-forming protein (perforin 1) isolated from H-2-restricted cytotoxic T cell granules. J Exp Med 164:144-155
    • (1986) J Exp Med , vol.164 , pp. 144-155
    • Young, J.D.1    Podack, E.R.2    Cohn, Z.A.3
  • 84
    • 34247577498 scopus 로고    scopus 로고
    • Delivering the kiss of death: Progress on understanding how perforin works
    • 17433871 1:CAS:528:DC%2BD2sXlt1agsbw%3D 10.1016/j.coi.2007.04.011
    • Pipkin ME, Lieberman J (2007) Delivering the kiss of death: progress on understanding how perforin works. Curr Opin Immunol 19:301-308
    • (2007) Curr Opin Immunol , vol.19 , pp. 301-308
    • Pipkin, M.E.1    Lieberman, J.2
  • 85
    • 38349110486 scopus 로고    scopus 로고
    • Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles
    • 18202661 1:CAS:528:DC%2BD1cXnt1GisA%3D%3D 10.1038/nature06479
    • Birmingham CL, Canadien V, Kaniuk NA, Steinberg BE, Higgins DE, Brumell JH (2008) Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles. Nature 451:350-354
    • (2008) Nature , vol.451 , pp. 350-354
    • Birmingham, C.L.1    Canadien, V.2    Kaniuk, N.A.3    Steinberg, B.E.4    Higgins, D.E.5    Brumell, J.H.6
  • 86
    • 33645553471 scopus 로고    scopus 로고
    • Membrane perforations inhibit lysosome fusion by altering pH and calcium in Listeria monocytogenes vacuoles
    • 16611227 1:CAS:528:DC%2BD28XkvVWhu74%3D 10.1111/j.1462-5822.2005.00665.x
    • Shaughnessy LM, Hoppe AD, Christensen KA, Swanson JA (2006) Membrane perforations inhibit lysosome fusion by altering pH and calcium in Listeria monocytogenes vacuoles. Cell Microbiol 8:781-792
    • (2006) Cell Microbiol , vol.8 , pp. 781-792
    • Shaughnessy, L.M.1    Hoppe, A.D.2    Christensen, K.A.3    Swanson, J.A.4
  • 87
    • 34447619164 scopus 로고    scopus 로고
    • The multiple mechanisms of Ca2+ signalling by listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenes
    • 17419718 1:CAS:528:DC%2BD2sXptV2it7o%3D 10.1111/j.1462-5822.2007.00932.x
    • Gekara NO, Westphal K, Ma B, Rohde M, Groebe L, Weiss S (2007) The multiple mechanisms of Ca2+ signalling by listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenes. Cell Microbiol 9:2008-2021
    • (2007) Cell Microbiol , vol.9 , pp. 2008-2021
    • Gekara, N.O.1    Westphal, K.2    Ma, B.3    Rohde, M.4    Groebe, L.5    Weiss, S.6
  • 88
    • 0025282764 scopus 로고
    • Pore-forming toxins: Experiments with S. aureus alpha-toxin, C. perfringens theta-toxin and E. coli haemolysin in lipid bilayers, liposomes and intact cells
    • 1697105 1:CAS:528:DyaK3cXksFCjsbg%3D 10.1016/0041-0101(90)90292-F
    • Menestrina G, Bashford CL, Pasternak CA (1990) Pore-forming toxins: experiments with S. aureus alpha-toxin, C. perfringens theta-toxin and E. coli haemolysin in lipid bilayers, liposomes and intact cells. Toxicon 28:477-491
    • (1990) Toxicon , vol.28 , pp. 477-491
    • Menestrina, G.1    Bashford, C.L.2    Pasternak, C.A.3
  • 89
    • 24944494048 scopus 로고    scopus 로고
    • Perforin triggers a plasma membrane-repair response that facilitates CTL induction of apoptosis
    • 16169498 1:CAS:528:DC%2BD2MXhtV2gt73P 10.1016/j.immuni.2005.08.001
    • Keefe D, Shi L, Feske S, Massol R, Navarro F, Kirchhausen T, Lieberman J (2005) Perforin triggers a plasma membrane-repair response that facilitates CTL induction of apoptosis. Immunity 23:249-262
    • (2005) Immunity , vol.23 , pp. 249-262
    • Keefe, D.1    Shi, L.2    Feske, S.3    Massol, R.4    Navarro, F.5    Kirchhausen, T.6    Lieberman, J.7
  • 90
    • 77949887174 scopus 로고    scopus 로고
    • Perforin activates clathrin- and dynamin-dependent endocytosis, which is required for plasma membrane repair and delivery of granzyme B for granzyme-mediated apoptosis
    • 20038786 1:CAS:528:DC%2BC3cXjtV2gtL0%3D 10.1182/blood-2009-10-246116
    • Thiery J, Keefe D, Saffarian S, Martinvalet D, Walch M, Boucrot E, Kirchhausen T, Lieberman J (2010) Perforin activates clathrin- and dynamin-dependent endocytosis, which is required for plasma membrane repair and delivery of granzyme B for granzyme-mediated apoptosis. Blood 115:1582-1593
    • (2010) Blood , vol.115 , pp. 1582-1593
    • Thiery, J.1    Keefe, D.2    Saffarian, S.3    Martinvalet, D.4    Walch, M.5    Boucrot, E.6    Kirchhausen, T.7    Lieberman, J.8
  • 92
    • 0028343363 scopus 로고
    • Molecular basis for cell membrane electroporation
    • 1:CAS:528:DyaK2MXkvFGlsg%3D%3D 10.1111/j.1749-6632.1994.tb30442.x
    • Weaver JC (1994) Molecular basis for cell membrane electroporation. Ann New York Acad Sci 720:141-152
    • (1994) Ann New York Acad Sci , vol.720 , pp. 141-152
    • Weaver, J.C.1
  • 93
    • 4944225045 scopus 로고    scopus 로고
    • Effect of lipids with different spontaneous curvature on the channel activity of colicin E1: Evidence in favor of a toroidal pore
    • 15474038 1:CAS:528:DC%2BD2cXot12ht7o%3D 10.1016/j.febslet.2004.09.016
    • Sobko AA, Kotova EA, Antonenko YN, Zakharov SD, Cramer WA (2004) Effect of lipids with different spontaneous curvature on the channel activity of colicin E1: evidence in favor of a toroidal pore. FEBS Lett 576:205-210
    • (2004) FEBS Lett , vol.576 , pp. 205-210
    • Sobko, A.A.1    Kotova, E.A.2    Antonenko, Y.N.3    Zakharov, S.D.4    Cramer, W.A.5
  • 94
    • 0242664967 scopus 로고    scopus 로고
    • Pore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures
    • 12944411 1:CAS:528:DC%2BD3sXosl2jsr8%3D 10.1074/jbc.M305916200
    • Anderluh G, Dalla Serra M, Viero G, Guella G, Maček P, Menestrina G (2003) Pore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures. J Biol Chem 278:45216-45223
    • (2003) J Biol Chem , vol.278 , pp. 45216-45223
    • Anderluh, G.1    Dalla Serra, M.2    Viero, G.3    Guella, G.4    Maček, P.5    Menestrina, G.6
  • 95
    • 0036435610 scopus 로고    scopus 로고
    • Direct evidence for membrane pore formation by the apoptotic protein Bax
    • 12419316 1:CAS:528:DC%2BD38Xot12ktrk%3D 10.1016/S0006-291X(02)02544-5
    • Epand RF, Martinou JC, Montessuit S, Epand RM, Yip CM (2002) Direct evidence for membrane pore formation by the apoptotic protein Bax. Biochem Biophys Res Commun 298:744-749
    • (2002) Biochem Biophys Res Commun , vol.298 , pp. 744-749
    • Epand, R.F.1    Martinou, J.C.2    Montessuit, S.3    Epand, R.M.4    Yip, C.M.5
  • 96
    • 0035004910 scopus 로고    scopus 로고
    • Effects of lipid composition on membrane permeabilization by sticholysin i and II, two cytolysins of the sea anemone Stichodactyla helianthus
    • 11371451 1:CAS:528:DC%2BD3MXkvFSqsbg%3D 10.1016/S0006-3495(01)76244-3
    • Valcarcel CA, Dalla Serra M, Potrich C, Bernhart I, Tejuca M, Martinez D, Pazos F, Lanio ME, Menestrina G (2001) Effects of lipid composition on membrane permeabilization by sticholysin I and II, two cytolysins of the sea anemone Stichodactyla helianthus. Biophys J 80:2761-2774
    • (2001) Biophys J , vol.80 , pp. 2761-2774
    • Valcarcel, C.A.1    Dalla Serra, M.2    Potrich, C.3    Bernhart, I.4    Tejuca, M.5    Martinez, D.6    Pazos, F.7    Lanio, M.E.8    Menestrina, G.9
  • 97
    • 84885186693 scopus 로고    scopus 로고
    • Pore-forming toxins
    • doi: 10.1002/9780470015902.a0002655.pub2
    • Dalla Serra M, Tejuca Martínez M (2001) Pore-forming toxins. eLS John Wiley & Sons. doi: 10.1002/9780470015902.a0002655.pub2
    • (2001) ELS John Wiley & Sons
    • Dalla Serra M, T.1
  • 100
    • 0035846909 scopus 로고    scopus 로고
    • Cytolysin-mediated translocation (CMT): A functional equivalent of type III secretion in Gram-positive bacteria
    • 11163247 1:CAS:528:DC%2BD3MXis1Oqs7s%3D 10.1016/S0092-8674(01)00198-2
    • Madden JC, Ruiz N, Caparon M (2001) Cytolysin-mediated translocation (CMT): a functional equivalent of type III secretion in Gram-positive bacteria. Cell 104:143-152
    • (2001) Cell , vol.104 , pp. 143-152
    • Madden, J.C.1    Ruiz, N.2    Caparon, M.3
  • 101
    • 77955515984 scopus 로고    scopus 로고
    • Human perforin permeabilizing activity, but not binding to lipid membranes, is affected by pH
    • 20580434 1:CAS:528:DC%2BC3cXhtVajtL3M 10.1016/j.molimm.2010.06.001
    • Praper T, Beseničar MP, Istinič H, Podlesek Z, Metkar SS, Froelich CJ, Anderluh G (2010) Human perforin permeabilizing activity, but not binding to lipid membranes, is affected by pH. Mol Immunol 47:2492-2504
    • (2010) Mol Immunol , vol.47 , pp. 2492-2504
    • Praper, T.1    Beseničar, M.P.2    Istinič, H.3    Podlesek, Z.4    Metkar, S.S.5    Froelich, C.J.6    Anderluh, G.7
  • 103
    • 0032147225 scopus 로고    scopus 로고
    • Entry and trafficking of granzyme B in target cells during granzyme B-perforin-mediated apoptosis
    • 9680374 1:CAS:528:DyaK1cXltVOrtr8%3D
    • Pinkoski MJ, Hobman M, Heibein JA, Tomaselli K, Li F, Seth P, Froelich CJ, Bleackley RC (1998) Entry and trafficking of granzyme B in target cells during granzyme B-perforin-mediated apoptosis. Blood 92:1044-1054
    • (1998) Blood , vol.92 , pp. 1044-1054
    • Pinkoski, M.J.1    Hobman, M.2    Heibein, J.A.3    Tomaselli, K.4    Li, F.5    Seth, P.6    Froelich, C.J.7    Bleackley, R.C.8
  • 104
    • 10544252275 scopus 로고    scopus 로고
    • New paradigm for lymphocyte granule-mediated cytotoxicity. Target cells bind and internalize granzyme B, but an endosomolytic agent is necessary for cytosolic delivery and subsequent apoptosis
    • 8910561 1:CAS:528:DyaK28XntFKlsbc%3D 10.1074/jbc.271.46.29073
    • Froelich CJ, Orth K, Turbov J, Seth P, Gottlieb R, Babior B, Shah GM, Bleackley RC, Dixit VM, Hanna W (1996) New paradigm for lymphocyte granule-mediated cytotoxicity. Target cells bind and internalize granzyme B, but an endosomolytic agent is necessary for cytosolic delivery and subsequent apoptosis. J Biol Chem 271:29073-29079
    • (1996) J Biol Chem , vol.271 , pp. 29073-29079
    • Froelich, C.J.1    Orth, K.2    Turbov, J.3    Seth, P.4    Gottlieb, R.5    Babior, B.6    Shah, G.M.7    Bleackley, R.C.8    Dixit, V.M.9    Hanna, W.10
  • 105
    • 0030892138 scopus 로고    scopus 로고
    • Granzyme B (GraB) autonomously crosses the cell membrane and perforin initiates apoptosis and GraB nuclear localization
    • 9120391 1:CAS:528:DyaK2sXhsFKgtr0%3D 10.1084/jem.185.5.855
    • Shi L, Mai S, Israels S, Browne K, Trapani JA, Greenberg AH (1997) Granzyme B (GraB) autonomously crosses the cell membrane and perforin initiates apoptosis and GraB nuclear localization. J Exp Med 185:855-866
    • (1997) J Exp Med , vol.185 , pp. 855-866
    • Shi, L.1    Mai, S.2    Israels, S.3    Browne, K.4    Trapani, J.A.5    Greenberg, A.H.6
  • 107
    • 82755193801 scopus 로고    scopus 로고
    • Intercellular communication via the endo-lysosomal system: Translocation of granzymes through membrane barriers
    • 21683168 1:CAS:528:DC%2BC3MXhsFOns7rP 10.1016/j.bbapap.2011.05.020
    • Stewart SE, D'Angelo ME, Bird PI (2012) Intercellular communication via the endo-lysosomal system: translocation of granzymes through membrane barriers. Biochim Biophys Acta 1824:59-67
    • (2012) Biochim Biophys Acta , vol.1824 , pp. 59-67
    • Stewart, S.E.1    D'Angelo, M.E.2    Bird, P.I.3
  • 109
    • 62249210955 scopus 로고    scopus 로고
    • Membrane scission by the ESCRT-III complex
    • 19234443 1:CAS:528:DC%2BD1MXitFKltrk%3D 10.1038/nature07836
    • Wollert T, Wunder C, Lippincott-Schwartz J, Hurley JH (2009) Membrane scission by the ESCRT-III complex. Nature 458:172-177
    • (2009) Nature , vol.458 , pp. 172-177
    • Wollert, T.1    Wunder, C.2    Lippincott-Schwartz, J.3    Hurley, J.H.4
  • 110
    • 0035889088 scopus 로고    scopus 로고
    • Generation of high curvature membranes mediated by direct endophilin bilayer interactions
    • 11604418 1:CAS:528:DC%2BD3MXnslGjurw%3D 10.1083/jcb.200107075
    • Farsad K, Ringstad N, Takei K, Floyd SR, Rose K, De CP (2001) Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J Cell Biol 155:193-200
    • (2001) J Cell Biol , vol.155 , pp. 193-200
    • Farsad, K.1    Ringstad, N.2    Takei, K.3    Floyd, S.R.4    Rose, K.5    De, C.P.6
  • 111
    • 0035937196 scopus 로고    scopus 로고
    • Structural analysis of the protein/lipid complexes associated with pore formation by the bacterial toxin pneumolysin
    • 11076935 1:CAS:528:DC%2BD3MXhs1Kmtrk%3D 10.1074/jbc.M005126200
    • Bonev BB, Gilbert RJ, Andrew PW, Byron O, Watts A (2001) Structural analysis of the protein/lipid complexes associated with pore formation by the bacterial toxin pneumolysin. J Biol Chem 276:5714-5719
    • (2001) J Biol Chem , vol.276 , pp. 5714-5719
    • Bonev, B.B.1    Gilbert, R.J.2    Andrew, P.W.3    Byron, O.4    Watts, A.5
  • 112
    • 0037034017 scopus 로고    scopus 로고
    • The pathogenic basis of malaria
    • 11832955 1:CAS:528:DC%2BD38XhsVCjtrk%3D 10.1038/415673a
    • Miller LH, Baruch DI, Marsh K, Doumbo OK (2002) The pathogenic basis of malaria. Nature 415:673-679
    • (2002) Nature , vol.415 , pp. 673-679
    • Miller, L.H.1    Baruch, D.I.2    Marsh, K.3    Doumbo, O.K.4
  • 113
    • 34047233006 scopus 로고    scopus 로고
    • Plasmodium berghei: Plasmodium perforin-like protein 5 is required for mosquito midgut invasion in Anopheles stephensi
    • 17367780 1:CAS:528:DC%2BD2sXmtlWit7w%3D 10.1016/j.exppara.2007.01.015
    • Ecker A, Pinto SB, Baker KW, Kafatos FC, Sinden RE (2007) Plasmodium berghei: plasmodium perforin-like protein 5 is required for mosquito midgut invasion in Anopheles stephensi. Exp Parasitol 116:504-508
    • (2007) Exp Parasitol , vol.116 , pp. 504-508
    • Ecker, A.1    Pinto, S.B.2    Baker, K.W.3    Kafatos, F.C.4    Sinden, R.E.5
  • 114
    • 51649089935 scopus 로고    scopus 로고
    • Reverse genetics screen identifies six proteins important for malaria development in the mosquito
    • 18761621 1:CAS:528:DC%2BD1cXht1amsL%2FO 10.1111/j.1365-2958.2008.06407.x
    • Ecker A, Bushell ES, Tewari R, Sinden RE (2008) Reverse genetics screen identifies six proteins important for malaria development in the mosquito. Mol Microbiol 70:209-220
    • (2008) Mol Microbiol , vol.70 , pp. 209-220
    • Ecker, A.1    Bushell, E.S.2    Tewari, R.3    Sinden, R.E.4
  • 116
    • 41849147939 scopus 로고    scopus 로고
    • Migration of Apicomplexa across biological barriers: The Toxoplasma and Plasmodium rides
    • 18194412 1:CAS:528:DC%2BD1cXlsVSrtLo%3D 10.1111/j.1600-0854.2008.00703.x
    • Tardieux I, Menard R (2008) Migration of Apicomplexa across biological barriers: the Toxoplasma and Plasmodium rides. Traffic 9:627-635
    • (2008) Traffic , vol.9 , pp. 627-635
    • Tardieux, I.1    Menard, R.2
  • 117
    • 22744456850 scopus 로고    scopus 로고
    • Intravital observation of Plasmodium berghei sporozoite infection of the liver
    • 15901208 10.1371/journal.pbio.0030192 1:CAS:528:DC%2BD2MXlsFKrt7c%3D
    • Frevert U, Engelmann S, Zougbede S, Stange J, Ng B, Matuschewski K, Liebes L, Yee H (2005) Intravital observation of Plasmodium berghei sporozoite infection of the liver. PLoS Biol 3:e192
    • (2005) PLoS Biol , vol.3 , pp. 192
    • Frevert, U.1    Engelmann, S.2    Zougbede, S.3    Stange, J.4    Ng, B.5    Matuschewski, K.6    Liebes, L.7    Yee, H.8
  • 118
    • 19344370327 scopus 로고    scopus 로고
    • Cell-passage activity is required for the malarial parasite to cross the liver sinusoidal cell layer
    • 14737184 10.1371/journal.pbio.0020004 1:CAS:528:DC%2BD2cXht1Krt7g%3D
    • Ishino T, Yano K, Chinzei Y, Yuda M (2004) Cell-passage activity is required for the malarial parasite to cross the liver sinusoidal cell layer. PLoS Biol 2:e4
    • (2004) PLoS Biol , vol.2 , pp. 4
    • Ishino, T.1    Yano, K.2    Chinzei, Y.3    Yuda, M.4
  • 119
    • 0036008548 scopus 로고    scopus 로고
    • Invasion of mammalian host cells by Plasmodium sporozoites
    • 11835279 10.1002/bies.10050
    • Mota MM, Rodriguez A (2002) Invasion of mammalian host cells by Plasmodium sporozoites. BioEssays 24:149-156
    • (2002) BioEssays , vol.24 , pp. 149-156
    • Mota, M.M.1    Rodriguez, A.2
  • 121
    • 8744252247 scopus 로고    scopus 로고
    • Essential role of membrane-attack protein in malarial transmission to mosquito host
    • 15520375 1:CAS:528:DC%2BD2cXhtVWks7bN 10.1073/pnas.0406187101
    • Kadota K, Ishino T, Matsuyama T, Chinzei Y, Yuda M (2004) Essential role of membrane-attack protein in malarial transmission to mosquito host. Proc Natl Acad Sci USA 101:16310-16315
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16310-16315
    • Kadota, K.1    Ishino, T.2    Matsuyama, T.3    Chinzei, Y.4    Yuda, M.5
  • 123
    • 33748310515 scopus 로고    scopus 로고
    • Differential gene expression in the ookinete stage of the malaria parasite Plasmodium berghei
    • 16908078 1:CAS:528:DC%2BD28XpsVWls7Y%3D 10.1016/j.molbiopara.2006.07.001
    • Raibaud A, Brahimi K, Roth CW, Brey PT, Faust DM (2006) Differential gene expression in the ookinete stage of the malaria parasite Plasmodium berghei. Mol Biochem Parasitol 150:107-113
    • (2006) Mol Biochem Parasitol , vol.150 , pp. 107-113
    • Raibaud, A.1    Brahimi, K.2    Roth, C.W.3    Brey, P.T.4    Faust, D.M.5
  • 124
    • 58849087549 scopus 로고    scopus 로고
    • Rapid membrane disruption by a perforin-like protein facilitates parasite exit from host cells
    • 19095897 1:CAS:528:DC%2BD1MXntFWktQ%3D%3D 10.1126/science.1165740
    • Kafsack BF, Pena JD, Coppens I, Ravindran S, Boothroyd JC, Carruthers VB (2009) Rapid membrane disruption by a perforin-like protein facilitates parasite exit from host cells. Science 323:530-533
    • (2009) Science , vol.323 , pp. 530-533
    • Kafsack, B.F.1    Pena, J.D.2    Coppens, I.3    Ravindran, S.4    Boothroyd, J.C.5    Carruthers, V.B.6
  • 125
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • 9182756 1:CAS:528:DyaK2sXjs1ejsrs%3D 10.1016/S0092-8674(00)80251-2
    • Rossjohn J, Feil SC, McKinstry WJ, Tweten RK, Parker MW (1997) Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 89:685-692
    • (1997) Cell , vol.89 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 126
    • 0018792428 scopus 로고
    • Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A
    • 537059 1:CAS:528:DyaL3cXjs1yjsQ%3D%3D 10.1016/0022-2836(79)90416-9
    • Stuart DI, Levine M, Muirhead H, Stammers DK (1979) Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A. J Mol Biol 134:109-142
    • (1979) J Mol Biol , vol.134 , pp. 109-142
    • Stuart, D.I.1    Levine, M.2    Muirhead, H.3    Stammers, D.K.4
  • 127
    • 0031084471 scopus 로고    scopus 로고
    • An alternating least squares approach to inferring phylogenies from pairwise distances
    • 11975348 1:STN:280:DC%2BD383js1yqug%3D%3D 10.1093/sysbio/46.1.101
    • Felsenstein J (1997) An alternating least squares approach to inferring phylogenies from pairwise distances. Syst Biol 46:101-111
    • (1997) Syst Biol , vol.46 , pp. 101-111
    • Felsenstein, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.