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Volumn 45, Issue 4, 2016, Pages 365-376

Measuring kinetic drivers of pneumolysin pore structure

Author keywords

Kinetics; MACPF CDC; Membrane structure; Oligomerization; Pore formation; Toroidal pore

Indexed keywords

CHOLESTEROL DEPENDENT CYTOLYSIN; MEMBRANE ATTACK COMPLEX PERFORIN; MEMBRANE PROTEIN; PNEUMOLYSIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; PLY PROTEIN, STREPTOCOCCUS PNEUMONIAE; STREPTOLYSIN;

EID: 84959135639     PISSN: 01757571     EISSN: 14321017     Source Type: Journal    
DOI: 10.1007/s00249-015-1106-x     Document Type: Article
Times cited : (22)

References (72)
  • 1
    • 84858967104 scopus 로고    scopus 로고
    • Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of the Membrane Attack Complex (MAC)
    • COI: 1:CAS:528:DC%2BC38XktlKrsro%3D
    • 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 the 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
  • 4
    • 0035179919 scopus 로고    scopus 로고
    • Synergistic effects of alpha-toxin and perfringolysin O in Clostridium perfringens-mediated gas gangrene
    • COI: 1:CAS:528:DC%2BD3MXos1OntLY%3D
    • Awad MM, Ellemor DM, Boyd RL, Emmins JJ, Rood JI (2001) Synergistic effects of alpha-toxin and perfringolysin O in Clostridium perfringens-mediated gas gangrene. Infect Immun 69:7904–7910
    • (2001) Infect Immun , vol.69 , pp. 7904-7910
    • Awad, M.M.1    Ellemor, D.M.2    Boyd, R.L.3    Emmins, J.J.4    Rood, J.I.5
  • 5
    • 0022881696 scopus 로고
    • Single-channel analysis of the conductance fluctuations induced in lipid bilayer membranes by complement proteins C5b-9
    • COI: 1:CAS:528:DyaL2sXmtlaqug%3D%3D
    • Benz R, Schmid A, Wiedmer T, Sims PJ (1986) Single-channel analysis of the conductance fluctuations induced in lipid bilayer membranes by complement proteins C5b-9. J Membr Biol 94:37–45
    • (1986) J Membr Biol , vol.94 , pp. 37-45
    • Benz, R.1    Schmid, A.2    Wiedmer, T.3    Sims, P.J.4
  • 6
    • 0042755077 scopus 로고
    • Comparative kinetics of hemolysis induced by bacterial and other hemolysins
    • COI: 1:CAS:528:DyaH2sXit1Omsg%3D%3D
    • Bernheimer AW (1947) Comparative kinetics of hemolysis induced by bacterial and other hemolysins. J Gen Physiol 30:337–353
    • (1947) J Gen Physiol , vol.30 , pp. 337-353
    • Bernheimer, A.W.1
  • 8
    • 0021971199 scopus 로고
    • Mechanism of membrane damage by streptolysin-O
    • COI: 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
  • 9
    • 38349110486 scopus 로고    scopus 로고
    • Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles
    • COI: 1:CAS:528:DC%2BD1cXnt1GisA%3D%3D
    • 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
  • 10
    • 37049050492 scopus 로고
    • Lesions in erythrocyte membranes caused by immune haemolysis
    • COI: 1:STN:280:DyaF2c7isFOmtw%3D%3D
    • Borsos T, Dourmashkin RR, Humphrey JH (1964) Lesions in erythrocyte membranes caused by immune haemolysis. Nature 202:251–252
    • (1964) Nature , vol.202 , pp. 251-252
    • Borsos, T.1    Dourmashkin, R.R.2    Humphrey, J.H.3
  • 11
    • 4444291857 scopus 로고    scopus 로고
    • Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane
    • COI: 1:CAS:528:DC%2BD2cXmslWhtb4%3D
    • 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
  • 13
    • 84862605391 scopus 로고    scopus 로고
    • Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins
    • COI: 1:CAS:528:DC%2BC38XotVaqu78%3D
    • 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 Op Struct Biol 22:342–349
    • (2012) Curr Op Struct Biol , vol.22 , pp. 342-349
    • Dunstone, M.A.1    Tweten, R.K.2
  • 14
    • 85047680317 scopus 로고
    • Effects of purified perforin and granzyme A from cytotoxic T lymphocytes on guinea pig ventricular myocytes
    • COI: 1:CAS:528:DyaK2cXlslOltro%3D
    • Felzen B, Berke G, Rosen D, Coleman R, Tschopp J, Young JD, Binah O (1994) Effects of purified perforin and granzyme A from cytotoxic T lymphocytes on guinea pig ventricular myocytes. Cardiovascular Res 28:643–649
    • (1994) Cardiovascular Res , vol.28 , pp. 643-649
    • Felzen, B.1    Berke, G.2    Rosen, D.3    Coleman, R.4    Tschopp, J.5    Young, J.D.6    Binah, O.7
  • 15
    • 84877768546 scopus 로고    scopus 로고
    • Calcium-dependent permeabilization of erythrocytes by a perforin-like protein during egress of malaria parasites
    • Garg S, Agarwal S, Kumar S, Yazdani SS, Chitnis CE, Singh S (2013) Calcium-dependent permeabilization of erythrocytes by a perforin-like protein during egress of malaria parasites. Nat Commun 4:1736
    • (2013) Nat Commun , vol.4 , pp. 1736
    • Garg, S.1    Agarwal, S.2    Kumar, S.3    Yazdani, S.S.4    Chitnis, C.E.5    Singh, S.6
  • 16
    • 16544370492 scopus 로고    scopus 로고
    • Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin
    • COI: 1:CAS:528:DC%2BD2cXhtVens7jP
    • 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
  • 17
    • 0036285870 scopus 로고    scopus 로고
    • Pore-forming toxins
    • COI: 1:CAS:528:DC%2BD38XlvFequ7s%3D
    • Gilbert RJ (2002) Pore-forming toxins. Cell Mol Life Sci 59:832–844
    • (2002) Cell Mol Life Sci , vol.59 , pp. 832-844
    • Gilbert, R.J.1
  • 18
    • 23444457403 scopus 로고    scopus 로고
    • Inactivation and activity of cholesterol-dependent cytolysins: what structural studies tell us
    • COI: 1:CAS:528:DC%2BD2MXntVOiu7s%3D
    • 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
  • 19
    • 77955973704 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins
    • COI: 1:CAS:528:DC%2BC3cXhs1WrsrvE
    • Gilbert RJ (2010) Cholesterol-dependent cytolysins. Adv Exp Med Biol 677:56–66
    • (2010) Adv Exp Med Biol , vol.677 , pp. 56-66
    • Gilbert, R.J.1
  • 20
    • 84901015540 scopus 로고    scopus 로고
    • Structural features of cholesterol dependent cytolysins and comparison to other MACPF-domain containing proteins
    • Anderluh G, Gilbert RJC, (eds), Springer, Dordrecht/NL
    • Gilbert RJC (2014) Structural features of cholesterol dependent cytolysins and comparison to other MACPF-domain containing proteins. In: Anderluh G, Gilbert RJC (eds) MACPF/CDC proteins—agents of defence, attack and invasion. Springer, Dordrecht/NL
    • (2014) MACPF/CDC proteins—agents of defence, attack and invasion
    • Gilbert, R.J.C.1
  • 22
    • 84956589172 scopus 로고    scopus 로고
    • Protein-lipid interactions and non-lamellar lipidic structures in membrane pore formation and membrane fusion
    • COI: 1:CAS:528:DC%2BC2MXhvFKisrjJ
    • Gilbert RJC (2016) Protein-lipid interactions and non-lamellar lipidic structures in membrane pore formation and membrane fusion. Biochimica Biophys Acta 1858:487–499
    • (2016) Biochimica Biophys Acta , vol.1858 , pp. 487-499
    • Gilbert, R.J.C.1
  • 25
    • 0033612389 scopus 로고    scopus 로고
    • Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae
    • COI: 1:CAS:528:DyaK1MXjs1yqtbc%3D
    • Gilbert RJ, Jimenez JL, Chen S, Tickle IJ, Rossjohn J, Parker M, Andrew PW, Saibil HR (1999b) 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
  • 28
    • 34548670476 scopus 로고    scopus 로고
    • Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense
    • COI: 1:CAS:528:DC%2BD2sXhtVejt7%2FN
    • 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
  • 29
    • 0025739648 scopus 로고
    • Kinetic aspects of the aggregation of Clostridium perfringens theta-toxin on erythrocyte membranes. A fluorescence energy transfer study
    • COI: 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
  • 30
    • 0033636662 scopus 로고    scopus 로고
    • Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes
    • COI: 1:CAS:528:DC%2BD3cXosV2mt7g%3D
    • Heuck AP, Hotze EM, Tweten RK, Johnson AE (2000) Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes. Mol Cell 6:1233–1242
    • (2000) Mol Cell , vol.6 , pp. 1233-1242
    • Heuck, A.P.1    Hotze, E.M.2    Tweten, R.K.3    Johnson, A.E.4
  • 32
    • 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
    • COI: 1:CAS:528:DC%2BD3MXitFKgsbg%3D
    • 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
  • 33
    • 0037192791 scopus 로고    scopus 로고
    • Monomer-monomer interactions drive the prepore to pore conversion of a beta-barrel-forming cholesterol-dependent cytolysin
    • COI: 1:CAS:528:DC%2BD38Xis1Kgt7g%3D
    • Hotze EM, Heuck AP, Czajkowsky DM, Shao Z, Johnson AE, Tweten RK (2002) Monomer-monomer interactions drive the prepore to pore conversion of a beta-barrel-forming cholesterol-dependent cytolysin. J Biol Chem 277:11597–11605
    • (2002) J Biol Chem , vol.277 , pp. 11597-11605
    • Hotze, E.M.1    Heuck, A.P.2    Czajkowsky, D.M.3    Shao, Z.4    Johnson, A.E.5    Tweten, R.K.6
  • 34
    • 0032007852 scopus 로고    scopus 로고
    • A conserved tryptophan in pneumolysin is a determinant of the characteristics of channels formed by pneumolysin in cells and planar lipid bilayers
    • COI: 1:CAS:528:DyaK1cXht1arsrY%3D
    • Korchev YE, Bashford CL, Pederzolli C, Pasternak CA, Morgan PJ, Andrew PW, Mitchell TJ (1998) A conserved tryptophan in pneumolysin is a determinant of the characteristics of channels formed by pneumolysin in cells and planar lipid bilayers. Biochem J 329:571–577
    • (1998) Biochem J , vol.329 , pp. 571-577
    • Korchev, Y.E.1    Bashford, C.L.2    Pederzolli, C.3    Pasternak, C.A.4    Morgan, P.J.5    Andrew, P.W.6    Mitchell, T.J.7
  • 36
    • 84876174174 scopus 로고    scopus 로고
    • Perforin forms transient pores on the target cell plasma membrane to facilitate rapid access of granzymes during killer cell attack
    • COI: 1:CAS:528:DC%2BC3sXlvVOjs78%3D
    • Lopez JA, Susanto O, Jenkins MR, Lukoyanova N, Sutton VR, Law RH, Johnston A, Bird CH, Bird PI, Whisstock JC et al (2013) Perforin forms transient pores on the target cell plasma membrane to facilitate rapid access of granzymes during killer cell attack. Blood 121:2659–2668
    • (2013) Blood , vol.121 , pp. 2659-2668
    • Lopez, J.A.1    Susanto, O.2    Jenkins, M.R.3    Lukoyanova, N.4    Sutton, V.R.5    Law, R.H.6    Johnston, A.7    Bird, C.H.8    Bird, P.I.9    Whisstock, J.C.10
  • 37
    • 38749123992 scopus 로고    scopus 로고
    • Friend or foe: the same fold for attack and defense
    • COI: 1:CAS:528:DC%2BD1cXhslGit7c%3D
    • 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
  • 39
    • 84885188901 scopus 로고    scopus 로고
    • What planar lipid membranes tell us about the pore-forming activity of cholesterol-dependent cytolysins
    • COI: 1:CAS:528:DC%2BC3sXhtFCktbrE
    • Marchioretto M, Podobnik M, Dalla Serra M, Anderluh G (2013) What planar lipid membranes tell us about the pore-forming activity of cholesterol-dependent cytolysins. Biophys Chem 182:64–70
    • (2013) Biophys Chem , vol.182 , pp. 64-70
    • Marchioretto, M.1    Podobnik, M.2    Dalla Serra, M.3    Anderluh, G.4
  • 40
    • 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
    • COI: 1:CAS:528:DyaK3cXksFCjsbg%3D
    • 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
  • 43
    • 0028062876 scopus 로고
    • Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form
    • COI: 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
  • 44
    • 84944382016 scopus 로고    scopus 로고
    • Directly observing the lipid-dependent self-assembly and pore-forming mechanism of the cytolytic toxin listeriolysin O
    • Mulvihill E, van Pee K, Mari SA, Muller DJ, Yildiz O (2015) Directly observing the lipid-dependent self-assembly and pore-forming mechanism of the cytolytic toxin listeriolysin O. Nano Lett 15:6965–6973
    • (2015) Nano Lett , vol.15 , pp. 6965-6973
    • Mulvihill, E.1    van Pee, K.2    Mari, S.A.3    Muller, D.J.4    Yildiz, O.5
  • 45
    • 2142825136 scopus 로고    scopus 로고
    • The role of cholesterol in the activity of pneumolysin, a bacterial protein toxin
    • Nollmann M, Gilbert R, Mitchell T, Sferrazza M, Byron O (2004) The role of cholesterol in the activity of pneumolysin, a bacterial protein toxin. Biophys J 86:3141–3151
    • (2004) Biophys J , vol.86 , pp. 3141-3151
    • Nollmann, M.1    Gilbert, R.2    Mitchell, T.3    Sferrazza, M.4    Byron, O.5
  • 46
    • 0015195762 scopus 로고
    • Characteristics of streptolysin O action
    • COI: 1:CAS:528:DyaE38XmvV2nsw%3D%3D
    • Oberley TD, Duncan JL (1971) Characteristics of streptolysin O action. Infect Immun 4:683–687
    • (1971) Infect Immun , vol.4 , pp. 683-687
    • Oberley, T.D.1    Duncan, J.L.2
  • 47
    • 0023783454 scopus 로고
    • Protease-nicked theta-toxin of Clostridium perfringens, a new membrane probe with no cytolytic effect, reveals two classes of cholesterol as toxin-binding sites on sheep erythrocytes
    • COI: 1:CAS:528:DyaL1cXlsVCgsb8%3D
    • Ohno-Iwashita Y, Iwamoto M, Mitsui K, Ando S, Nagai Y (1988) Protease-nicked theta-toxin of Clostridium perfringens, a new membrane probe with no cytolytic effect, reveals two classes of cholesterol as toxin-binding sites on sheep erythrocytes. Eur J Biochem 176:95–101
    • (1988) Eur J Biochem , vol.176 , pp. 95-101
    • Ohno-Iwashita, Y.1    Iwamoto, M.2    Mitsui, K.3    Ando, S.4    Nagai, Y.5
  • 48
    • 84883238674 scopus 로고    scopus 로고
    • Membrane cholesterol and sphingomyelin, and ostreolysin A are obligatory for pore-formation by a MACPF/CDC-like pore-forming protein, pleurotolysin B
    • COI: 1:CAS:528:DC%2BC3sXhtVOrsL7K
    • Ota K, Leonardi A, Mikelj M, Skocaj M, Wohlschlager T, Kunzler M, Aebi M, Narat M, Krizaj I, Anderluh G et al (2013) Membrane cholesterol and sphingomyelin, and ostreolysin A are obligatory for pore-formation by a MACPF/CDC-like pore-forming protein, pleurotolysin B. Biochimie 95:1855–1864
    • (2013) Biochimie , vol.95 , pp. 1855-1864
    • Ota, K.1    Leonardi, A.2    Mikelj, M.3    Skocaj, M.4    Wohlschlager, T.5    Kunzler, M.6    Aebi, M.7    Narat, M.8    Krizaj, I.9    Anderluh, G.10
  • 49
    • 0029032460 scopus 로고
    • Kinetics of streptolysin O self-assembly
    • COI: 1:CAS:528:DyaK2MXmvFOgt78%3D
    • Palmer M, Valeva A, Kehoe M, Bhakdi S (1995) Kinetics of streptolysin O self-assembly. Eur J Biochem/FEBS 231:388–395
    • (1995) Eur J Biochem/FEBS , vol.231 , pp. 388-395
    • Palmer, M.1    Valeva, A.2    Kehoe, M.3    Bhakdi, S.4
  • 50
    • 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
    • COI: 1:CAS:528:DyaK1cXit1Gitrw%3D
    • 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
  • 51
    • 0020679842 scopus 로고
    • Assembly of two types of tubules with putative cytolytic function by cloned natural killer cells
    • COI: 1:STN:280:DyaL3s7mslCqug%3D%3D
    • 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
  • 54
    • 84923269229 scopus 로고    scopus 로고
    • A new model for pore formation by cholesterol-dependent cytolysins
    • Reboul CF, Whisstock JC, Dunstone MA (2014) A new model for pore formation by cholesterol-dependent cytolysins. PLoS Comput Biol 10:e1003791
    • (2014) PLoS Comput Biol , vol.10 , pp. e1003791
    • Reboul, C.F.1    Whisstock, J.C.2    Dunstone, M.A.3
  • 55
    • 84956796258 scopus 로고    scopus 로고
    • Giant MACPF/CDC pore forming toxins: a class of their own
    • COI: 1:CAS:528:DC%2BC2MXhvVykurbP
    • Reboul CF, Whisstock J, Dunstone MA (2016) Giant MACPF/CDC pore forming toxins: a class of their own. Biochim Biophys Acta 1858:475–486
    • (2016) Biochim Biophys Acta , vol.1858 , pp. 475-486
    • Reboul, C.F.1    Whisstock, J.2    Dunstone, M.A.3
  • 57
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins
    • COI: 1:CAS:528:DyaK1MXnt1Gqs70%3D
    • 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
  • 58
    • 0032514655 scopus 로고    scopus 로고
    • Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: an alpha-helical to beta-sheet transition identified by fluorescence spectroscopy
    • COI: 1:CAS:528:DyaK1cXmtFaktLg%3D
    • Shepard LA, Heuck AP, Hamman BD, Rossjohn J, Parker MW, Ryan KR, Johnson AE, Tweten RK (1998) Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: an alpha-helical to beta-sheet transition identified by fluorescence spectroscopy. Biochemistry 37:14563–14574
    • (1998) Biochemistry , vol.37 , pp. 14563-14574
    • Shepard, L.A.1    Heuck, A.P.2    Hamman, B.D.3    Rossjohn, J.4    Parker, M.W.5    Ryan, K.R.6    Johnson, A.E.7    Tweten, R.K.8
  • 59
    • 3042855150 scopus 로고    scopus 로고
    • The solution structure and oligomerization behavior of two bacterial toxins: pneumolysin and perfringolysin O
    • COI: 1:CAS:528:DC%2BD2cXmtVelsLw%3D
    • Solovyova AS, Nollmann M, Mitchell TJ, Byron O (2004) The solution structure and oligomerization behavior of two bacterial toxins: pneumolysin and perfringolysin O. Biophys J 87:540–552
    • (2004) Biophys J , vol.87 , pp. 540-552
    • Solovyova, A.S.1    Nollmann, M.2    Mitchell, T.J.3    Byron, O.4
  • 60
    • 84906317003 scopus 로고    scopus 로고
    • Structural biology of the membrane attack complex
    • COI: 1:CAS:528:DC%2BC2MXovFaqtLk%3D
    • Sonnen AF, Henneke P (2014) Structural biology of the membrane attack complex. Sub Cell Biochem 80:83–116
    • (2014) Sub Cell Biochem , vol.80 , pp. 83-116
    • Sonnen, A.F.1    Henneke, P.2
  • 61
    • 84901044466 scopus 로고    scopus 로고
    • Incomplete pneumolysin oligomers form membrane pores
    • Sonnen AF, Plitzko J, Gilbert RJC (2014) Incomplete pneumolysin oligomers form membrane pores. R Soc Open Biol 4:140044
    • (2014) R Soc Open Biol , vol.4 , pp. 140044
    • Sonnen, A.F.1    Plitzko, J.2    Gilbert, R.J.C.3
  • 62
    • 84908200578 scopus 로고    scopus 로고
    • Assembly of streptolysin O pores assessed by quartz crystal microbalance and atomic force microscopy provides evidence for the formation of anchored but incomplete oligomers
    • COI: 1:CAS:528:DC%2BC2cXhslOkt77E
    • Stewart SE, D’Angelo ME, Paintavigna S, Tabor RF, Martin LL, Bird PI (2015) Assembly of streptolysin O pores assessed by quartz crystal microbalance and atomic force microscopy provides evidence for the formation of anchored but incomplete oligomers. Biochim Biophys Acta 1848:115–126
    • (2015) Biochim Biophys Acta , vol.1848 , pp. 115-126
    • Stewart, S.E.1    D’Angelo, M.E.2    Paintavigna, S.3    Tabor, R.F.4    Martin, L.L.5    Bird, P.I.6
  • 63
    • 17444405610 scopus 로고    scopus 로고
    • Structural basis of pore formation by the bacterial toxin pneumolysin
    • COI: 1:CAS:528:DC%2BD2MXjvV2jtb0%3D
    • 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
  • 64
    • 0021264462 scopus 로고
    • Ultrastructure of the membrane attack complex of complement. Heterogeneity of the complex caused by different degree of C9 polymerization
    • COI: 1:CAS:528:DyaL2cXksFejtL4%3D
    • Tschopp J (1984) Ultrastructure of the membrane attack complex of complement. Heterogeneity of the complex caused by different degree of C9 polymerization. J Biol Chem 259:7857–7863
    • (1984) J Biol Chem , vol.259 , pp. 7857-7863
    • Tschopp, J.1
  • 65
    • 25444452398 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins
    • COI: 1:CAS:528:DC%2BD2MXhtVyhur3M
    • Tweten RK (2005) Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins. Infect Immun 73:6199–6209
    • (2005) Infect Immun , vol.73 , pp. 6199-6209
    • Tweten, R.K.1
  • 66
    • 84945276222 scopus 로고    scopus 로고
    • The unique molecular choreography of giant pore formation by the cholesterol-dependent cytolysins of gram-positive bacteria
    • COI: 1:CAS:528:DC%2BC2MXhslSru7vF
    • Tweten RK, Hotze EM, Wade KR (2015) The unique molecular choreography of giant pore formation by the cholesterol-dependent cytolysins of gram-positive bacteria. Annu Rev Microbiol 69:323–340
    • (2015) Annu Rev Microbiol , vol.69 , pp. 323-340
    • Tweten, R.K.1    Hotze, E.M.2    Wade, K.R.3
  • 67
    • 33845199637 scopus 로고    scopus 로고
    • Perforin-mediated target-cell death and immune homeostasis
    • COI: 1:CAS:528:DC%2BD28Xht1Clsr7F
    • 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
  • 68
    • 0028343363 scopus 로고
    • Molecular basis for cell membrane electroporation
    • COI: 1:CAS:528:DyaK2MXkvFGlsg%3D%3D
    • Weaver JC (1994) Molecular basis for cell membrane electroporation. Ann N Y Acad Sci 720:141–152
    • (1994) Ann N Y Acad Sci , vol.720 , pp. 141-152
    • Weaver, J.C.1
  • 69
    • 0022497854 scopus 로고
    • Purification and characterization of a cytolytic pore-forming protein from granules of cloned lymphocytes with natural killer activity
    • COI: 1:CAS:528:DyaL28XitVGgt7o%3D
    • Young JD, Hengartner H, Podack ER, Cohn ZA (1986a) 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
    • 0022494081 scopus 로고
    • Properties of a purified pore-forming protein (perforin 1) isolated from H-2-restricted cytotoxic T cell granules
    • COI: 1:CAS:528:DyaL28XksF2gtrY%3D
    • Young JD, Podack ER, Cohn ZA (1986c) 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
  • 72
    • 0025077187 scopus 로고
    • Perforin-mediated myocardial damage in acute myocarditis
    • COI: 1:STN:280:DyaK3M%2FhsVeksA%3D%3D
    • 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


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