메뉴 건너뛰기




Volumn 6, Issue , 2017, Pages

CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin

Author keywords

[No Author keywords available]

Indexed keywords

LIPOSOME; PNEUMOLYSIN; BACTERIAL PROTEIN; PLY PROTEIN, STREPTOCOCCUS PNEUMONIAE; STREPTOLYSIN;

EID: 85019237271     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.23644     Document Type: Article
Times cited : (115)

References (57)
  • 1
    • 84858967104 scopus 로고    scopus 로고
    • Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC)
    • PMID: 22267737
    • 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). Journal of Biological Chemistry 287:10210–10222. doi: 10.1074/jbc.M111.327809, PMID: 22267737
    • (2012) Journal of Biological Chemistry , 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
  • 2
    • 84927628815 scopus 로고    scopus 로고
    • Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase
    • PMID: 25707805
    • Allegretti M, Klusch N, Mills DJ, Vonck J, Kühlbrandt W, Davies KM. 2015. Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase. Nature 521:237–240. doi: 10.1038/nature14185, PMID: 25707805
    • (2015) Nature , vol.521 , pp. 237-240
    • Allegretti, M.1    Klusch, N.2    Mills, D.J.3    Vonck, J.4    Kühlbrandt, W.5    Davies, K.M.6
  • 3
    • 84898761737 scopus 로고    scopus 로고
    • Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector
    • PMID: 24569482
    • Allegretti M, Mills DJ, McMullan G, Kühlbrandt W, Vonck J. 2014. Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector. eLife 3:e01963. doi: 10.7554/eLife.01963, PMID: 24569482
    • (2014) Elife , vol.3
    • Allegretti, M.1    Mills, D.J.2    McMullan, G.3    Kühlbrandt, W.4    Vonck, J.5
  • 4
    • 81255210901 scopus 로고    scopus 로고
    • Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1
    • PMID: 21909073
    • Althoff T, Mills DJ, Popot JL, Kühlbrandt W. 2011. Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1. The EMBO Journal 30:4652–4664. doi: 10.1038/emboj.2011.324, PMID: 21909073
    • (2011) The EMBO Journal , vol.30 , pp. 4652-4664
    • Althoff, T.1    Mills, D.J.2    Popot, J.L.3    Kühlbrandt, W.4
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4, PMID: 15299374
    • Collaborative Computational Project, Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallographica. Section D, Biological Crystallography 50:760–763. doi: 10.1107/S0907444994003112, PMID: 15299374
    • (1994) Acta Crystallographica. Section D, Biological Crystallography , vol.50 , pp. 760-763
  • 6
    • 4444291857 scopus 로고    scopus 로고
    • Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane
    • PMID: 15297878
    • Czajkowsky DM, Hotze EM, Shao Z, Tweten RK. 2004. Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane. The EMBO Journal 23:3206–3215. doi: 10.1038/sj.emboj.7600350, PMID: 15297878
    • (2004) The EMBO Journal , vol.23 , pp. 3206-3215
    • Czajkowsky, D.M.1    Hotze, E.M.2    Shao, Z.3    Tweten, R.K.4
  • 7
    • 15444378399 scopus 로고    scopus 로고
    • Prepore to pore transition of a cholesterol-dependent cytolysin visualized by electron microscopy
    • PMID: 15797734
    • Dang TX, Hotze EM, Rouiller I, Tweten RK, Wilson-Kubalek EM. 2005. Prepore to pore transition of a cholesterol-dependent cytolysin visualized by electron microscopy. Journal of Structural Biology 150:100–108. doi: 10.1016/j.jsb.2005.02.003, PMID: 15797734
    • (2005) Journal of Structural Biology , vol.150 , pp. 100-108
    • Dang, T.X.1    Hotze, E.M.2    Rouiller, I.3    Tweten, R.K.4    Wilson-Kubalek, E.M.5
  • 8
    • 0028895031 scopus 로고
    • Hyperexpression of listeriolysin in the nonpathogenic species Listeria innocua and high yield purification
    • PMID: 8590646
    • Darji A, Chakraborty T, Niebuhr K, Tsonis N, Wehland J, Weiss S. 1995. Hyperexpression of listeriolysin in the nonpathogenic species Listeria innocua and high yield purification. Journal of Biotechnology 43:205–212. doi: 10.1016/0168-1656(95)00138-7, PMID: 8590646
    • (1995) Journal of Biotechnology , vol.43 , pp. 205-212
    • Darji, A.1    Chakraborty, T.2    Niebuhr, K.3    Tsonis, N.4    Wehland, J.5    Weiss, S.6
  • 12
    • 77749292162 scopus 로고    scopus 로고
    • Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface
    • PMID: 20145114
    • 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. PNAS 107:4341–4346. doi: 10.1073/pnas.0911581107, PMID: 20145114
    • (2010) PNAS , vol.107 , pp. 4341-4346
    • Farrand, A.J.1    Lachapelle, S.2    Hotze, E.M.3    Johnson, A.E.4    Tweten, R.K.5
  • 13
    • 0035783287 scopus 로고    scopus 로고
    • Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion
    • PMID: 11722164
    • Frangakis AS, Hegerl R. 2001. Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion. Journal of Structural Biology 135:239–250. doi: 10.1006/jsbi.2001.4406, PMID: 11722164
    • (2001) Journal of Structural Biology , vol.135 , pp. 239-250
    • Frangakis, A.S.1    Hegerl, R.2
  • 14
    • 23444457403 scopus 로고    scopus 로고
    • Inactivation and activity of cholesterol-dependent cytolysins: What structural studies tell us
    • PMID: 16084382
    • Gilbert RJ. 2005. Inactivation and activity of cholesterol-dependent cytolysins: what structural studies tell us. Structure 13:1097–1106. doi: 10.1016/j.str.2005.04.019, PMID: 16084382
    • (2005) Structure , vol.13 , pp. 1097-1106
    • Gilbert, R.J.1
  • 15
    • 84930634509 scopus 로고    scopus 로고
    • Measuring the optimal exposure for single particle cryo-EM using a 2.6 å reconstruction of rotavirus VP6
    • PMID: 26023829
    • Grant T, Grigorieff N. 2015. Measuring the optimal exposure for single particle cryo-EM using a 2.6 å reconstruction of rotavirus VP6. eLife 4:e06980. doi: 10.7554/eLife.06980, PMID: 26023829
    • (2015) Elife , vol.4
    • Grant, T.1    Grigorieff, N.2
  • 16
    • 84989815878 scopus 로고    scopus 로고
    • The architecture of the mammalian respirasome
    • PMID: 27654917
    • Gu J, Wu M, Guo R, Yan K, Lei J, Gao N, Yang M. 2016. The architecture of the mammalian respirasome. Nature 537:639–643. doi: 10.1038/nature19359, PMID: 27654917
    • (2016) Nature , vol.537 , pp. 639-643
    • Gu, J.1    Wu, M.2    Guo, R.3    Yan, K.4    Lei, J.5    Gao, N.6    Yang, M.7
  • 17
    • 84978484141 scopus 로고    scopus 로고
    • Structure of a complete ATP synthase dimer reveals the molecular basis of inner mitochondrial membrane morphology
    • PMID: 27373333
    • Hahn A, Parey K, Bublitz M, Mills DJ, Zickermann V, Vonck J, Kühlbrandt W, Meier T. 2016. Structure of a complete ATP synthase dimer reveals the molecular basis of inner mitochondrial membrane morphology. Molecular Cell 63:445–456. doi: 10.1016/j.molcel.2016.05.037, PMID: 27373333
    • (2016) Molecular Cell , vol.63 , pp. 445-456
    • Hahn, A.1    Parey, K.2    Bublitz, M.3    Mills, D.J.4    Zickermann, V.5    Vonck, J.6    Kühlbrandt, W.7    Meier, T.8
  • 18
    • 78649908803 scopus 로고    scopus 로고
    • Cholesterol microcrystals and cochleate cylinders: Attachment of pyolysin oligomers and domain 4
    • PMID: 20682347
    • 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. Journal of Structural Biology 173:38–45. doi: 10.1016/j.jsb.2010.07.010, PMID: 20682347
    • (2011) Journal of Structural Biology , 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
  • 19
    • 84857650341 scopus 로고    scopus 로고
    • Membrane assembly of the cholesterol-dependent cytolysin pore complex
    • PMID: 21835159
    • Hotze EM, Tweten RK. 2012. Membrane assembly of the cholesterol-dependent cytolysin pore complex. Biochimica Et Biophysica Acta (BBA)-Biomembranes 1818:1028–1038. doi: 10.1016/j.bbamem.2011.07.036, PMID: 21835159
    • (2012) Biochimica Et Biophysica Acta (Bba)-Biomembranes , vol.1818 , pp. 1028-1038
    • Hotze, E.M.1    Tweten, R.K.2
  • 20
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. 1993. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. Journal of Applied Crystallography 26:795–800. doi: 10.1107/S0021889893005588
    • (1993) Journal of Applied Crystallography , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 21
    • 85015864190 scopus 로고    scopus 로고
    • Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2
    • PMID: 27845625
    • Kimanius D, Forsberg BO, Scheres SH, Lindahl E. 2016. Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2. eLife 5:e18722. doi: 10.7554/eLife.18722, PMID: 27845625
    • (2016) Elife , vol.5
    • Kimanius, D.1    Forsberg, B.O.2    Scheres, S.H.3    Lindahl, E.4
  • 22
    • 29644447798 scopus 로고    scopus 로고
    • Construction and immunological characterization of a novel nontoxic protective pneumolysin mutant for use in future pneumococcal vaccines
    • PMID: 1636 9015
    • Kirkham LA, Kerr AR, Douce GR, Paterson GK, Dilts DA, Liu DF, Mitchell TJ. 2006. Construction and immunological characterization of a novel nontoxic protective pneumolysin mutant for use in future pneumococcal vaccines. Infection and Immunity 74:586–593. doi: 10.1128/IAI.74.1.586-593.2006, PMID: 1636 9015
    • (2006) Infection and Immunity , vol.74 , pp. 586-593
    • Kirkham, L.A.1    Kerr, A.R.2    Douce, G.R.3    Paterson, G.K.4    Dilts, D.A.5    Liu, D.F.6    Mitchell, T.J.7
  • 23
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • PMID: 8742726
    • Kremer JR, Mastronarde DN, McIntosh JR. 1996. Computer visualization of three-dimensional image data using IMOD. Journal of Structural Biology 116:71–76. doi: 10.1006/jsbi.1996.0013, PMID: 8742726
    • (1996) Journal of Structural Biology , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 25
    • 84897000286 scopus 로고    scopus 로고
    • Biochemistry. The resolution revolution
    • PMID: 24675944
    • Kühlbrandt W. 2014. Biochemistry. The resolution revolution. Science 343:1443–1444. doi: 10.1126/science.1251652, PMID: 24675944
    • (2014) Science , vol.343 , pp. 1443-1444
    • Kühlbrandt, W.1
  • 27
    • 84989935276 scopus 로고    scopus 로고
    • The architecture of respiratory supercomplexes
    • PMID: 27654913
    • Letts JA, Fiedorczuk K, Sazanov LA. 2016. The architecture of respiratory supercomplexes. Nature 537:644–648. doi: 10.1038/nature19774, PMID: 27654913
    • (2016) Nature , vol.537 , pp. 644-648
    • Letts, J.A.1    Fiedorczuk, K.2    Sazanov, L.A.3
  • 29
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • PMID: 23644547
    • Li X, Mooney P, Zheng S, Booth CR, Braunfeld MB, Gubbens S, Agard DA, Cheng Y. 2013. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nature Methods 10:584–590. doi: 10.1038/nmeth.2472, PMID: 23644547
    • (2013) Nature Methods , vol.10 , pp. 584-590
    • Li, X.1    Mooney, P.2    Zheng, S.3    Booth, C.R.4    Braunfeld, M.B.5    Gubbens, S.6    Agard, D.A.7    Cheng, Y.8
  • 30
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • PMID: 24305160
    • Liao M, Cao E, Julius D, Cheng Y. 2013. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504:107–112. doi: 10.1038/nature12822, PMID: 24305160
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 33
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with phaser
    • PMID: 17164524
    • McCoy AJ. 2007. Solving structures of protein complexes by molecular replacement with phaser. Acta Crystallographica Section D Biological Crystallography 63:32–41. doi: 10.1107/S0907444906045975, PMID: 17164524
    • (2007) Acta Crystallographica Section D Biological Crystallography , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 34
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • PMID: 12781660
    • Mindell JA, Grigorieff N. 2003. Accurate determination of local defocus and specimen tilt in electron microscopy. Journal of Structural Biology 142:334–347. doi: 10.1016/S1047-8477(03)00069-8, PMID: 12781660
    • (2003) Journal of Structural Biology , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 35
    • 84944382016 scopus 로고    scopus 로고
    • Directly observing the lipid-dependent self-assembly and pore-forming mechanism of the cytolytic toxin listeriolysin O
    • PMID: 26302195
    • Mulvihill E, van Pee K, Mari SA, Müller DJ, Yildiz Ö. 2015. Directly observing the lipid-dependent self-assembly and pore-forming mechanism of the cytolytic toxin listeriolysin O. Nano Letters 15:6965–6973. doi: 10.1021/acs.nanolett.5b02963, PMID: 26302195
    • (2015) Nano Letters , vol.15 , pp. 6965-6973
    • Mulvihill, E.1    Van Pee, K.2    Mari, S.A.3    Müller, D.J.4    Yildiz, Ö.5
  • 37
    • 33747598723 scopus 로고    scopus 로고
    • The molecular architecture of axonemes revealed by cryoelectron tomography
    • PMID: 16917055
    • Nicastro D, Schwartz C, Pierson J, Gaudette R, Porter ME, McIntosh JR. 2006. The molecular architecture of axonemes revealed by cryoelectron tomography. Science 313:944–948. doi: 10.1126/science.1128618, PMID: 16917055
    • (2006) Science , vol.313 , pp. 944-948
    • Nicastro, D.1    Schwartz, C.2    Pierson, J.3    Gaudette, R.4    Porter, M.E.5    McIntosh, J.R.6
  • 38
    • 0027526035 scopus 로고
    • The projection structure of perfringolysin O (Clostridium perfringens theta-toxin)
    • PMID: 8454043
    • Olofsson A, Hebert H, Thelestam M. 1993. The projection structure of perfringolysin O (Clostridium perfringens theta-toxin). FEBS Letters 319:125–127. doi: 10.1016/0014-5793(93)80050-5, PMID: 8454043
    • (1993) FEBS Letters , vol.319 , pp. 125-127
    • Olofsson, A.1    Hebert, H.2    Thelestam, M.3
  • 40
    • 0036830653 scopus 로고    scopus 로고
    • Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin
    • PMID: 12368903
    • Ramachandran R, Heuck AP, Tweten RK, Johnson AE. 2002. Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin. Nature Structural Biology 9:823–827. doi: 10.1038/nsb855, PMID: 12368903
    • (2002) Nature Structural Biology , vol.9 , pp. 823-827
    • Ramachandran, R.1    Heuck, A.P.2    Tweten, R.K.3    Johnson, A.E.4
  • 41
    • 18844417932 scopus 로고    scopus 로고
    • The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation
    • PMID: 15878993
    • Ramachandran R, Tweten RK, Johnson AE. 2005. The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation. PNAS 102:7139–7144. doi: 10.1073/pnas.0500556102, PMID: 15878993
    • (2005) PNAS , vol.102 , pp. 7139-7144
    • Ramachandran, R.1    Tweten, R.K.2    Johnson, A.E.3
  • 42
    • 84879123070 scopus 로고    scopus 로고
    • Disulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel
    • PMID: 23563525
    • Sato TK, Tweten RK, Johnson AE. 2013. Disulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel. Nature Chemical Biology 9:383–389. doi: 10.1038/nchembio.1228, PMID: 23563525
    • (2013) Nature Chemical Biology , vol.9 , pp. 383-389
    • Sato, T.K.1    Tweten, R.K.2    Johnson, A.E.3
  • 43
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a bayesian approach to cryo-EM structure determination
    • PMID: 23000701
    • Scheres SH. 2012. RELION: implementation of a bayesian approach to cryo-EM structure determination. Journal of Structural Biology 180:519–530. doi: 10.1016/j.jsb.2012.09.006, PMID: 23000701
    • (2012) Journal of Structural Biology , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 44
    • 84922727036 scopus 로고    scopus 로고
    • Semi-automated selection of cryo-EM particles in RELION-1.3
    • PMID: 25486611
    • Scheres SH. 2015. Semi-automated selection of cryo-EM particles in RELION-1.3. Journal of Structural Biology 189:114–122. doi: 10.1016/j.jsb.2014.11.010, PMID: 25486611
    • (2015) Journal of Structural Biology , vol.189 , pp. 114-122
    • Scheres, S.H.1
  • 46
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
    • PMID: 10555145
    • 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. doi: 10.1016/s0092-8674(00)81660-8, PMID: 10555145
    • (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
  • 47
    • 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
    • PMID: 9772185
    • 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. doi: 10.1021/bi981452f, PMID: 9772185
    • (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
  • 48
    • 34447536854 scopus 로고    scopus 로고
    • Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin
    • PMID: 17412689
    • Soltani CE, Hotze EM, Johnson AE, Tweten RK. 2007a. Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin. Journal of Biological Chemistry 282:15709–15716. doi: 10.1074/jbc.M701173200, PMID: 17412689
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 15709-15716
    • Soltani, C.E.1    Hotze, E.M.2    Johnson, A.E.3    Tweten, R.K.4
  • 49
    • 38049125626 scopus 로고    scopus 로고
    • Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions
    • PMID: 18077338
    • Soltani CE, Hotze EM, Johnson AE, Tweten RK. 2007b. Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions. PNAS 104:20226–20231. doi: 10.1073/pnas.0708104105, PMID: 18077338
    • (2007) PNAS , vol.104 , pp. 20226-20231
    • Soltani, C.E.1    Hotze, E.M.2    Johnson, A.E.3    Tweten, R.K.4
  • 51
    • 2142689200 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution, density modification and model building
    • PMID: 14646132
    • Terwilliger T. 2004. SOLVE and RESOLVE: automated structure solution, density modification and model building. Journal of Synchrotron Radiation 11:49–52. doi: 10.1107/S0909049503023938, PMID: 14646132
    • (2004) Journal of Synchrotron Radiation , vol.11 , pp. 49-52
    • Terwilliger, T.1
  • 52
    • 17444405610 scopus 로고    scopus 로고
    • Structural basis of pore formation by the bacterial toxin pneumolysin
    • PMID: 15851031
    • 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. doi: 10.1016/j.cell.2005.02.033, PMID: 15851031
    • (2005) Cell , vol.121 , pp. 247-256
    • Tilley, S.J.1    Orlova, E.V.2    Gilbert, R.J.3    Rew, P.W.4    Saibil, H.R.5
  • 54
    • 25444452398 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins
    • PMID: 16177291
    • Tweten RK. 2005. Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins. Infection and Immunity 73:6199–6209. doi: 10.1128/IAI.73.10.6199-6209.2005, PMID: 16177291
    • (2005) Infection and Immunity , vol.73 , pp. 6199-6209
    • Tweten, R.K.1
  • 55
    • 85006246927 scopus 로고    scopus 로고
    • Unraveling the pore-Forming steps of pneumolysin from Streptococcus pneumoniae
    • PMID: 27796097
    • van Pee K, Mulvihill E, Müller DJ, Yildiz Ö. 2016. Unraveling the pore-Forming steps of pneumolysin from Streptococcus pneumoniae. Nano Letters 16:7915–7924. doi: 10.1021/acs.nanolett.6b04219, PMID: 27796097
    • (2016) Nano Letters , vol.16 , pp. 7915-7924
    • Van Pee, K.1    Mulvihill, E.2    Müller, D.J.3    Yildiz, Ö.4
  • 56
    • 0035830656 scopus 로고    scopus 로고
    • Streptolysin O: The C-terminal, tryptophan-rich domain carries functional sites for both membrane binding and self-interaction but not for stable oligomerization
    • PMID: 11342166
    • Weis S, Palmer M. 2001. Streptolysin O: the C-terminal, tryptophan-rich domain carries functional sites for both membrane binding and self-interaction but not for stable oligomerization. Biochimica Et Biophysica Acta (BBA)-Biomembranes 1510:292–299. doi: 10.1016/S0005-2736(00)00360-6, PMID: 11342166
    • (2001) Biochimica Et Biophysica Acta (Bba)-Biomembranes , vol.1510 , pp. 292-299
    • Weis, S.1    Palmer, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.