메뉴 건너뛰기




Volumn 7, Issue 12, 1997, Pages

Toxin structure: Part of a hole?

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0031457628     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0960-9822(06)00399-x     Document Type: Review
Times cited : (47)

References (23)
  • 1
    • 0030865151 scopus 로고    scopus 로고
    • Channel-forming toxins: Tales of transformation
    • Gouaux E: Channel-forming toxins: tales of transformation. Curr Opin Struct Biol 1997, 7:566-573.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 566-573
    • Gouaux, E.1
  • 2
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • Rossjohn J, Fell SC, McKinstry WJ, Tweten RK, Parker MW: Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 1997, 89:685-692.
    • (1997) Cell , vol.89 , pp. 685-692
    • Rossjohn, J.1    Fell, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 3
    • 0002027172 scopus 로고
    • The family of the antigenically-related, cholesterol-binding ('sulfhydryl-activated') cytolytic toxins
    • Edited by Alouf JE, Freer JH. London: Academic Press
    • Alouf JE, Geoffroy C: The family of the antigenically-related, cholesterol-binding ('sulfhydryl-activated') cytolytic toxins. In Sourcebook of bacterial protein toxins. Edited by Alouf JE, Freer JH. London: Academic Press; 1991:147-186.
    • (1991) Sourcebook of Bacterial Protein Toxins , pp. 147-186
    • Alouf, J.E.1    Geoffroy, C.2
  • 6
    • 0026695462 scopus 로고
    • Differential sensitivity of pneumolysin-induced channels to gating by divalent cations
    • Korchev YE, Bashford CL, Pasternak CA: Differential sensitivity of pneumolysin-induced channels to gating by divalent cations. J Membr Biol 1992, 127:195-203.
    • (1992) J Membr Biol , vol.127 , pp. 195-203
    • Korchev, Y.E.1    Bashford, C.L.2    Pasternak, C.A.3
  • 7
    • 0028106748 scopus 로고
    • Proteinaceous bacterial toxins and pathogenesis of sepsis syndrome and septic shock: The unknown connection
    • Bhakdi S, Grimminger F, Suttorp N, Walmrath D, Seeger W: Proteinaceous bacterial toxins and pathogenesis of sepsis syndrome and septic shock: the unknown connection. Med Microbiol Immunol 1994, 183:119-144.
    • (1994) Med Microbiol Immunol , vol.183 , pp. 119-144
    • Bhakdi, S.1    Grimminger, F.2    Suttorp, N.3    Walmrath, D.4    Seeger, W.5
  • 8
    • 0021796923 scopus 로고
    • Complement activation and attack on autologous cell membranes induced by streptolysin O
    • Bhakdi S, Tranum-Jensen J: Complement activation and attack on autologous cell membranes induced by streptolysin O. Infect Immun 1985, 48:713-719.
    • (1985) Infect Immun , vol.48 , pp. 713-719
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 9
    • 0029972377 scopus 로고    scopus 로고
    • Contribution of individual tryptophan residues to the structure and activity of θ-toxin (perfringolysin O), a cholesterol-binding cytolysin
    • Sekino-Suzuki N, Nakamura M, Mitsui K, Ohno-Iwashita Y: Contribution of individual tryptophan residues to the structure and activity of θ-toxin (perfringolysin O), a cholesterol-binding cytolysin. Eur J Biochem 1996, 241:941-947.
    • (1996) Eur J Biochem , vol.241 , pp. 941-947
    • Sekino-Suzuki, N.1    Nakamura, M.2    Mitsui, K.3    Ohno-Iwashita, Y.4
  • 10
    • 0028988973 scopus 로고
    • Interaction of θ-toxin (perfringolysin O), a cholesterol-binding cytolysin, with liposomal membranes: Change in the aromatic side chains upon binding and insertion
    • Nakamura M, Sekino N, Iwamoto M, Ohno-Iwashita Y: Interaction of θ-toxin (perfringolysin O), a cholesterol-binding cytolysin, with liposomal membranes: change in the aromatic side chains upon binding and insertion. Biochemistry 1995, 34:6513-6520.
    • (1995) Biochemistry , vol.34 , pp. 6513-6520
    • Nakamura, M.1    Sekino, N.2    Iwamoto, M.3    Ohno-Iwashita, Y.4
  • 11
    • 0029103215 scopus 로고
    • Characterization and modeling of membrane proteins using sequence analysis
    • Reithmeier RAF: Characterization and modeling of membrane proteins using sequence analysis. Curr Opin Struct Biol 1995, 5:491-500.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 491-500
    • Reithmeier, R.A.F.1
  • 12
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix
    • Blake C, Serpell L: Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix. Structure 1996, 4:989-998.
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 16
    • 0028979464 scopus 로고
    • Crystal structure of the Cys2 activator-binding domain of protein kinase Cδ in complex with phorbol ester
    • Zhang G, Kazanietz MG, Blumberg PM, Hurley JH: Crystal structure of the Cys2 activator-binding domain of protein kinase Cδ in complex with phorbol ester. Cell 1995, 81:917-924.
    • (1995) Cell , vol.81 , pp. 917-924
    • Zhang, G.1    Kazanietz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4
  • 17
    • 0029909653 scopus 로고    scopus 로고
    • Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis
    • Palmer M, Saweljew P, Vulicevic I, Valeva A, Kehoe M, Bhakdi S: Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis. J Biol Chem 1996, 271:26664-26667.
    • (1996) J Biol Chem , vol.271 , pp. 26664-26667
    • Palmer, M.1    Saweljew, P.2    Vulicevic, I.3    Valeva, A.4    Kehoe, M.5    Bhakdi, S.6
  • 18
    • 0029924449 scopus 로고    scopus 로고
    • Molecular architecture of a toxin pore: A 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin
    • Valeva A, Weisser A, Walker B, Kehoe M, Bayley H, Bhakdi S, Palmer M: Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin. EMBO J 1996, 15:1857-1864.
    • (1996) EMBO J , vol.15 , pp. 1857-1864
    • Valeva, A.1    Weisser, A.2    Walker, B.3    Kehoe, M.4    Bayley, H.5    Bhakdi, S.6    Palmer, M.7
  • 19
    • 13144295748 scopus 로고    scopus 로고
    • The organization of the pore-forming domain of staphylococcal alpha-toxin differs in susceptible and resistant cells
    • in press
    • Valeva A, Walev I, Pinkernell M, Bayley H, Walker B, Palmer M, Bhakdi S: The organization of the pore-forming domain of staphylococcal alpha-toxin differs in susceptible and resistant cells. Proc Natl Acad Sci USA 1997, in press.
    • (1997) Proc Natl Acad Sci USA
    • Valeva, A.1    Walev, I.2    Pinkernell, M.3    Bayley, H.4    Walker, B.5    Palmer, M.6    Bhakdi, S.7
  • 20
    • 0001350946 scopus 로고    scopus 로고
    • Organization of diphtheria toxin T domain in bilayers: A site-directed spin labeling study
    • Oh KJ, Zhan H, Cui C, Hideg K, Collier RJ, Hubbell WL: Organization of diphtheria toxin T domain in bilayers: a site-directed spin labeling study. Science 1996, 273:810-812.
    • (1996) Science , vol.273 , pp. 810-812
    • Oh, K.J.1    Zhan, H.2    Cui, C.3    Hideg, K.4    Collier, R.J.5    Hubbell, W.L.6
  • 21
    • 0029860763 scopus 로고    scopus 로고
    • On the use of thiol-modifying reagents to determine channel topology
    • Holmgren M, Liu Y, Xu Y, Yellen G: On the use of thiol-modifying reagents to determine channel topology. Neuropharmacology 1996, 35:797-804.
    • (1996) Neuropharmacology , vol.35 , pp. 797-804
    • Holmgren, M.1    Liu, Y.2    Xu, Y.3    Yellen, G.4
  • 22
    • 0030611388 scopus 로고    scopus 로고
    • The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane
    • Hamman BD, Chen J-C, Johnson EE, Johnson AE: The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane. Cell 1997, 89:535-544.
    • (1997) Cell , vol.89 , pp. 535-544
    • Hamman, B.D.1    Chen, J.-C.2    Johnson, E.E.3    Johnson, A.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.