메뉴 건너뛰기




Volumn 1418, Issue 1, 1999, Pages 117-126

Water transport by the bacterial channel α-hemolysin

Author keywords

Hemolysin; Biological membrane; Pore size; Water channel; Water transport

Indexed keywords

HEMOLYSIN;

EID: 0032941774     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(99)00031-0     Document Type: Article
Times cited : (15)

References (34)
  • 1
    • 0025787798 scopus 로고
    • Alpha-toxin of Staphylococcus aureus
    • S. Bhakdi, J. Tranum-Jensen, Alpha-toxin of Staphylococcus aureus, Microbiol. Rev. 55 (1991) 733-751.
    • (1991) Microbiol. Rev. , vol.55 , pp. 733-751
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 2
    • 85033090757 scopus 로고    scopus 로고
    • Building doors into cells
    • H. Bayley, Building doors into cells, Sci. Am. 277 (1997) 61-67.
    • (1997) Sci. Am. , vol.277 , pp. 61-67
    • Bayley, H.1
  • 3
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • L. Song, M.R. Hobaugh, C. Shustak, S. Cheley, H. Bayley, J.E. Gouaux, Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore, Science 274 (1996) 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
  • 5
    • 0022504362 scopus 로고
    • Ionic channels formed by Staphylococcus aureus alpha-toxin: Voltage-dependent inhibition by divalent and trivalent cations
    • G. Menestrina, Ionic channels formed by Staphylococcus aureus alpha-toxin: voltage-dependent inhibition by divalent and trivalent cations, J. Membr. Biol. 90 (1986) 177-190.
    • (1986) J. Membr. Biol. , vol.90 , pp. 177-190
    • Menestrina, G.1
  • 6
    • 0023071990 scopus 로고
    • Pore formation by Staphylocoocus aureus alpha-toxin in lipid bilayers. Dependence upon temperature and toxin concentration
    • G. Belmonte, L. Cescatti, B. Ferrari, T. Nicolussi, M. Ropele, G. Menestrina, Pore formation by Staphylocoocus aureus alpha-toxin in lipid bilayers. Dependence upon temperature and toxin concentration, Eur. Biophys. J. 14 (1987) 349-358.
    • (1987) Eur. Biophys. J. , vol.14 , pp. 349-358
    • Belmonte, G.1    Cescatti, L.2    Ferrari, B.3    Nicolussi, T.4    Ropele, M.5    Menestrina, G.6
  • 7
    • 0028980231 scopus 로고
    • Protonation dynamics of the α-toxin ion channel from spectral analysis of pH-dependent current fluctuations
    • J. Kasianowicz, S. Bezrukov, Protonation dynamics of the α-toxin ion channel from spectral analysis of pH-dependent current fluctuations, Biophys. J. 69 (1995) 94-105.
    • (1995) Biophys. J. , vol.69 , pp. 94-105
    • Kasianowicz, J.1    Bezrukov, S.2
  • 8
    • 0022273189 scopus 로고
    • The ubiquitous presence of channels with wide lumens and their gating by voltage
    • A. Finkelstein, The ubiquitous presence of channels with wide lumens and their gating by voltage, Ann. N. Y. Acad. Sci. 456 (1985) 26-32.
    • (1985) Ann. N. Y. Acad. Sci. , vol.456 , pp. 26-32
    • Finkelstein, A.1
  • 9
    • 0024509049 scopus 로고
    • Simultaneous optical measurement of osmotic and diffusional water permeability in cells and liposomes
    • R. Ye, A.S. Verkman, Simultaneous optical measurement of osmotic and diffusional water permeability in cells and liposomes, Biochemistry 28 (1989) 824-829.
    • (1989) Biochemistry , vol.28 , pp. 824-829
    • Ye, R.1    Verkman, A.S.2
  • 10
    • 0026011530 scopus 로고
    • Water and urea permeability properties of Xenopus oocytes: Expression of mRNA from toad urinary bladder
    • R. Zhang, A.S. Verkman, Water and urea permeability properties of Xenopus oocytes: expression of mRNA from toad urinary bladder, Am. J. Physiol. 280 (1991) C26-33.
    • (1991) Am. J. Physiol. , vol.280
    • Zhang, R.1    Verkman, A.S.2
  • 11
    • 0024265414 scopus 로고
    • Assay of hemolytic toxins
    • A. Bernheimer, Assay of hemolytic toxins, Methods Enzymol. 165 (1988) 213-217.
    • (1988) Methods Enzymol. , vol.165 , pp. 213-217
    • Bernheimer, A.1
  • 12
    • 0016360444 scopus 로고
    • Preparation of impermeable ghosts and inside-out vesicles from human erythrocyte membranes
    • T. Steck, J.A. Kant, Preparation of impermeable ghosts and inside-out vesicles from human erythrocyte membranes, Methods Enzymol. 31 (1974) 172-180.
    • (1974) Methods Enzymol. , vol.31 , pp. 172-180
    • Steck, T.1    Kant, J.A.2
  • 13
    • 0001062701 scopus 로고
    • Osmotic properties and water permeability of phospholipid liquid crystals
    • A.D. Bangham, J. De Gier, G.D. Greville, Osmotic properties and water permeability of phospholipid liquid crystals, Chem. Phys. Lipids 1 (1967) 225-246.
    • (1967) Chem. Phys. Lipids , vol.1 , pp. 225-246
    • Bangham, A.D.1    De Gier, J.2    Greville, G.D.3
  • 14
    • 0019460215 scopus 로고
    • Osmotic water permeability of human red cells
    • T. Terwilliger, A.K. Solomon, Osmotic water permeability of human red cells, J. Gen. Physiol. 77 (1981) 549-570.
    • (1981) J. Gen. Physiol. , vol.77 , pp. 549-570
    • Terwilliger, T.1    Solomon, A.K.2
  • 15
    • 0027372441 scopus 로고
    • Osmotic behaviour and permeability properties of liposomes
    • J. De Gier, Osmotic behaviour and permeability properties of liposomes, Chem. Phys. Lipids 64 (1993) 187-196.
    • (1993) Chem. Phys. Lipids , vol.64 , pp. 187-196
    • De Gier, J.1
  • 16
    • 0028936860 scopus 로고
    • A comparative study of diffusive and osmotic water permeation across bilayers composed of phospholipids with different head groups and fatty acyl chains
    • M. Jansen, A. Blume, A comparative study of diffusive and osmotic water permeation across bilayers composed of phospholipids with different head groups and fatty acyl chains, Biophys. J. 68 (1995) 997-1008.
    • (1995) Biophys. J. , vol.68 , pp. 997-1008
    • Jansen, M.1    Blume, A.2
  • 17
    • 0004063752 scopus 로고
    • Blackwell Scientific Publications Ltd., Oxford
    • T.A.J. Prankerd, The Red Cell, Blackwell Scientific Publications Ltd., Oxford, 1961.
    • (1961) The Red Cell
    • Prankerd, T.A.J.1
  • 19
    • 0017845979 scopus 로고
    • Interaction of water and ions in gramicidin a channels. Streaming potentials across lipid bilayer membranes
    • P.A. Rosenberg, A. Finkelstein, Interaction of water and ions in gramicidin A channels. Streaming potentials across lipid bilayer membranes, J. Gen. Physiol. 72 (1978) 327-340.
    • (1978) J. Gen. Physiol. , vol.72 , pp. 327-340
    • Rosenberg, P.A.1    Finkelstein, A.2
  • 20
    • 0027366423 scopus 로고
    • Secondary structure analysis of purified functional CHIP28 water channels by CD and FTIR spectroscopy
    • A.N. Van Hoek, M. Wiener, S. Bicknese, L. Miercke, J. Biwersi, A.S. Verkman, Secondary structure analysis of purified functional CHIP28 water channels by CD and FTIR spectroscopy, Biochemistry 32 (1993) 11847-11856.
    • (1993) Biochemistry , vol.32 , pp. 11847-11856
    • Van Hoek, A.N.1    Wiener, M.2    Bicknese, S.3    Miercke, L.4    Biwersi, J.5    Verkman, A.S.6
  • 21
    • 0002646587 scopus 로고
    • A.F. Rowley, N.A. Ratcliffe (Eds.), Cambridge University Press, Cambridge
    • R. Parmley, in: A.F. Rowley, N.A. Ratcliffe (Eds.), Vertebrate Blood Cells, Cambridge University Press, Cambridge, 1988, pp. 337-424.
    • (1988) Vertebrate Blood Cells , pp. 337-424
    • Parmley, R.1
  • 23
    • 0022065511 scopus 로고
    • Water and urea transport in renal microvillus membrane vesicles
    • A.S. Verkman, J.A. Dix, J.L. Seifter, Water and urea transport in renal microvillus membrane vesicles, Am. J. Physiol. 248 (1985) F650-655.
    • (1985) Am. J. Physiol. , vol.248
    • Verkman, A.S.1    Dix, J.A.2    Seifter, J.L.3
  • 24
    • 0029882410 scopus 로고    scopus 로고
    • Osmotic gradient-induced water permeation across the sarcolemma of rabbit ventricular myocytes
    • M.A. Suleymanian, C.M. Baumgarten, Osmotic gradient-induced water permeation across the sarcolemma of rabbit ventricular myocytes, J. Gen. Physiol. 107 (1996) 503-514.
    • (1996) J. Gen. Physiol. , vol.107 , pp. 503-514
    • Suleymanian, M.A.1    Baumgarten, C.M.2
  • 26
    • 0000560829 scopus 로고
    • Filtration, diffusion, and molecular sieving through porous cellulose membranes
    • E.M. Renkin, Filtration, diffusion, and molecular sieving through porous cellulose membranes, J. Gen. Physiol. 38 (1954) 225-243.
    • (1954) J. Gen. Physiol. , vol.38 , pp. 225-243
    • Renkin, E.M.1
  • 27
    • 0001658983 scopus 로고
    • The rate of exchange of tritiated water across the human red cell membrane
    • C.V. Paganelli, A.K. Solomon, The rate of exchange of tritiated water across the human red cell membrane, J. Gen. Physiol. 41 (1957) 259-277.
    • (1957) J. Gen. Physiol. , vol.41 , pp. 259-277
    • Paganelli, C.V.1    Solomon, A.K.2
  • 28
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphosphatidyl-choline bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure
    • M.C. Wiener, S.H. White, Structure of a fluid dioleoylphosphatidyl-choline bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure, Biophys. J. 61 (1992) 437-447.
    • (1992) Biophys. J. , vol.61 , pp. 437-447
    • Wiener, M.C.1    White, S.H.2
  • 29
    • 0024399624 scopus 로고
    • Staphylococcal α-toxin increases the permeability of lipid vesicles cholesterol- and pH-dependent assembly of oligomeric channels
    • S. Forti, G. Menestrina, Staphylococcal α-toxin increases the permeability of lipid vesicles cholesterol- and pH-dependent assembly of oligomeric channels, J. Biochem. 181 (1989) 767-773.
    • (1989) J. Biochem. , vol.181 , pp. 767-773
    • Forti, S.1    Menestrina, G.2
  • 30
    • 0024282476 scopus 로고
    • Escherichia coli hemolysin permeabilizes small unilamellar vesicles loaded with calcein by a single-hit mechanism
    • G. Menestrina, Escherichia coli hemolysin permeabilizes small unilamellar vesicles loaded with calcein by a single-hit mechanism, FEBS Lett. 232 (1988) 217-220.
    • (1988) FEBS Lett. , vol.232 , pp. 217-220
    • Menestrina, G.1
  • 31
    • 0030710585 scopus 로고    scopus 로고
    • The charge state of an ion channel controls neutral polymer entry into its pore
    • S. Bezrukov, J. Kasianowicz, The charge state of an ion channel controls neutral polymer entry into its pore, Eur. Biophys. J. 26 (1997) 471-476.
    • (1997) Eur. Biophys. J. , vol.26 , pp. 471-476
    • Bezrukov, S.1    Kasianowicz, J.2
  • 33
    • 0026024029 scopus 로고
    • Modification of lysine residues of Staphylococcus aureus α-toxin: Effects on its channel forming properties
    • L. Cescatti, C. Pederzolli, G. Menestrina, Modification of lysine residues of Staphylococcus aureus α-toxin: effects on its channel forming properties, J. Membr. Biol. 119 (1991) 53-54.
    • (1991) J. Membr. Biol. , vol.119 , pp. 53-54
    • Cescatti, L.1    Pederzolli, C.2    Menestrina, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.