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Volumn 89, Issue 5, 2005, Pages 3059-3070

Conductance and ion selectivity of a mesoscopic protein nanopore probed with cysteine scanning mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; ION CHANNEL; PROTEIN;

EID: 27744482622     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.066472     Document Type: Article
Times cited : (52)

References (60)
  • 2
    • 0025665205 scopus 로고
    • Memory is a property of an ion channels pool-ion channels formed by Staphylococcus aureus α-toxin
    • Krasilnikov, O. V., P. G. Merzliak, R. Z. Sabirov, and B. A. Tashmukhamedov. 1990. Memory is a property of an ion channels pool-ion channels formed by Staphylococcus aureus α-toxin. Gen. Physiol. Biophys. 9:569-575.
    • (1990) Gen. Physiol. Biophys. , vol.9 , pp. 569-575
    • Krasilnikov, O.V.1    Merzliak, P.G.2    Sabirov, R.Z.3    Tashmukhamedov, B.A.4
  • 3
    • 0000067560 scopus 로고
    • Current noise reveals protonation kinetics and number of ionizable sites in an open protein ion channel
    • Bezrukov, S. M., and J. J. Kasianowicz. 1993. Current noise reveals protonation kinetics and number of ionizable sites in an open protein ion channel. Phys. Rev. Lett. 70:2352-2355.
    • (1993) Phys. Rev. Lett. , vol.70 , pp. 2352-2355
    • Bezrukov, S.M.1    Kasianowicz, J.J.2
  • 4
    • 0028980231 scopus 로고
    • Protonation dynamics of the α-toxin ion-channel from spectral-analysis of pH-dependent current fluctuations
    • Kasianowicz, J. J., and S. M. Bezrukov. 1995. Protonation dynamics of the α-toxin ion-channel from spectral-analysis of pH-dependent current fluctuations. Biophys. J. 69:94-105.
    • (1995) Biophys. J. , vol.69 , pp. 94-105
    • Kasianowicz, J.J.1    Bezrukov, S.M.2
  • 5
    • 0030465241 scopus 로고    scopus 로고
    • Characterization of individual polymucleotide molecules using a membrane channel
    • Kasianowicz, J. J., E. Brandin, D. Branton, and D. W. Deamer. 1996. Characterization of individual polymucleotide molecules using a membrane channel. Proc. Natl. Acad. Sci USA. 93:13770-13773.
    • (1996) Proc. Natl. Acad. Sci USA. , vol.93 , pp. 13770-13773
    • Kasianowicz, J.J.1    Brandin, E.2    Branton, D.3    Deamer, D.W.4
  • 8
    • 0032987931 scopus 로고    scopus 로고
    • Genetically engineered metal ion binding sites on the outside of a channel's transmembrane β-barrel
    • Kasianowicz, J. J., D. L. Burden, L. C. Han, S. Cheley, and H. Bayley. 1999. Genetically engineered metal ion binding sites on the outside of a channel's transmembrane β-barrel. Biophys. J. 76:837-845.
    • (1999) Biophys. J. , vol.76 , pp. 837-845
    • Kasianowicz, J.J.1    Burden, D.L.2    Han, L.C.3    Cheley, S.4    Bayley, H.5
  • 10
    • 0012272038 scopus 로고    scopus 로고
    • Physics of DNA threading through a nanometer pore and applications to simultaneous multi-analyte sensing
    • J. J. Kasianowicz, M. Kellermayer, and D. W. Deamer, editors. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Kasianowicz, J. J., S. E. Henrickson, M. Misakian, H. H. Weetall, B. Robertson, and V. Stanford. 2002. Physics of DNA threading through a nanometer pore and applications to simultaneous multi-analyte sensing. In Structure and Dynamics of Confined Polymers. J. J. Kasianowicz, M. Kellermayer, and D. W. Deamer, editors. Kluwer Academic Publishers, Dordrecht, The Netherlands. 141-163.
    • (2002) Structure and Dynamics of Confined Polymers , pp. 141-163
    • Kasianowicz, J.J.1    Henrickson, S.E.2    Misakian, M.3    Weetall, H.H.4    Robertson, B.5    Stanford, V.6
  • 11
    • 4444247468 scopus 로고    scopus 로고
    • Functional engineered channels and pores (Review)
    • Bayley, H., and L. Jayasinghe. 2004. Functional engineered channels and pores (Review). Mol. Membr. Biol. 21:209-220.
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 209-220
    • Bayley, H.1    Jayasinghe, L.2
  • 13
    • 0348014625 scopus 로고    scopus 로고
    • Synthetic Single-nanopore and nanotube membranes
    • Harrell, C. C., S. B. Lee, and C. R. Martin. 2003. Synthetic Single-nanopore and nanotube membranes. Anal. Chem. 75:6861-6867.
    • (2003) Anal. Chem. , vol.75 , pp. 6861-6867
    • Harrell, C.C.1    Lee, S.B.2    Martin, C.R.3
  • 14
    • 0042285088 scopus 로고    scopus 로고
    • Fabrication of solid-state nanopores with single-nanometre precision
    • Storm, A. J., J. H. Chen, X. S. Ling, H. W. Zandbergen, and C. Dekker. 2003. Fabrication of solid-state nanopores with single-nanometre precision. Nat. Mater. 2:537-540.
    • (2003) Nat. Mater. , vol.2 , pp. 537-540
    • Storm, A.J.1    Chen, J.H.2    Ling, X.S.3    Zandbergen, H.W.4    Dekker, C.5
  • 15
    • 0242637006 scopus 로고    scopus 로고
    • Electrokinetic microchannel battery by means of electrokinetic and microfluidic phenomena
    • Yang, J., F. Lu, L. W. Kostiuk, and D. Y. Kwok. 2003. Electrokinetic microchannel battery by means of electrokinetic and microfluidic phenomena. J. Micromech. Microeng. 13:963-970.
    • (2003) J. Micromech. Microeng. , vol.13 , pp. 963-970
    • Yang, J.1    Lu, F.2    Kostiuk, L.W.3    Kwok, D.Y.4
  • 16
    • 0031708266 scopus 로고    scopus 로고
    • Electrostatics and the ion selectivity of ligand-gated channels
    • Adcock, C., G. R. Smith, and M. S. P. Sansom. 1998. Electrostatics and the ion selectivity of ligand-gated channels. Biophys. J. 75:1211-1222.
    • (1998) Biophys. J. , vol.75 , pp. 1211-1222
    • Adcock, C.1    Smith, G.R.2    Sansom, M.S.P.3
  • 17
    • 0033813781 scopus 로고    scopus 로고
    • The intrinsic electrostatic potential and the intermediate ring of charge in the acetylcholine receptor channel
    • Wilson, G. G., J. M. Pascual, N. Brooijmans, D. Murray, and A. Karlin. 2000. The intrinsic electrostatic potential and the intermediate ring of charge in the acetylcholine receptor channel. J. Gen. Physiol. 115:93-106.
    • (2000) J. Gen. Physiol. , vol.115 , pp. 93-106
    • Wilson, G.G.1    Pascual, J.M.2    Brooijmans, N.3    Murray, D.4    Karlin, A.5
  • 19
    • 15244338641 scopus 로고    scopus 로고
    • Ion permeation through the α-hemolysin channel: Theoretical studies based on Brownian dynamics and Poisson-Nernst-Plank electrodiffusion theory
    • Noskov, S. Y., W. Im, and B. Roux. 2004. Ion permeation through the α-hemolysin channel: Theoretical studies based on Brownian dynamics and Poisson-Nernst-Plank electrodiffusion theory. Biophys. J. 87:2299-2309.
    • (2004) Biophys. J. , vol.87 , pp. 2299-2309
    • Noskov, S.Y.1    Im, W.2    Roux, B.3
  • 20
    • 15244355046 scopus 로고    scopus 로고
    • Fifty years of progress in ion channel research
    • Jordan, P. C. 2005. Fifty years of progress in ion channel research. IEEE Trans. Nanobioscience. 4:3-9.
    • (2005) IEEE Trans. Nanobioscience , vol.4 , pp. 3-9
    • Jordan, P.C.1
  • 21
    • 0025787798 scopus 로고
    • Alpha-toxin of Staphylococcus Aureus
    • Bhakdi, S., and J. Tranum-Jensen. 1991. Alpha-toxin of Staphylococcus Aureus. Microbiol. Rev. 55:733-751.
    • (1991) Microbiol. Rev. , vol.55 , pp. 733-751
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 22
    • 0028567173 scopus 로고
    • Subunit stoichiometry of Staphylococcal α-hemolysin in crystals and on membranes: A heptameric transmembrane pore
    • Gouaux, J. E., O. Braha, M. R. Hobaugh, L. Z. Song, S, Cheley, C. Shustak, and H. Bayley. 1994. Subunit stoichiometry of Staphylococcal α-hemolysin in crystals and on membranes: a heptameric transmembrane pore. Proc. Natl. Acad. Sci. USA. 91:12828-12831.
    • (1994) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 12828-12831
    • Gouaux, J.E.1    Braha, O.2    Hobaugh, M.R.3    Song, L.Z.4    Cheley, S.5    Shustak, C.6    Bayley, H.7
  • 23
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song, L. Z., M. R. Hobaugh, C. Shustak, S. Cheley, H. Bayley, and J. E. Gouaux. 1996. Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science. 274:1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.Z.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 24
    • 0033779406 scopus 로고    scopus 로고
    • Electrophysiological evidence for heptameric stoichiometry of ion channels formed by Staphylococcus aureus α-toxin in planar lipid bilayers
    • Krasilnikov, O. V., P. G. Merzlyak, L. N. Yuldasheva, C. G. Rodrigues, S. Bhakdi, and A. Valeva. 2000. Electrophysiological evidence for heptameric stoichiometry of ion channels formed by Staphylococcus aureus α-toxin in planar lipid bilayers. Mol. Microbiol. 37:1372-1378.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1372-1378
    • Krasilnikov, O.V.1    Merzlyak, P.G.2    Yuldasheva, L.N.3    Rodrigues, C.G.4    Bhakdi, S.5    Valeva, A.6
  • 26
    • 0242297427 scopus 로고    scopus 로고
    • Sizing channels with neutral polymers
    • J. J. Kasianowicz, M. S. Z. Kellermayer, and D. W. Deamer, editors. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Krasilnikov, O. V. 2002. Sizing channels with neutral polymers. In Structure and Dynamics of Confined Polymers. J. J. Kasianowicz, M. S. Z. Kellermayer, and D. W. Deamer, editors. Kluwer Academic Publishers, Dordrecht, The Netherlands. 97-115.
    • (2002) Structure and Dynamics of Confined Polymers , pp. 97-115
    • Krasilnikov, O.V.1
  • 28
    • 0024676138 scopus 로고
    • Ion transport through channels formed in lipid bilayers by Staphylococcus aureus α-toxin. Gen
    • Krasilnikov, O. V., and R. Z. Sabirov. 1989. Ion transport through channels formed in lipid bilayers by Staphylococcus aureus α-toxin. Gen. Physiol. Biophys. 8:213-222.
    • (1989) Physiol. Biophys. , vol.8 , pp. 213-222
    • Krasilnikov, O.V.1    Sabirov, R.Z.2
  • 31
    • 0035025417 scopus 로고    scopus 로고
    • Location of a constriction in the lumen of a transmembrane pore by targeted covalent attachment of polymer molecules
    • Movileanu, L., S. Cheley, S. Howorka, O. Braha, and H. Bayley. 2001. Location of a constriction in the lumen of a transmembrane pore by targeted covalent attachment of polymer molecules. J. Gen. Physiol. 117:239-251.
    • (2001) J. Gen. Physiol. , vol.117 , pp. 239-251
    • Movileanu, L.1    Cheley, S.2    Howorka, S.3    Braha, O.4    Bayley, H.5
  • 32
    • 17744414381 scopus 로고
    • Properties of α-staphylotoxin-induced conductivity channels in bilayer phospholipid-membranes
    • Krasilnikov, O. V., V. I. Ternovsky, and B. A. Tashmukhamedov. 1981. Properties of α-staphylotoxin-induced conductivity channels in bilayer phospholipid-membranes. Biofizika. 26:271-276.
    • (1981) Biofizika , vol.26 , pp. 271-276
    • Krasilnikov, O.V.1    Ternovsky, V.I.2    Tashmukhamedov, B.A.3
  • 33
    • 0022504362 scopus 로고
    • Ionic channels formed by Staphylococcus aureus α-toxin: Voltage-dependent inhibition by divalent and trivalent cations
    • Menestrina, G. 1986. Ionic channels formed by Staphylococcus aureus α-toxin: voltage-dependent inhibition by divalent and trivalent cations. J. Membr. Biol. 90:177-190.
    • (1986) J. Membr. Biol. , vol.90 , pp. 177-190
    • Menestrina, G.1
  • 35
    • 0242301631 scopus 로고    scopus 로고
    • Electrostatic influence on ion transport through the α HL channel
    • Misakian, M., and J. J. Kasianowicz. 2003. Electrostatic influence on ion transport through the α HL channel. J. Membr. Biol. 195:137-146.
    • (2003) J. Membr. Biol. , vol.195 , pp. 137-146
    • Misakian, M.1    Kasianowicz, J.J.2
  • 36
    • 7244251461 scopus 로고    scopus 로고
    • Control of ion selectivity in potassium channels by electrostatic and dynamic properties of carbonyl ligands
    • Noskov, S. Y., S. Berneche, and B. Roux. 2004. Control of ion selectivity in potassium channels by electrostatic and dynamic properties of carbonyl ligands. Nature. 431:830-834.
    • (2004) Nature , vol.431 , pp. 830-834
    • Noskov, S.Y.1    Berneche, S.2    Roux, B.3
  • 37
    • 0030384264 scopus 로고    scopus 로고
    • Dynamics and free energy of polymers partitioning into a nanoscale pore
    • Bezrukov, S. M., I. Vodyanoy, R. A. Brutyan, and J. J. Kasianowicz. 1996. Dynamics and free energy of polymers partitioning into a nanoscale pore. Macromolecules. 29:8517-8522.
    • (1996) Macromolecules , vol.29 , pp. 8517-8522
    • Bezrukov, S.M.1    Vodyanoy, I.2    Brutyan, R.A.3    Kasianowicz, J.J.4
  • 38
    • 2042418523 scopus 로고    scopus 로고
    • Dynamic partitioning of neutral polymers into a single ion channel
    • J. J. Kasianowicz, M. S. Z. Kellermayer, and D. W. Deamer, editors. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Bezrukov, S. M., and J. J. Kasianowicz. 2002. Dynamic partitioning of neutral polymers into a single ion channel. In Structure and Dynamics of Confined Polymers. J. J. Kasianowicz, M. S. Z. Kellermayer, and D. W. Deamer, editors. Kluwer Academic Publishers, Dordrecht, The Netherlands. 117-130.
    • (2002) Structure and Dynamics of Confined Polymers , pp. 117-130
    • Bezrukov, S.M.1    Kasianowicz, J.J.2
  • 39
    • 16344384707 scopus 로고    scopus 로고
    • Polymer partitioning from nonideal solutions into protein voids
    • Krasilnikov, O. V., and S. M. Bezrukov. 2004. Polymer partitioning from nonideal solutions into protein voids. Macromolecules. 37:2650-2657.
    • (2004) Macromolecules , vol.37 , pp. 2650-2657
    • Krasilnikov, O.V.1    Bezrukov, S.M.2
  • 40
    • 2942571557 scopus 로고    scopus 로고
    • Nanopores: Flossing with DNA
    • Kasianowicz, J. J. 2004. Nanopores: flossing with DNA. Nat. Mater. 3:355-356.
    • (2004) Nat. Mater. , vol.3 , pp. 355-356
    • Kasianowicz, J.J.1
  • 41
    • 16344373084 scopus 로고    scopus 로고
    • Field-dependent effect of crown ether (18-crown-6) on ionic conductance of α-hemolysin channels
    • Bezrukov, S. M., O. V. Krasilnikov, L. N. Yuldasheva, A. M. Berezhkovskii, and C. G. Rodrigues. 2004. Field-dependent effect of crown ether (18-crown-6) on ionic conductance of α-hemolysin channels. Biophys. J. 87:3162-3171.
    • (2004) Biophys. J. , vol.87 , pp. 3162-3171
    • Bezrukov, S.M.1    Krasilnikov, O.V.2    Yuldasheva, L.N.3    Berezhkovskii, A.M.4    Rodrigues, C.G.5
  • 42
    • 0030710585 scopus 로고    scopus 로고
    • The charge state of an ion channel controls neutral polymer entry into its pore
    • Bezrukov, S. M., and J. J. Kasianowicz. 1997. The charge state of an ion channel controls neutral polymer entry into its pore. Eur. Biophys. J. 26:471-476.
    • (1997) Eur. Biophys. J. , vol.26 , pp. 471-476
    • Bezrukov, S.M.1    Kasianowicz, J.J.2
  • 43
    • 0026485739 scopus 로고
    • Acetylcholine-receptor channel structure probed in cysteine-substitution mutants
    • Akabas, M. H., D. A. Stauffer, M. Xu, and A. Karlin. 1992. Acetylcholine-receptor channel structure probed in cysteine-substitution mutants. Science. 258:307-310.
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 44
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties
    • Montal, M., and P. Mueller. 1972. Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties. Proc. Natl. Acad. Sci. USA. 69:3561-3566.
    • (1972) Proc. Natl. Acad. Sci. USA. , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 46
    • 0025774354 scopus 로고
    • Liquid junction potentials and small-cell effects in patch-clamp analysis
    • Barry, P. H., and J. W. Lynch. 1991. Liquid junction potentials and small-cell effects in patch-clamp analysis. J. Membr. Biol. 121:101-117.
    • (1991) J. Membr. Biol. , vol.121 , pp. 101-117
    • Barry, P.H.1    Lynch, J.W.2
  • 47
    • 0028895922 scopus 로고
    • The measurement of ionic conductivities and mobilities of certain less common organic ions needed for junction potential corrections in electrophysiology
    • Ng, B., and P. H. Barry. 1995. The measurement of ionic conductivities and mobilities of certain less common organic ions needed for junction potential corrections in electrophysiology. J. Neurosci. Methods. 56:37-41.
    • (1995) J. Neurosci. Methods. , vol.56 , pp. 37-41
    • Ng, B.1    Barry, P.H.2
  • 48
    • 0030970096 scopus 로고    scopus 로고
    • Staphylococcal α-toxin: The role of the N-terminus in formation of the heptameric pore-a fluorescence study
    • Valeva, A., J. Pongs, S. Bhakdi, and M. Palmer. 1997. Staphylococcal α-toxin: the role of the N-terminus in formation of the heptameric pore-a fluorescence study. Biochim. Biophys. Acta. 1325:281-286.
    • (1997) Biochim. Biophys. Acta. , vol.1325 , pp. 281-286
    • Valeva, A.1    Pongs, J.2    Bhakdi, S.3    Palmer, M.4
  • 49
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., and M. C. Peitsch. 1997. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis. 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 50
    • 0014713619 scopus 로고
    • Ion flux across lipid bilayer membranes with charged surfaces
    • Neumcke, B. 1970. Ion flux across lipid bilayer membranes with charged surfaces. Biophysik. 6:231-240.
    • (1970) Biophysik , vol.6 , pp. 231-240
    • Neumcke, B.1
  • 52
    • 0021309504 scopus 로고
    • Effects of phospholipid surface-charge on ion conduction in the K+ channel of sarcoplasmic-reticulum
    • Bell, J. E., and C. Miller. 1984. Effects of phospholipid surface-charge on ion conduction in the K+ channel of sarcoplasmic-reticulum. Biophys. J. 45:279-287.
    • (1984) Biophys. J. , vol.45 , pp. 279-287
    • Bell, J.E.1    Miller, C.2
  • 53
    • 0030975688 scopus 로고    scopus 로고
    • Influence of Cys-130 S-aureus α-toxin on planar lipid bilayer and erythrocyte membranes
    • Krasilnikov, O. V., M. F. P. Capistrano, L. N. Yuldasheva, and R. A. Nogueira. 1997. Influence of Cys-130 S-aureus α-toxin on planar lipid bilayer and erythrocyte membranes. J. Membr. Biol. 156:157-172.
    • (1997) J. Membr. Biol. , vol.156 , pp. 157-172
    • Krasilnikov, O.V.1    Capistrano, M.F.P.2    Yuldasheva, L.N.3    Nogueira, R.A.4
  • 54
    • 0024119703 scopus 로고
    • Influence of pH on the potential-dependence of Staphylococcal toxin channels functioning in phosphatidylcholine bilayer
    • Krasilnikov, O. V., P. G. Merzlyak, R. Z. Sabirov, V. I. Ternovsky, and R. K. Zaripova. 1988. Influence of pH on the potential-dependence of Staphylococcal toxin channels functioning in phosphatidylcholine bilayer. Ukr. Biokhim. Zh. 60:60-66.
    • (1988) Ukr. Biokhim. Zh. , vol.60 , pp. 60-66
    • Krasilnikov, O.V.1    Merzlyak, P.G.2    Sabirov, R.Z.3    Ternovsky, V.I.4    Zaripova, R.K.5
  • 55
    • 0030708510 scopus 로고    scopus 로고
    • The hinge portion of the S. aureus α-toxin crosses the lipid bilayer and is part of the trans-mouth of the channel
    • Krasilnikov, O. V., L. N. Yuldasheva, P. G. Merzlyak, M. F. P. Capistrano, and R. A. Nogueira. 1997. The hinge portion of the S. aureus α-toxin crosses the lipid bilayer and is part of the trans-mouth of the channel. Biochim. Biophys. Acta. 1329:51-60.
    • (1997) Biochim. Biophys. Acta. , vol.1329 , pp. 51-60
    • Krasilnikov, O.V.1    Yuldasheva, L.N.2    Merzlyak, P.G.3    Capistrano, M.F.P.4    Nogueira, R.A.5
  • 59
    • 0034680253 scopus 로고    scopus 로고
    • Determination of the pK(a) value of C115 in MurA (UDP-N-acetylglucosamine enolpyruvyltransferase) from Enterobacter cloacae
    • Krekel, F., A. K. Samland, P. Macheroux, N. Amrhein, and J. N. S. Evans. 2000. Determination of the pK(a) value of C115 in MurA (UDP-N-acetylglucosamine enolpyruvyltransferase) from Enterobacter cloacae. Biochemistry. 39:12671-12677.
    • (2000) Biochemistry , vol.39 , pp. 12671-12677
    • Krekel, F.1    Samland, A.K.2    Macheroux, P.3    Amrhein, N.4    Evans, J.N.S.5
  • 60
    • 0029924449 scopus 로고    scopus 로고
    • Molecular architecture of a toxin pore: A 15-residue sequence lines the transmembrane channel of Staphylococcal α-toxin
    • Valeva, A., A. Weisser, B. Walker, M. Kehoe, H. Bayley, S. Bhakdi, and M. Palmer. 1996. Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of Staphylococcal α-toxin. EMBO J. 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


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