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Volumn 10, Issue 1, 1999, Pages 94-103

Designed membrane channels and pores

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 0032921876     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(99)80017-2     Document Type: Article
Times cited : (82)

References (72)
  • 2
    • 0029150299 scopus 로고
    • Design of molecular function: Channels of communication
    • Montal M Design of molecular function: channels of communication. Annu Rev Biophys Biomol Struct. 24:1995;31-57.
    • (1995) Annu Rev Biophys Biomol Struct , vol.24 , pp. 31-57
    • Montal, M.1
  • 4
    • 0031902085 scopus 로고    scopus 로고
    • Protein design - On the threshold of functional properties
    • A useful overview of the TASP (template-assisted synthetic protein) approach to protein design and assembly, including some comments on applications to channel proteins. TASP methodology has the potential to define and orient transmembrane structures more precisely than can be done by relying upon the spontaneous oligomerization of short membrane-active peptides.
    • Tuchscherer G, Scheibler L, Dumy P, Mutter M Protein design - on the threshold of functional properties. Biopolymers. 47:1998;63-73. A useful overview of the TASP (template-assisted synthetic protein) approach to protein design and assembly, including some comments on applications to channel proteins. TASP methodology has the potential to define and orient transmembrane structures more precisely than can be done by relying upon the spontaneous oligomerization of short membrane-active peptides.
    • (1998) Biopolymers , vol.47 , pp. 63-73
    • Tuchscherer, G.1    Scheibler, L.2    Dumy, P.3    Mutter, M.4
  • 5
    • 0027403316 scopus 로고
    • Design, synthesis and functional characterization of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor
    • Montal MO, Iwamoto T, Tomich JM, Montal M Design, synthesis and functional characterization of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor. FEBS Lett. 320:1993;261-266.
    • (1993) FEBS Lett , vol.320 , pp. 261-266
    • Montal, M.O.1    Iwamoto, T.2    Tomich, J.M.3    Montal, M.4
  • 6
    • 0028127099 scopus 로고
    • Template-assembled melittin: Structural and functional characterization of a designed, synthetic channel-forming protein
    • Pawlak M, Meseth U, Dhanapal B, Mutter M, Vogel H Template-assembled melittin: structural and functional characterization of a designed, synthetic channel-forming protein. Protein Sci. 3:1994;1788-1805.
    • (1994) Protein Sci , vol.3 , pp. 1788-1805
    • Pawlak, M.1    Meseth, U.2    Dhanapal, B.3    Mutter, M.4    Vogel, H.5
  • 7
    • 1842555216 scopus 로고    scopus 로고
    • Ion channels of cyclic template-assembled alamethicins that emulate the pore structure predicted by the barrel stave model
    • Matsubara A, Asami K, Akagi A, Nishino N: Ion channels of cyclic template-assembled alamethicins that emulate the pore structure predicted by the barrel stave model. J Chem Soc Chem Commun 1996, 2069-2070.
    • (1996) J Chem Soc Chem Commun , pp. 2069-2070
    • Matsubara, A.1    Asami, K.2    Akagi, A.3    Nishino, N.4
  • 10
    • 0030964855 scopus 로고    scopus 로고
    • De novo design, synthesis, and characterization of a pore-forming small globular protein and its insertion into lipid bilayers
    • A 69 amino acid four-helix bundle, in which a hydrophobic helix is surrounded by three others, was synthesized following a design loosely based on the structures of channel-forming bacterial colicins. The polypeptide, which is a globular monomer in solution, assembles into membranes to form low conductance channels. Further progress in this area will require definitive structural information on both the water-soluble and assembled forms of the protein.
    • Lee S, Kiyota T, Kunitake T, Matsumoto E, Yamashita S, Anzai K, Sugihara G De novo design, synthesis, and characterization of a pore-forming small globular protein and its insertion into lipid bilayers. Biochemistry. 36:1997;3782-3791. A 69 amino acid four-helix bundle, in which a hydrophobic helix is surrounded by three others, was synthesized following a design loosely based on the structures of channel-forming bacterial colicins. The polypeptide, which is a globular monomer in solution, assembles into membranes to form low conductance channels. Further progress in this area will require definitive structural information on both the water-soluble and assembled forms of the protein.
    • (1997) Biochemistry , vol.36 , pp. 3782-3791
    • Lee, S.1    Kiyota, T.2    Kunitake, T.3    Matsumoto, E.4    Yamashita, S.5    Anzai, K.6    Sugihara, G.7
  • 11
    • 0031857720 scopus 로고    scopus 로고
    • Peptide nanotubes and beyond
    • A review of recent progress on nanotubes based on cyclic peptides, which self assemble in lipid bilayers in a predictable way to form well-defined transmembrane channels. The first examples contained an even number of alternating D- and L-α-amino acids. Recently, cyclic β peptides have been used to make a new class of nanotubes.
    • Hartgerink JD, Clark TD, Ghadiri MR Peptide nanotubes and beyond. Chem Eur J. 4:1998;1367-1372. A review of recent progress on nanotubes based on cyclic peptides, which self assemble in lipid bilayers in a predictable way to form well-defined transmembrane channels. The first examples contained an even number of alternating D- and L-α-amino acids. Recently, cyclic β peptides have been used to make a new class of nanotubes.
    • (1998) Chem Eur J , vol.4 , pp. 1367-1372
    • Hartgerink, J.D.1    Clark, T.D.2    Ghadiri, M.R.3
  • 12
  • 13
    • 0346249753 scopus 로고    scopus 로고
    • Electrical activity of artificial ion channels incorporated into planar lipid bilayers
    • Voyer N, Potvin L, Rousseau E: Electrical activity of artificial ion channels incorporated into planar lipid bilayers. J Chem Soc Perkin Trans 2 1997, 1469-1471.
    • (1997) J Chem Soc Perkin Trans 2 , pp. 1469-1471
    • Voyer, N.1    Potvin, L.2    Rousseau, E.3
  • 14
    • 0030905756 scopus 로고    scopus 로고
    • A synthetic transmembrane ion channel active in lipid bilayers
    • Meillon JC, Voyer N A synthetic transmembrane ion channel active in lipid bilayers. Angew Chem Int Ed Engl. 36:1997;967-969.
    • (1997) Angew Chem Int Ed Engl , vol.36 , pp. 967-969
    • Meillon, J.C.1    Voyer, N.2
  • 16
    • 0032478974 scopus 로고    scopus 로고
    • Importance of tryptophan dipoles for protein function - 5-fluorination of tryptophans in gramicidin A channels
    • Andersen OS, Greathouse DV, Providence LL, Becker MD, Koeppe RE Importance of tryptophan dipoles for protein function - 5-fluorination of tryptophans in gramicidin A channels. J Am Chem Soc. 120:1998;5142-5146.
    • (1998) J Am Chem Soc , vol.120 , pp. 5142-5146
    • Andersen, O.S.1    Greathouse, D.V.2    Providence, L.L.3    Becker, M.D.4    Koeppe, R.E.5
  • 17
    • 0001630589 scopus 로고
    • Characterization of thermal isomerization at the single molecule level
    • Jaikaran DCJ, Woolley GA Characterization of thermal isomerization at the single molecule level. J Phys Chem. 99:1995;13352-13355.
    • (1995) J Phys Chem , vol.99 , pp. 13352-13355
    • Jaikaran, D.C.J.1    Woolley, G.A.2
  • 20
    • 0031194564 scopus 로고    scopus 로고
    • Designed protein pores as components for biosensors
    • An engineered staphylococcal α-hemolysin is described with a divalent metal cation binding site in the lumen of the transmembrane channel. By exploiting single-channel recording, the designed pore can be used as an element in a stochastic sensor, which both identifies metal ions and quantitates them. The paper also introduces technology for purifying hetero-oligomeric channels and pores.
    • Braha O, Walker B, Cheley S, Kasianowicz JJ, Song L, Gouaux JE, Bayley H Designed protein pores as components for biosensors. Chem Biol. 4:1997;497-505. An engineered staphylococcal α-hemolysin is described with a divalent metal cation binding site in the lumen of the transmembrane channel. By exploiting single-channel recording, the designed pore can be used as an element in a stochastic sensor, which both identifies metal ions and quantitates them. The paper also introduces technology for purifying hetero-oligomeric channels and pores.
    • (1997) Chem Biol , vol.4 , pp. 497-505
    • Braha, O.1    Walker, B.2    Cheley, S.3    Kasianowicz, J.J.4    Song, L.5    Gouaux, J.E.6    Bayley, H.7
  • 21
    • 0031853989 scopus 로고    scopus 로고
    • Porin mutants with new channel properties
    • Mutations in a porin from Rhodopseudomonas blastica are described, which affect single channel conductance. The crystal structures of many of the new proteins are described, putting the analysis of their functional properties on far more solid ground than is usual.
    • Schmid B, Maveyraud L, Kromer M, Schulz GE Porin mutants with new channel properties. Protein Sci. 7:1998;1603-1611. Mutations in a porin from Rhodopseudomonas blastica are described, which affect single channel conductance. The crystal structures of many of the new proteins are described, putting the analysis of their functional properties on far more solid ground than is usual.
    • (1998) Protein Sci , vol.7 , pp. 1603-1611
    • Schmid, B.1    Maveyraud, L.2    Kromer, M.3    Schulz, G.E.4
  • 23
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside living cells
    • A paper that will make us think anew about the targeted modification of proteins, including channels and pores. Methods that go beyond single-cysteine modification are needed. This paper presents one possibility, two-pronged trivalent arsenic reagents directed at tetracysteine motifs, and may stimulate renewed effort in this area.
    • Griffin BA, Adams SR, Tsien RY Specific covalent labeling of recombinant protein molecules inside living cells. Science. 281:1998;269-272. A paper that will make us think anew about the targeted modification of proteins, including channels and pores. Methods that go beyond single-cysteine modification are needed. This paper presents one possibility, two-pronged trivalent arsenic reagents directed at tetracysteine motifs, and may stimulate renewed effort in this area.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 24
    • 0030895628 scopus 로고    scopus 로고
    • Caged cysteine and thiophosphoryl peptides
    • Pan P, Bayley H Caged cysteine and thiophosphoryl peptides. FEBS Lett. 405:1997;81-85.
    • (1997) FEBS Lett , vol.405 , pp. 81-85
    • Pan, P.1    Bayley, H.2
  • 25
    • 0031260274 scopus 로고    scopus 로고
    • Site-specific incorporation of biotinylated amino acids to identify surface-exposed residues in integral membrane proteins
    • Gallivan JP, Lester HA, Dougherty DA Site-specific incorporation of biotinylated amino acids to identify surface-exposed residues in integral membrane proteins. Chem Biol. 4:1997;739-749.
    • (1997) Chem Biol , vol.4 , pp. 739-749
    • Gallivan, J.P.1    Lester, H.A.2    Dougherty, D.A.3
  • 26
    • 0032055921 scopus 로고    scopus 로고
    • Flash decaging of tyrosine sidechains in an ion channel
    • In this and related papers, the Caltech researchers apply non-natural amino acid mutagenesis to make modified eukaryotic ion channels in oocytes. Here, tyrosine with a photoremovable protecting group is introduced at a key position in the a subunit of the ligand-gated acetylcholine receptor, producing a channel protein that can be activated by light. Similar technology might be applied to the in vitro synthesis of a variety of modified channels and pores.
    • Miller JC, Silverman SK, England PM, Dougherty DA, Lester HA Flash decaging of tyrosine sidechains in an ion channel. Neuron. 20:1998;619-624. In this and related papers, the Caltech researchers apply non-natural amino acid mutagenesis to make modified eukaryotic ion channels in oocytes. Here, tyrosine with a photoremovable protecting group is introduced at a key position in the a subunit of the ligand-gated acetylcholine receptor, producing a channel protein that can be activated by light. Similar technology might be applied to the in vitro synthesis of a variety of modified channels and pores.
    • (1998) Neuron , vol.20 , pp. 619-624
    • Miller, J.C.1    Silverman, S.K.2    England, P.M.3    Dougherty, D.A.4    Lester, H.A.5
  • 28
    • 0031322936 scopus 로고    scopus 로고
    • Biosynthetic systems for nonribosomal antibiotic assembly
    • Mootz HD, Marahiel MA Biosynthetic systems for nonribosomal antibiotic assembly. Curr Opin Chem Biol. 1:1997;543-551.
    • (1997) Curr Opin Chem Biol , vol.1 , pp. 543-551
    • Mootz, H.D.1    Marahiel, M.A.2
  • 29
    • 0032475992 scopus 로고    scopus 로고
    • Harnessing the biosynthetic code-combinations, permutations, and mutations
    • Hybrid modular synthetases have been heavily exploited for the synthesis of various natural products, especially the polyketides. It is possible that a vast array of channel-forming peptides could be produced by similar means.
    • Cane DE, Walsh CT, Khosla C Harnessing the biosynthetic code-combinations, permutations, and mutations. Science. 282:1998;63-68. Hybrid modular synthetases have been heavily exploited for the synthesis of various natural products, especially the polyketides. It is possible that a vast array of channel-forming peptides could be produced by similar means.
    • (1998) Science , vol.282 , pp. 63-68
    • Cane, D.E.1    Walsh, C.T.2    Khosla, C.3
  • 31
    • 0001073480 scopus 로고
    • Supramolecular design by covalent capture. Design of a peptide cylinder via hydrogen-bond-promoted intermolecular olefin metathesis
    • Clark TD, Ghadiri MR Supramolecular design by covalent capture. Design of a peptide cylinder via hydrogen-bond-promoted intermolecular olefin metathesis. J Am Chem Soc. 117:1995;12364-12365.
    • (1995) J Am Chem Soc , vol.117 , pp. 12364-12365
    • Clark, T.D.1    Ghadiri, M.R.2
  • 32
    • 0031434205 scopus 로고    scopus 로고
    • Non-native architectures in protein design and mimicry
    • Mutter M, Tuchscherer G Non-native architectures in protein design and mimicry. Cellular Molec Life Sci. 53:1997;851-863.
    • (1997) Cellular Molec Life Sci , vol.53 , pp. 851-863
    • Mutter, M.1    Tuchscherer, G.2
  • 33
    • 0030867021 scopus 로고    scopus 로고
    • Assembling of the four individual helices corresponding to the transmembrane segments (S4 in repeats I-IV) of the sodium channel
    • Four different synthetic helices based on sodium channel sequences were attached at specific positions to a peptide template. The assembled helices exhibited channel activity; however, it is unlikely that this results from any resemblance to the natural channel structure. At this stage, the work is most notable for the synthetic methodology, which might be further exploited with respect for new knowledge about channel structure and function.
    • Futaki S, Aoki M, Fukuda M, Kondo F, Niwa M, Kitagawa K, Nakaya Y Assembling of the four individual helices corresponding to the transmembrane segments (S4 in repeats I-IV) of the sodium channel. Tetrahedron Lett. 38:1997;7071-7074. Four different synthetic helices based on sodium channel sequences were attached at specific positions to a peptide template. The assembled helices exhibited channel activity; however, it is unlikely that this results from any resemblance to the natural channel structure. At this stage, the work is most notable for the synthetic methodology, which might be further exploited with respect for new knowledge about channel structure and function.
    • (1997) Tetrahedron Lett , vol.38 , pp. 7071-7074
    • Futaki, S.1    Aoki, M.2    Fukuda, M.3    Kondo, F.4    Niwa, M.5    Kitagawa, K.6    Nakaya, Y.7
  • 34
    • 0032932083 scopus 로고    scopus 로고
    • Crystal structure of staphyococcal lukF delineates conformational changes accompanying formation of a transmembrane channel
    • in press. LukF is homologous to staphylococcal α-hemolysin, for which the structure of the fully assembled heptameric transmembrane pore has been determined. Therefore, this structure of a water-soluble monomer provides insight into the assembly process with atomic detail. Information such as this is invaluable for the rational design of self assembling channels and pores
    • Olson R, Nariya H, Yokota K, Kamio Y, Gouaux E: Crystal structure of staphyococcal lukF delineates conformational changes accompanying formation of a transmembrane channel. Nat Struct Biol 1999, in press. LukF is homologous to staphylococcal α-hemolysin, for which the structure of the fully assembled heptameric transmembrane pore has been determined. Therefore, this structure of a water-soluble monomer provides insight into the assembly process with atomic detail. Information such as this is invaluable for the rational design of self assembling channels and pores.
    • (1999) Nat Struct Biol
    • Olson, R.1    Nariya, H.2    Yokota, K.3    Kamio, Y.4    Gouaux, E.5
  • 35
    • 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. 15:1996;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
  • 36
    • 0031404458 scopus 로고    scopus 로고
    • Spontaneous oligomerization of a staphylococcal α-hemolysin conformationally constrained by removal of residues that form the transmembrane β barrel
    • Cheley S, Malghani MS, Song L, Hobaugh M, Gouaux JE, Yang J, Bayley H Spontaneous oligomerization of a staphylococcal α-hemolysin conformationally constrained by removal of residues that form the transmembrane β barrel. Protein Eng. 10:1997;1433-1443.
    • (1997) Protein Eng , vol.10 , pp. 1433-1443
    • Cheley, S.1    Malghani, M.S.2    Song, L.3    Hobaugh, M.4    Gouaux, J.E.5    Yang, J.6    Bayley, H.7
  • 37
    • 0030974351 scopus 로고    scopus 로고
    • Electrostatic effects on ion selectivity and rectification in designed ion channel peptides
    • Lear JD, Schneider JP, Kienker PK, DeGrado WF Electrostatic effects on ion selectivity and rectification in designed ion channel peptides. J Am Chem Soc. 119:1997;3212-3217.
    • (1997) J Am Chem Soc , vol.119 , pp. 3212-3217
    • Lear, J.D.1    Schneider, J.P.2    Kienker, P.K.3    Degrado, W.F.4
  • 39
    • 0031554429 scopus 로고    scopus 로고
    • A biosensor that uses ion-channel switches
    • Tethered supported bilayers containing the channel-forming gramicidin A peptide have been made that respond to large and small analytes, which alter the density of open channels. It has proved difficult to place functional channels in supported bilayers and the work is distinguished in this regard. However, while the devices are robust, versatile and highly sensitive, they are complex assemblies, which would benefit from simplification.
    • Cornell BA, Braach-Maksvytis VLB, King LG, Osman PDJ, Raguse B, Wieczorek L, Pace RJ A biosensor that uses ion-channel switches. Nature. 387:1997;580-583. Tethered supported bilayers containing the channel-forming gramicidin A peptide have been made that respond to large and small analytes, which alter the density of open channels. It has proved difficult to place functional channels in supported bilayers and the work is distinguished in this regard. However, while the devices are robust, versatile and highly sensitive, they are complex assemblies, which would benefit from simplification.
    • (1997) Nature , vol.387 , pp. 580-583
    • Cornell, B.A.1    Braach-Maksvytis, V.L.B.2    King, L.G.3    Osman, P.D.J.4    Raguse, B.5    Wieczorek, L.6    Pace, R.J.7
  • 40
    • 0030569732 scopus 로고    scopus 로고
    • Supported membranes: Scientific and practical applications
    • Sackmann E Supported membranes: scientific and practical applications. Science. 271:1996;43-48.
    • (1996) Science , vol.271 , pp. 43-48
    • Sackmann, E.1
  • 41
    • 0032070193 scopus 로고    scopus 로고
    • Impedance spectroscopy of porin and gramicidin pores reconstituted into supported bilayers on indium-tin-oxide electrodes
    • Gritsch S, Nollert P, Jähnig F, Sackmann E Impedance spectroscopy of porin and gramicidin pores reconstituted into supported bilayers on indium-tin-oxide electrodes. Langmuir. 14:1998;3118-3125.
    • (1998) Langmuir , vol.14 , pp. 3118-3125
    • Gritsch, S.1    Nollert, P.2    Jähnig, F.3    Sackmann, E.4
  • 43
    • 0032513708 scopus 로고    scopus 로고
    • Oriented self-assembly of cyclic peptide nanotubes in lipid membranes
    • Kim HS, Hartgerink JD, Ghadiri MR Oriented self-assembly of cyclic peptide nanotubes in lipid membranes. J Am Chem Soc. 120:1998;4417-4424.
    • (1998) J Am Chem Soc , vol.120 , pp. 4417-4424
    • Kim, H.S.1    Hartgerink, J.D.2    Ghadiri, M.R.3
  • 44
    • 1842410757 scopus 로고    scopus 로고
    • Diffusion-limited size-selective ion sensing based on SAM-supported peptide nanotubes
    • Peptide nanotubes were incorporated into monolayers supported on a gold surface. The 7.5 Å diameter of the channels dictated the accessibility of the gold surface to electroactive ions. The work therefore forms the basis of a rugged sensor based on size selectivity as well as electrochemistry.
    • Motesharei K, Ghadiri MR Diffusion-limited size-selective ion sensing based on SAM-supported peptide nanotubes. J Am Chem Soc. 119:1997;11306-11312. Peptide nanotubes were incorporated into monolayers supported on a gold surface. The 7.5 Å diameter of the channels dictated the accessibility of the gold surface to electroactive ions. The work therefore forms the basis of a rugged sensor based on size selectivity as well as electrochemistry.
    • (1997) J Am Chem Soc , vol.119 , pp. 11306-11312
    • Motesharei, K.1    Ghadiri, M.R.2
  • 45
    • 0032513080 scopus 로고    scopus 로고
    • Self-assembled α-hemolysin pores in an S-layer supported lipid bilayer
    • Planar bilayers were supported by S layers, which are two-dimensional porous crystalline arrays of protein that envelope many bacteria. Functional pores were subsequently assembled into the bilayers. Although this is a promising approach, further development is required to determine whether it can compete with conventional means for bilayer stabilization.
    • Schuster B, Pum D, Braha O, Bayley H, Sleytr UB Self-assembled α-hemolysin pores in an S-layer supported lipid bilayer. Biochim Biophys Acta. 1370:1998;280-288. Planar bilayers were supported by S layers, which are two-dimensional porous crystalline arrays of protein that envelope many bacteria. Functional pores were subsequently assembled into the bilayers. Although this is a promising approach, further development is required to determine whether it can compete with conventional means for bilayer stabilization.
    • (1998) Biochim Biophys Acta , vol.1370 , pp. 280-288
    • Schuster, B.1    Pum, D.2    Braha, O.3    Bayley, H.4    Sleytr, U.B.5
  • 46
    • 0032472790 scopus 로고    scopus 로고
    • Voltage clamp studies on S-layer supported tetraether lipid membranes
    • Schuster B, Pum D, Sleytr UB Voltage clamp studies on S-layer supported tetraether lipid membranes. Biochim Biophys Acta. 1369:1998;51-60.
    • (1998) Biochim Biophys Acta , vol.1369 , pp. 51-60
    • Schuster, B.1    Pum, D.2    Sleytr, U.B.3
  • 47
    • 0027954789 scopus 로고
    • Channel-mediated transport of glucose across lipid bilayers
    • Granja JR, Ghadiri MR Channel-mediated transport of glucose across lipid bilayers. J Am Chem Soc. 116:1994;10785-10786.
    • (1994) J Am Chem Soc , vol.116 , pp. 10785-10786
    • Granja, J.R.1    Ghadiri, M.R.2
  • 48
    • 0031229957 scopus 로고    scopus 로고
    • Building doors into cells
    • A brief overview of work on staphylococcal α-hemolysin with built-in triggers and switches.
    • Bayley H Building doors into cells. Sci Am. 277:1997;62-67. A brief overview of work on staphylococcal α-hemolysin with built-in triggers and switches.
    • (1997) Sci Am , vol.277 , pp. 62-67
    • Bayley, H.1
  • 49
    • 0029941746 scopus 로고    scopus 로고
    • Tumor protease-activated, pore-forming toxins from a combinatorial library
    • Panchal RG, Cusack E, Cheley S, Bayley H Tumor protease-activated, pore-forming toxins from a combinatorial library. Nat Biotechnol. 14:1996;852-856.
    • (1996) Nat Biotechnol , vol.14 , pp. 852-856
    • Panchal, R.G.1    Cusack, E.2    Cheley, S.3    Bayley, H.4
  • 50
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song L, Hobaugh MR, Shustak C, Cheley S, Bayley H, Gouaux JE Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science. 274:1996;1859-1865.
    • (1996) Science , vol.274 , pp. 1859-1865
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 51
    • 0029240394 scopus 로고
    • An intermediate in the assembly of a pore-forming protein trapped with a genetically engineered switch
    • Walker B, Braha O, Cheley S, Bayley H An intermediate in the assembly of a pore-forming protein trapped with a genetically engineered switch. Chem Biol. 2:1995;99-105.
    • (1995) Chem Biol , vol.2 , pp. 99-105
    • Walker, B.1    Braha, O.2    Cheley, S.3    Bayley, H.4
  • 52
    • 33748241762 scopus 로고    scopus 로고
    • Control of the structure and functions of biomaterials by light
    • Willner I, Shai R Control of the structure and functions of biomaterials by light. Angew Chem Int Ed Engl. 35:1996;367-385.
    • (1996) Angew Chem Int Ed Engl , vol.35 , pp. 367-385
    • Willner, I.1    Shai, R.2
  • 53
    • 0032987931 scopus 로고    scopus 로고
    • Genetically engineered metal ion binding sites on the outside of a channel's transmembrane β barrel
    • in press
    • Kasianowicz JJ, Burden DL, Han LC, Cheley S, Bayley H: Genetically engineered metal ion binding sites on the outside of a channel's transmembrane β barrel. Biophys J 1999, in press.
    • (1999) Biophys J
    • Kasianowicz, J.J.1    Burden, D.L.2    Han, L.C.3    Cheley, S.4    Bayley, H.5
  • 54
    • 0029788128 scopus 로고    scopus 로고
    • A chemical-detecting system based on a cross-reactive optical sensor array
    • Dickinson TA, White J, Kauer JS, Walt DR A chemical-detecting system based on a cross-reactive optical sensor array. Nature. 382:1996;687-700.
    • (1996) Nature , vol.382 , pp. 687-700
    • Dickinson, T.A.1    White, J.2    Kauer, J.S.3    Walt, D.R.4
  • 56
    • 0000379657 scopus 로고    scopus 로고
    • Fiber optic imaging sensors
    • A great deal of the potential in sensor technology is in microarrays of sensor elements. Here, technologies using fluorescence detection are described. Sensors based on designed channels and pores could be made considerably more powerful by employing related approaches.
    • Walt D Fiber optic imaging sensors. Acc Chem Res. 31:1998;267-278. A great deal of the potential in sensor technology is in microarrays of sensor elements. Here, technologies using fluorescence detection are described. Sensors based on designed channels and pores could be made considerably more powerful by employing related approaches.
    • (1998) Acc Chem Res , vol.31 , pp. 267-278
    • Walt, D.1
  • 57
    • 0027183815 scopus 로고
    • A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes
    • Bhakdi S, Weller U, Walev I, Martin E, Jonas D, Palmer M A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes. Med Microbiol Immunol. 182:1993;167-175.
    • (1993) Med Microbiol Immunol , vol.182 , pp. 167-175
    • Bhakdi, S.1    Weller, U.2    Walev, I.3    Martin, E.4    Jonas, D.5    Palmer, M.6
  • 58
    • 0030942859 scopus 로고    scopus 로고
    • Reversible permeabilization of plasma membranes with an engineered switchable pore
    • The first example of what might prove to be an important application of pore-forming proteins with built-in switches: the reversible permeabilization of cells. Here a staphylococcal α-hemolysin regulated by divalent metal ions is used. Applications in basic science, especially cell biology, and biotechnology (e.g. cryoprotection) are anticipated.
    • Russo MJ, Bayley H, Toner M Reversible permeabilization of plasma membranes with an engineered switchable pore. Nat Biotechnol. 15:1997;278-282. The first example of what might prove to be an important application of pore-forming proteins with built-in switches: the reversible permeabilization of cells. Here a staphylococcal α-hemolysin regulated by divalent metal ions is used. Applications in basic science, especially cell biology, and biotechnology (e.g. cryoprotection) are anticipated.
    • (1997) Nat Biotechnol , vol.15 , pp. 278-282
    • Russo, M.J.1    Bayley, H.2    Toner, M.3
  • 59
    • 0032411644 scopus 로고    scopus 로고
    • Phosphorylation of photolyzed rhodopsin is calcium-insensitive in retina permeabilized by α-toxin
    • Otto-Bruc AE, Fariss RN, Van Hooser JP, Palczewski K Phosphorylation of photolyzed rhodopsin is calcium-insensitive in retina permeabilized by α-toxin. Proc Natl Acad Sci USA. 95:1998;15014-15019.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15014-15019
    • Otto-Bruc, A.E.1    Fariss, R.N.2    Van Hooser, J.P.3    Palczewski, K.4
  • 60
    • 0031457628 scopus 로고    scopus 로고
    • Toxin structure: Part of a hole?
    • Bayley H Toxin structure: part of a hole? Current Biol. 7:1997;R763-R767.
    • (1997) Current Biol , vol.7
    • Bayley, H.1
  • 61
    • 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
    • Palmer M, Harris R, Freytag C, Kehoe M, Tranum-Jensen J, Bhakdi S 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. 17:1998;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
  • 62
    • 0029257531 scopus 로고
    • Biochemical and cytotoxic properties of conjugates of transferrin with equinatoxin II, a cytolysin from a sea anemone
    • Pederzolli C, Belmonte G, Serra MD, Macek P, Menestrina G Biochemical and cytotoxic properties of conjugates of transferrin with equinatoxin II, a cytolysin from a sea anemone. Bioconjugate Chem. 6:1995;166-173.
    • (1995) Bioconjugate Chem , vol.6 , pp. 166-173
    • Pederzolli, C.1    Belmonte, G.2    Serra, M.D.3    Macek, P.4    Menestrina, G.5
  • 63
    • 0030197995 scopus 로고    scopus 로고
    • Cell targeting of a pore-forming toxin, CytA δ-endotoxin from Bacillus thuringiensis subspecies israelensis, by conjugating CytA with anti-Thy1 monoclonal antibodies and insulin
    • Al-yahyaee SAS, Ellar DJ Cell targeting of a pore-forming toxin, CytA δ-endotoxin from Bacillus thuringiensis subspecies israelensis, by conjugating CytA with anti-Thy1 monoclonal antibodies and insulin. Bioconjugate Chem. 7:1996;451-460.
    • (1996) Bioconjugate Chem , vol.7 , pp. 451-460
    • Al-Yahyaee, S.A.S.1    Ellar, D.J.2
  • 65
    • 0030465241 scopus 로고    scopus 로고
    • Characterization of individual polynucleotide molecules using a membrane channel
    • Kasianowicz JJ, Brandin E, Branton D, Deamer DW Characterization of individual polynucleotide molecules using a membrane channel. Proc Natl Acad Sci USA. 93:1996;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
  • 66
    • 0343145679 scopus 로고    scopus 로고
    • Bacterial and archaeal S-layer proteins: Structure-function relationships and their biotechnological applications
    • Sleytr UB, Sára M Bacterial and archaeal S-layer proteins: structure-function relationships and their biotechnological applications. Trends Biotechnol. 15:1997;20-26.
    • (1997) Trends Biotechnol , vol.15 , pp. 20-26
    • Sleytr, U.B.1    Sára, M.2
  • 67
    • 0032067947 scopus 로고    scopus 로고
    • Ferrying proteins to the other side
    • Peptides and proteins that ferry cargoes, including other proteins and nucleic acids, into cells have received considerable attention in the past year. Applications in basic science and biotechnology, such as drug delivery, are immediately apparent. Designers of self assembling channels and pores might contribute in this area; the ferry proteins assemble into bilayers, but also exit the bilayer on the far side.
    • Fernandez T, Bayley H Ferrying proteins to the other side. Nat Biotechnol. 16:1998;418-420. Peptides and proteins that ferry cargoes, including other proteins and nucleic acids, into cells have received considerable attention in the past year. Applications in basic science and biotechnology, such as drug delivery, are immediately apparent. Designers of self assembling channels and pores might contribute in this area; the ferry proteins assemble into bilayers, but also exit the bilayer on the far side.
    • (1998) Nat Biotechnol , vol.16 , pp. 418-420
    • Fernandez, T.1    Bayley, H.2
  • 68
    • 0023645080 scopus 로고
    • Tinkering with enzymes: What are we learning?
    • Knowles JR Tinkering with enzymes: what are we learning? Science. 236:1987;1252-1258.
    • (1987) Science , vol.236 , pp. 1252-1258
    • Knowles, J.R.1
  • 69
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • See note added in proof.
    • Locher KP, Rees B, Koebnik R, Mitschler A, Moulinier L, Rosenbusch JP, Moras D Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell. 95:1998;771-778. See note added in proof.
    • (1998) Cell , vol.95 , pp. 771-778
    • Locher, K.P.1    Rees, B.2    Koebnik, R.3    Mitschler, A.4    Moulinier, L.5    Rosenbusch, J.P.6    Moras, D.7
  • 70
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • See note added in proof.
    • Ferguson AD, Hofman E, Coulton JW, Diedrichs K, Welte W Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science. 282:1998;2215-2220. See note added in proof.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofman, E.2    Coulton, J.W.3    Diedrichs, K.4    Welte, W.5
  • 72
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • See note added in proof.
    • Chang G, Spencer RH, Lee AT, Barclay MT, Rees DC Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science. 282:1998;2220-2226. See note added in proof.
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.