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Volumn 33, Issue 10, 2008, Pages 482-490

Disparate proteins use similar architectures to damage membranes

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CHOLESTEROL; COLICIN; COMPLEMENT MEMBRANE ATTACK COMPLEX; CYTOLYSIN; PORE FORMING CYTOTOXIC PROTEIN; PROTEIN BCL 2; VIRULENCE FACTOR;

EID: 52949087550     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2008.07.004     Document Type: Review
Times cited : (123)

References (78)
  • 1
    • 5244224827 scopus 로고    scopus 로고
    • L, an inhibitor of programmed cell death
    • L, an inhibitor of programmed cell death. Nature 381 (1996) 335-341
    • (1996) Nature , vol.381 , pp. 335-341
    • Muchmore, S.W.1
  • 2
    • 9244244760 scopus 로고    scopus 로고
    • A new lectin family with structure similarity to actinoporins revealed by the crystal structure of Xerocomus chrysenteron lectin XCL
    • Birck C., et al. A new lectin family with structure similarity to actinoporins revealed by the crystal structure of Xerocomus chrysenteron lectin XCL. J. Mol. Biol. 344 (2004) 1409-1420
    • (2004) J. Mol. Biol. , vol.344 , pp. 1409-1420
    • Birck, C.1
  • 3
    • 3542993232 scopus 로고    scopus 로고
    • Clostridium perfringens ε-toxin shows structural similarity to the pore-forming toxin aerolysin
    • Cole A.R., et al. Clostridium perfringens ε-toxin shows structural similarity to the pore-forming toxin aerolysin. Nat. Struct. Mol. Biol. 11 (2004) 797-798
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 797-798
    • Cole, A.R.1
  • 4
    • 20444471526 scopus 로고    scopus 로고
    • Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars
    • Mancheño J.M., et al. Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars. J. Biol. Chem. 280 (2005) 17251-17259
    • (2005) J. Biol. Chem. , vol.280 , pp. 17251-17259
    • Mancheño, J.M.1
  • 5
    • 21744447839 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore
    • Olson R., and Gouaux E. Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore. J. Mol. Biol. 350 (2005) 997-1016
    • (2005) J. Mol. Biol. , vol.350 , pp. 997-1016
    • Olson, R.1    Gouaux, E.2
  • 6
    • 33645032104 scopus 로고    scopus 로고
    • Nontoxic crystal protein from Bacillus thuringiensis demonstrates a remarkable structural similarity to β-pore-forming toxins
    • Akiba T., et al. Nontoxic crystal protein from Bacillus thuringiensis demonstrates a remarkable structural similarity to β-pore-forming toxins. Proteins 63 (2006) 243-248
    • (2006) Proteins , vol.63 , pp. 243-248
    • Akiba, T.1
  • 7
    • 34548670476 scopus 로고    scopus 로고
    • Structure of C8α-MACPF reveals mechanism of membrane attack in complement immune defense
    • Hadders M.A., et al. Structure of C8α-MACPF reveals mechanism of membrane attack in complement immune defense. Science 317 (2007) 1552-1554
    • (2007) Science , vol.317 , pp. 1552-1554
    • Hadders, M.A.1
  • 8
    • 34548666167 scopus 로고    scopus 로고
    • A common fold mediates vertebrate defense and bacterial attack
    • Rosado C.J., et al. A common fold mediates vertebrate defense and bacterial attack. Science 317 (2007) 1548-1551
    • (2007) Science , vol.317 , pp. 1548-1551
    • Rosado, C.J.1
  • 9
    • 43049094015 scopus 로고    scopus 로고
    • Crystal structure of the MACPF domain of human complement protein C8α in complex with the C8γ subunit
    • Slade D.J., et al. Crystal structure of the MACPF domain of human complement protein C8α in complex with the C8γ subunit. J. Mol. Biol. 379 (2008) 331-342
    • (2008) J. Mol. Biol. , vol.379 , pp. 331-342
    • Slade, D.J.1
  • 10
    • 0030865151 scopus 로고    scopus 로고
    • Channel-forming toxins: tales of transformation
    • Gouaux E. Channel-forming toxins: tales of transformation. Curr. Opin. Struct. Biol. 7 (1997) 566-573
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 566-573
    • Gouaux, E.1
  • 11
    • 9244241054 scopus 로고    scopus 로고
    • Pore-forming protein toxins: from structure to function
    • Parker M.W., and Feil S.C. Pore-forming protein toxins: from structure to function. Prog. Biophys. Mol. Biol. 88 (2005) 91-142
    • (2005) Prog. Biophys. Mol. Biol. , vol.88 , pp. 91-142
    • Parker, M.W.1    Feil, S.C.2
  • 12
    • 0027443116 scopus 로고
    • Rendering a membrane protein soluble in water: a common packing motif in bacterial protein toxins
    • Parker M.W., and Pattus F. Rendering a membrane protein soluble in water: a common packing motif in bacterial protein toxins. Trends Biochem. Sci. 18 (1993) 391-395
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 391-395
    • Parker, M.W.1    Pattus, F.2
  • 13
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • Bechinger B., and Lohner K. Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochim. Biophys. Acta 1758 (2006) 1529-1539
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 14
    • 37349002470 scopus 로고    scopus 로고
    • Zwitterionic phospholipids and sterols modulate antimicrobial peptide-induced membrane destabilization
    • Mason A.J., et al. Zwitterionic phospholipids and sterols modulate antimicrobial peptide-induced membrane destabilization. Biophys. J. 93 (2007) 4289-4299
    • (2007) Biophys. J. , vol.93 , pp. 4289-4299
    • Mason, A.J.1
  • 15
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane surfaces
    • Wimley W.C., and White S.H. Experimentally determined hydrophobicity scale for proteins at membrane surfaces. Nat. Struct. Biol. 3 (1996) 842-848
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 16
    • 40949131305 scopus 로고    scopus 로고
    • Thermodynamics of the interactions of tryptophan-rich cathelicidin antimicrobial peptides with model and natural membranes
    • Andrushchenko V.V., et al. Thermodynamics of the interactions of tryptophan-rich cathelicidin antimicrobial peptides with model and natural membranes. Biochim. Biophys. Acta 1778 (2008) 1004-1014
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1004-1014
    • Andrushchenko, V.V.1
  • 17
    • 0025833449 scopus 로고
    • Hemolytic and antimicrobial activities of the twenty-four individual omission analogues of melittin
    • Blondelle S.E., and Houghten R.A. Hemolytic and antimicrobial activities of the twenty-four individual omission analogues of melittin. Biochemistry 30 (1991) 4671-4678
    • (1991) Biochemistry , vol.30 , pp. 4671-4678
    • Blondelle, S.E.1    Houghten, R.A.2
  • 18
    • 35848964760 scopus 로고    scopus 로고
    • Effect of micelle interface on the binding of anticoccidial PW2 peptide
    • Tinoco L.W., et al. Effect of micelle interface on the binding of anticoccidial PW2 peptide. J. Biomol. NMR 39 (2007) 315-322
    • (2007) J. Biomol. NMR , vol.39 , pp. 315-322
    • Tinoco, L.W.1
  • 19
    • 0024961641 scopus 로고
    • Structure of the membrane-pore-forming fragment of colicin-A
    • Parker M.W., et al. Structure of the membrane-pore-forming fragment of colicin-A. Nature 337 (1989) 93-96
    • (1989) Nature , vol.337 , pp. 93-96
    • Parker, M.W.1
  • 20
    • 0027459747 scopus 로고
    • Structural alignment of globins, phycocyanins and colicin A
    • Holm L., and Sander C. Structural alignment of globins, phycocyanins and colicin A. FEBS Lett. 315 (1993) 301-306
    • (1993) FEBS Lett. , vol.315 , pp. 301-306
    • Holm, L.1    Sander, C.2
  • 21
    • 20544475665 scopus 로고    scopus 로고
    • Membrane-protein interactions in cell signaling and membrane trafficking
    • Cho W., and Stahelin R.V. Membrane-protein interactions in cell signaling and membrane trafficking. Annu. Rev. Biophys. Biomol. Struct. 34 (2005) 119-151
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 119-151
    • Cho, W.1    Stahelin, R.V.2
  • 22
    • 0034880806 scopus 로고    scopus 로고
    • Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina
    • Athanasiadis A., et al. Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina. Structure 9 (2001) 341-346
    • (2001) Structure , vol.9 , pp. 341-346
    • Athanasiadis, A.1
  • 23
    • 25444452398 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins
    • Tweten R.K. Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins. Infect. Immun. 73 (2005) 6199-6209
    • (2005) Infect. Immun. , vol.73 , pp. 6199-6209
    • Tweten, R.K.1
  • 24
    • 0036829075 scopus 로고    scopus 로고
    • Two-step membrane binding by equinatoxin II, a pore-forming toxin from the sea anemone, involves an exposed aromatic cluster and a flexible helix
    • Hong Q., et al. Two-step membrane binding by equinatoxin II, a pore-forming toxin from the sea anemone, involves an exposed aromatic cluster and a flexible helix. J. Biol. Chem. 277 (2002) 41916-41924
    • (2002) J. Biol. Chem. , vol.277 , pp. 41916-41924
    • Hong, Q.1
  • 25
    • 0038604282 scopus 로고    scopus 로고
    • A novel mechanism of pore formation - membrane penetration by the N-terminal amphipathic region of equinatoxin
    • Malovrh P., et al. A novel mechanism of pore formation - membrane penetration by the N-terminal amphipathic region of equinatoxin. J. Biol. Chem. 278 (2003) 22678-22685
    • (2003) J. Biol. Chem. , vol.278 , pp. 22678-22685
    • Malovrh, P.1
  • 26
    • 49649095215 scopus 로고    scopus 로고
    • Molecular determinants of sphingomyelin specificity of a eukaryotic pore forming toxin
    • Bakrač B., et al. Molecular determinants of sphingomyelin specificity of a eukaryotic pore forming toxin. J. Biol. Chem. 283 (2008) 18665-18667
    • (2008) J. Biol. Chem. , vol.283 , pp. 18665-18667
    • Bakrač, B.1
  • 27
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • Rossjohn J., et al. Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 89 (1997) 685-692
    • (1997) Cell , vol.89 , pp. 685-692
    • Rossjohn, J.1
  • 28
    • 38049125626 scopus 로고    scopus 로고
    • Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions
    • Soltani C.E., et al. Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 20226-20231
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 20226-20231
    • Soltani, C.E.1
  • 29
    • 0036830653 scopus 로고    scopus 로고
    • Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin
    • Ramachandran R., et al. Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin. Nat. Struct. Biol. 9 (2002) 823-827
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 823-827
    • Ramachandran, R.1
  • 30
    • 17444405610 scopus 로고    scopus 로고
    • Structural basis of pore formation by the bacterial toxin pneumolysin
    • Tilley S.J., et al. Structural basis of pore formation by the bacterial toxin pneumolysin. Cell 121 (2005) 247-256
    • (2005) Cell , vol.121 , pp. 247-256
    • Tilley, S.J.1
  • 31
    • 0032932083 scopus 로고    scopus 로고
    • Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
    • Olson R., et al. Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nat. Struct. Biol. 6 (1999) 134-140
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 134-140
    • Olson, R.1
  • 32
    • 0037427958 scopus 로고    scopus 로고
    • β-barrel membrane protein folding and structure viewed through the lens of α-hemolysin
    • Montoya M., and Gouaux E. β-barrel membrane protein folding and structure viewed through the lens of α-hemolysin. Biochim. Biophys. Acta 1609 (2003) 19-27
    • (2003) Biochim. Biophys. Acta , vol.1609 , pp. 19-27
    • Montoya, M.1    Gouaux, E.2
  • 33
    • 32344442117 scopus 로고    scopus 로고
    • Structure and activity of the N-terminal region of the eukaryotic cytolysin equinatoxin II
    • Drechsler A., et al. Structure and activity of the N-terminal region of the eukaryotic cytolysin equinatoxin II. Biochemistry 45 (2006) 1818-1828
    • (2006) Biochemistry , vol.45 , pp. 1818-1828
    • Drechsler, A.1
  • 34
    • 33645739372 scopus 로고    scopus 로고
    • Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II
    • Casallanovo F., et al. Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II. Biopolymers 84 (2006) 169-180
    • (2006) Biopolymers , vol.84 , pp. 169-180
    • Casallanovo, F.1
  • 35
    • 0242542032 scopus 로고    scopus 로고
    • Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation
    • Mancheño J.M., et al. Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation. Structure 11 (2003) 1319-1328
    • (2003) Structure , vol.11 , pp. 1319-1328
    • Mancheño, J.M.1
  • 36
    • 15444371776 scopus 로고    scopus 로고
    • The antineoplastic lectin of the common edible mushroom (Agaricus bisporus) has two binding sites, each specific for a different configuration at a single epimeric hydroxyl
    • Carrizo M.E., et al. The antineoplastic lectin of the common edible mushroom (Agaricus bisporus) has two binding sites, each specific for a different configuration at a single epimeric hydroxyl. J. Biol. Chem. 280 (2005) 10614-10623
    • (2005) J. Biol. Chem. , vol.280 , pp. 10614-10623
    • Carrizo, M.E.1
  • 37
    • 34147102176 scopus 로고    scopus 로고
    • Structural basis for the carbohydrate recognition of the Sclerotium rolfsii lectin
    • Leonidas D.D., et al. Structural basis for the carbohydrate recognition of the Sclerotium rolfsii lectin. J. Mol. Biol. 368 (2007) 1145-1161
    • (2007) J. Mol. Biol. , vol.368 , pp. 1145-1161
    • Leonidas, D.D.1
  • 38
    • 33748745476 scopus 로고    scopus 로고
    • Membrane binding of zebrafish actinoporin-like protein: AF domains, a novel superfamily of cell membrane binding domains
    • Gutiérrez-Aguirre I., et al. Membrane binding of zebrafish actinoporin-like protein: AF domains, a novel superfamily of cell membrane binding domains. Biochem. J. 398 (2006) 381-392
    • (2006) Biochem. J. , vol.398 , pp. 381-392
    • Gutiérrez-Aguirre, I.1
  • 39
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: receptor binding, internalization, pore formation, and translocation
    • Young J.A., and Collier R.J. Anthrax toxin: receptor binding, internalization, pore formation, and translocation. Annu. Rev. Biochem. 76 (2007) 243-265
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 243-265
    • Young, J.A.1    Collier, R.J.2
  • 42
    • 41149178966 scopus 로고    scopus 로고
    • Conformation of the closed channel state of colicin A in proteoliposomes: an umbrella model
    • Padmavathi P.V., and Steinhoff H.J. Conformation of the closed channel state of colicin A in proteoliposomes: an umbrella model. J. Mol. Biol. 378 (2008) 204-214
    • (2008) J. Mol. Biol. , vol.378 , pp. 204-214
    • Padmavathi, P.V.1    Steinhoff, H.J.2
  • 43
    • 0029872191 scopus 로고    scopus 로고
    • Major transmembrane movement associated with colicin Ia channel gating
    • Qiu X.Q., et al. Major transmembrane movement associated with colicin Ia channel gating. J. Gen. Physiol. 107 (1996) 313-328
    • (1996) J. Gen. Physiol. , vol.107 , pp. 313-328
    • Qiu, X.Q.1
  • 44
    • 33845273500 scopus 로고    scopus 로고
    • The N-terminal domain of Bcl-xL reversibly binds membranes in a pH-dependent manner
    • Thuduppathy G.R., et al. The N-terminal domain of Bcl-xL reversibly binds membranes in a pH-dependent manner. Biochemistry 45 (2006) 14533-14542
    • (2006) Biochemistry , vol.45 , pp. 14533-14542
    • Thuduppathy, G.R.1
  • 45
    • 33744799480 scopus 로고    scopus 로고
    • Evidence that membrane insertion of the cytosolic domain of Bcl-xL is governed by an electrostatic mechanism
    • Thuduppathy G.R., et al. Evidence that membrane insertion of the cytosolic domain of Bcl-xL is governed by an electrostatic mechanism. J. Mol. Biol. 359 (2006) 1045-1058
    • (2006) J. Mol. Biol. , vol.359 , pp. 1045-1058
    • Thuduppathy, G.R.1
  • 46
    • 36349002883 scopus 로고    scopus 로고
    • Helix orientations in membrane-associated Bcl-X(L) determined by (15)N-solid-state NMR spectroscopy
    • Aisenbrey C., et al. Helix orientations in membrane-associated Bcl-X(L) determined by (15)N-solid-state NMR spectroscopy. Eur. Biophys. J. 37 (2007) 71-80
    • (2007) Eur. Biophys. J. , vol.37 , pp. 71-80
    • Aisenbrey, C.1
  • 47
    • 33947304650 scopus 로고    scopus 로고
    • A structural viral mimic of prosurvival Bcl-2: a pivotal role for sequestering proapoptotic Bax and Bak
    • Kvansakul M., et al. A structural viral mimic of prosurvival Bcl-2: a pivotal role for sequestering proapoptotic Bax and Bak. Mol. Cell 25 (2007) 933-942
    • (2007) Mol. Cell , vol.25 , pp. 933-942
    • Kvansakul, M.1
  • 48
    • 6344235539 scopus 로고    scopus 로고
    • Bcl-2 homodimerization involves two distinct binding surfaces, a topographic arrangement that provides an effective mechanism for Bcl-2 to capture activated Bax
    • Zhang Z., et al. Bcl-2 homodimerization involves two distinct binding surfaces, a topographic arrangement that provides an effective mechanism for Bcl-2 to capture activated Bax. J. Biol. Chem. 279 (2004) 43920-43928
    • (2004) J. Biol. Chem. , vol.279 , pp. 43920-43928
    • Zhang, Z.1
  • 49
    • 0034650523 scopus 로고    scopus 로고
    • Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria
    • Antonsson B., et al. Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem. J. 345 (2000) 271-278
    • (2000) Biochem. J. , vol.345 , pp. 271-278
    • Antonsson, B.1
  • 50
    • 0036435610 scopus 로고    scopus 로고
    • Direct evidence for membrane pore formation by the apoptotic protein Bax
    • Epand R.F., et al. Direct evidence for membrane pore formation by the apoptotic protein Bax. Biochem. Biophys. Res. Commun. 298 (2002) 744-749
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 744-749
    • Epand, R.F.1
  • 51
    • 14644435747 scopus 로고    scopus 로고
    • Gating movements of colicin A and colicin Ia are different
    • Slatin S.L., et al. Gating movements of colicin A and colicin Ia are different. J. Membr. Biol. 202 (2004) 73-83
    • (2004) J. Membr. Biol. , vol.202 , pp. 73-83
    • Slatin, S.L.1
  • 52
    • 22244493864 scopus 로고    scopus 로고
    • Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins
    • Garcia-Sáez A.J., et al. Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins. Biophys. J. 88 (2005) 3976-3990
    • (2005) Biophys. J. , vol.88 , pp. 3976-3990
    • Garcia-Sáez, A.J.1
  • 53
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: opposing activities that mediate cell death
    • Youle R.J., and Strasser A. The BCL-2 protein family: opposing activities that mediate cell death. Nat. Rev. Mol. Cell Biol. 9 (2008) 47-59
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 54
    • 0033564222 scopus 로고    scopus 로고
    • Colicin E1 forms a dimer after urea-induced unfolding
    • Steer B.A., et al. Colicin E1 forms a dimer after urea-induced unfolding. Biochem. J. 340 (1999) 631-638
    • (1999) Biochem. J. , vol.340 , pp. 631-638
    • Steer, B.A.1
  • 55
    • 30744475208 scopus 로고    scopus 로고
    • BCL-XL dimerization by three-dimensional domain swapping
    • O'Neill J.W., et al. BCL-XL dimerization by three-dimensional domain swapping. J. Mol. Biol. 356 (2006) 367-381
    • (2006) J. Mol. Biol. , vol.356 , pp. 367-381
    • O'Neill, J.W.1
  • 56
    • 0029996132 scopus 로고    scopus 로고
    • The structural homology between uteroglobin and the pore-forming domain of colicin A suggests a possible mechanism of action for uteroglobin
    • De la Cruz X., and Lee B. The structural homology between uteroglobin and the pore-forming domain of colicin A suggests a possible mechanism of action for uteroglobin. Protein Sci. 5 (1996) 857-861
    • (1996) Protein Sci. , vol.5 , pp. 857-861
    • De la Cruz, X.1    Lee, B.2
  • 57
    • 29244448306 scopus 로고    scopus 로고
    • Lipid binding proteins in membrane digestion, antigen presentation and antimicrobial defense
    • Kolter T., et al. Lipid binding proteins in membrane digestion, antigen presentation and antimicrobial defense. J. Biol. Chem. 280 (2005) 41125-41128
    • (2005) J. Biol. Chem. , vol.280 , pp. 41125-41128
    • Kolter, T.1
  • 58
    • 1842689787 scopus 로고    scopus 로고
    • The identification and structure of the membrane-spanning domain of the Clostridium septicum alpha toxin
    • Melton J.A., et al. The identification and structure of the membrane-spanning domain of the Clostridium septicum alpha toxin. J. Biol. Chem. 279 (2004) 14315-14322
    • (2004) J. Biol. Chem. , vol.279 , pp. 14315-14322
    • Melton, J.A.1
  • 59
    • 32544443056 scopus 로고    scopus 로고
    • A rivet model for channel formation by aerolysin-like pore-forming toxins
    • Iacovache I., et al. A rivet model for channel formation by aerolysin-like pore-forming toxins. EMBO J. 25 (2006) 457-466
    • (2006) EMBO J. , vol.25 , pp. 457-466
    • Iacovache, I.1
  • 60
    • 0033529592 scopus 로고    scopus 로고
    • Analysis of receptor binding by the channel-forming toxin aerolysin using surface plasmon resonance
    • MacKenzie C.R., et al. Analysis of receptor binding by the channel-forming toxin aerolysin using surface plasmon resonance. J. Biol. Chem. 274 (1999) 22604-22609
    • (1999) J. Biol. Chem. , vol.274 , pp. 22604-22609
    • MacKenzie, C.R.1
  • 61
    • 38749123992 scopus 로고    scopus 로고
    • Friend or foe: the same fold for attack and defense
    • Lukoyanova N., and Saibil H.R. Friend or foe: the same fold for attack and defense. Trends Immunol. 29 (2008) 51-53
    • (2008) Trends Immunol. , vol.29 , pp. 51-53
    • Lukoyanova, N.1    Saibil, H.R.2
  • 62
    • 34249031315 scopus 로고    scopus 로고
    • Characterization of PsTX-60B, a new membrane-attack complex/perforin (MACPF) family toxin, from the venomous sea anemone Phyllodiscus semoni
    • Satoh H., et al. Characterization of PsTX-60B, a new membrane-attack complex/perforin (MACPF) family toxin, from the venomous sea anemone Phyllodiscus semoni. Toxicon 49 (2007) 1208-1210
    • (2007) Toxicon , vol.49 , pp. 1208-1210
    • Satoh, H.1
  • 63
    • 0242664967 scopus 로고    scopus 로고
    • Pore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures
    • Anderluh G., et al. Pore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures. J. Biol. Chem. 278 (2003) 45216-45223
    • (2003) J. Biol. Chem. , vol.278 , pp. 45216-45223
    • Anderluh, G.1
  • 64
    • 4944225045 scopus 로고    scopus 로고
    • Effect of lipids with different spontaneous curvature on the channel activity of colicin E1: evidence in favor of a toroidal pore
    • Sobko A.A., et al. Effect of lipids with different spontaneous curvature on the channel activity of colicin E1: evidence in favor of a toroidal pore. FEBS Lett. 576 (2004) 205-210
    • (2004) FEBS Lett. , vol.576 , pp. 205-210
    • Sobko, A.A.1
  • 65
    • 42149130277 scopus 로고    scopus 로고
    • Tilted peptides: a structural motif involved in protein membrane insertion?
    • Lins L., and Brasseur R. Tilted peptides: a structural motif involved in protein membrane insertion?. J. Pept. Sci. 14 (2008) 416-422
    • (2008) J. Pept. Sci. , vol.14 , pp. 416-422
    • Lins, L.1    Brasseur, R.2
  • 66
    • 0027976196 scopus 로고
    • Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states
    • Parker M.W., et al. Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature 367 (1994) 292-295
    • (1994) Nature , vol.367 , pp. 292-295
    • Parker, M.W.1
  • 67
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song L., et al. Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 274 (1996) 1859-1866
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1
  • 68
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., et al. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1
  • 69
    • 0032528046 scopus 로고    scopus 로고
    • Crystal structure of a colicin N fragment suggests a model for toxicity
    • Vetter I.R., et al. Crystal structure of a colicin N fragment suggests a model for toxicity. Structure 6 (1998) 863-887
    • (1998) Structure , vol.6 , pp. 863-887
    • Vetter, I.R.1
  • 70
    • 0035884406 scopus 로고    scopus 로고
    • Membrane binding assays for peripheral proteins
    • Cho W., et al. Membrane binding assays for peripheral proteins. Anal. Biochem. 296 (2001) 153-161
    • (2001) Anal. Biochem. , vol.296 , pp. 153-161
    • Cho, W.1
  • 71
    • 33746728985 scopus 로고    scopus 로고
    • Surface plasmon resonance in protein-membrane interactions
    • Beseničar M., et al. Surface plasmon resonance in protein-membrane interactions. Chem. Phys. Lipids 141 (2006) 169-178
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 169-178
    • Beseničar, M.1
  • 72
    • 14344260441 scopus 로고    scopus 로고
    • 2 hydrolysis of supported phospholipid bilayers: a neutron reflectivity and ellipsometry study
    • 2 hydrolysis of supported phospholipid bilayers: a neutron reflectivity and ellipsometry study. Biochemistry 44 (2005) 2811-2821
    • (2005) Biochemistry , vol.44 , pp. 2811-2821
    • Vacklin, H.P.1
  • 73
    • 33646192301 scopus 로고    scopus 로고
    • Structural bioinformatics prediction of membrane-binding proteins
    • Bhardwaj N., et al. Structural bioinformatics prediction of membrane-binding proteins. J. Mol. Biol. 359 (2006) 486-495
    • (2006) J. Mol. Biol. , vol.359 , pp. 486-495
    • Bhardwaj, N.1
  • 74
    • 34547618240 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in positioning of peripheral proteins in membranes
    • Lomize A.L., et al. The role of hydrophobic interactions in positioning of peripheral proteins in membranes. BMC Struct. Biol. 7 (2007) 44
    • (2007) BMC Struct. Biol. , vol.7 , pp. 44
    • Lomize, A.L.1
  • 75
    • 43749094980 scopus 로고    scopus 로고
    • Stormo, G.D. (2006) An introduction to recognizing functional domains. Curr. Protoc. Bioinformatics. Chapter 2, Unit 2.1.
    • Stormo, G.D. (2006) An introduction to recognizing functional domains. Curr. Protoc. Bioinformatics. Chapter 2, Unit 2.1.
  • 76
    • 0031022750 scopus 로고    scopus 로고
    • Crystal structure of colicin Ia
    • Wiener M., et al. Crystal structure of colicin Ia. Nature 385 (1997) 461-464
    • (1997) Nature , vol.385 , pp. 461-464
    • Wiener, M.1
  • 77
    • 0031052342 scopus 로고    scopus 로고
    • Crystal structure of the anthrax toxin protective antigen
    • Petosa C., et al. Crystal structure of the anthrax toxin protective antigen. Nature 385 (1997) 833-838
    • (1997) Nature , vol.385 , pp. 833-838
    • Petosa, C.1
  • 78
    • 33947501381 scopus 로고    scopus 로고
    • The folding and evolution of multidomain proteins
    • Han J.H., et al. The folding and evolution of multidomain proteins. Nat. Rev. Mol. Cell Biol. 8 (2007) 319-330
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 319-330
    • Han, J.H.1


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