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Volumn 1838, Issue 7, 2014, Pages 1777-1784

A conserved tetrameric interaction of cry toxin helix α3 suggests a functional role for toxin oligomerization

Author keywords

Coiled coil; Cry toxin; Evolutionary conservation; Membrane insertion; Oligomerization

Indexed keywords

ARGININE; BETAINE; CARBON 14; CRYSTAL TOXIN; GLUTAMIC ACID; MONOMER; SYNTHETIC PEPTIDE; TETRAMER; TOXIN; UNCLASSIFIED DRUG;

EID: 84899034273     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2014.03.006     Document Type: Article
Times cited : (11)

References (67)
  • 2
    • 0024337104 scopus 로고
    • Insecticidal crystal proteins of Bacillus thuringiensis
    • H. Hofte, and H.R. Whiteley Insecticidal crystal proteins of Bacillus thuringiensis Microbiol. Rev. 53 1989 242 255
    • (1989) Microbiol. Rev. , vol.53 , pp. 242-255
    • Hofte, H.1    Whiteley, H.R.2
  • 3
    • 0033784615 scopus 로고    scopus 로고
    • Protein machines and lipid assemblies: Current views of cell membrane fusion
    • B.R. Lentz, V. Malinin, M.E. Haque, and K. Evans Protein machines and lipid assemblies: current views of cell membrane fusion Curr. Opin. Struct. Biol. 10 2000 607 615
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 607-615
    • Lentz, B.R.1    Malinin, V.2    Haque, M.E.3    Evans, K.4
  • 4
    • 16244392435 scopus 로고    scopus 로고
    • Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications
    • P. Boonserm, P. Davis, D.J. Ellar, and J. Li Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications J. Mol. Biol. 348 2005 363 382
    • (2005) J. Mol. Biol. , vol.348 , pp. 363-382
    • Boonserm, P.1    Davis, P.2    Ellar, D.J.3    Li, J.4
  • 5
    • 0037348708 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of a mosquito-larvicidal toxin from Bacillus thuringiensis subsp. Israelensis
    • P. Boonserm, D.J. Ellar, and J. Li Crystallization and preliminary X-ray diffraction studies of a mosquito-larvicidal toxin from Bacillus thuringiensis subsp. israelensis Acta Crystallogr. D Biol. Crystallogr. 59 2003 591 594
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 591-594
    • Boonserm, P.1    Ellar, D.J.2    Li, J.3
  • 7
    • 0030785699 scopus 로고    scopus 로고
    • Restriction of intramolecular movements within the Cry1Aa toxin molecule of Bacillus thuringiensis through disulfide bond engineering
    • J.L. Schwartz, M. Juteau, P. Grochulski, M. Cygler, G. Prefontaine, R. Brousseau, and L. Masson Restriction of intramolecular movements within the Cry1Aa toxin molecule of Bacillus thuringiensis through disulfide bond engineering FEBS Lett. 410 1997 397 402
    • (1997) FEBS Lett. , vol.410 , pp. 397-402
    • Schwartz, J.L.1    Juteau, M.2    Grochulski, P.3    Cygler, M.4    Prefontaine, G.5    Brousseau, R.6    Masson, L.7
  • 9
    • 0028986449 scopus 로고
    • Delta-endotoxins induce cation channels in Spodoptera frugiperda brush border membranes in suspension and in planar lipid bilayers
    • A. Lorence, A. Darszon, C. Diaz, A. Lievano, R. Quintero, and A. Bravo Delta-endotoxins induce cation channels in Spodoptera frugiperda brush border membranes in suspension and in planar lipid bilayers FEBS Lett. 360 1995 217 222
    • (1995) FEBS Lett. , vol.360 , pp. 217-222
    • Lorence, A.1    Darszon, A.2    Diaz, C.3    Lievano, A.4    Quintero, R.5    Bravo, A.6
  • 10
    • 0029930607 scopus 로고    scopus 로고
    • Domain III substitution in Bacillus thuringiensis delta-endotoxin CryIA(b) results in superior toxicity for Spodoptera exigua and altered membrane protein recognition
    • R.A. De Maagd, M.S.G. Kwa, H.D. Van Klei, T. Yamamoto, B. Schipper, J.M. Vlak, W.J. Stiekema, and D. Bosch Domain III substitution in Bacillus thuringiensis delta-endotoxin CryIA(b) results in superior toxicity for Spodoptera exigua and altered membrane protein recognition Appl. Environ. Microbiol. 62 1996 1537 1543
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1537-1543
    • De Maagd, R.A.1    Kwa, M.S.G.2    Van Klei, H.D.3    Yamamoto, T.4    Schipper, B.5    Vlak, J.M.6    Stiekema, W.J.7    Bosch, D.8
  • 11
    • 84870955143 scopus 로고    scopus 로고
    • Bacillus thuringiensis insecticidal three-domain Cry toxins: Mode of action, insect resistance and consequences for crop protection
    • L. Pardo-Lopez, M. Soberon, and A. Bravo Bacillus thuringiensis insecticidal three-domain Cry toxins: mode of action, insect resistance and consequences for crop protection FEMS Microbiol. Rev. 37 2013 3 22
    • (2013) FEMS Microbiol. Rev. , vol.37 , pp. 3-22
    • Pardo-Lopez, L.1    Soberon, M.2    Bravo, A.3
  • 12
    • 0028002221 scopus 로고
    • Mechanism of action of Bacillus thuringiensis Insecticidal delta-endotoxins
    • B.H. Knowles Mechanism of action of Bacillus thuringiensis Insecticidal delta-endotoxins Adv. Insect Physiol. 24 1994 275 308
    • (1994) Adv. Insect Physiol. , vol.24 , pp. 275-308
    • Knowles, B.H.1
  • 14
    • 33645223519 scopus 로고    scopus 로고
    • Role of the PAR1 receptor 8th helix in signaling: The 7-8-1 receptor activation mechanism, in
    • S. Swift, A.J. Leger, J. Talavera, L. Zhang, A. Bohm, and A. Kuliopulos Role of the PAR1 receptor 8th helix in signaling: the 7-8-1 receptor activation mechanism, in J. Biol. Chem. 281 2006 4109 4116
    • (2006) J. Biol. Chem. , vol.281 , pp. 4109-4116
    • Swift, S.1    Leger, A.J.2    Talavera, J.3    Zhang, L.4    Bohm, A.5    Kuliopulos, A.6
  • 15
    • 1642534361 scopus 로고    scopus 로고
    • Role of toxin activation on binding and pore formation activity of the Bacillus thuringiensis Cry3 toxins in membranes of Leptinotarsa decemlineata (Say)
    • C. Rausell, I. Garcia-Robles, J. Sanchez, C. Munoz-Garay, A.C. Martinez-Ramirez, M.D. Real, and A. Bravo Role of toxin activation on binding and pore formation activity of the Bacillus thuringiensis Cry3 toxins in membranes of Leptinotarsa decemlineata (Say) Biochim. Biophys. Acta 1660 2004 99 105
    • (2004) Biochim. Biophys. Acta , vol.1660 , pp. 99-105
    • Rausell, C.1    Garcia-Robles, I.2    Sanchez, J.3    Munoz-Garay, C.4    Martinez-Ramirez, A.C.5    Real, M.D.6    Bravo, A.7
  • 16
    • 0037181168 scopus 로고    scopus 로고
    • Cadherin-like receptor binding facilitates proteolytic cleavage of helix α-1 in domain i and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin
    • I. Gomez, J. Sanchez, R. Miranda, A. Bravo, and M. Soberon Cadherin-like receptor binding facilitates proteolytic cleavage of helix α-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin FEBS Lett. 513 2002 242 246
    • (2002) FEBS Lett. , vol.513 , pp. 242-246
    • Gomez, I.1    Sanchez, J.2    Miranda, R.3    Bravo, A.4    Soberon, M.5
  • 17
    • 60749126637 scopus 로고    scopus 로고
    • Enhancement of insecticidal activity of Bacillus thuringiensis Cry1A toxins by fragments of a toxin-binding cadherin correlates with oligomer formation
    • S. Pacheco, I. Gomez, S.S. Gill, A. Bravo, and M. Soberon Enhancement of insecticidal activity of Bacillus thuringiensis Cry1A toxins by fragments of a toxin-binding cadherin correlates with oligomer formation Peptides 30 2009 583 588
    • (2009) Peptides , vol.30 , pp. 583-588
    • Pacheco, S.1    Gomez, I.2    Gill, S.S.3    Bravo, A.4    Soberon, M.5
  • 18
    • 82755176200 scopus 로고    scopus 로고
    • Single molecule fluorescence study of the Bacillus thuringiensis toxin Cry1Aa reveals tetramerization
    • N. Groulx, H. McGuire, R. Laprade, J.L. Schwartz, and R. Blunck Single molecule fluorescence study of the Bacillus thuringiensis toxin Cry1Aa reveals tetramerization J. Biol. Chem. 286 2011 42274 42282
    • (2011) J. Biol. Chem. , vol.286 , pp. 42274-42282
    • Groulx, N.1    McGuire, H.2    Laprade, R.3    Schwartz, J.L.4    Blunck, R.5
  • 20
    • 0026050639 scopus 로고
    • Crystal structure of insecticidal delta-endotoxin from Bacillus thuringiensis at 2.5 A resolution
    • J.D. Li, J. Carroll, and D.J. Ellar Crystal structure of insecticidal delta-endotoxin from Bacillus thuringiensis at 2.5 A resolution Nature 353 1991 815 821
    • (1991) Nature , vol.353 , pp. 815-821
    • Li, J.D.1    Carroll, J.2    Ellar, D.J.3
  • 21
    • 0037066630 scopus 로고    scopus 로고
    • Amino acid and divalent ion permeability of the pores formed by the Bacillus thuringiensis toxins Cry1Aa and Cry1Ac in insect midgut brush border membrane vesicles
    • M. Kirouac, V. Vachon, J.F. Noel, F. Girard, J.L. Schwartz, and R. Laprade Amino acid and divalent ion permeability of the pores formed by the Bacillus thuringiensis toxins Cry1Aa and Cry1Ac in insect midgut brush border membrane vesicles Biochim. Biophys. Acta 1561 2002 171 179
    • (2002) Biochim. Biophys. Acta , vol.1561 , pp. 171-179
    • Kirouac, M.1    Vachon, V.2    Noel, J.F.3    Girard, F.4    Schwartz, J.L.5    Laprade, R.6
  • 22
    • 0035882546 scopus 로고    scopus 로고
    • A new method to model membrane protein structure based on silent amino acid substitutions
    • J.A.G. Briggs, J. Torres, and I.T. Arkin A new method to model membrane protein structure based on silent amino acid substitutions Proteins Struct. Funct. Genet. 44 2001 370 375
    • (2001) Proteins Struct. Funct. Genet. , vol.44 , pp. 370-375
    • Briggs, J.A.G.1    Torres, J.2    Arkin, I.T.3
  • 23
    • 0037333304 scopus 로고    scopus 로고
    • Membrane proteins: The 'Wild West' of structural biology
    • J. Torres, T.J. Stevens, and M. Samso Membrane proteins: the 'Wild West' of structural biology Trends Biochem. Sci. 28 2003 137 144
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 137-144
    • Torres, J.1    Stevens, T.J.2    Samso, M.3
  • 24
    • 21244448326 scopus 로고    scopus 로고
    • The transmembrane oligomers of coronavirus protein e
    • J. Torres, J. Wang, K. Parthasarathy, and D.X. Liu The transmembrane oligomers of coronavirus protein E Biophys. J. 88 2005 1283 1290
    • (2005) Biophys. J. , vol.88 , pp. 1283-1290
    • Torres, J.1    Wang, J.2    Parthasarathy, K.3    Liu, D.X.4
  • 25
    • 33645020555 scopus 로고    scopus 로고
    • Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved
    • X. Lin, S.M. Tan, S.K.A. Law, and J. Torres Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved Proteins 63 2006 16 23
    • (2006) Proteins , vol.63 , pp. 16-23
    • Lin, X.1    Tan, S.M.2    Law, S.K.A.3    Torres, J.4
  • 26
    • 33749038910 scopus 로고    scopus 로고
    • Unambiguous prediction of human integrin transmembrane heterodimer interactions using only homologous sequences
    • X. Lin, S.M. Tan, S.K.A. Law, and J. Torres Unambiguous prediction of human integrin transmembrane heterodimer interactions using only homologous sequences Proteins Struct. Funct. Genet. 65 2006 274 279
    • (2006) Proteins Struct. Funct. Genet. , vol.65 , pp. 274-279
    • Lin, X.1    Tan, S.M.2    Law, S.K.A.3    Torres, J.4
  • 27
    • 33846500705 scopus 로고    scopus 로고
    • The transmembrane homotrimer of ADAM 1 in model lipid bilayers
    • S.W. Gan, L. Xin, and J. Torres The transmembrane homotrimer of ADAM 1 in model lipid bilayers Protein Sci. 16 2007 285 292
    • (2007) Protein Sci. , vol.16 , pp. 285-292
    • Gan, S.W.1    Xin, L.2    Torres, J.3
  • 30
    • 0029557910 scopus 로고
    • Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban
    • P.D. Adams, I.T. Arkin, D.M. Engelman, and A.T. Brunger Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban Nat. Struct. Biol. 2 1995 154 162
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 154-162
    • Adams, P.D.1    Arkin, I.T.2    Engelman, D.M.3    Brunger, A.T.4
  • 31
    • 0036111126 scopus 로고    scopus 로고
    • Contribution of energy values to the analysis of global searching molecular dynamics simulations of transmembrane helical bundles
    • J. Torres, J.A. Briggs, and I.T. Arkin Contribution of energy values to the analysis of global searching molecular dynamics simulations of transmembrane helical bundles Biophys. J. 82 2002 3063 3071
    • (2002) Biophys. J. , vol.82 , pp. 3063-3071
    • Torres, J.1    Briggs, J.A.2    Arkin, I.T.3
  • 32
    • 38349165311 scopus 로고    scopus 로고
    • A trimeric building block model for Cry toxins in vitro ion channel formation
    • J. Torres, X. Lin, and P. Boonserm A trimeric building block model for Cry toxins in vitro ion channel formation Biochim. Biophys. Acta 1778 2008 392 397
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 392-397
    • Torres, J.1    Lin, X.2    Boonserm, P.3
  • 35
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • B. Hess, H. Bekker, H.J.C. Berendsen, and J. Fraaije LINCS: a linear constraint solver for molecular simulations J. Comput. Chem. 18 1997 1463 1472
    • (1997) J. Comput. Chem. , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.4
  • 37
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • G. Bussi, D. Donadio, and M. Parrinello Canonical sampling through velocity rescaling J. Chem. Phys. 126 2007 014101 014107
    • (2007) J. Chem. Phys. , vol.126 , pp. 014101-014107
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 38
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • (29-32)
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55 (29-32)
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 39
    • 0034697895 scopus 로고    scopus 로고
    • 18O, in the determination of a structural model of phospholamban in a lipid bilayer. Spatial restraints resolve the ambiguity arising from interpretations of mutagenesis data
    • 18O, in the determination of a structural model of phospholamban in a lipid bilayer. Spatial restraints resolve the ambiguity arising from interpretations of mutagenesis data J. Mol. Biol. 300 2000 677 685
    • (2000) J. Mol. Biol. , vol.300 , pp. 677-685
    • Torres, J.1    Adams, P.D.2    Arkin, I.T.3
  • 41
    • 0030819982 scopus 로고    scopus 로고
    • Site-directed dichroism as a method for obtaining rotational and orientational constraints for oriented polymers
    • I.T. Arkin, K.R. MacKenzie, and A.T. Brunger Site-directed dichroism as a method for obtaining rotational and orientational constraints for oriented polymers J. Am. Chem. Soc. 119 1997 8973 8980
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8973-8980
    • Arkin, I.T.1    Mackenzie, K.R.2    Brunger, A.T.3
  • 43
    • 0033554426 scopus 로고    scopus 로고
    • Total chemical synthesis of the integral membrane protein influenza A virus M2: Role of its C-terminal domain in tetramer assembly 1
    • G.G. Kochendoerfer, D. Salom, J.D. Lear, R. Wilk-Orescan, S.B. Kent, and W.F. DeGrado Total chemical synthesis of the integral membrane protein influenza A virus M2: role of its C-terminal domain in tetramer assembly 1 Biochemistry 38 1999 11905 11913
    • (1999) Biochemistry , vol.38 , pp. 11905-11913
    • Kochendoerfer, G.G.1    Salom, D.2    Lear, J.D.3    Wilk-Orescan, R.4    Kent, S.B.5    Degrado, W.F.6
  • 46
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • P. Schuck On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation Anal. Biochem. 320 2003 104 124
    • (2003) Anal. Biochem. , vol.320 , pp. 104-124
    • Schuck, P.1
  • 47
    • 0032734050 scopus 로고    scopus 로고
    • Quantitation of secondary structure in ATR infrared spectroscopy
    • D. Marsh Quantitation of secondary structure in ATR infrared spectroscopy Biophys. J. 77 1999 2630 2637
    • (1999) Biophys. J. , vol.77 , pp. 2630-2637
    • Marsh, D.1
  • 49
    • 0032514753 scopus 로고    scopus 로고
    • The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis delta-endotoxin are consistent with an "umbrella-like" structure of the pore
    • E. Gazit, P. La Rocca, M.S.P. Sansom, and Y. Shai The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis delta-endotoxin are consistent with an "umbrella-like" structure of the pore Proc. Natl. Acad. Sci. U. S. A. 95 1998 12289 12294
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12289-12294
    • Gazit, E.1    La Rocca, P.2    Sansom, M.S.P.3    Shai, Y.4
  • 50
    • 65849141019 scopus 로고    scopus 로고
    • Dominant negative mutants of bacillus thuringiensis Cry1Ab toxin function as anti-toxins: Demonstration of the role of oligomerization in toxicity
    • C. Rodriguez-Almazan, L.E. Zavala, C. Munoz-Garay, N. Jimenez-Juarez, S. Pacheco, L. Masson, M. Soberon, and A. Bravo Dominant negative mutants of bacillus thuringiensis Cry1Ab toxin function as anti-toxins: demonstration of the role of oligomerization in toxicity PLoS ONE 4 2009
    • (2009) PLoS ONE , vol.4
    • Rodriguez-Almazan, C.1    Zavala, L.E.2    Munoz-Garay, C.3    Jimenez-Juarez, N.4    Pacheco, S.5    Masson, L.6    Soberon, M.7    Bravo, A.8
  • 51
    • 46049110693 scopus 로고    scopus 로고
    • The interplay of functional tuning, drug resistance, and thermodynamic stability in the evolution of the M2 proton channel from the influenza A virus
    • A.L. Stouffer, C. Ma, L. Cristian, Y. Ohigashi, R.A. Lamb, J.D. Lear, L.H. Pinto, and W.F. DeGrado The interplay of functional tuning, drug resistance, and thermodynamic stability in the evolution of the M2 proton channel from the influenza A virus Structure 16 2008 1067 1076
    • (2008) Structure , vol.16 , pp. 1067-1076
    • Stouffer, A.L.1    Ma, C.2    Cristian, L.3    Ohigashi, Y.4    Lamb, R.A.5    Lear, J.D.6    Pinto, L.H.7    Degrado, W.F.8
  • 52
    • 0023183759 scopus 로고
    • Colloid-osmotic lysis is a general feature of the mechanism of action of Bacillus thuringiensis d-endotoxins with different insect specificity
    • B.H. Knowles, and D.J. Ellar Colloid-osmotic lysis is a general feature of the mechanism of action of Bacillus thuringiensis d-endotoxins with different insect specificity Biochim. Biophys. Acta Gen. Subj. 924 1987 509 518
    • (1987) Biochim. Biophys. Acta Gen. Subj. , vol.924 , pp. 509-518
    • Knowles, B.H.1    Ellar, D.J.2
  • 53
    • 0343714762 scopus 로고    scopus 로고
    • Evidence for intermolecular interaction as a necessary step for pore-formation activity and toxicity of Bacillus thuringiensis Cry1Ab toxin
    • M. Soberon, R.V. Perez, M.E. Nunez-Valdez, A. Lorence, I. Gomez, J. Sanchez, and A. Bravo Evidence for intermolecular interaction as a necessary step for pore-formation activity and toxicity of Bacillus thuringiensis Cry1Ab toxin FEMS Microbiol. Lett. 191 2000 221 225
    • (2000) FEMS Microbiol. Lett. , vol.191 , pp. 221-225
    • Soberon, M.1    Perez, R.V.2    Nunez-Valdez, M.E.3    Lorence, A.4    Gomez, I.5    Sanchez, J.6    Bravo, A.7
  • 55
    • 0032976138 scopus 로고    scopus 로고
    • Aggregation of Bacillus thuringiensis Cry1A toxins upon binding to target insect larval midgut vesicles
    • A.I. Aronson, C.X. Geng, and L. Wu Aggregation of Bacillus thuringiensis Cry1A toxins upon binding to target insect larval midgut vesicles Appl. Environ. Microbiol. 65 1999 2503 2507
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2503-2507
    • Aronson, A.I.1    Geng, C.X.2    Wu, L.3
  • 56
    • 0035656776 scopus 로고    scopus 로고
    • The alpha-helix 4 residue, Asn135, is involved in the oligomerization of Cry1Ac1 and Cry1Ab5 Bacillus thuringiensis toxins
    • N.J. Tigue, J. Jacoby, and D.J. Ellar The alpha-helix 4 residue, Asn135, is involved in the oligomerization of Cry1Ac1 and Cry1Ab5 Bacillus thuringiensis toxins Appl. Environ. Microbiol. 67 2001 5715 5720
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 5715-5720
    • Tigue, N.J.1    Jacoby, J.2    Ellar, D.J.3
  • 57
    • 0032870058 scopus 로고    scopus 로고
    • Analysis of mutations in the pore-forming region essential for insecticidal activity of a Bacillus thuringiensis delta-endotoxin
    • A.S.M. Kumar, and A.I. Aronson Analysis of mutations in the pore-forming region essential for insecticidal activity of a Bacillus thuringiensis delta-endotoxin J. Bacteriol. 181 1999 6103 6107
    • (1999) J. Bacteriol. , vol.181 , pp. 6103-6107
    • Kumar, A.S.M.1    Aronson, A.I.2
  • 60
    • 34547899224 scopus 로고    scopus 로고
    • Two conformational states of the membrane-associated Bacillus thuringiensis Cry4Ba delta-endotoxin complex revealed by electron crystallography: Implications for toxin-pore formation
    • P. Ounjai, V.M. Unger, F.J. Sigworth, and C. Angsuthanasombat Two conformational states of the membrane-associated Bacillus thuringiensis Cry4Ba delta-endotoxin complex revealed by electron crystallography: Implications for toxin-pore formation Biochem. Biophys. Res. Commun. 361 2007 890 895
    • (2007) Biochem. Biophys. Res. Commun. , vol.361 , pp. 890-895
    • Ounjai, P.1    Unger, V.M.2    Sigworth, F.J.3    Angsuthanasombat, C.4
  • 61
    • 0347357931 scopus 로고    scopus 로고
    • Tryptophan spectroscopy studies and black lipid bilayer analysis indicate that the oligomeric structure of Cry1Ab toxin from Bacillus thuringiensis is the membrane-insertion intermediate
    • C. Rausell, C. Munoz-Garay, R. Miranda-CassoLuengo, I. Gomez, E. Rudino-Pinera, M. Soberon, and A. Bravo Tryptophan spectroscopy studies and black lipid bilayer analysis indicate that the oligomeric structure of Cry1Ab toxin from Bacillus thuringiensis is the membrane-insertion intermediate Biochemistry 43 2004 166 174
    • (2004) Biochemistry , vol.43 , pp. 166-174
    • Rausell, C.1    Munoz-Garay, C.2    Miranda-Cassoluengo, R.3    Gomez, I.4    Rudino-Pinera, E.5    Soberon, M.6    Bravo, A.7
  • 62
    • 11244299331 scopus 로고    scopus 로고
    • Unfolding events in the water-soluble monomeric Cry1Ab toxin during transition to oligomeric pre-pore and membrane-inserted pore channel
    • C. Rausell, L. Pardo-Lopez, J. Sanchez, C. Munoz-Garay, C. Morera, M. Soberon, and A. Bravo Unfolding events in the water-soluble monomeric Cry1Ab toxin during transition to oligomeric pre-pore and membrane-inserted pore channel J. Biol. Chem. 279 2004 55168 55175
    • (2004) J. Biol. Chem. , vol.279 , pp. 55168-55175
    • Rausell, C.1    Pardo-Lopez, L.2    Sanchez, J.3    Munoz-Garay, C.4    Morera, C.5    Soberon, M.6    Bravo, A.7
  • 63
    • 0034604645 scopus 로고    scopus 로고
    • Insertion and organization within membranes of the delta-endotoxin pore-forming domain, helix 4-loop-helix 5, and inhibition of its activity by a mutant helix 4 peptide
    • D. Gerber, and Y. Shai Insertion and organization within membranes of the delta-endotoxin pore-forming domain, helix 4-loop-helix 5, and inhibition of its activity by a mutant helix 4 peptide J. Biol. Chem. 275 2000 23602 23607
    • (2000) J. Biol. Chem. , vol.275 , pp. 23602-23607
    • Gerber, D.1    Shai, Y.2
  • 64
    • 0033527563 scopus 로고    scopus 로고
    • Helix 4 of the Bacillus thuringiensis Cry1Aa toxin lines the lumen of the ion channel
    • L. Masson, B.E. Tabashnik, L. Yong-Biao, R. Brousseau, and J.-L. Schwartz Helix 4 of the Bacillus thuringiensis Cry1Aa toxin lines the lumen of the ion channel J. Biol. Chem. 274 1999 31996 32000
    • (1999) J. Biol. Chem. , vol.274 , pp. 31996-32000
    • Masson, L.1    Tabashnik, B.E.2    Yong-Biao, L.3    Brousseau, R.4    Schwartz, J.-L.5
  • 66
    • 58849125465 scopus 로고    scopus 로고
    • Lipid-induced conformation of helix 7 from the pore-forming domain of the Bacillus thuringiensis Cry4Ba toxin: Implications for toxicity mechanism
    • K. Tiewsiri, W.B. Fischer, and C. Angsuthanasombat Lipid-induced conformation of helix 7 from the pore-forming domain of the Bacillus thuringiensis Cry4Ba toxin: implications for toxicity mechanism Arch. Biochem. Biophys. 482 2009 17 24
    • (2009) Arch. Biochem. Biophys. , vol.482 , pp. 17-24
    • Tiewsiri, K.1    Fischer, W.B.2    Angsuthanasombat, C.3
  • 67
    • 33745597608 scopus 로고    scopus 로고
    • A mechanism of cell death involving an adenylyl cyclase/PKA signaling pathway is induced by the Cry1Ab toxin of Bacillus thuringiensis
    • X. Zhang, M. Candas, N.B. Griko, R. Taussig, and L.A. Bulla Jr. A mechanism of cell death involving an adenylyl cyclase/PKA signaling pathway is induced by the Cry1Ab toxin of Bacillus thuringiensis Proc. Natl. Acad. Sci. U. S. A. 103 2006 9897 9902
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 9897-9902
    • Zhang, X.1    Candas, M.2    Griko, N.B.3    Taussig, R.4    Bulla, Jr.L.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.