메뉴 건너뛰기




Volumn 495, Issue 7442, 2013, Pages 520-523

A syringe-like injection mechanism in Photorhabdus luminescens toxins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; TOXIN COMPLEX C; TOXIN COMPLEX DA1; UNCLASSIFIED DRUG;

EID: 84875620662     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11987     Document Type: Article
Times cited : (114)

References (25)
  • 1
    • 33645876474 scopus 로고    scopus 로고
    • The regulation of pathogenicity and mutualism in Photorhabdus
    • Joyce, S. A., Watson, R. J. & Clarke, D. J. The regulation of pathogenicity and mutualism in Photorhabdus. Curr. Opin. Microbiol. 9, 127-132 (2006).
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 127-132
    • Joyce, S.A.1    Watson, R.J.2    Clarke, D.J.3
  • 2
    • 0034085695 scopus 로고    scopus 로고
    • Novel insecticidal toxins from nematode-symbiotic bacteria
    • ffrench-Constant, R. H. & Bowen, D. J. Novel insecticidal toxins from nematode-symbiotic bacteria. Cell. Mol. Life Sci. 57, 828-833 (2000).
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 828-833
    • Ffrench-Constant, R.H.1    Bowen, D.J.2
  • 4
    • 79959549094 scopus 로고    scopus 로고
    • Insecticidal toxin complex proteins from Xenorhabdus nematophilus: Structure and pore formation
    • Sheets, J. J. et al. Insecticidal toxin complex proteins from Xenorhabdus nematophilus: structure and pore formation. J. Biol. Chem. 286, 22742-22749 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 22742-22749
    • Sheets, J.J.1
  • 5
    • 77649193972 scopus 로고    scopus 로고
    • Photorhabdus luminescens toxins ADP-ribosylate actin and RhoA to force actin clustering
    • Lang, A. E. et al. Photorhabdus luminescens toxins ADP-ribosylate actin and RhoA to force actin clustering. Science 327, 1139-1142 (2010).
    • (2010) Science , vol.327 , pp. 1139-1142
    • Lang, A.E.1
  • 6
    • 79954610769 scopus 로고    scopus 로고
    • Targeting of the actin cytoskeleton by insecticidal toxins from Photorhabdus luminescens
    • Lang, A. E., Schmidt, G., Sheets, J. J. & Aktories, K. Targeting of the actin cytoskeleton by insecticidal toxins from Photorhabdus luminescens. Naunyn Schmiedebergs Arch. Pharmacol. 383, 227-235 (2011).
    • (2011) Naunyn Schmiedebergs Arch. Pharmacol. , vol.383 , pp. 227-235
    • Lang, A.E.1    Schmidt, G.2    Sheets, J.J.3    Aktories, K.4
  • 7
    • 80051693604 scopus 로고    scopus 로고
    • Actin as target for modification by bacterial protein toxins
    • Aktories, K., Lang, A. E., Schwan, C. & Mannherz, H. G. Actin as target for modification by bacterial protein toxins. FEBS J. 278, 4526-4543 (2011).
    • (2011) FEBS J. , vol.278 , pp. 4526-4543
    • Aktories, K.1    Lang, A.E.2    Schwan, C.3    Mannherz, H.G.4
  • 8
    • 0032568883 scopus 로고    scopus 로고
    • Insecticidal toxins from the bacterium Photorhabdus luminescens
    • Bowen, D. et al. Insecticidal toxins from the bacterium Photorhabdus luminescens. Science 280, 2129-2132 (1998).
    • (1998) Science , vol.280 , pp. 2129-2132
    • Bowen, D.1
  • 9
    • 84855505454 scopus 로고    scopus 로고
    • 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity
    • Landsberg, M. J. et al. 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity. Proc. Natl Acad. Sci. USA 108, 20544-20549 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 20544-20549
    • Landsberg, M.J.1
  • 10
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: Receptor binding, internalization, pore formation, and translocation
    • Young, J. A. T. & Collier, R. J. Anthrax toxin: receptor binding, internalization, pore formation, and translocation. Annu. Rev. Biochem. 76, 243-265 (2007).
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 243-265
    • Young, J.A.T.1    Collier, R.J.2
  • 11
    • 77649244670 scopus 로고    scopus 로고
    • Three-dimensional structure of the anthrax toxin pore inserted into lipid nanodiscs and lipid vesicles
    • Katayama, H. et al. Three-dimensional structure of the anthrax toxin pore inserted into lipid nanodiscs and lipid vesicles. Proc. Natl Acad. Sci. USA 107, 3453-3457 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 3453-3457
    • Katayama, H.1
  • 12
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal a-hemolysin, a heptameric transmembrane pore
    • Song, L. et al. Structure of staphylococcal a-hemolysin, a heptameric transmembrane pore. Science 274, 1859-1865 (1996).
    • (1996) Science , vol.274 , pp. 1859-1865
    • Song, L.1
  • 13
    • 33750684655 scopus 로고    scopus 로고
    • Bacterial protein toxins and lipids: Pore formation or toxin entry into cells
    • Geny, B. & Popoff, M. R. Bacterial protein toxins and lipids: pore formation or toxin entry into cells. Biol. Cell 98, 667-678 (2006).
    • (2006) Biol. Cell , vol.98 , pp. 667-678
    • Geny, B.1    Popoff, M.R.2
  • 14
    • 9244241054 scopus 로고    scopus 로고
    • Pore-forming protein toxins: From structure to function
    • Parker, M. W. & Feil, S. C. Pore-forming protein toxins: from structure to function. Prog. Biophys. Mol. Biol. 88, 91-142 (2005).
    • (2005) Prog. Biophys. Mol. Biol. , vol.88 , pp. 91-142
    • Parker, M.W.1    Feil, S.C.2
  • 16
    • 33745748447 scopus 로고    scopus 로고
    • Cytotoxin ClyA from Escherichia coli assembles to a 13-meric pore independent of its redox-state
    • Eifler, N. et al. Cytotoxin ClyA from Escherichia coli assembles to a 13-meric pore independent of its redox-state. EMBO J. 25, 2652-2661 (2006).
    • (2006) EMBO J. , vol.25 , pp. 2652-2661
    • Eifler, N.1
  • 17
    • 34347236541 scopus 로고    scopus 로고
    • Critical role of electrostatic interactions of amino acids at the cytoplasmic regionofhelices3and6inrhodopsin conformationalproperties and activation
    • Ramon, E. et al. Critical role of electrostatic interactions of amino acids at the cytoplasmic regionofhelices3and6inrhodopsin conformationalproperties and activation. J. Biol. Chem. 282, 14272-14282 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 14272-14282
    • Ramon, E.1
  • 18
    • 0021417293 scopus 로고
    • Extremely high pH in biological systems: A model for carbonate transport
    • Dow, J. A. Extremely high pH in biological systems: a model for carbonate transport. Am. J. Physiol. 246, R633-R636 (1984).
    • (1984) Am. J. Physiol. , vol.246
    • Dow, J.A.1
  • 19
    • 0013100556 scopus 로고
    • Heterorhabditis bacteriophora as a vector for introducing its associated bacterium into the hemocoel of Galleria mellonella larvae
    • Milstead, J. E. Heterorhabditis bacteriophora as a vector for introducing its associated bacterium into the hemocoel of Galleria mellonella larvae. J. Invertebr. Pathol. 33, 324-327 (1979).
    • (1979) J. Invertebr. Pathol. , vol.33 , pp. 324-327
    • Milstead, J.E.1
  • 20
    • 0037268543 scopus 로고    scopus 로고
    • Photorhabdus: Towardsa functional genomic analysis ofa symbiont and pathogen
    • Ffrench-Constant, R, et al. Photorhabdus: towardsa functional genomic analysis ofa symbiont and pathogen. FEMS Microbiol. Rev. 26, 433-456 (2003).
    • (2003) FEMS Microbiol. Rev. , vol.26 , pp. 433-456
    • Ffrench-Constant, R.1
  • 21
    • 33845296470 scopus 로고    scopus 로고
    • SPARX, a new environment for cryo-EM image processing
    • Hohn, M. et al. SPARX, a new environment for cryo-EM image processing. J. Struct. Biol. 157, 47-55 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 47-55
    • Hohn, M.1
  • 22
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determinationof localdefocus and specimen tilt in electron microscopy
    • Mindell, J. A. & Grigorieff, N. Accurate determinationof localdefocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 23
    • 80053642374 scopus 로고    scopus 로고
    • The Phenix software for automated determination of macromolecular structures
    • Adams, P. D. et al. The Phenix software for automated determination of macromolecular structures. Methods 55, 94-106 (2011).
    • (2011) Methods , vol.55 , pp. 94-106
    • Adams, P.D.1
  • 24
    • 84860577952 scopus 로고    scopus 로고
    • Automated tracing of filaments in 3D electron tomography reconstructions using Sculptor and Situs
    • Rusu, M., Starosolski, Z., Wahle, M., Rigort, A. & Wriggers, W. Automated tracing of filaments in 3D electron tomography reconstructions using Sculptor and Situs. J. Struct. Biol. 178, 121-128 (2012).
    • (2012) J. Struct. Biol. , vol.178 , pp. 121-128
    • Rusu, M.1    Starosolski, Z.2    Wahle, M.3    Rigort, A.4    Wriggers, W.5
  • 25
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.