The mechanism of pore formation by bacterial toxins.

Rapid membrane disruption by a perforin-like protein facilitates parasite exit from host cells. Science (2008) 2.15

Midgut bacteria required for Bacillus thuringiensis insecticidal activity. Proc Natl Acad Sci U S A (2006) 2.15

The MACPF/CDC family of pore-forming toxins. Cell Microbiol (2008) 2.15

Role of pore-forming toxins in bacterial infectious diseases. Microbiol Mol Biol Rev (2013) 1.91

Structure of transmembrane pore induced by Bax-derived peptide: evidence for lipidic pores. Proc Natl Acad Sci U S A (2008) 1.70

Mitochondrial outer membrane proteins assist Bid in Bax-mediated lipidic pore formation. Mol Biol Cell (2009) 1.48

Direct three-dimensional visualization of membrane disruption by amyloid fibrils. Proc Natl Acad Sci U S A (2012) 1.24

Continuous differential impedance spectroscopy of single cells. Microfluid Nanofluidics (2009) 1.23

Identification of a prepore large-complex stage in the mechanism of action of Clostridium perfringens enterotoxin. Infect Immun (2007) 1.23

A Bayesian inference scheme to extract diffusivity and potential fields from confined single-molecule trajectories. Biophys J (2012) 1.08

The pore-forming toxin β hemolysin/cytolysin triggers p38 MAPK-dependent IL-10 production in macrophages and inhibits innate immunity. PLoS Pathog (2012) 1.05

Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence. Biophys J (2008) 1.01

Impact of distant charge reversals within a robust beta-barrel protein pore. J Phys Chem B (2010) 0.96

Structural and functional analysis of the pore-forming toxin NetB from Clostridium perfringens. MBio (2013) 0.95

The influence of membrane lipids in Staphylococcus aureus gamma-hemolysins pore formation. J Membr Biol (2008) 0.92

Risk assessment of toxins derived from Bacillus thuringiensis-synergism, efficacy, and selectivity. Environ Sci Pollut Res Int (2009) 0.92

Observing the confinement potential of bacterial pore-forming toxin receptors inside rafts with nonblinking Eu(3+)-doped oxide nanoparticles. Biophys J (2012) 0.91

Visual and functional demonstration of growing Bax-induced pores in mitochondrial outer membranes. Mol Biol Cell (2014) 0.91

Three-dimensional structure of different functional forms of the Vibrio cholerae hemolysin oligomer: a cryo-electron microscopic study. J Bacteriol (2010) 0.91

Toxins from bacteria. EXS (2010) 0.87

Probing membrane protein interactions with their lipid raft environment using single-molecule tracking and Bayesian inference analysis. PLoS One (2013) 0.86

A non-classical assembly pathway of Escherichia coli pore-forming toxin cytolysin A. J Biol Chem (2013) 0.85

Interferons increase cell resistance to Staphylococcal alpha-toxin. Infect Immun (2007) 0.84

Phobalysin, a Small β-Pore-Forming Toxin of Photobacterium damselae subsp. damselae. Infect Immun (2015) 0.83

Pro-apoptotic Bax molecules densely populate the edges of membrane pores. Sci Rep (2016) 0.82

Unravelling the bcl-2 apoptosis code with a simple model system. PLoS Biol (2008) 0.82

Sequential steps in the assembly of the multimeric outer membrane secretin PulD. J Biol Chem (2013) 0.82

Functional mapping of the lectin activity site on the β-prism domain of vibrio cholerae cytolysin: implications for the membrane pore-formation mechanism of the toxin. J Biol Chem (2012) 0.82

Evidence that membrane rafts are not required for the action of Clostridium perfringens enterotoxin. Infect Immun (2008) 0.81

Engineered nanoparticles mimicking cell membranes for toxin neutralization. Adv Drug Deliv Rev (2015) 0.81

Bayesian decision tree for the classification of the mode of motion in single-molecule trajectories. PLoS One (2013) 0.80

Crystallization and preliminary crystallographic analysis of the Clostridium perfringens enterotoxin. Acta Crystallogr Sect F Struct Biol Cryst Commun (2010) 0.79

Haemolytic actinoporins interact with carbohydrates using their lipid-binding module. Philos Trans R Soc Lond B Biol Sci (2017) 0.78

Clostridium perfringens Delta-Toxin Induces Rapid Cell Necrosis. PLoS One (2016) 0.77

Identification of a Membrane-bound Prepore Species Clarifies the Lytic Mechanism of Actinoporins. J Biol Chem (2016) 0.76

Cationic polymers inhibit the conductance of lysenin channels. ScientificWorldJournal (2013) 0.76

Toxicological Evaluation of a Potential Immunosensitizer for Use as a Mucosal Adjuvant-Bacillus thuringiensis Cry1Ac Spore-Crystals: A Possible Inverse Agonist that Deserves Further Investigation. Toxins (Basel) (2015) 0.75

Rapid conditional targeted ablation model for hemolytic anemia in the rat. Physiol Genomics (2016) 0.75

Light Scattering By Optically-Trapped Vesicles Affords Unprecedented Temporal Resolution Of Lipid-Raft Dynamics. Sci Rep (2017) 0.75

The protofilament structure of insulin amyloid fibrils. Proc Natl Acad Sci U S A (2002) 4.08

Structural basis of pore formation by the bacterial toxin pneumolysin. Cell (2005) 2.87

Structure of an Hsp90-Cdc37-Cdk4 complex. Mol Cell (2006) 2.62

Structural basis for the regulated protease and chaperone function of DegP. Nature (2008) 2.56

Structure of a type IV secretion system core complex. Science (2009) 2.36

The structural basis for membrane binding and pore formation by lymphocyte perforin. Nature (2010) 2.23

The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter. Proc Natl Acad Sci U S A (2005) 2.02

Friend or foe: the same fold for attack and defense. Trends Immunol (2008) 1.99

Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites. Nat Commun (2011) 1.96

Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes. Nat Struct Mol Biol (2006) 1.94

Atomic structure and hierarchical assembly of a cross-β amyloid fibril. Proc Natl Acad Sci U S A (2013) 1.75

Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell (2007) 1.56

Perforin forms transient pores on the target cell plasma membrane to facilitate rapid access of granzymes during killer cell attack. Blood (2013) 1.53

Topologies of a substrate protein bound to the chaperonin GroEL. Mol Cell (2007) 1.52

Recognition and separation of single particles with size variation by statistical analysis of their images. J Mol Biol (2004) 1.45

Detection and separation of heterogeneity in molecular complexes by statistical analysis of their two-dimensional projections. J Struct Biol (2007) 1.45

The calcium channel alpha2delta-2 subunit partitions with CaV2.1 into lipid rafts in cerebellum: implications for localization and function. J Neurosci (2006) 1.42

ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin. Cell (2012) 1.41

Visualization of macromolecular structures. Nat Methods (2010) 1.34

Motor mechanism for protein threading through Hsp104. Mol Cell (2009) 1.33

Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system. Proc Natl Acad Sci U S A (2009) 1.29

Dodecameric structure of the small heat shock protein Acr1 from Mycobacterium tuberculosis. J Biol Chem (2005) 1.24

Direct three-dimensional visualization of membrane disruption by amyloid fibrils. Proc Natl Acad Sci U S A (2012) 1.24

Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils. J Mol Biol (2009) 1.21

RNA channelling by the eukaryotic exosome. EMBO Rep (2010) 1.16

Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF. Science (2013) 1.13

Multiple states of a nucleotide-bound group 2 chaperonin. Structure (2008) 1.11

Elongated oligomers assemble into mammalian PrP amyloid fibrils. J Mol Biol (2006) 1.10

Chlamydiae assemble a pathogen synapse to hijack the host endoplasmic reticulum. Traffic (2012) 1.09

Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. Structure (2006) 1.06

Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs. Curr Opin Struct Biol (2004) 1.06

A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation. Nat Struct Mol Biol (2004) 1.05

Go hybrid: EM, crystallography, and beyond. Curr Opin Struct Biol (2012) 1.01

Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes. EMBO J (2003) 1.01

Amyloid-β nanotubes are associated with prion protein-dependent synaptotoxicity. Nat Commun (2013) 1.00

Methods for three-dimensional reconstruction of heterogeneous assemblies. Methods Enzymol (2010) 0.95

Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Nat Struct Mol Biol (2012) 0.93

An expanded and flexible form of the vacuolar ATPase membrane sector. Structure (2006) 0.92

Pathogen-host reorganization during Chlamydia invasion revealed by cryo-electron tomography. Cell Microbiol (2014) 0.91

Location of auxilin within a clathrin cage. J Mol Biol (2004) 0.90

An expanded protein folding cage in the GroEL-gp31 complex. J Mol Biol (2006) 0.90

Cryo electron microscopy structures of Hsp100 proteins: crowbars in or out? Biochem Cell Biol (2010) 0.88

ATP-driven molecular chaperone machines. Biopolymers (2013) 0.86

Separating and visualising protein assemblies by means of preparative mass spectrometry and microscopy. J Struct Biol (2010) 0.85