Membrane pores: from structure and assembly, to medicine and technology

Membrane pores: from structure and assembly, to medicine and technology

Bibliografische gegevens
Hoofdauteurs:	Gilbert, RJC, Bayley, H, Anderluh, G
Formaat:	Journal article
Taal:	English
Gepubliceerd in:	Royal Society 2017

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Membrane pore formation at protein-lipid interfaces.
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Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae.
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Protein-lipid interactions and non-lamellar lipidic structures in membrane pore formation and membrane fusion
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Permeation of styryl dyes through nanometer-scale pores in membranes.
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Effects of the eukaryotic pore-forming cytolysin Equinatoxin II on lipid membranes and the role of sphingomyelin.
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Single-molecule kinetics of pore assembly by the membrane attack complex
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Surface labeling of key residues during assembly of the transmembrane pore formed by staphylococcal alpha-hemolysin.
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Inhibition of Pore-Forming Proteins
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Architecture of human perforin pore in pure lipid bilayers
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Interview: Enriching the pore. Interviewed by Hannah Stanwix.
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Incomplete pneumolysin oligomers form membrane pores.
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Engineered transmembrane pores.
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Membrane-protein structure: Piercing insights.
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PH dependence of listeriolysin O aggregation and pore-forming ability
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Temperature-responsive protein pores.
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Stochastic sensing with protein pores
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pH dependence of listeriolysin O aggregation and pore-forming ability.
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Incomplete pneumolysin oligomers form membrane pores
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Assembly of transmembrane pores from mirror-image peptides
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Exportins can inhibit major mitotic assembly events in vitro: membrane fusion, nuclear pore formation, and spindle assembly
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Polymers through pores: single-molecule experiments with nucleic acids, polypeptides and polysaccharides
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Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.
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Properties of Bacillus cereus hemolysin II: a heptameric transmembrane pore.
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Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin.
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Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin
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Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification.
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