Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore. - Wikidata - wikimedia - TriplyDB

Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.

Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.

http://www.wikidata.org/entity/Q36006598

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Highly accurate classification of Watson-Crick basepairs on termini of single DNA molecules Exotoxins of Staphylococcus aureus Characterization of individual polynucleotide molecules using a membrane channel Staphylococcus aureus α-toxin: nearly a century of intrigue Obstructing toxin pathways by targeted pore blockage The Protective Antigen Component of Anthrax Toxin Forms Functional Octameric Complexes Bacterial microcompartment shells of diverse functional types possess pentameric vertex proteins Residues Essential for Panton-Valentine Leukocidin S Component Binding to Its Cell Receptor Suggest Both Plasticity and Adaptability in Its Interaction Surface Staphylococcus aureus Pore-Forming Toxins.Detection of 3'-end RNA uridylation with a protein nanopore.An engineered dimeric protein pore that spans adjacent lipid bilayers.Subunit dimers of alpha-hemolysin expand the engineering toolbox for protein nanopores Distinction between pore assembly by staphylococcal alpha-toxin versus leukotoxins.Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.The leukocidin pore: evidence for an octamer with four LukF subunits and four LukS subunits alternating around a central axis.Interactions of peptides with a protein pore.Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore.Membrane insertion of the heptameric staphylococcal alpha-toxin pore. A domino-like structural transition that is allosterically modulated by the target cell membrane.A functional protein pore with a "retro" transmembrane domain.Genetically engineered metal ion binding sites on the outside of a Channel's transmembrane beta-barrel.alpha-Hemolysin, gamma-hemolysin, and leukocidin from Staphylococcus aureus: distant in sequence but similar in structure.Membrane insertion: The strategies of toxins (review).Partial C-terminal unfolding is required for channel formation by staphylococcal alpha-toxin.Stochastic assembly of two-component staphylococcal gamma-hemolysin into heteroheptameric transmembrane pores with alternate subunit arrangements in ratios of 3:4 and 4:3.Duration learning for analysis of nanopore ionic current blockades Clustering ionic flow blockade toggles with a mixture of HMMs.Secreted virulence factor comparison between methicillin-resistant and methicillin-sensitive Staphylococcus aureus, and its relevance to atopic dermatitis.Purification and biochemical characterization of the lambda holin.Separation of heteromeric potassium channel Kcv towards probing subunit composition-regulated ion permeation and gating.Probing single nanometer-scale pores with polymeric molecular rulers.Protonation dynamics of the alpha-toxin ion channel from spectral analysis of pH-dependent current fluctuations.Polymeric nonelectrolytes to probe pore geometry: application to the alpha-toxin transmembrane channel.Field-dependent effect of crown ether (18-crown-6) on ionic conductance of alpha-hemolysin channels Conductance and ion selectivity of a mesoscopic protein nanopore probed with cysteine scanning mutagenesis.The evolution of nanopore sequencing.Membrane protein biosensing with plasmonic nanopore arrays and pore-spanning lipid membranes.Regulation of the membrane insertion and conductance activity of the metamorphic chloride intracellular channel protein CLIC1 by cholesterol.Logic Gate Operation by DNA Translocation through Biological Nanopores.Crystallization and preliminary crystallographic studies of both components of the staphylococcal LukE-LukD leukotoxin.Structure and biological activities of beta toxin from Staphylococcus aureus.

P2860

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P2860

Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.

http://www.wikidata.org/entity/Q36006598

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1994 nî lūn-bûn

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Subunit stoichiometry of staph ...... heptameric transmembrane pore.

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P2860

Alpha-toxin of Staphylococcus aureus

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Solvent content of protein crystals

The aerolysin membrane channel is formed by heptamerization of the monomer.

Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER.

Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis.

Three-dimensional crystals of membrane proteins: bacteriorhodopsin.

Staphylococcal alpha-toxin: oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate detergent micelles.

Conformational alteration in alpha-toxin from Staphylococcus aureus concomitant with the transformation of the water-soluble monomer to the membrane oligomer.

Physical states of staphylococcal alpha-toxin.

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