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Ion selectivity of gram-negative bacterial porins
Zero-current potential measurements in the presence of salt gradients across lipid bilayer membranes containing individual porins gave results that were consistent with the conclusions drawn from the single-channel experiments, indicating that the ions were moving inside the pores in a fashion similar to their movement in the aqueous phase.
Regulation of adenylyl cyclase from Paramecium by an intrinsic potassium conductance.
A hyperpolarization-activated K+ efflux appears to directly regulate adenylyl cyclase activity in vivo, and is associated with secondary function as carrier of the K+ resting conductance.
Folding and membrane insertion of the trimeric beta-barrel protein OmpF.
The dependence of the yield of refolding, membrane insertion, and trimerization on pH, lipid concentration, and the presence of detergent was investigated.
Pore formation by the Escherichia coli hemolysin: evidence for an association-dissociation equilibrium of the pore-forming aggregates
Zero-current membrane potential experiments showed that the hemolysin channel is cation selective, and the mobility sequence of the cations in the channel was similar to their mobility sequence in the aqueous phase, which was consistent with the assumption that the Hemoly sin channel is wide and that the interior field strength is not very high.
Modulation of Neisseria Porin (PorB) by Cytosolic ATP/GTP of Target Cells: Parallels between Pathogen Accommodation and Mitochondrial Endosymbiosis
Patch-clamp analyses indicate that PorB channel activity is tightly regulated in intact epithelial cells, which provide important mechanistic clues on the intracellular pathogen accommodation reminiscent of mitochondrial endosymbiosis.
Mechanism of sugar transport through the sugar-specific LamB channel ofEscherichia coli outer membrane
The LamB channel of Escherichia coli outer membrane was highly cation selective, both in the presence and absence of sugars, which may be explained by the existence of carbonyl groups inside the channel.
Crystal structure of the human liver X receptor beta ligand-binding domain in complex with a synthetic agonist.
The X-ray crystal structure of the LXRbeta ligand-binding domain in complex with a synthetic agonist is reported and a binding mode and a mechanism of action for the putative natural ligands, oxidised derivatives of cholesterol are proposed.
Frigocyclinone, a Novel Angucyclinone Antibiotic Produced by a Streptomyces griseus Strain from Antarctica†
A new angucyclinone antibiotic, frigocyclinone, was isolated from Streptomyces griseus strain NTK 97, consisting of a tetrangomycin moiety attached through a C-glycosidic linkage with the
Single-channel analysis of the conductance fluctuations induced in lipid bilayer membranes by complement proteins C5b-9
Single-channel analysis of electrical fluctuations induced in planar bilayer membranes by the purified human complement proteins C5b6, C7, C8, and C9 has been analyzed and indicated that the ions move inside the complement pore in a manner similar to the way they move in the aqueous phase.
Pore formation by LamB of Escherichia coli in lipid bilayer membranes
It is concluded that the structure of the LamB channels is quite different from the structures of the channels of general diffusion porins, such as OmpF and OmpC.