Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli.
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Identification of two porins in Pelobacter venetianus fermenting high-molecular-mass polyethylene glycolsAn RND-type efflux system in Borrelia burgdorferi is involved in virulence and resistance to antimicrobial compoundsRv1698 of Mycobacterium tuberculosis represents a new class of channel-forming outer membrane proteinsMolecular basis of bacterial outer membrane permeabilityClostridium perfringens delta toxin is sequence related to beta toxin, NetB, and Staphylococcus pore-forming toxins, but shows functional differences.The periplasmic maltose-binding protein modifies the channel-forming characteristics of maltoporinO-mycoloylated proteins from Corynebacterium: an unprecedented post-translational modification in bacteriaCross-reactivity of anthrax and C2 toxin: protective antigen promotes the uptake of botulinum C2I toxin into human endothelial cellsThe C terminus of component C2II of Clostridium botulinum C2 toxin is essential for receptor binding.Partitioning of differently sized poly(ethylene glycol)s into OmpF porinResidue ionization and ion transport through OmpF channels.Salting out the ionic selectivity of a wide channel: the asymmetry of OmpFElectrostatic modeling of ion pores. Energy barriers and electric field profilesElectrostatic modeling of ion pores. II. Effects attributable to the membrane dipole potentialDipA, a pore-forming protein in the outer membrane of Lyme disease spirochetes exhibits specificity for the permeation of dicarboxylatesElimination of channel-forming activity by insertional inactivation of the p13 gene in Borrelia burgdorferiTime-resolved molecular transport across living cell membranes.A novel outer-membrane anion channel (porin) as part of a putatively two-component transport system for 4-toluenesulphonate in Comamonas testosteroni T-2.Identification and characterization of a novel porin family highlights a major difference in the outer membrane of chlamydial symbionts and pathogens.Corynebacterium jeikeium jk0268 constitutes for the 40 amino acid long PorACj, which forms a homooligomeric and anion-selective cell wall channel.Structure-activity relationships of carbapenems that determine their dependence on porin protein D2 for activity against Pseudomonas aeruginosa.The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.Channel-forming activity and channel size of the RTX toxins ApxI, ApxII, and ApxIII of Actinobacillus pleuropneumoniae.Pore forming activity of the potent RTX-toxin produced by pediatric pathogen Kingella kingae: Characterization and comparison to other RTX-family members.Characterization of a porin from the outer membrane of Vibrio anguillarum.OmpW of Caulobacter crescentus Functions as an Outer Membrane Channel for CationsOuter membrane protein P of Pseudomonas aeruginosa: regulation by phosphate deficiency and formation of small anion-specific channels in lipid bilayer membranes.Corynebacterium diphtheriae: identification and characterization of a channel-forming protein in the cell wallPorin channels in Escherichia coli: studies with beta-lactams in intact cellsPorin channels in Escherichia coli: studies with liposomes reconstituted from purified proteinsOuter membrane protein K of Escherichia coli: purification and pore-forming properties in lipid bilayer membranes.Characterization of a membrane pore-forming protein from Entamoeba histolytica.Purification of Legionella pneumophila major outer membrane protein and demonstration that it is a porin.Mechanism of ion transport through the anion-selective channel of the Pseudomonas aeruginosa outer membraneHydrostatic pressures developed by osmotically swelling vesicles bound to planar membranes.Pore-forming ability of major outer membrane proteins from Wolinella recta ATCC 33238.Oms38 is the first identified pore-forming protein in the outer membrane of relapsing fever spirochetes.Isolation of Neisseria meningitidis mutants deficient in class 1 (porA) and class 3 (porB) outer membrane proteinsAerolysin of Aeromonas sobria: evidence for formation of ion-permeable channels and comparison with alpha-toxin of Staphylococcus aureus.Outer membrane permeability and antibiotic resistance.
P2860
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P2860
Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli.
description
1979 nî lūn-bûn
@nan
1979年の論文
@ja
1979年論文
@yue
1979年論文
@zh-hant
1979年論文
@zh-hk
1979年論文
@zh-mo
1979年論文
@zh-tw
1979年论文
@wuu
1979年论文
@zh
1979年论文
@zh-cn
name
Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli.
@en
type
label
Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli.
@en
prefLabel
Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli.
@en
P2093
P1476
Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli.
@en
P2093
P304
P577
1979-03-01T00:00:00Z