Substrate Specificity within a Family of Outer Membrane Carboxylate Channels - Wikidata - awgldk - TriplyDB

Substrate Specificity within a Family of Outer Membrane Carboxylate Channels

Substrate Specificity within a Family of Outer Membrane Carboxylate Channels

http://www.wikidata.org/entity/Q27676856

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Molecular Simulations of Gram-Negative Bacterial Membranes: A Vignette of Some Recent Successes Watching single proteins using engineered nanopores Structural Basis for Outer Membrane Sugar Uptake in Pseudomonads Toward Understanding the Outer Membrane Uptake of Small Molecules by Pseudomonas aeruginosa Structure of the virulence-associated protein VapD from the intracellular pathogenRhodococcus equi Dual roles of Pseudomonas aeruginosa AlgE in secretion of the virulence factor alginate and formation of the secretion complex The OpdQ porin of Pseudomonas aeruginosa is regulated by environmental signals associated with cystic fibrosis including nitrate-induced regulation involving the NarXL two-component system The RCSB Protein Data Bank: new resources for research and education Quasithermodynamic contributions to the fluctuations of a protein nanopore.Does the lipid environment impact the open-state conductance of an engineered β-barrel protein nanopore?Cation selectivity is a conserved feature in the OccD subfamily of Pseudomonas aeruginosa.An outer membrane protein undergoes enthalpy- and entropy-driven transitions OccK channels from Pseudomonas aeruginosa exhibit diverse single-channel electrical signatures but conserved anion selectivity CHEXVIS: a tool for molecular channel extraction and visualization The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria.Properties and Phylogeny of 76 Families of Bacterial and Eukaryotic Organellar Outer Membrane Pore-Forming Proteins Global redesign of a native β-barrel scaffold.In Silico Structure and Sequence Analysis of Bacterial Porins and Specific Diffusion Channels for Hydrophilic Molecules: Conservation, Multimericity and Multifunctionality.Fit and resistant is a worst case scenario with bacterial pathogens Enhanced in vivo fitness of carbapenem-resistant oprD mutants of Pseudomonas aeruginosa revealed through high-throughput sequencing.The Transmembrane Domain of a Bicomponent ABC Transporter Exhibits Channel-Forming Activity.Probing the binding affinities of imipenem and ertapenem for outer membrane carboxylate channel D1 (OccD1) from P. aeruginosa: simulation studies.Identification of unique in-frame deletions in OprD among clinical isolates of Pseudomonas aeruginosa.Exploring bacterial outer membrane barrier to combat bad bugs.Atomistic molecular-dynamics simulations enable prediction of the arginine permeation pathway through OccD1/OprD from Pseudomonas aeruginosa.The Acinetobacter Outer Membrane Contains Multiple Specific Channels for Carbapenem β-Lactams as Revealed by Kinetic Characterization Analyses of Imipenem Permeation into Acinetobacter baylyi Cells.Mechanisms of intrinsic resistance and acquired susceptibility of Pseudomonas aeruginosa isolated from cystic fibrosis patients to temocillin, a revived antibiotic.Exploring metal effects and synergistic interactions of ferric stimulation on azo-dye decolorization by new indigenous Acinetobacter guillouiae Ax-9 and Rahnella aquatilis DX2b.Structure, function and regulation of Pseudomonas aeruginosa porins.Understanding antibiotic resistance via outer membrane permeability.Community-led comparative genomic and phenotypic analysis of the aquaculture pathogen Pseudomonas baetica a390T sequenced by Ion semiconductor and Nanopore technologies.Theoretical analysis of ion conductance and gating transitions in the OpdK (OccK1) channel In silico proteomic and phylogenetic analysis of the outer membrane protein repertoire of gastric Helicobacter species

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Substrate Specificity within a Family of Outer Membrane Carboxylate Channels

http://www.wikidata.org/entity/Q27676856

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2012 nî lūn-bûn

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2012 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2012 թվականի հունվարին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Substrate Specificity within a Family of Outer Membrane Carboxylate Channels

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Substrate Specificity within a Family of Outer Membrane Carboxylate Channels

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Substrate Specificity within a Family of Outer Membrane Carboxylate Channels

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Substrate Specificity within a Family of Outer Membrane Carboxylate Channels

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JOURNAL.PBIO.1001242

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Substrate Specificity within a Family of Outer Membrane Carboxylate Channels

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Belete R Cheneke

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Bryan W Lepore

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Debra S Touw

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Elif Eren

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Jagamya Vijayaraghavan

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Jiaming Liu

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Mridhu Indic

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P2860

Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen

X-ray structure of a protein-conducting channel

An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane

Structural insight into OprD substrate specificity

Crystal structure of the outer membrane protein OpdK from Pseudomonas aeruginosa

Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB

Structure of a putative BenF-like porin from Pseudomonas fluorescens Pf-5 at 2.6 Å resolution

Ligand-gated diffusion across the bacterial outer membrane

Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway

Coot: model-building tools for molecular graphics

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e1001242

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scholarly article

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2165373

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10.1371/JOURNAL.PBIO.1001242

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P433

1

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10

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Liviu Movileanu

Bert van den Berg

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2012-01-01T00:00:00Z

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221772661

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22272184

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3260308

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