Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution - Wikidata - awgldk - TriplyDB

Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

http://www.wikidata.org/entity/Q27730332

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Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site OmpT: molecular dynamics simulations of an outer membrane enzyme Crystal structure at 2.6-A resolution of human macrophage migration inhibitory factor Structure, function, and evolution of bacterial ATP-binding cassette systems Interaction of bacteriophage l with its E. coli receptor, LamB Structural details of an interaction between cardiolipin and an integral membrane protein Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane Structural basis for alginate secretion across the bacterial outer membrane Structural Basis for Outer Membrane Sugar Uptake in Pseudomonads Wzi Is an Outer Membrane Lectin that Underpins Group 1 Capsule Assembly in Escherichia coli Structural basis for substrate specificity in the Escherichia coli maltose transport system Structure and function of the PorB porin from disseminating Neisseria gonorrhoeae Structural and functional characterization of OmpF porin mutants selected for larger pore size. I. Crystallographic analysis Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation A feast of membrane protein structures in Madrid. Workshop: Pumps, channels and transporters: structure and function Molecular basis of bacterial outer membrane permeability revisited Membrane integration of an essential β-barrel protein prerequires burial of an extracellular loop.Conformation-specific labeling of BamA and suppressor analysis suggest a cyclic mechanism for β-barrel assembly in Escherichia coli Gating and conduction of nano-channel forming proteins: a computational approach.OccK channels from Pseudomonas aeruginosa exhibit diverse single-channel electrical signatures but conserved anion selectivity Folding studies of purified LamB protein, the maltoporin from the Escherichia coli outer membrane: trimer dissociation can be separated from unfolding.The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel Crystallization of Escherichia coli maltoporin in the trigonal space group R3.Redesign of a plugged beta-barrel membrane protein.Membrane interactions control residue fluctuations of outer membrane porins.Porins in prokaryotes and eukaryotes: common themes and variations.Proteomic analysis of Neorickettsia sennetsu surface-exposed proteins and porin activity of the major surface protein P51 Elucidating in vivo structural dynamics in integral membrane protein by hydroxyl radical footprinting Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation.High resolution crystal structures and molecular dynamics studies reveal substrate binding in the porin Omp32.Homology modelling of transferrin-binding protein A from Neisseria meningitidis.Crystal structure of the bacterial nucleoside transporter Tsx.Assembly of TolC, a structurally unique and multifunctional outer membrane protein of Escherichia coli K-12 Functional reconstitution, gene isolation and topology modelling of porins from Burkholderia pseudomallei and Burkholderia thailandensis Role of surface-exposed loops of Haemophilus influenzae protein P2 in the mitogen-activated protein kinase cascade Topology of the Erwinia chrysanthemi oligogalacturonate porin KdgM.The beta-barrel finder (BBF) program, allowing identification of outer membrane beta-barrel proteins encoded within prokaryotic genomes.A 3D model of the voltage-dependent anion channel (VDAC).

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P2860

Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

http://www.wikidata.org/entity/Q27730332

description

1995 nî lūn-bûn

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1995 թուականի Յունուարին հրատարակուած գիտական յօդուած

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1995年の論文

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Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

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Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

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Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

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Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

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Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

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Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

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Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

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Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

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Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

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Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

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J P Rosenbusch

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T A Keller

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T Schirmer

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Y F Wang

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P2860

Crystal structures explain functional properties of two E. coli porins

Structural principles of alpha/beta barrel proteins: the packing of the interior of the sheet

Molecular architecture and electrostatic properties of a bacterial porin.

A common channel-forming motif in evolutionarily distant porins.

Stoichiometry of maltodextrin-binding sites in LamB, an outer membrane protein from Escherichia coli.

Prediction of membrane-spanning beta-strands and its application to maltoporin.

Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli

Selectivity in solute transport: binding sites and channel structure in maltoporin and other bacterial sugar transport proteins.

Maltose transport and starch binding in phage-resistant point mutants of maltoporin. Functional and topological implications.

Selectivity for maltose and maltodextrins of maltoporin, a pore-forming protein of E. coli outer membrane.

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