Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane.
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The structural biology of β-barrel membrane proteins: a summary of recent reportsProtein-protein interactions and the spatiotemporal dynamics of bacterial outer membrane proteinsThe molecular mechanism of bacterial lipoprotein modification--how, when and why?Structure and Functional Analysis of LptC, a Conserved Membrane Protein Involved in the Lipopolysaccharide Export Pathway in Escherichia coliThe Escherichia coli Lpt Transenvelope Protein Complex for Lipopolysaccharide Export Is Assembled via Conserved Structurally Homologous DomainsLptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface.Structural basis for outer membrane lipopolysaccharide insertionCrystal structure of LptH, the periplasmic component of the lipopolysaccharide transport machinery from Pseudomonas aeruginosaGenetic interaction maps in Escherichia coli reveal functional crosstalk among cell envelope biogenesis pathwaysLipopolysaccharide (LPS) inner-core phosphates are required for complete LPS synthesis and transport to the outer membrane in Pseudomonas aeruginosa PAO1Cytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. coliStructural basis for lipopolysaccharide insertion in the bacterial outer membraneEvidence Suggesting That Francisella tularensis O-Antigen Capsule Contains a Lipid A-Like Molecule That Is Structurally Distinct from the More Abundant Free Lipid AAll-atom 3D structure prediction of transmembrane β-barrel proteins from sequencesMaking a membrane on the other side of the wall.Characterization of a stalled complex on the β-barrel assembly machine.Consensus computational network analysis for identifying candidate outer membrane proteins from Borrelia spirochetes.Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens.Lipopolysaccharide transport to the cell surface: periplasmic transport and assembly into the outer membrane.Outer membrane lipoprotein biogenesis: Lol is not the end.Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins.Accumulation of phosphatidic acid increases vancomycin resistance in Escherichia coli.Protease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli.Dominant negative lptE mutation that supports a role for LptE as a plug in the LptD barrel.Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide exportOuter membrane biogenesis in Escherichia coli, Neisseria meningitidis, and Helicobacter pylori: paradigm deviations in H. pyloriThe Bam machine: a molecular cooper.Lipoprotein LptE is required for the assembly of LptD by the beta-barrel assembly machine in the outer membrane of Escherichia coli.The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrelThe protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.Lipopolysaccharide Density and Structure Govern the Extent and Distance of Nanoparticle Interaction with Actual and Model Bacterial Outer Membranes.Concentration-dependent oligomerization and oligomeric arrangement of LptA.Nonconsecutive disulfide bond formation in an essential integral outer membrane proteinFolding LacZ in the periplasm of Escherichia coli.Adaptation and preadaptation of Salmonella enterica to Bile.Inhibition of lipopolysaccharide transport to the outer membrane in Pseudomonas aeruginosa by peptidomimetic antibiotics.Osmoporin OmpC forms a complex with MlaA to maintain outer membrane lipid asymmetry in Escherichia coli.A mutant Escherichia coli that attaches peptidoglycan to lipopolysaccharide and displays cell wall on its surface.Dissecting Escherichia coli outer membrane biogenesis using differential proteomics.TGD1, -2, and -3 proteins involved in lipid trafficking form ATP-binding cassette (ABC) transporter with multiple substrate-binding proteins.
P2860
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P2860
Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane.
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Characterization of the two-pr ...... ssembly at the outer membrane.
@ast
Characterization of the two-pr ...... ssembly at the outer membrane.
@en
type
label
Characterization of the two-pr ...... ssembly at the outer membrane.
@ast
Characterization of the two-pr ...... ssembly at the outer membrane.
@en
prefLabel
Characterization of the two-pr ...... ssembly at the outer membrane.
@ast
Characterization of the two-pr ...... ssembly at the outer membrane.
@en
P2860
P50
P356
P1476
Characterization of the two-pr ...... assembly at the outer membrane
@en
P2093
Daniel Kahne
Gitanjali Chimalakonda
P2860
P304
P356
10.1073/PNAS.0912872107
P407
P577
2010-03-04T00:00:00Z