Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli
about
Structure, function, and evolution of bacterial ATP-binding cassette systemsTransport of lipopolysaccharide across the cell envelope: the long road of discoveryFunctional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coliStructure 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 DomainsStructure ofNeisseria meningitidislipoprotein GNA1162Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transportLptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface.Structural insights into cardiolipin transfer from the Inner membrane to the outer membrane by PbgA in Gram-negative bacteriaGenetic interaction maps in Escherichia coli reveal functional crosstalk among cell envelope biogenesis pathwaysCytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. coliStructural basis for lipopolysaccharide insertion in the bacterial outer membraneA thiolate anion buried within the hydrocarbon ruler perturbs PagP lipid acyl chain selectionMaking a membrane on the other side of the wall.Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens.Accumulation of phosphatidic acid increases vancomycin resistance in Escherichia coli.Involvement of Neisseria meningitidis lipoprotein GNA2091 in the assembly of a subset of outer membrane proteinsDegP primarily functions as a protease for the biogenesis of β-barrel outer membrane proteins in the Gram-negative bacterium 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.Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex.The 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.Molecular mechanism for lateral lipid diffusion between the outer membrane external leaflet and a beta-barrel hydrocarbon rulerCharacterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics.Proteins that bind and move lipids: MsbA and NPC1.The antimicrobial mechanism of action of epsilon-poly-l-lysine.Concentration-dependent oligomerization and oligomeric arrangement of LptA.Development of an activity assay for discovery of inhibitors of lipopolysaccharide transport.Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane.The bacterial cell envelope.Nonconsecutive disulfide bond formation in an essential integral outer membrane proteinFolding LacZ in the periplasm of Escherichia coli.Bacterial cell wall. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis.Functional equivalence and evolutionary convergence in complex communities of microbial sponge symbionts.Structure-function analysis of MurJ reveals a solvent-exposed cavity containing residues essential for peptidoglycan biogenesis in Escherichia coliAnalysis of surface protein expression reveals the growth pattern of the gram-negative outer membrane.Charge requirements of lipid II flippase activity in Escherichia coliDiscovery of new biosynthetic pathways: the lipid A story.Validation of inhibitors of an ABC transporter required to transport lipopolysaccharide to the cell surface in Escherichia coli.
P2860
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P2860
Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli
description
2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
article publié dans les Procee ...... f the United States of America
@fr
artículu científicu espublizáu en 2008
@ast
im April 2008 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2008/04/08)
@sk
vědecký článek publikovaný v roce 2008
@cs
wetenschappelijk artikel (gepubliceerd op 2008/04/08)
@nl
наукова стаття, опублікована у квітні 2008
@uk
name
Identification of two inner-me ...... r membrane of Escherichia coli
@ast
Identification of two inner-me ...... r membrane of Escherichia coli
@en
Identification of two inner-me ...... r membrane of Escherichia coli
@nl
type
label
Identification of two inner-me ...... r membrane of Escherichia coli
@ast
Identification of two inner-me ...... r membrane of Escherichia coli
@en
Identification of two inner-me ...... r membrane of Escherichia coli
@nl
prefLabel
Identification of two inner-me ...... r membrane of Escherichia coli
@ast
Identification of two inner-me ...... r membrane of Escherichia coli
@en
Identification of two inner-me ...... r membrane of Escherichia coli
@nl
P2860
P50
P3181
P356
P1476
Identification of two inner-me ...... r membrane of Escherichia coli
@en
P2093
Luisa S. Gronenberg
P2860
P304
P3181
P356
10.1073/PNAS.0801196105
P407
P577
2008-04-08T00:00:00Z