Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface - Wikidata - wikimedia - TriplyDB

Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface

Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface

http://www.wikidata.org/entity/Q24563106

about

Membrane protein insertion: mixing eukaryotic and prokaryotic concepts.Cyanobacterial heterocysts Structure, function, and evolution of bacterial ATP-binding cassette systems Transport of lipopolysaccharide across the cell envelope: the long road of discovery Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli Lipid A modification systems in gram-negative bacteria Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli Conserved and variable functions of the sigmaE stress response in related genomes.The molecular mechanism of bacterial lipoprotein modification--how, when and why?Structure and function of an essential component of the outer membrane protein assembly machine Structure and Functional Analysis of LptC, a Conserved Membrane Protein Involved in the Lipopolysaccharide Export Pathway in Escherichia coli Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli Cytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. coli Characterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli Structural basis for lipopolysaccharide insertion in the bacterial outer membrane Characterization of a stalled complex on the β-barrel assembly machine.Lipopolysaccharide transport to the cell surface: periplasmic transport and assembly into the outer membrane.Involvement of Neisseria meningitidis lipoprotein GNA2091 in the assembly of a subset of outer membrane proteins Protease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli.Outer membrane biogenesis in Escherichia coli, Neisseria meningitidis, and Helicobacter pylori: paradigm deviations in H. pylori Genetic, biochemical, and molecular characterization of the polypeptide transport-associated domain of Escherichia coli BamA.Assembly of the β-Barrel Outer Membrane Proteins in Gram-Negative Bacteria, Mitochondria, and Chloroplasts.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.Dissection of β-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli.Involvement and necessity of the Cpx regulon in the event of aberrant beta-barrel outer membrane protein assembly.Borrelia burgdorferi locus BB0795 encodes a BamA orthologue required for growth and efficient localization of outer membrane proteins The beta-barrel outer membrane protein assembly complex of Neisseria meningitidis.Structural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membrane Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli.Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif.YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli.Evolution of the general protein import pathway of plastids (review).Genomic content of Neisseria species Concentration-dependent oligomerization and oligomeric arrangement of LptA.Loss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant.Synergistic effect of imp/ostA and msbA in hydrophobic drug resistance of Helicobacter pylori.Development of an activity assay for discovery of inhibitors of lipopolysaccharide transport.Quantitative proteomics of the Neisseria gonorrhoeae cell envelope and membrane vesicles for the discovery of potential therapeutic targets.

P2860

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P2860

Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface

http://www.wikidata.org/entity/Q24563106

description

2004 nî lūn-bûn

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2004 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2004 թվականի հունիսին հրատարակված գիտական հոդված

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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name

Identification of an outer mem ...... to the bacterial cell surface

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Identification of an outer mem ...... to the bacterial cell surface

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Identification of an outer mem ...... to the bacterial cell surface

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type

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Identification of an outer mem ...... to the bacterial cell surface

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Identification of an outer mem ...... to the bacterial cell surface

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Identification of an outer mem ...... to the bacterial cell surface

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Identification of an outer mem ...... to the bacterial cell surface

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Identification of an outer mem ...... to the bacterial cell surface

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Identification of an outer mem ...... to the bacterial cell surface

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Proceedings of the National Academy of Sciences of the United States of America

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Identification of an outer mem ...... to the bacterial cell surface

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P2093

Jan Tommassen

http://www.w3.org/2001/XMLSchema#string

Jeroen Geurtsen

http://www.w3.org/2001/XMLSchema#string

Martine P Bos

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P2860

Complete Genome Sequence of Neisseria meningitidis Serogroup B Strain MC58

Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491

Lipopolysaccharide endotoxins

An essential role of Sam50 in the protein sorting and assembly machinery of the mitochondrial outer membrane.

The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria.

Evolutionary conservation of biogenesis of beta-barrel membrane proteins.

Function of Escherichia coli MsbA, an essential ABC family transporter, in lipid A and phospholipid biosynthesis

Role of a highly conserved bacterial protein in outer membrane protein assembly

In vitro folding of Escherichia coli outer-membrane phospholipase A.

A PhoP/PhoQ-induced Lipase (PagL) that catalyzes 3-O-deacylation of lipid A precursors in membranes of Salmonella typhimurium.

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10.1073/PNAS.0402340101

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15192148

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lipopolysaccharide

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438991

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