YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli.
about
Rooting the tree of life by transition analysesMycobacterial outer membranes: in search of proteinsIdentification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coliA growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesisFrom evolution to pathogenesis: the link between β-barrel assembly machineries in the outer membrane of mitochondria and gram-negative bacteriaFold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranesCrystal Structure of YaeT: Conformational Flexibility and Substrate RecognitionStructure of Escherichia coli BamB and its interaction with POTRA domains of BamAContact-Dependent Growth Inhibition (CDI) and CdiB/CdiA Two-Partner Secretion ProteinsProteomic profiling of the outer membrane fraction of the obligate intracellular bacterial pathogen Ehrlichia ruminantiumFrom Chaperones to the Membrane with a BAM!BamA POTRA Domain Interacts with a Native Lipid Membrane SurfaceClassifying β-Barrel Assembly Substrates by Manipulating Essential Bam Complex Members.Maximized Autotransporter-Mediated Expression (MATE) for Surface Display and Secretion of Recombinant Proteins in Escherichia coliAssembly of the secretion pores GspD, Wza and CsgG into bacterial outer membranes does not require the Omp85 proteins BamA or TamA.The chloroplast outer envelope protein P39 in Arabidopsis thaliana belongs to the Omp85 protein family.In vivo roles of BamA, BamB and BamD in the biogenesis of BamA, a core protein of the β-barrel assembly machine of Escherichia coli.Genetic assessment of the role of AcrB β-hairpins in the assembly of the TolC-AcrAB multidrug efflux pump of Escherichia coliSpecies-specificity of the BamA component of the bacterial outer membrane protein-assembly machinery.Structural modeling and physicochemical characterization provide evidence that P66 forms a β-barrel in the Borrelia burgdorferi outer membrane.The β-barrel assembly machinery (BAM) is required for the assembly of a primitive S-layer protein in the ancient outer membrane of Thermus thermophilus.Outer membrane biogenesis in Escherichia coli, Neisseria meningitidis, and Helicobacter pylori: paradigm deviations in H. pyloriConserved residues of the putative L6 loop of Escherichia coli BamA play a critical role in the assembly of β-barrel outer membrane proteins, including that of BamA itselfDissecting the Escherichia coli periplasmic chaperone network using differential proteomics.The bacterial outer membrane β-barrel assembly machinery.Genetic, biochemical, and molecular characterization of the polypeptide transport-associated domain of Escherichia coli BamA.BB0324 and BB0028 are constituents of the Borrelia burgdorferi β-barrel assembly machine (BAM) complex.Activation of the Escherichia coli β-barrel assembly machine (Bam) is required for essential components to interact properly with substrate.Assembly of the β-Barrel Outer Membrane Proteins in Gram-Negative Bacteria, Mitochondria, and Chloroplasts.Two-partner secretion of gram-negative bacteria: a single β-barrel protein enables transport across the outer membraneAssembly of Outer Membrane β-Barrel Proteins: the Bam Complex.Substitutions in the BamA β-barrel domain overcome the conditional lethal phenotype of a ΔbamB ΔbamE strain of Escherichia coliThe fimbrial usher FimD follows the SurA-BamB pathway for its assembly in the outer membrane of Escherichia coliThe essential β-barrel assembly machinery complex components BamD and BamA are required for autotransporter biogenesis.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 proteinsThe BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane {beta}-barrel proteins in Caulobacter crescentus.The beta-barrel outer membrane protein assembly complex of Neisseria meningitidis.Biogenesis of beta-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence.
P2860
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P2860
YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
YaeT (Omp85) affects the assem ...... proteins of Escherichia coli.
@en
YaeT
@nl
type
label
YaeT (Omp85) affects the assem ...... proteins of Escherichia coli.
@en
YaeT
@nl
prefLabel
YaeT (Omp85) affects the assem ...... proteins of Escherichia coli.
@en
YaeT
@nl
P2860
P1476
YaeT (Omp85) affects the assem ...... proteins of Escherichia coli.
@en
P2093
John Werner
Rajeev Misra
P2860
P304
P356
10.1111/J.1365-2958.2005.04775.X
P407
P577
2005-09-01T00:00:00Z