Periplasmic chaperone FkpA is essential for imported colicin M toxicity.
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Crystal Structure of Colicin M, a Novel Phosphatase Specifically Imported by Escherichia coli>Activation of Colicin M by the FkpA Prolyl Cis-Trans Isomerase/ChaperoneFunctional and Structural Characterization of PaeM, a Colicin M-like Bacteriocin Produced by Pseudomonas aeruginosaThe Bam machine: a molecular cooper.Mapping functional domains of colicin M.Genome-wide screens: novel mechanisms in colicin import and cytotoxicity.Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.Identification of a target cell permissive factor required for contact-dependent growth inhibition (CDI).Role for Skp in LptD assembly in Escherichia coli.FhuA (TonA), the career of a protein.Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic ExpressionTonB or not TonB: is that the question?Nuclease colicins and their immunity proteins.Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.Deciphering the catalytic domain of colicin M, a peptidoglycan lipid II-degrading enzyme.Proteome Dynamics of the Specialist Oxalate Degrader Oxalobacter formigenes.Protein folding in the cell envelope of Escherichia coli.Structure and uptake mechanism of bacteriocins targeting peptidoglycan renewal.The phage tail tape measure protein, an inner membrane protein and a periplasmic chaperone play connected roles in the genome injection process of E. coli phage HK97.Toxicity of the colicin M catalytic domain exported to the periplasm is FkpA independent.CbrA is a flavin adenine dinucleotide protein that modifies the Escherichia coli outer membrane and confers specific resistance to Colicin MColicin M, a peptidoglycan lipid-II-degrading enzyme: potential use for antibacterial means?The ColM Family, Polymorphic Toxins Breaching the Bacterial Cell Wall.Import of periplasmic bacteriocins targeting the murein.Structural and functional analysis of cyclophilin PpiB mutants supports an in vivo function not limited to prolyl isomerization activity.A phospholipase A1 antibacterial Type VI secretion effector interacts directly with the C-terminal domain of the VgrG spike protein for delivery.
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P2860
Periplasmic chaperone FkpA is essential for imported colicin M toxicity.
description
2008 nî lūn-bûn
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2008年の論文
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年學術文章
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name
Periplasmic chaperone FkpA is essential for imported colicin M toxicity.
@en
Periplasmic chaperone FkpA is essential for imported colicin M toxicity.
@nl
type
label
Periplasmic chaperone FkpA is essential for imported colicin M toxicity.
@en
Periplasmic chaperone FkpA is essential for imported colicin M toxicity.
@nl
prefLabel
Periplasmic chaperone FkpA is essential for imported colicin M toxicity.
@en
Periplasmic chaperone FkpA is essential for imported colicin M toxicity.
@nl
P2093
P2860
P1476
Periplasmic chaperone FkpA is essential for imported colicin M toxicity.
@en
P2093
Christin Römer
Julia Hullmann
Klaus Hantke
Silke I Patzer
Volkmar Braun
P2860
P304
P356
10.1111/J.1365-2958.2008.06327.X
P407
P577
2008-06-28T00:00:00Z