The TolB protein interacts with the porins of Escherichia coli.
about
In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactionsColicin biologyThe crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicinsCoxiella burnetii glycomics and proteomics--tools for linking structure to function.Role of TolR N-terminal, central, and C-terminal domains in dimerization and interaction with TolA and tolQ.The Tol proteins of Escherichia coli and their involvement in the uptake of biomolecules and outer membrane stability.Cell entry mechanism of enzymatic bacterial colicins: porin recruitment and the thermodynamics of receptor binding.Identification and genetic characterization of PmrA-regulated genes and genes involved in polymyxin B resistance in Salmonella enterica serovar typhimuriumPolar localization of Escherichia coli chemoreceptors requires an intact Tol-Pal complexCompetitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9.Directed evolution of efficient secretion in the SRP-dependent export of TolB.Functional domains present in the mycobacterial hemagglutinin, HBHAIdentification by genetic suppression of Escherichia coli TolB residues important for TolB-Pal interactionEnergy-dependent conformational change in the TolA protein of Escherichia coli involves its N-terminal domain, TolQ, and TolR.Escherichia coli tol-pal mutants form outer membrane vesiclesColicin import into Escherichia coli cells.Mutational analysis of the Escherichia coli K-12 TolA N-terminal region and characterization of its TolQ-interacting domain by genetic suppression.RegA, iron, and growth phase regulate expression of the Pseudomonas aeruginosa tol-oprL gene cluster.Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity.Role of Pseudomonas putida tol-oprL gene products in uptake of solutes through the cytoplasmic membrane.The Salmonella enterica serovar Typhi tsx gene, encoding a nucleoside-specific porin, is essential for prototrophic growth in the absence of nucleosides.The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB.Control of the Salmonella ugd gene by three two-component regulatory systems.Deletion analyses of the peptidoglycan-associated lipoprotein Pal reveals three independent binding sequences including a TolA box.
P2860
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P2860
The TolB protein interacts with the porins of Escherichia coli.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
The TolB protein interacts with the porins of Escherichia coli.
@ast
The TolB protein interacts with the porins of Escherichia coli.
@en
type
label
The TolB protein interacts with the porins of Escherichia coli.
@ast
The TolB protein interacts with the porins of Escherichia coli.
@en
prefLabel
The TolB protein interacts with the porins of Escherichia coli.
@ast
The TolB protein interacts with the porins of Escherichia coli.
@en
P2093
P2860
P1476
The TolB protein interacts with the porins of Escherichia coli.
@en
P2093
P2860
P304
P356
10.1128/JB.179.23.7274-7279.1997
P407
P577
1997-12-01T00:00:00Z