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Recent findings about the Yersinia enterocolitica phage shock protein responseVIPP1 Has a Disordered C-Terminal Tail Necessary for Protecting Photosynthetic Membranes against StressPspF-binding domain PspA1-144 and the PspA·F complex: New insights into the coiled-coil-dependent regulation of AAA+ proteinsThe phage shock protein PspA facilitates divalent metal transport and is required for virulence of Salmonella enterica sv. Typhimurium.Membrane association of PspA depends on activation of the phage-shock-protein response in Yersinia enterocoliticaProteomic response of Bacillus subtilis to lantibiotics reflects differences in interaction with the cytoplasmic membrane.The HtrA-like serine protease PepD interacts with and modulates the Mycobacterium tuberculosis 35-kDa antigen outer envelope protein.Membrane stresses induced by overproduction of free fatty acids in Escherichia coli.Activity of a bacterial cell envelope stress response is controlled by the interaction of a protein binding domain with different partners.TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.Identification of the major functional proteins of prokaryotic lipid droplets.Two Novel Vesicle-Inducing Proteins in Plastids 1 Genes Cloned and Characterized in Triticum urartu.Physiological changes in rhizobia after growth in peat extract may be related to improved desiccation tolerance.Rv2744c Is a PspA Ortholog That Regulates Lipid Droplet Homeostasis and Nonreplicating Persistence in Mycobacterium tuberculosis.In vivo localizations of membrane stress controllers PspA and PspG in Escherichia coli.Structure and dynamics of thylakoids in land plants.Twin-Arginine Protein Translocation.Evaluating the role of phage-shock protein A in Burkholderia pseudomallei.The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli.In-depth profiling of the LiaR response of Bacillus subtilis.The vesicle-inducing protein 1 from Synechocystis sp. PCC 6803 organizes into diverse higher-ordered ring structuresA lower-order oligomer form of phage shock protein A (PspA) stably associates with the hexameric AAA(+) transcription activator protein PspF for negative regulation.Subcellular localization, interactions and dynamics of the phage-shock protein-like Lia response in Bacillus subtilis.Essential role of VIPP1 in chloroplast envelope maintenance in Arabidopsis.Membrane chaperoning by members of the PspA/IM30 protein family.Evidence for a role of VIPP1 in the structural organization of the photosynthetic apparatus in Chlamydomonas.Association of Mycobacterium proteins to lipid droplets.
P2860
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P2860
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
PspA can form large scaffolds in Escherichia coli.
@en
PspA can form large scaffolds in Escherichia coli.
@nl
type
label
PspA can form large scaffolds in Escherichia coli.
@en
PspA can form large scaffolds in Escherichia coli.
@nl
prefLabel
PspA can form large scaffolds in Escherichia coli.
@en
PspA can form large scaffolds in Escherichia coli.
@nl
P2093
P2860
P1433
P1476
PspA can form large scaffolds in Escherichia coli.
@en
P2093
Denise Mehner
Felix Berthelmann
Gerd Hause
Hendrik Osadnik
Kerstin Standar
Thomas Brüser
P2860
P304
P356
10.1016/J.FEBSLET.2008.09.002
P407
P577
2008-10-10T00:00:00Z