Isolation and amino acid sequence of a new 22-kDa FKBP-like peptidyl-prolyl cis/trans-isomerase of Escherichia coli. Similarity to Mip-like proteins of pathogenic bacteria.
about
Global genomic analysis of AlgU (sigma(E))-dependent promoters (sigmulon) in Pseudomonas aeruginosa and implications for inflammatory processes in cystic fibrosisChaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli.Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.Prolyl isomerases in a minimal cell. Catalysis of protein folding by trigger factor from Mycoplasma genitalium.Inhibitor-induced conformational stabilization and structural alteration of a mip-like peptidyl prolyl cis-trans isomerase and its C-terminal domainFK506-Binding protein 22 from a psychrophilic bacterium, a cold shock-inducible peptidyl prolyl isomerase with the ability to assist in protein folding.Decreased intracellular survival of an fkpA mutant of Salmonella typhimurium CopenhagenSequence-based classification scheme for the genus Legionella targeting the mip gene.Biochemical and genetic characterization of an FK506-sensitive peptidyl prolyl cis-trans isomerase from a thermophilic archaeon, Methanococcus thermolithotrophicus.Biochemical and functional analyses of the Mip protein: influence of the N-terminal half and of peptidylprolyl isomerase activity on the virulence of Legionella pneumophila.The PPIase active site of Legionella pneumophila Mip protein is involved in the infection of eukaryotic host cells.Demarcating SurA activities required for outer membrane targeting of Yersinia pseudotuberculosis adhesins.Varying dependency of periplasmic peptidylprolyl cis-trans isomerases in promoting Yersinia pseudotuberculosis stress tolerance and pathogenicity.Characterization of Medicago truncatula (barrel medic) hydroperoxide lyase (CYP74C3), a water-soluble detergent-free cytochrome P450 monomer whose biological activity is defined by monomer-micelle associationThe Escherichia coli FKBP-type PPIase SlyD is required for the stabilization of the E lysis protein of bacteriophage phi X174.Collagen binding protein Mip enables Legionella pneumophila to transmigrate through a barrier of NCI-H292 lung epithelial cells and extracellular matrix.Binding analysis of a psychrotrophic FKBP22 to a folding intermediate of protein using surface plasmon resonance.Sequence diversification of the FK506-binding proteins in several different genomes.Proline substitutions in a Mip-like peptidyl-prolyl cis-trans isomerase severely affect its structure, stability, shape and activity.
P2860
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P2860
Isolation and amino acid sequence of a new 22-kDa FKBP-like peptidyl-prolyl cis/trans-isomerase of Escherichia coli. Similarity to Mip-like proteins of pathogenic bacteria.
description
1996 nî lūn-bûn
@nan
1996 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Isolation and amino acid seque ...... oteins of pathogenic bacteria.
@ast
Isolation and amino acid seque ...... oteins of pathogenic bacteria.
@en
type
label
Isolation and amino acid seque ...... oteins of pathogenic bacteria.
@ast
Isolation and amino acid seque ...... oteins of pathogenic bacteria.
@en
prefLabel
Isolation and amino acid seque ...... oteins of pathogenic bacteria.
@ast
Isolation and amino acid seque ...... oteins of pathogenic bacteria.
@en
P2093
P2860
P356
P1476
Isolation and amino acid seque ...... oteins of pathogenic bacteria.
@en
P2093
Rahfeld JU
Rücknagel KP
Schierhorn A
P2860
P304
22130-22138
P356
10.1074/JBC.271.36.22130
P407
P577
1996-09-01T00:00:00Z