Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity
about
Protein quality control in the bacterial periplasmActivation of Colicin M by the FkpA Prolyl Cis-Trans Isomerase/ChaperoneStructural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90Crystal structure of N-domain of FKBP22 from Shewanella sp. SIB1: Dimer dissociation by disruption of Val-Leu knotStructure of human peptidyl-prolylcis-transisomerase FKBP22 containing two EF-hand motifsCharacterization of the ribosome biogenesis landscape in E. coli using quantitative mass spectrometryFrom Chaperones to the Membrane with a BAM!The Bam machine: a molecular cooper.Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein.Polypeptide binding proteins: what remains to be discovered?Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coliStructure of a designed protein cage that self-assembles into a highly porous cube.Strain engineering for improved expression of recombinant proteins in bacteriaLegionella pneumophila Mip, a surface-exposed peptidylproline cis-trans-isomerase, promotes the presence of phospholipase C-like activity in culture supernatantsInhibitor-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.Cross-linking measurements of in vivo protein complex topologies.Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps.Interactions between folding factors and bacterial outer membrane proteins.Role for Skp in LptD assembly in Escherichia coli.Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?Single-Domain Peptidyl-Prolyl cis/trans Isomerase FkpA from Corynebacterium glutamicum Improves the Biomass Yield at Increased Growth Temperatures.Deciphering the catalytic domain of colicin M, a peptidoglycan lipid II-degrading enzyme.Protein folding in the cell envelope of Escherichia coli.Co-expression of Skp and FkpA chaperones improves cell viability and alters the global expression of stress response genes during scFvD1.3 production.Cooperation of both, the FKBP_N-like and the DSBA-like, domains is necessary for the correct function of FTS_1067 protein involved in Francisella tularensis virulence and pathogenesis.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.A Legionella pneumophila peptidyl-prolyl cis-trans isomerase present in culture supernatants is necessary for optimal growth at low temperaturesMultifaceted SlyD from Helicobacter pylori: implication in [NiFe] hydrogenase maturation.Periplasmic chaperone FkpA is essential for imported colicin M toxicity.De novo design and evolution of artificial disulfide isomerase enzymes analogous to the bacterial DsbC.C-H…O hydrogen bonds in FK506-binding protein-ligand interactions.Binding analysis of a psychrotrophic FKBP22 to a folding intermediate of protein using surface plasmon resonance.Conformational dynamics of Peb4 exhibit "mother's arms" chain model: a molecular dynamics study.Import of periplasmic bacteriocins targeting the murein.Analyzing the Role of Periplasmic Folding Factors in the Biogenesis of OMPs and Members of the Type V Secretion System.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
Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Structural and functional stud ...... merase with chaperone activity
@ast
Structural and functional stud ...... merase with chaperone activity
@en
Structural and functional stud ...... merase with chaperone activity
@nl
type
label
Structural and functional stud ...... merase with chaperone activity
@ast
Structural and functional stud ...... merase with chaperone activity
@en
Structural and functional stud ...... merase with chaperone activity
@nl
prefLabel
Structural and functional stud ...... merase with chaperone activity
@ast
Structural and functional stud ...... merase with chaperone activity
@en
Structural and functional stud ...... merase with chaperone activity
@nl
P2093
P3181
P1476
Structural and functional stud ...... merase with chaperone activity
@en
P2093
B Vulliez-le Normand
G A Bentley
J-M Betton
P304
P3181
P356
10.1016/J.JMB.2003.10.056
P407
P577
2004-01-09T00:00:00Z