Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies.
about
Protein quality control in the bacterial periplasmCrystal structure of a defective folding proteinStructural Basis for Protein Antiaggregation Activity of the Trigger Factor ChaperoneStructural basis for the antifolding activity of a molecular chaperoneReversible formation of on-pathway macroscopic aggregates during the folding of maltose binding proteinFolding and trimerization of signal sequence-less mature TolC in the cytoplasm of Escherichia coliDisulfide-dependent folding and export of Escherichia coli DsbC.Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli.Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway.Engineering antibody fitness and function using membrane-anchored display of correctly folded proteins.Towards revealing the structure of bacterial inclusion bodies.FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm.Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein.Strategies for achieving high-level expression of genes in Escherichia coli.Folding of a large protein at high structural resolution.Extracellular nucleotide catabolism by the Group B Streptococcus ectonucleotidase NudP increases bacterial survival in blood.Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli.Fine-tuning of the Escherichia coli sigmaE envelope stress response relies on multiple mechanisms to inhibit signal-independent proteolysis of the transmembrane anti-sigma factor, RseA.Diversity and junction residues as hotspots of binding energy in an antibody neutralizing the dengue virus.A rapid protein folding assay for the bacterial periplasm.The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation.Stability of a guest protein depends on stability of a host protein in insertional fusion.Iron-sulfur cluster biosynthesis: biochemical characterization of the conformational dynamics of Thermotoga maritima IscU and the relevance for cellular cluster assembly.Solubility and proteolysis of the Zb-MalE and Zb-MalE31 proteins during overproduction in Escherichia coli.RseB binding to the periplasmic domain of RseA modulates the RseA:sigmaE interaction in the cytoplasm and the availability of sigmaE.RNA polymerase.Folding of maltose binding protein outside of and in GroEL.Protein fusion tags for efficient expression and purification of recombinant proteins in the periplasmic space of E. coli.Reconstitution, spectroscopy, and redox properties of the photosynthetic recombinant cytochrome b(559) from higher plants.Unfolding of proteins and long transient conformations detected by single nanopore recording.Formation of active inclusion bodies in the periplasm of Escherichia coli.Development an effective system to expression recombinant protein in E. coli via comparison and optimization of signal peptides: Expression of Pseudomonas fluorescens BJ-10 thermostable lipase as case study.Continuous directed evolution of proteins with improved soluble expressionDeterminants of Translocation and Folding of TreF, a Trehalase ofEscherichia coli
P2860
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P2860
Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies.
description
1996 nî lūn-bûn
@nan
1996 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի ապրիլին 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
Folding of a mutant maltose-bi ...... which forms inclusion bodies.
@ast
Folding of a mutant maltose-bi ...... which forms inclusion bodies.
@en
Folding of a mutant maltose-bi ...... which forms inclusion bodies.
@nl
type
label
Folding of a mutant maltose-bi ...... which forms inclusion bodies.
@ast
Folding of a mutant maltose-bi ...... which forms inclusion bodies.
@en
Folding of a mutant maltose-bi ...... which forms inclusion bodies.
@nl
prefLabel
Folding of a mutant maltose-bi ...... which forms inclusion bodies.
@ast
Folding of a mutant maltose-bi ...... which forms inclusion bodies.
@en
Folding of a mutant maltose-bi ...... which forms inclusion bodies.
@nl
P2860
P356
P1476
Folding of a mutant maltose-bi ...... which forms inclusion bodies.
@en
P2093
P2860
P304
P356
10.1074/JBC.271.14.8046
P407
P577
1996-04-01T00:00:00Z