about
Quality control of inclusion bodies in Escherichia coliSequence determinants of protein aggregation: tools to increase protein solubility.Comparative modelling of protein structure and its impact on microbial cell factories.Characterization of the aggregates formed during recombinant protein expression in bacteriaAggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteinsRepA-WH1, the agent of an amyloid proteinopathy in bacteria, builds oligomeric pores through lipid vesicles.Polyhydroyxalkanoate synthase fusions as a strategy for oriented enzyme immobilisation.Artificial environments for the co-translational stabilization of cell-free expressed proteinsProtein recovery from inclusion bodies of Escherichia coli using mild solubilization process.Bacterial inclusion bodies contain amyloid-like structureProtein aggregation profile of the bacterial cytosol.A variant of green fluorescent protein exclusively deposited to active intracellular inclusion bodies.Activity of maize transglutaminase overexpressed in Escherichia coli inclusion bodies: an alternative to protein refolding.Protein-folding landscapes in multichain systems.In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence.Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones.Isolation of cell-free bacterial inclusion bodies.Kinetics of inclusion body formation and its correlation with the characteristics of protein aggregates in Escherichia coli.Influence of pH control in the formation of inclusion bodies during production of recombinant sphingomyelinase-D in Escherichia coliMultidimensional structure-activity relationship of a protein in its aggregated states.The relationship between aggregation and toxicity of polyglutamine-containing ataxin-3 in the intracellular environment of Escherichia coli.A consensus method for the prediction of 'aggregation-prone' peptides in globular proteins.Active protein aggregates induced by terminally attached self-assembling peptide ELK16 in Escherichia coliTowards revealing the structure of bacterial inclusion bodies.Sequestration of toxic oligomers by HspB1 as a cytoprotective mechanism.Small surfactant-like peptides can drive soluble proteins into active aggregates.Defined DNA sequences promote the assembly of a bacterial protein into distinct amyloid nanostructures.Biochemical nature of Russell Bodies.Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview.Active inclusion bodies of acid phosphatase PhoC: aggregation induced by GFP fusion and activities modulated by linker flexibility.Studies on bacterial inclusion bodies.Functional inclusion bodies produced in the yeast Pichia pastoris.TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells."Native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus and its biological implications.Prediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes.Biological role of bacterial inclusion bodies: a model for amyloid aggregation.Prediction of amyloid aggregation in vivo.The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells.Post-production protein stability: trouble beyond the cell factory.Eukaryotic aggresomes: from a model of conformational diseases to an emerging type of immobilized biocatalyzers.
P2860
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P2860
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Amyloid-like properties of bacterial inclusion bodies.
@en
Amyloid-like properties of bacterial inclusion bodies.
@nl
type
label
Amyloid-like properties of bacterial inclusion bodies.
@en
Amyloid-like properties of bacterial inclusion bodies.
@nl
prefLabel
Amyloid-like properties of bacterial inclusion bodies.
@en
Amyloid-like properties of bacterial inclusion bodies.
@nl
P2093
P1476
Amyloid-like properties of bacterial inclusion bodies
@en
P2093
Andrea Vera
Mar Carrió
Nuria González-Montalbán
P304
P356
10.1016/J.JMB.2005.02.030
P407
P577
2005-04-01T00:00:00Z