Characterization of the aggregates formed during recombinant protein expression in bacteria
about
Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteinsSimplified screening for the detection of soluble fusion constructs expressed in E. coli using a modular set of vectorsTo fuse or not to fuse: what is your purpose?Enzyme Engineering for In Situ ImmobilizationRecombinant protein quality evaluation: proposal for a minimal information standardHeating as a rapid purification method for recovering correctly-folded thermotolerant VH and VHH domains.Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coliIdentification of soluble protein fragments by gene fragmentation and genetic selection.Monodispersity of recombinant Cre recombinase correlates with its effectiveness in vivo.Cultivation to improve in vivo solubility of overexpressed arginine deiminases in Escherichia coli and the enzyme characteristicsA receptor-based switch that regulates anthrax toxin pore formation.Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones.Side effects of chaperone gene co-expression in recombinant protein production.Isolation of cell-free bacterial inclusion bodies.Influence of pH control in the formation of inclusion bodies during production of recombinant sphingomyelinase-D in Escherichia coliOptimization of a one-step heat-inducible in vivo mini DNA vector production systemGroundnut bud necrosis virus encoded NSm associates with membranes via its C-terminal domain.Synonymous rare arginine codons and tRNA abundance affect protein production and quality of TEV protease variant.Active protein aggregates produced in Escherichia coliStrain-dependent profile of misfolded prion protein aggregates.Studies on bacterial inclusion bodies.Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology.Biological role of bacterial inclusion bodies: a model for amyloid aggregation.Immunogenicity of therapeutic proteins: influence of aggregation.The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells.Critical role of the proline-rich region in Huntingtin for aggregation and cytotoxicity in yeast.Localization of functional polypeptides in bacterial inclusion bodies.The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum.Rehosting of bacterial chaperones for high-quality protein production.Components of the E. coli envelope are affected by and can react to protein over-production in the cytoplasm.Learning about protein solubility from bacterial inclusion bodies.Engineering building blocks for self-assembling protein nanoparticlesEffect of temperature on protein quality in bacterial inclusion bodies.The evaluation of the factors that cause aggregation during recombinant expression in E. coli is simplified by the employment of an aggregation-sensitive reporter.Nanoparticulate architecture of protein-based artificial viruses is supported by protein-DNA interactions.Inhibited fragmentation of mAbs in buffered ionic liquids.Investigation of amino acid specificity in the CydX small protein shows sequence plasticity at the functional level.Biomedical Applications of Bacterial Inclusion Bodies
P2860
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P2860
Characterization of the aggregates formed during recombinant protein expression in bacteria
description
2005 nî lūn-bûn
@nan
2005 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Characterization of the aggreg ...... protein expression in bacteria
@ast
Characterization of the aggreg ...... protein expression in bacteria
@en
Characterization of the aggreg ...... protein expression in bacteria
@nl
type
label
Characterization of the aggreg ...... protein expression in bacteria
@ast
Characterization of the aggreg ...... protein expression in bacteria
@en
Characterization of the aggreg ...... protein expression in bacteria
@nl
prefLabel
Characterization of the aggreg ...... protein expression in bacteria
@ast
Characterization of the aggreg ...... protein expression in bacteria
@en
Characterization of the aggreg ...... protein expression in bacteria
@nl
P2860
P356
P1433
P1476
Characterization of the aggreg ...... protein expression in bacteria
@en
P2093
Andrea Schrödel
Ario de Marco
P2860
P2888
P356
10.1186/1471-2091-6-10
P407
P577
2005-05-31T00:00:00Z
P5875
P6179
1031949502