Refolding of proteins from inclusion bodies: rational design and recipes.
about
An automatic refolding apparatus for preparative-scale protein productionRecombinant protein expression in Escherichia coli: advances and challengesExpression of a fungal manganese peroxidase in Escherichia coli: a comparison between the soluble and refolded enzymesCharacterization of Polyamidoamino (PAMAM) Dendrimers Using In-Line Reversed Phase LC Electrospray Ionization Mass Spectrometry.Dynamic transcriptional response of Escherichia coli to inclusion body formation.Protein refolding using chemical refolding additives.Antigen generation and display in therapeutic antibody drug discovery -- a neglected but critical player.Targeting kallikrein-related peptidases in prostate cancer.Inclusion bodies: not that bad….Sophisticated Cloning, Fermentation, and Purification Technologies for an Enhanced Therapeutic Protein Production: A Review.Microbial platform technology for recombinant antibody fragment production: A review.Periplasmic Export of Bile Salt Hydrolase in Escherichia coli by the Twin-Arginine Signal Peptides.Soluble expression of pullulanase from Bacillus acidopullulyticus in Escherichia coli by tightly controlling basal expression.Chaotropic heat treatment resolves native-like aggregation of a heterologously produced hyperthermostable laminarinase.A camelid nanobody against EGFR was easily obtained through refolding of inclusion body expressed in Escherichia coli.Process development in the QbD paradigm: Role of process integration in process optimization for production of biotherapeutics.Large-scale purification and characterization of recombinant human stem cell factor in Escherichia coli.Statistical vs. stochastic experimental design: an experimental comparison on the example of protein refolding.Unravelling the mechanisms of a protein refolding process based on the association of detergents and co-solvents.Differential Precipitation and Solubilization of Proteins.Protein fusion tags for efficient expression and purification of recombinant proteins in the periplasmic space of E. coli.The aggregation of cytochrome C may be linked to its flexibility during refolding.Development of a direct ELISA based on carboxy-terminal of penicillin-binding protein BlaR for the detection of β-lactam antibiotics in foods.Production and Purification of Recombinant Proteins fromEscherichia coliHydrophobic supplements in cell-free systems: Designing artificial environments for membrane proteinsLarge-Scale Expression, Purification of Bioactive Recombinant Human FGF6 in E. coli and the Mechanisms of Its Myocardial Protection
P2860
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P2860
Refolding of proteins from inclusion bodies: rational design and recipes.
description
2011 nî lūn-bûn
@nan
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Refolding of proteins from inclusion bodies: rational design and recipes.
@ast
Refolding of proteins from inclusion bodies: rational design and recipes.
@en
Refolding of proteins from inclusion bodies: rational design and recipes.
@nl
type
label
Refolding of proteins from inclusion bodies: rational design and recipes.
@ast
Refolding of proteins from inclusion bodies: rational design and recipes.
@en
Refolding of proteins from inclusion bodies: rational design and recipes.
@nl
prefLabel
Refolding of proteins from inclusion bodies: rational design and recipes.
@ast
Refolding of proteins from inclusion bodies: rational design and recipes.
@en
Refolding of proteins from inclusion bodies: rational design and recipes.
@nl
P2860
P1476
Refolding of proteins from inclusion bodies: rational design and recipes
@en
P2093
Susanna Su Jan Leong
P2860
P2888
P304
P356
10.1007/S00253-011-3513-Y
P407
P50
P577
2011-08-07T00:00:00Z
P5875
P6179
1017919827