Targeted expression, purification, and cleavage of fusion proteins from inclusion bodies in Escherichia coli.
about
Maltose-binding protein fusion allows for high level bacterial expression and purification of bioactive mammalian cytokine derivativesRational Design of a Carrier Protein for the Production of Recombinant Toxic Peptides in Escherichia coliRecombinant production of medium- to large-sized peptides in Escherichia coli using a cleavable self-aggregating tagRecombinant protein expression in Escherichia coli: advances and challengesA single freeze-thawing cycle for highly efficient solubilization of inclusion body proteins and its refolding into bioactive formHigh Level Expression and Purification of Recombinant Proteins from Escherichia coli with AK-TAG.Recombinant Expression and Characterization of α-Conotoxin LvIA in Escherichia coli.Recombinant production of influenza hemagglutinin and HIV-1 GP120 antigenic peptides using a cleavable self-aggregating tag.Advanced technologies for improved expression of recombinant proteins in bacteria: perspectives and applications.Current strategies for protein production and purification enabling membrane protein structural biology.An optimized Npro-based method for the expression and purification of intrinsically disordered proteins for an NMR study.Peptide Synthesis through Cell-Free Expression of Fusion Proteins Incorporating Modified Amino Acids as Latent Cleavage Sites for Peptide Release.Instantaneous ion configurations in the K+ ion channel selectivity filter revealed by 2D IR spectroscopy.Probing the Effects of Gating on the Ion Occupancy of the K+ Channel Selectivity Filter Using Two-Dimensional Infrared SpectroscopyApplication of an E. coli signal sequence as a versatile inclusion body tagQuarterly intrinsic disorder digest (January-February-March, 2014).Efficient solubilization and purification of highly insoluble membrane proteins expressed as inclusion bodies using perfluorooctanoic acid.Designing and overproducing a tandem epitope of gp350/220 that shows a potential to become an EBV vaccine.
P2860
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P2860
Targeted expression, purification, and cleavage of fusion proteins from inclusion bodies in Escherichia coli.
description
2013 nî lūn-bûn
@nan
2013 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Targeted expression, purificat ...... on bodies in Escherichia coli.
@ast
Targeted expression, purificat ...... on bodies in Escherichia coli.
@en
Targeted expression, purificat ...... on bodies in Escherichia coli.
@nl
type
label
Targeted expression, purificat ...... on bodies in Escherichia coli.
@ast
Targeted expression, purificat ...... on bodies in Escherichia coli.
@en
Targeted expression, purificat ...... on bodies in Escherichia coli.
@nl
prefLabel
Targeted expression, purificat ...... on bodies in Escherichia coli.
@ast
Targeted expression, purificat ...... on bodies in Escherichia coli.
@en
Targeted expression, purificat ...... on bodies in Escherichia coli.
@nl
P2093
P2860
P1433
P1476
Targeted expression, purificat ...... on bodies in Escherichia coli.
@en
P2093
Brian D Sykes
Jonathan S Pan
Peter M Hwang
P2860
P304
P356
10.1016/J.FEBSLET.2013.09.028
P407
P577
2013-09-27T00:00:00Z