Tuned Escherichia coli as a host for the expression of disulfide-rich proteins.
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Efficient production of (2)H, (13)C, (15)N-enriched industrial enzyme Rhizopus chinensis lipase with native disulfide bonds.Matrix-assisted refolding and purification of placenta-derived recombinant human interleukin-6 produced in Escherichia coli.Interactions outside the proteinase-binding loop contribute significantly to the inhibition of activated coagulation factor XII by its canonical inhibitor from corn.Production and preclinical evaluation of Plasmodium falciparum MSP-119 and MSP-311 chimeric protein, PfMSP-Fu24Recombinant production of human interleukin 6 in Escherichia coliHigh throughput screening identifies disulfide isomerase DsbC as a very efficient partner for recombinant expression of small disulfide-rich proteins in E. coli.Production of recombinant disulfide-rich venom peptides for structural and functional analysis via expression in the periplasm of E. coli.Expression and purification of the antimicrobial peptide GSL1 in bacteria for raising antibodiesFunctional diversity of secreted cestode Kunitz proteins: Inhibition of serine peptidases and blockade of cation channels.Tuning different expression parameters to achieve soluble recombinant proteins in E. coli: advantages of high-throughput screening.Unnatural amino acid incorporation in E. coli: current and future applications in the design of therapeutic proteinsAssociation between foldability and aggregation propensity in small disulfide-rich proteinsSoluble Expression of Recombinant Nerve Growth Factor in Cytoplasm of Escherichia coli.Comparison of periplasmic and intracellular expression of Arabidopsis thionin proproteins in E. coli.Production, in Pichia pastoris, of a recombinant monomeric mapacalcine, a protein with anti-ischemic properties.A Strategy for Production of Correctly Folded Disulfide-Rich Peptides in the Periplasm of E. coli.Refined method to study the posttranslational regulation of alternative oxidases from Arabidopsis thaliana in vitro.Use of the SHuffle Strains in Production of Proteins.
P2860
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P2860
Tuned Escherichia coli as a host for the expression of disulfide-rich proteins.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 13 May 2011
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Tuned Escherichia coli as a host for the expression of disulfide-rich proteins.
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Tuned Escherichia coli as a host for the expression of disulfide-rich proteins.
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type
label
Tuned Escherichia coli as a host for the expression of disulfide-rich proteins.
@en
Tuned Escherichia coli as a host for the expression of disulfide-rich proteins.
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prefLabel
Tuned Escherichia coli as a host for the expression of disulfide-rich proteins.
@en
Tuned Escherichia coli as a host for the expression of disulfide-rich proteins.
@nl
P2093
P2860
P356
P1476
Tuned Escherichia coli as a host for the expression of disulfide-rich proteins.
@en
P2093
Cecilia Fernández
Gustavo Salinas
Leonardo Pellizza
Mariana Margenat
Martín Fló
P2860
P304
P356
10.1002/BIOT.201000335
P577
2011-05-13T00:00:00Z