Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation.
about
Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasmFull capacity of recombinant Escherichia coli heat-stable enterotoxin fusion proteins for extracellular secretion, antigenicity, disulfide bond formation, and activity.Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies.DsbC activation by the N-terminal domain of DsbD.Native disulfide bond formation in proteinsIndustrial production of recombinant therapeutics in Escherichia coli and its recent advancements.Secretion of anti-Plasmodium effector proteins from a natural Pantoea agglomerans isolate by using PelB and HlyA secretion signalsRecent advances towards development and commercialization of plant cell culture processes for the synthesis of biomoleculesKey players involved in bacterial disulfide-bond formation.The role of Dsb proteins of Gram-negative bacteria in the process of pathogenesis.Induction of partial protection against foot and mouth disease virus in guinea pigs by neutralization with the integrin β6-1 subunit.Use of folding modulators to improve heterologous protein production in Escherichia coli.Optimization of codon composition and regulatory elements for expression of human insulin like growth factor-1 in transgenic chloroplasts and evaluation of structural identity and functionOptimisation of signal peptide for recombinant protein secretion in bacterial hosts.Plant-produced human recombinant erythropoietic growth factors support erythroid differentiation in vitro.Expression of active human tissue-type plasminogen activator in Escherichia coli.Overexpression of protein disulfide isomerase DsbC stabilizes multiple-disulfide-bonded recombinant protein produced and transported to the periplasm in Escherichia coli.Improved secretion of native human insulin-like growth factor 1 from gas1 mutant Saccharomyces cerevisiae cellsZebrafish eggs used as bioreactors for the production of bioactive tilapia insulin-like growth factors.Recombinant production of mecasermin in E. coli expression systemOptimizing heterologous protein production in the periplasm of E. coli by regulating gene expression levels.Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli.Selective and efficient extraction of recombinant proteins from the periplasm of Escherichia coli using low concentrations of chemicals.High-yield export of a native heterologous protein to the periplasm by the tat translocation pathway in Escherichia coli.Protein fusion tags for efficient expression and purification of recombinant proteins in the periplasmic space of E. coli.Properties, Potentials, and Prospects of Antifreeze Proteins
P2860
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P2860
Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Overexpression of Escherichia ...... growth factor-I accumulation.
@ast
Overexpression of Escherichia ...... growth factor-I accumulation.
@en
type
label
Overexpression of Escherichia ...... growth factor-I accumulation.
@ast
Overexpression of Escherichia ...... growth factor-I accumulation.
@en
prefLabel
Overexpression of Escherichia ...... growth factor-I accumulation.
@ast
Overexpression of Escherichia ...... growth factor-I accumulation.
@en
P2093
P2860
P921
P356
P1476
Overexpression of Escherichia ...... growth factor-I accumulation.
@en
P2093
P2860
P304
P356
10.1073/PNAS.95.6.2773
P407
P577
1998-03-01T00:00:00Z