The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures.
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Protein production and purificationNovel lipolytic enzymes identified from metagenomic library of deep-sea sediment.A simple and efficient method for generating high-quality recombinant Mical enzyme for in vitro assaysSoluble prokaryotic overexpression and purification of bioactive human granulocyte colony-stimulating factor by maltose binding protein and protein disulfide isomerase.Recombinant functional multidomain hemoglobin from the gastropod Biomphalaria glabrata.Expression, isolation, and purification of soluble and insoluble biotinylated proteins for nerve tissue regeneration.Inclusion bodies: a new conceptRecombinant protein expression in Escherichia coli: advances and challengesSoluble expression of human leukemia inhibitory factor with protein disulfide isomerase in Escherichia coli and its simple purification.Soluble overexpression and purification of bioactive human CCL2 in E. coli by maltose-binding protein.Active protein aggregates produced in Escherichia coliProtein purification using PDZ affinity chromatography.Inclusion bodies as potential vehicles for recombinant protein delivery into epithelial cells.Expression and functional characterization of the first bacteriophage-encoded chaperonin.Bacterial expression and purification of interleukin-2 tyrosine kinase: single step separation of the chaperonin impurityHow to achieve high-level expression of microbial enzymes: strategies and perspectives.Engineering inclusion bodies for non denaturing extraction of functional proteins.Studies on bacterial inclusion bodies.Sense and nonsense from a systems biology approach to microbial recombinant protein production.Tuning different expression parameters to achieve soluble recombinant proteins in E. coli: advantages of high-throughput screening.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.Fluorescent proteins in microbial biotechnology--new proteins and new applications.Post-production protein stability: trouble beyond the cell factory.Dual transcriptional-translational cascade permits cellular level tuneable expression control.Functional protein aggregates: just the tip of the iceberg.A combinatorial approach of N-terminus blocking and codon optimization strategies to enhance the soluble expression of recombinant hIL-7 in E. coli fed-batch culture.Optimized condition for enhanced soluble-expression of recombinant mutant anabaena variabilis phenylalanine ammonia lyase.Localization of functional polypeptides in bacterial inclusion bodies.A nanostructured bacterial bioscaffold for the sustained bottom-up delivery of protein drugs.Crystal structure of a phosphoribosyl anthranilate isomerase from the hyperthermophilic archaeon Thermococcus kodakaraensis.Functional inclusion bodies produced in bacteria as naturally occurring nanopills for advanced cell therapies.Synthesis and evaluation of xylopyranoside derivatives as "decoy acceptors" of human β-1,4-galactosyltransferase 7.Bioinformatic mapping and production of recombinant N-terminal domains of human cardiac ryanodine receptor 2Identification and characterization of the LysR-type transcriptional regulator HsdR for steroid-inducible expression of the 3α-hydroxysteroid dehydrogenase/carbonyl reductase gene in Comamonas testosteroni.The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum.Soluble Expression of Recombinant Nerve Growth Factor in Cytoplasm of Escherichia coli.High throughput quantitative expression screening and purification applied to recombinant disulfide-rich venom proteins produced in E. coli.Effect of temperature and sorbitol in improving the solubility of carboxylesterases protein CpCE-1 from Cydia pomonella and biochemical characterization.Learning about protein solubility from bacterial inclusion bodies.
P2860
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P2860
The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh-hant
name
The conformational quality of ...... ed at low growth temperatures.
@en
The conformational quality of ...... ed at low growth temperatures.
@nl
type
label
The conformational quality of ...... ed at low growth temperatures.
@en
The conformational quality of ...... ed at low growth temperatures.
@nl
prefLabel
The conformational quality of ...... ed at low growth temperatures.
@en
The conformational quality of ...... ed at low growth temperatures.
@nl
P2093
P356
P1476
The conformational quality of ...... ed at low growth temperatures.
@en
P2093
Andrea Vera
Nuria González-Montalbán
P304
P356
10.1002/BIT.21218
P577
2007-04-01T00:00:00Z