Engineering inclusion bodies for non denaturing extraction of functional proteins. - Wikidata - awgldk - TriplyDB

Engineering inclusion bodies for non denaturing extraction of functional proteins.

Engineering inclusion bodies for non denaturing extraction of functional proteins.

http://www.wikidata.org/entity/Q37072928

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Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process.Deletional protein engineering based on stable fold.Isolation of biologically active nanomaterial (inclusion bodies) from bacterial cells.A variant of green fluorescent protein exclusively deposited to active intracellular inclusion bodies.Side effects of chaperone gene co-expression in recombinant protein production.Isolation of cell-free bacterial inclusion bodies.Kinetics of inclusion body formation and its correlation with the characteristics of protein aggregates in Escherichia coli.Influence of pH control in the formation of inclusion bodies during production of recombinant sphingomyelinase-D in Escherichia coli Inclusion bodies: a new concept Active protein aggregates induced by terminally attached self-assembling peptide ELK16 in Escherichia coli Towards revealing the structure of bacterial inclusion bodies.A single freeze-thawing cycle for highly efficient solubilization of inclusion body proteins and its refolding into bioactive form Active protein aggregates produced in Escherichia coli Characterization of the 4,6-α-glucanotransferase GTFB enzyme of Lactobacillus reuteri 121 isolated from inclusion bodies.Inclusion bodies as potential vehicles for recombinant protein delivery into epithelial cells.Production and characterization of a novel antifungal chitinase identified by functional screening of a suppressive-soil metagenome Active inclusion bodies of acid phosphatase PhoC: aggregation induced by GFP fusion and activities modulated by linker flexibility.Screening and discovery of nitro-benzoxadiazole compounds activating epidermal growth factor receptor (EGFR) in cancer cells.Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology.Fluorescent proteins in microbial biotechnology--new proteins and new applications.Post-production protein stability: trouble beyond the cell factory.Functional protein aggregates: just the tip of the iceberg.Eukaryotic aggresomes: from a model of conformational diseases to an emerging type of immobilized biocatalyzers.A novel method to recover inclusion body protein from recombinant E. coli fed-batch processes based on phage ΦX174-derived lysis protein E.A nanostructured bacterial bioscaffold for the sustained bottom-up delivery of protein drugs.Functional inclusion bodies produced in bacteria as naturally occurring nanopills for advanced cell therapies.Bioadhesiveness and efficient mechanotransduction stimuli synergistically provided by bacterial inclusion bodies as scaffolds for tissue engineering.Modeling amyloids in bacteria.Bacterial mimetics of endocrine secretory granules as immobilized in vivo depots for functional protein drugs.MB109 as bioactive human bone morphogenetic protein-9 refolded and purified from E. coli inclusion bodies Learning about protein solubility from bacterial inclusion bodies.Packaging protein drugs as bacterial inclusion bodies for therapeutic applications Nanotechnology, bionanotechnology and microbial cell factories.Why and how protein aggregation has to be studied in vivo.Teaching an old pET new tricks: tuning of inclusion body formation and properties by a mixed feed system in E. coli.Reassessment of inclusion body-based production as a versatile opportunity for difficult-to-express recombinant proteins.A recombinant cystatin from Ascaris lumbricoides attenuates inflammation of DSS-induced colitis.Inclusion bodies of fuculose-1-phosphate aldolase as stable and reusable biocatalysts.Positive in vitro wound healing effects of functional inclusion bodies of a lipoxygenase from the Mexican axolotl.Proof of concept in utilizing in-trans surface display system of Lactobacillus plantarum as mucosal tuberculosis vaccine via oral administration in mice

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Engineering inclusion bodies for non denaturing extraction of functional proteins.

http://www.wikidata.org/entity/Q37072928

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on December 2008

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Engineering inclusion bodies for non denaturing extraction of functional proteins.

@en

Engineering inclusion bodies for non denaturing extraction of functional proteins.

@nl

type

label

Engineering inclusion bodies for non denaturing extraction of functional proteins.

@en

Engineering inclusion bodies for non denaturing extraction of functional proteins.

@nl

prefLabel

Engineering inclusion bodies for non denaturing extraction of functional proteins.

@en

Engineering inclusion bodies for non denaturing extraction of functional proteins.

@nl

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Microbial Cell Factories

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Engineering inclusion bodies for non denaturing extraction of functional proteins.

@en

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Joze Grdadolnik

http://www.w3.org/2001/XMLSchema#string

Radovan Komel

http://www.w3.org/2001/XMLSchema#string

Spela Peternel

http://www.w3.org/2001/XMLSchema#string

Vladka Gaberc-Porekar

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P2860

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins

Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusion bodies.

The use and misuse of FTIR spectroscopy in the determination of protein structure.

Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones.

Factors influencing inclusion body formation in the production of a fused protein in Escherichia coli.

Protein quality in bacterial inclusion bodies.

Improvement of potential therapeutic value of tumor necrosis-alpha (TNF-alpha) by charge modulation in the tip region.

In vitro bioassay with enhanced sensitivity for human granulocyte colony-stimulating factor.

Cysteine to serine substitutions in basic fibroblast growth factor: effect on inclusion body formation and proteolytic susceptibility during in vitro refolding.

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34

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scholarly article

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10.1186/1475-2859-7-34

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7

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2008-12-01T00:00:00Z

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23559393

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1051008859

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19046444

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2630956

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