Protein aggregation as bacterial inclusion bodies is reversible. - Wikidata - wikimedia - TriplyDB

Protein aggregation as bacterial inclusion bodies is reversible.

Protein aggregation as bacterial inclusion bodies is reversible.

http://www.wikidata.org/entity/Q34513908

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Evidence that membrane insertion of the cytosolic domain of Bcl-xL is governed by an electrostatic mechanism Unscrambling an egg: protein disaggregation by AAA+ proteins Strategies for the recovery of active proteins through refolding of bacterial inclusion body proteins The small heat-shock proteins IbpA and IbpB reduce the stress load of recombinant Escherichia coli and delay degradation of inclusion bodies A step ahead: combining protein purification and correct folding selection Characterization of the aggregates formed during recombinant protein expression in bacteria Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins A Glutathione-independent Glyoxalase of the DJ-1 Superfamily Plays an Important Role in Managing Metabolically Generated Methylglyoxal in Candida albicans Recombinant streptavidin nanopeptamer anti-immunocomplex assay for noncompetitive detection of small analytes Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli Highly efficient production of soluble proteins from insoluble inclusion bodies by a two-step-denaturing and refolding method Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones.Isolation of cell-free bacterial inclusion bodies.Kinetics of inclusion body formation and its correlation with the characteristics of protein aggregates in Escherichia coli.Recombinant protein expression in Escherichia coli: advances and challenges Localization of chaperones DnaK and GroEL in bacterial inclusion bodies Antigenic hepatitis A virus structures may be produced in Escherichia coli Active protein aggregates produced in Escherichia coli Two distinct states of Escherichia coli cells that overexpress recombinant heterogeneous β-galactosidase Transient sampling of aggregation-prone conformations causes pathogenic instability of a parkinsonian mutant of DJ-1 at physiological temperature.Understanding the relationship between the primary structure of proteins and its propensity to be soluble on overexpression in Escherichia coli.Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry.Heterologous expression of plasmodial proteins for structural studies and functional annotation.Studies on bacterial inclusion bodies.Toxin Fused with SUMO Tag: A New Expression Vector Strategy to Obtain Recombinant Venom Toxins with Easy Tag Removal inside the Bacteria.Biological role of bacterial inclusion bodies: a model for amyloid aggregation.Recombinant polypeptide production in E. coli: towards a rational approach to improve the yields of functional proteins.The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells.Localization of functional polypeptides in bacterial inclusion bodies.A novel fed-batch based cultivation method provides high cell-density and improves yield of soluble recombinant proteins in shaken cultures Rehosting of bacterial chaperones for high-quality protein production.N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers Repetitive Gly-Leu-Lys-Gly-Glu-Asn-Arg-Gly-Asp peptide derived from collagen and fibronectin for improving cell-scaffold interaction.The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions.Protein bodies in nature and biotechnology.A fed-batch based cultivation mode in Escherichia coli results in improved specific activity of a novel chimeric-truncated form of tissue plasminogen activator.Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy.Role of molecular chaperones in inclusion body formation.GroEL/ES mediated the in vivo recovery of TRAIL inclusion bodies in Escherichia coli

P2860

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P2860

Protein aggregation as bacterial inclusion bodies is reversible.

http://www.wikidata.org/entity/Q34513908

description

2001 nî lūn-bûn

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2001 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի հունվարին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年论文

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name

Protein aggregation as bacterial inclusion bodies is reversible.

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Protein aggregation as bacterial inclusion bodies is reversible.

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Protein aggregation as bacterial inclusion bodies is reversible.

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type

label

Protein aggregation as bacterial inclusion bodies is reversible.

@ast

Protein aggregation as bacterial inclusion bodies is reversible.

@en

Protein aggregation as bacterial inclusion bodies is reversible.

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prefLabel

Protein aggregation as bacterial inclusion bodies is reversible.

@ast

Protein aggregation as bacterial inclusion bodies is reversible.

@en

Protein aggregation as bacterial inclusion bodies is reversible.

@nl

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Protein aggregation as bacterial inclusion bodies is reversible.

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P2860

Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer

Posttranslational quality control: folding, refolding, and degrading proteins.

Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies.

Fine architecture of bacterial inclusion bodies.

Structure and morphology of protein inclusion bodies in Escherichia coli.

Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils.

Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease.

Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains.

Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies.

Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins.

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