Learning about protein solubility from bacterial inclusion bodies.
about
Aberrant O-GlcNAcylation disrupts GNE enzyme activity in GNE myopathy.Galectin-1 as a fusion partner for the production of soluble and folded human beta-1,4-galactosyltransferase-T7 in E. coli.A Novel Chimeric Endolysin with Antibacterial Activity against Methicillin-Resistant Staphylococcus aureus.Side effects of chaperone gene co-expression in recombinant protein production.Isolation of cell-free bacterial inclusion bodies.A synthetic biology approach to self-regulatory recombinant protein production in Escherichia coli.Inclusion bodies: a new conceptReversible, Specific, Active Aggregates of Endogenous Proteins Assemble upon Heat StressActive protein aggregates induced by terminally attached self-assembling peptide ELK16 in Escherichia coliTowards revealing the structure of bacterial inclusion bodies.Comparison of two codon optimization strategies to enhance recombinant protein production in Escherichia coli.Co-production of GroELS discriminates between intrinsic and thermally-induced recombinant protein aggregation during substrate quality control.Formation of active inclusion bodies induced by hydrophobic self-assembling peptide GFIL8Inclusion bodies as potential vehicles for recombinant protein delivery into epithelial cells.Microbial factories for recombinant pharmaceuticalsThe effect of protein acetylation on the formation and processing of inclusion bodies and endogenous protein aggregates in Escherichia coli cells.Biological role of bacterial inclusion bodies: a model for amyloid aggregation.Dunaliella salina as a novel host for the production of recombinant proteins.Post-production protein stability: trouble beyond the cell factory.Eukaryotic aggresomes: from a model of conformational diseases to an emerging type of immobilized biocatalyzers.A nanostructured bacterial bioscaffold for the sustained bottom-up delivery of protein drugs.Bioadhesiveness and efficient mechanotransduction stimuli synergistically provided by bacterial inclusion bodies as scaffolds for tissue engineering.Rehosting of bacterial chaperones for high-quality protein production.Toward a cell-free hydantoinase process: screening for expression optimization and one-step purification as well as immobilization of hydantoinase and carbamoylase.Application of an E. coli signal sequence as a versatile inclusion body tagNanotechnology, bionanotechnology and microbial cell factories.Engineering building blocks for self-assembling protein nanoparticlesCross-system excision of chaperone-mediated proteolysis in chaperone-assisted recombinant protein productionFlow cytometric analysis of E. coli on agar plates: implications for recombinant protein production.Recombinant expression of antimicrobial peptides using a novel self-cleaving aggregation tag in Escherichia coli.Strategies for the production of difficult-to-express full-length eukaryotic proteins using microbial cell factories: production of human alpha-galactosidase A.Biomedical Applications of Bacterial Inclusion Bodies
P2860
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P2860
Learning about protein solubility from bacterial inclusion bodies.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Learning about protein solubility from bacterial inclusion bodies.
@en
Learning about protein solubility from bacterial inclusion bodies.
@nl
type
label
Learning about protein solubility from bacterial inclusion bodies.
@en
Learning about protein solubility from bacterial inclusion bodies.
@nl
prefLabel
Learning about protein solubility from bacterial inclusion bodies.
@en
Learning about protein solubility from bacterial inclusion bodies.
@nl
P2093
P2860
P356
P1476
Learning about protein solubility from bacterial inclusion bodies.
@en
P2093
Antonio Villaverde
Mónica Martínez-Alonso
Nuria González-Montalbán
P2860
P2888
P356
10.1186/1475-2859-8-4
P577
2009-01-08T00:00:00Z
P5875
P6179
1018158825