Ubiquitin fusion augments the yield of cloned gene products in Escherichia coli.
about
Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fusedSingle amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteinsUbiquitin fusion expression and tissue-dependent targeting of hG-CSF in transgenic tobacco.Novel protein purification system utilizing an N-terminal fusion protein and a caspase-3 cleavable linker.Protein folding absent selection.An efficient system for high-level expression and easy purification of authentic recombinant proteinsStrategies for achieving high-level expression of genes in Escherichia coli.Analyses of the effects of all ubiquitin point mutants on yeast growth rate.Reconstitution of the vitamin D-responsive osteocalcin transcription unit in Saccharomyces cerevisiae.Early hydrogen-bonding events in the folding reaction of ubiquitin.Enhanced protein expression in the baculovirus/insect cell system using engineered SUMO fusions.Toxins from cone snails: properties, applications and biotechnological production.Ubiquitin-like prokaryotic MoaD as a fusion tag for expression of heterologous proteins in Escherichia coli.Strategies to optimize protein expression in E. coli.Plant biofarming: novel insights for peptide expression in heterologous systems.Fluorescent probes reveal a minimal ligase recognition motif in the prokaryotic ubiquitin-like protein from Mycobacterium tuberculosis.Recombinant expression of human mast cell proteases chymase and tryptase.Nasal immunization with a fusion protein consisting of the hemagglutinin A antigenic region and the maltose-binding protein elicits CD11c(+) CD8(+) dendritic cells for induced long-term protective immunity.Use of Ubp1 protease analog to produce recombinant human growth hormone in Escherichia coli.A novel Ecotin-Ubiquitin-Tag (ECUT) for efficient, soluble peptide production in the periplasm of Escherichia coli.Engineering of Baeyer-Villiger monooxygenase-based Escherichia coli biocatalyst for large scale biotransformation of ricinoleic acid into (Z)-11-(heptanoyloxy)undec-9-enoic acid.Enhanced expression of rabies virus surface G-protein in Escherichia coli using SUMO fusion.Tyrosinase production in recombinant E. coli containing trp promoter and ubiquitin sequence.Screening Fusion Tags for Improved Recombinant Protein Expression in E. coli with the Expresso® Solubility and Expression Screening System.The yeast homolog of mammalian ribosomal protein S30 is expressed from a duplicated gene without a ubiquitin-like protein fusion sequence. Evolutionary implications.A ubiquitin-based vector for the co-ordinated synthesis of multiple proteins in plants.Cell-free production and streamlined assay of cytosol-penetrating antibodies.
P2860
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P2860
Ubiquitin fusion augments the yield of cloned gene products in Escherichia coli.
description
1989 nî lūn-bûn
@nan
1989 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Ubiquitin fusion augments the yield of cloned gene products in Escherichia coli.
@ast
Ubiquitin fusion augments the yield of cloned gene products in Escherichia coli.
@en
type
label
Ubiquitin fusion augments the yield of cloned gene products in Escherichia coli.
@ast
Ubiquitin fusion augments the yield of cloned gene products in Escherichia coli.
@en
prefLabel
Ubiquitin fusion augments the yield of cloned gene products in Escherichia coli.
@ast
Ubiquitin fusion augments the yield of cloned gene products in Escherichia coli.
@en
P2093
P2860
P356
P1476
Ubiquitin fusion augments the yield of cloned gene products in Escherichia coli.
@en
P2093
Jonnalagadda S
Sternberg EJ
P2860
P304
P356
10.1073/PNAS.86.8.2540
P407
P577
1989-04-01T00:00:00Z