Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli - Wikidata - awgldk - TriplyDB

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

http://www.wikidata.org/entity/Q24802856

about

Renewable energy from Cyanobacteria: energy production optimization by metabolic pathway engineering.Production of glycoprotein vaccines in Escherichia coli Sequence determinants of protein aggregation: tools to increase protein solubility.Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins A novel expression system of domain I of human beta2 glycoprotein I in Escherichia coli Effects of Environmental Factors on Soluble Expression of a Humanized Anti-TNF-α scFv Antibody in Escherichia coli Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system Ancestral mutations as a tool for solubilizing proteins: The case of a hydrophobic phosphate-binding protein High-throughput recombinant protein expression in Escherichia coli: current status and future perspectives Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase components Enabling low cost biopharmaceuticals: high level interferon alpha-2b production in Trichoderma reesei Identification of three ookinete-specific genes and evaluation of their transmission-blocking potentials in Plasmodium berghei Efficient production of (2)H, (13)C, (15)N-enriched industrial enzyme Rhizopus chinensis lipase with native disulfide bonds.Prokaryotic expression and purification of soluble maize Ac transposase.Module structure of interphotoreceptor retinoid-binding protein (IRBP) may provide bases for its complex role in the visual cycle - structure/function study of Xenopus IRBP.Comparative genomics in acid mine drainage biofilm communities reveals metabolic and structural differentiation of co-occurring archaea Engineering membrane protein overproduction in Escherichia coli.Disulfide bond formation and activation of Escherichia coli β-galactosidase under oxidizing conditions The replication initiator of the cholera pathogen's second chromosome shows structural similarity to plasmid initiators.Exploring codon optimization and response surface methodology to express biologically active transmembrane RANKL in E. coli.Expression, isolation, and purification of soluble and insoluble biotinylated proteins for nerve tissue regeneration.Towards universal systems for recombinant gene expression.A protocol for phage display and affinity selection using recombinant protein baits.Novel, versatile, and tightly regulated expression system for Escherichia coli strains.Side effects of chaperone gene co-expression in recombinant protein production.An improved method and cost effective strategy for soluble expression and purification of human N-myristoyltransferase 1 in E. coli.GFP facilitates native purification of recombinant perlucin derivatives and delays the precipitation of calcium carbonate Production of active recombinant eIF5A: reconstitution in E.coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymes.High throughput screening identifies disulfide isomerase DsbC as a very efficient partner for recombinant expression of small disulfide-rich proteins in E. coli.Protein interaction module-assisted function X (PIMAX) approach to producing challenging proteins including hyperphosphorylated tau and active CDK5/p25 kinase complex Soluble expression of human leukemia inhibitory factor with protein disulfide isomerase in Escherichia coli and its simple purification.Co-production of GroELS discriminates between intrinsic and thermally-induced recombinant protein aggregation during substrate quality control.Nitrate levels modulate the abundance of Paracoccus sp. in a biofilm community.Active protein aggregates produced in Escherichia coli Effect of osmotic stress and heat shock in recombinant protein overexpression and crystallization.Two distinct states of Escherichia coli cells that overexpress recombinant heterogeneous β-galactosidase Trigger factor assisted soluble expression of recombinant spike protein of porcine epidemic diarrhea virus in Escherichia coli A fluorescence polarization assay using an engineered human respiratory syncytial virus F protein as a direct screening platform Expression and purification of the membrane enzyme selenoprotein K Leptospirosis vaccines.

P2860

Q21994492-2452C2A4-114A-4CD5-9BA6-DEF5D9566FEA Q24628546-82977D30-6275-4D84-9BB6-930A7437B8BF Q24795353-5B4EB031-AF6B-4EAD-8D0E-06FE7E45E414 Q24815513-24FC3B25-21C2-4969-96AB-CCC273BC218A Q25255895-77B73E7F-E2EF-436B-B66B-513BAD067B7A Q26773076-02348E60-72DD-458C-A762-88A345176F9D Q27001688-2B95FE5F-22E4-4DF2-AFC2-0EF1AC4B5670 Q27681569-FF207AFD-C616-430C-9D6A-B65F64EC287A Q28066811-AAF3A87D-8552-4343-BF8F-55D07C8E0049 Q28482052-80B15F4B-F3A8-4068-9AA7-6D6FD2F9AF31 Q28601364-7F12856A-7093-4160-B8E7-6EA1C1569424 Q30043378-4B2E1915-C06C-40E6-AA7A-6E1DB082C4A8 Q30390491-8B0A6F9D-A3F2-42DD-9AF3-8B6E042EBC11 Q30422436-BACA1FFE-22C0-4483-A530-1E592692AF85 Q30444373-2500D5C4-B911-4F12-89F3-11ACAA684E6D Q30543365-193FFBCC-AD23-4407-B882-ECCB00A1F10E Q30841537-6B6E7B79-7272-45B8-85B4-CA15409D9802 Q31046717-6C1B72A4-2842-4A41-B7DB-1F942DBED72A Q33580258-71917E05-13A4-4412-A732-B46C12AE25AD Q33583910-57789A34-CDDA-4D5C-8AE5-0DF3B474220D Q33872665-8C199283-9442-43D2-B768-B6E551E2B03A Q33875357-7CF4DE84-27D3-4387-99EC-666943F8CC2F Q34014597-09530E14-8967-466E-AED7-4D98D7166B43 Q34045980-78B2AF4B-4D69-4E3D-8857-3B077A2A16B9 Q34148952-3DC33A75-0EB4-4D17-B892-162ED8CBAA79 Q34412045-949ECDF2-29B5-48CC-B483-DCA683F0A120 Q34441797-4D17F665-5B6E-4A8D-9DB8-797E284B4923 Q34571712-356BCA4F-130E-42BB-9A19-05800DDB2E4E Q34680566-8C7A8CC5-D169-453A-83CE-4AD26A27794C Q34884230-196E2BA1-7080-422B-98D0-D043DDF1F969 Q35073178-C86249AB-1C64-4526-8379-5503CE4448EB Q35520931-48F18CAB-4280-45D6-BB7A-81256F49D412 Q35594673-E9C35E98-9828-4219-BE23-B60B8B75E6F1 Q35600257-B48FFF49-C292-4BD0-AB2C-4F7F9BCE9853 Q35781971-45326710-7528-4174-BF98-166E5AA1F923 Q35841975-F2913F51-981D-4194-B791-3126F3F157D3 Q36007800-EBAB4AFD-A43F-4D2E-8CD1-75293F311139 Q36291082-C120E52E-ADDB-4D90-AD89-D643FBFE0ACB Q36354370-4B5E8B1A-77BB-4E67-AB9D-558E098205EF Q36440093-A18A1B8E-A096-44D3-ACB4-4D8C89413756

P2860

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

http://www.wikidata.org/entity/Q24802856

description

2005 nî lūn-bûn

@nan

2005 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

name

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

@ast

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

@en

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

@nl

type

label

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

@ast

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

@en

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

@nl

prefLabel

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

@ast

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

@en

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

@nl

P1433

Q24802856-9707C9FF-658A-47C1-BCD1-E07570A11A66

P1476

Q24802856-DE96FA75-1FB7-4FDC-ABB4-23D537F595E1

P2093

Q24802856-95AFD100-7797-43D6-A081-020DE211C8B6

Q24802856-AF37A7E5-D521-4F0A-929C-722BB647BCA3

P2860

Q24802856-00B4F0E2-A83A-40CA-967E-8B1D922541A9

Q24802856-047E954C-A500-4F0E-916F-394DBB4CA1A2

Q24802856-0734FC39-1575-4601-97DE-C4492384DBDD

Q24802856-09B265D8-7295-4DCD-A66F-8866A8C7B718

Q24802856-0E69A6BF-DD35-43C1-8B4B-CCEF074D9BDB

Q24802856-0FA0D913-70F4-4ADF-BA4E-8BFCD539FCFB

Q24802856-16EB6CB1-9901-4D07-8376-EB91D9568AB0

Q24802856-19A81BD8-3D61-475E-AA3D-402E0B70DFB5

Q24802856-2569DC36-6E53-4F9E-8E92-4C1C3E35F319

Q24802856-25E2DFCA-A44A-485E-ABC6-20652E0B933D

P2888

Q24802856-CABB2716-7941-428B-BF4D-9EFF792928FF

P304

Q24802856-0BDBFEBC-1D78-4F42-8ACC-A26D958C06B9

P31

Q24802856-2D266E45-6116-4D96-A777-37CF7D5F9A5B

P3181

Q24802856-A254E9A5-E9F7-4914-A10F-196583503DC2

P356

Q24802856-BB9E8D6D-3E97-421C-A05C-0E67BBD604EA

P433

Q24802856-F01473BA-1A22-407B-9255-C2C47318290D

P478

Q24802856-29581D7F-7C45-449D-882F-778067BE2D53

P577

Q24802856-B5464C18-A916-44DD-B7D5-99F58010654F

P5875

Q24802856-4CE5E23D-D771-46F8-869C-547E764424AA

P6179

Q24802856-398E36E3-7CDA-4661-ABE9-114164F0B2B4

P698

Q24802856-FA4071BB-C76B-4B63-A7E1-03072A73003B

P921

Q24802856-AAEDBA18-8D2F-4E1E-974C-9EF25D24EBB2

Q24802856-D9A87892-761A-4F1D-BA45-EB377C168C83

P932

Q24802856-24AE69D5-67B9-4199-B34A-727743EB46A5

P3181

P356

P1433

Microbial Cell Factories

P1476

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

@en

P2093

Hans Peter Sørensen

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

Kim Kusk Mortensen

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

P2860

Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm

Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused

Molecular chaperones in the cytosol: from nascent chain to folded protein

Principles that govern the folding of protein chains

Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli

Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins

Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels

The effect of molecular chaperones on in vivo and in vitro folding processes.

Directed enzyme evolution.

Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies.

P2888

P304

1

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

P31

scholarly article

P3181

98262

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

P356

10.1186/1475-2859-4-1

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

P433

1

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

P478

4

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

P577

2005-01-04T00:00:00Z

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

P5875

8102044

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

P6179

1048360411

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

P698

15629064

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

P921

Escherichia coli

P932

544838

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