Strain engineering for improved expression of recombinant proteins in bacteria
about
Finding and Producing Probiotic Glycosylases for the Biocatalysis of Ginsenosides: A Mini ReviewRecombinant antibody production evolves into multiple options aimed at yielding reagents suitable for application-specific needsGenetically modified proteins: functional improvement and chimeragenesisFusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 systemIndividual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli.Disulfide bond formation and activation of Escherichia coli β-galactosidase under oxidizing conditionsRecombinant Fasciola hepatica fatty acid binding protein suppresses toll-like receptor stimulation in response to multiple bacterial ligandsMulti-copy genes that enhance the yield of mammalian G protein-coupled receptors in Escherichia coli.Enhanced secretion of recombinant proteins via signal recognition particle (SRP)-dependent secretion pathway by deletion of rrsE in Escherichia coli.Screening through the PLICable promoter toolbox enhances protein production in Escherichia coli.Downsizing a pullulanase to a small molecule with improved soluble expression and secretion efficiency in Escherichia coliComparison of Three Escherichia coli Strains in Recombinant Production of Reteplase.Towards a whole-cell modeling approach for synthetic biology.Extracellular expression of glutamate decarboxylase B in Escherichia coli to improve gamma-aminobutyric acid production.High-yield production of functional soluble single-domain antibodies in the cytoplasm of Escherichia coli.Antigen generation and display in therapeutic antibody drug discovery -- a neglected but critical player.Recombinant polypeptide production in E. coli: towards a rational approach to improve the yields of functional proteins.Heterologous production of active ribonuclease inhibitor in Escherichia coli by redox state control and chaperonin coexpressionPost-production protein stability: trouble beyond the cell factory.Optimization of the Expression of DT386-BR2 Fusion Protein in Escherichia coli using Response Surface MethodologyTools to cope with difficult-to-express proteins.Is it possible to optimize the protein production yield by the generation of homomultimeric fusion enzymes?Strategies for production of active eukaryotic proteins in bacterial expression system.PprM, a Cold Shock Domain-Containing Protein from Deinococcus radiodurans, Confers Oxidative Stress Tolerance to Escherichia coliRepurposing a bacterial quality control mechanism to enhance enzyme production in living cellsTrans-sialidase-based vaccine candidate protects against Trypanosoma cruzi infection, not only inducing an effector immune response but also affecting cells with regulatory/suppressor phenotype.Recent contributions in the field of the recombinant expression of disulfide bonded proteins in bacteria.Modified 'one amino acid-one codon' engineering of high GC content TaqII-coding gene from thermophilic Thermus aquaticus results in radical expression increaseOptimization of a single-chain antibody fragment overexpression in Escherichia coli using response surface methodology.Pseudomonas 2.0: genetic upgrading of P. putida KT2440 as an enhanced host for heterologous gene expression.Functional expression of full-length TrkA in the prokaryotic host Magnetospirillum magneticum AMB-1 by using a magnetosome display system.Imaging bacterial protein expression using genetically encoded RNA sensors.Bacterial secretion of soluble and functional trivalent scFv-based N-terminal trimerbodies.Systems metabolic engineering, industrial biotechnology and microbial cell factories.High-level production of membrane proteins in E. coli BL21(DE3) by omitting the inducer IPTG.Thermostable proteins bioprocesses: The activity of restriction endonuclease-methyltransferase from Thermus thermophilus (RM.TthHB27I) cloned in Escherichia coli is critically affected by the codon composition of the synthetic geneOptimizing heterologous protein production in the periplasm of E. coli by regulating gene expression levels.Improved production of propionic acid using genome shuffling.Directed evolution to improve protein folding in vivo.Reassessment of inclusion body-based production as a versatile opportunity for difficult-to-express recombinant proteins.
P2860
Q26747713-C273FBD1-FB65-441E-82A7-E097E9F6A3B3Q26795434-AB2331A8-860C-496E-AA76-6B6160F087D6Q26799506-560485DA-4071-45C2-90D3-78881DFFF015Q27001688-25A07489-8822-42DB-91E6-0E85E3C2E8C2Q27320857-C609B73F-B8A1-4B24-8483-C284C38A3894Q31046717-21D9E567-9C35-4CE5-AFBA-5F5948380D1EQ33906000-BD5336A5-786C-4A45-9CFF-6E758DAF0F97Q34275344-ECB5AC69-6C05-45C4-B474-A088F70C592BQ35998152-295F379A-0637-4A69-A448-6B57D92E5330Q36165783-E9EBA9F1-4F9D-4BAE-90EB-885217E4D3DDQ36461505-FE08971A-39CF-405B-8D39-2F6EF6E39DF3Q36475806-2CB457A4-08C0-4A62-BE94-02C17D420872Q36964778-8D4BAC35-680A-4661-BB2C-B38ABC4242DAQ37194840-8DBD9840-44A0-4809-9D60-3672EAF4BA96Q37283860-E5FF5255-6597-4A53-99CC-B07253036C38Q38058763-BEE0B203-C321-41A3-9B1F-910BD1B34312Q38157206-32B98F6E-F44E-46B0-A939-717702A98748Q38261572-276E3746-2804-407C-80EB-9C6CF495A0EDQ38264351-5AEAF655-64D8-44B5-A060-1D8A3AE1D570Q38738810-45103848-F7D5-4059-819E-BCADF5E86CA9Q38808506-A0D50C5B-0907-45D7-B0E9-F4B8D6F5F0D8Q38882901-60049379-58A2-4D24-AC30-41199458847BQ39337526-9DC37E7D-8D7A-4C6F-9549-9CA5AA43CA41Q41075702-2867139A-4C02-4496-8DA0-45C27B34F880Q41542953-8B78A422-7587-4A0C-87A5-B891DEE47EEAQ41709177-2DE3C88C-9740-4005-91AB-1F8BB6F0E1F5Q41809225-2EA6BB5A-CD90-4441-8D03-CCB04E5FD19EQ41874787-039F0059-A3DB-43B2-A118-7149DBDD148BQ41902560-7452CDC1-3410-449D-9ADF-A92C142BAD8DQ41914986-CAF7D6D1-24CC-4EBA-B092-7A18CCCF38BEQ42118648-CAEF3254-4430-432A-9710-E3B68E464A5DQ42254374-289C4C7C-B228-4B89-BB2B-63EF2B557634Q42413225-1708A52A-8D35-49E4-877B-F138105AA84DQ42575388-F7FFE9EB-947D-4D1C-B28A-D697D223982FQ42584571-05AE05C3-15EE-4B03-9D1E-E5C93A77C812Q42656840-8B013687-73EA-4D03-8242-4CA68919C7FFQ43220567-A5A51B77-B1D3-436B-A2BD-F2C58684F176Q46475781-B9E3F8A1-0DD6-435F-9CE3-9F20D69C2E4FQ47253797-27161E59-DB52-4D57-9D3B-644F0106E3C6Q47362457-4B0C31E4-2B97-4152-9BE4-D88A2B1FF35C
P2860
Strain engineering for improved expression of recombinant proteins in bacteria
description
2011 nî lūn-bûn
@nan
2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Strain engineering for improved expression of recombinant proteins in bacteria
@ast
Strain engineering for improved expression of recombinant proteins in bacteria
@en
type
label
Strain engineering for improved expression of recombinant proteins in bacteria
@ast
Strain engineering for improved expression of recombinant proteins in bacteria
@en
prefLabel
Strain engineering for improved expression of recombinant proteins in bacteria
@ast
Strain engineering for improved expression of recombinant proteins in bacteria
@en
P2093
P2860
P921
P356
P1476
Strain engineering for improved expression of recombinant proteins in bacteria
@en
P2093
George Georgiou
Georgios Skretas
Tomohiro Makino
P2860
P2888
P356
10.1186/1475-2859-10-32
P577
2011-05-14T00:00:00Z
P5875
P6179
1044043216