Bacterial bioreactors for high yield production of recombinant protein.
about
Fully automated high-quality NMR structure determination of small 2H-enriched proteinsThe use of the condensed single protein production system for isotope-labeled outer membrane proteins, OmpA and OmpX in E. coliUnique opportunities for NMR methods in structural genomics.Advances in protein NMR provided by the NIGMS Protein Structure Initiative: impact on drug discovery.Preparation of protein samples for NMR structure, function, and small-molecule screening studiesEfficient condensed-phase production of perdeuterated soluble and membrane proteinsSegmental isotope labeling of proteins for NMR structural study using a protein S tag for higher expression and solubilityProduction of membrane proteins for NMR studies using the condensed single protein (cSPP) production system.Use of amino acids as inducers for high-level protein expression in the single-protein production systemCondensed E. coli cultures for highly efficient production of proteins containing unnatural amino acidsThe E. coli single protein production system for production and structural analysis of membrane proteinsSecretion of human superoxide dismutase in Escherichia coli using the condensed single-protein-production systemAuto-induction medium containing glyphosate for high-level incorporation of unusual aromatic amino acids into proteins.Suppression of phospholipid biosynthesis by cerulenin in the condensed Single-Protein-Production (cSPP) systemLatest approaches for efficient protein production in drug discovery.Suppression of the toxicity of Bac7 (1-35), a bovine peptide antibiotic, and its production in E. coli.Replacement of all arginine residues with canavanine in MazF-bs mRNA interferase changes its specificityHeterologous expression of plasmodial proteins for structural studies and functional annotation.Independently inducible system of gene expression for condensed single protein production (cSPP) suitable for high efficiency isotope enrichmentToxins-antitoxins: diversity, evolution and function.Comparative transcriptomic profile analysis of fed-batch cultures expressing different recombinant proteins in Escherichia coli.Super RLuc8-sFv; a new luciferase-labeled probe for detection of human CD4+ cells.Purification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide.Significant bias against the ACA triplet in the tmRNA sequence of Escherichia coli K-12.1H, 13C and 15N backbone and side-chain chemical shift assignment of the Fyn SH2 domain and its complex with a phosphotyrosine peptide.Cold-Shock Expression System in E. coli for Protein NMR Studies.Characterization of recombinant human gastrointestinal glutathione peroxidase mutant produced in Escherichia coli.Toxin-Antitoxin Systems in Bacteria and Archaea
P2860
Q27664145-E80DAA54-A3E7-4941-9BB2-D6DE98762203Q30156043-81F4A824-7536-4CF7-AA88-2A8E805EEC54Q30375573-6552307D-EBA7-46DA-A6BE-86A3F5077B63Q30388819-F89BDB55-DAFA-41A8-A9D7-57C93BDB7A4DQ30400391-CA379082-0439-4811-8026-74DF94254644Q33545267-DDA30314-4FAA-412C-99AE-6C1CC3708F80Q33981360-7CF1A9FA-FA5E-46A8-9B35-691FBF184F67Q34074092-10B326E1-E39C-4429-A123-F7D368B3E77AQ34119604-D8850493-CFB4-4888-8D37-85AFAA15E759Q34138973-2E3428DF-F9C6-4CFF-988F-AE4CA3CFE35BQ34309289-C3D8A511-DE72-49F9-BCED-FEAFE07329F7Q34436472-1C66BC1E-A1B9-482E-A2E4-049092A12DA2Q34501937-036664AD-2A99-449D-A5D5-93FECF69A7D9Q35189863-6193D31E-C880-4CAC-B202-F31BE7015696Q35209937-42429D5E-12E6-4889-9C74-6B8867333B0DQ36643857-4E3EB9CC-6A57-42F8-B84F-927E5837B6E3Q36685144-A9CD847A-6E6B-4660-A6B6-3C7A8462D86BQ36938795-D84654E6-0522-42BE-A900-93EBD5F8E5B8Q36982410-8F775387-9DBA-4DA0-B0AD-CCC92EBFDED0Q37912155-8F38EE38-169B-4BA7-B731-16EBA7415BB7Q39064962-2B80C787-A7B0-4733-812E-600A923178B7Q40362118-68D07A4B-1BB7-4744-A972-1060DEFD2F28Q41931642-67942CE5-A423-40FA-9D34-30EA396198C6Q42561222-1F1BFBCF-22DA-459A-9A67-EDB6BF8CC506Q44436279-DE38C8AB-6C3B-469C-AF4A-E5D38AFF347EQ50255115-D7314F11-B5EF-406D-B095-C63ECD305C86Q54276945-9AC74FED-173D-4448-BACD-796CDA459465Q57987392-BCE9AB8F-570C-4025-B419-CADD67CD6DF8
P2860
Bacterial bioreactors for high yield production of recombinant protein.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
Bacterial bioreactors for high yield production of recombinant protein.
@en
Bacterial bioreactors for high yield production of recombinant protein.
@nl
type
label
Bacterial bioreactors for high yield production of recombinant protein.
@en
Bacterial bioreactors for high yield production of recombinant protein.
@nl
prefLabel
Bacterial bioreactors for high yield production of recombinant protein.
@en
Bacterial bioreactors for high yield production of recombinant protein.
@nl
P2093
P2860
P356
P1476
Bacterial bioreactors for high yield production of recombinant protein.
@en
P2093
Haiyan Zheng
Masayori Inouye
Motoo Suzuki
Nancy Woychik
Rohini Roy
P2860
P304
37559-37565
P356
10.1074/JBC.M608806200
P407
P577
2006-10-04T00:00:00Z