Selection for a periplasmic factor improving phage display and functional periplasmic expression.
about
The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.The scope of phage display for membrane proteins.Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide.Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.Isolation and characterisation of the ylmE homologue of Thermus thermophilus.The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cis-prolines.Single-chain Fv phage display propensity exhibits strong positive correlation with overall expression levelsFlow-cytometric isolation of human antibodies from a nonimmune Saccharomyces cerevisiae surface display library.Selection of an active enzyme by phage display on the basis of the enzyme's catalytic activity in vivo.Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli.Affinity-matured recombinant antibody fragments analyzed by single-molecule force spectroscopyPeriplasmic expression of soluble single chain T cell receptors is rescued by the chaperone FkpA.Characterization of six lipoproteins in the sigmaE regulon.Molecular considerations for development of phage antibody libraries.Improved fluoroquinolone detection in ELISA through engineering of a broad-specific single-chain variable fragment binding simultaneously to 20 fluoroquinolones.scFv antibody: principles and clinical applicationInteractions between folding factors and bacterial outer membrane proteins.Structure of a novel c7-type three-heme cytochrome domain from a multidomain cytochrome c polymerUse of folding modulators to improve heterologous protein production in Escherichia coli.Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.Expression of recombinant antibodies.Using protein-DNA chimeras to detect and count small numbers of molecules.Protein folding in the cell envelope of Escherichia coli.Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli.Signal sequence mutations as tools for the characterization of LamB folding intermediates.A rapid protein folding assay for the bacterial periplasm.TcpH influences virulence gene expression in Vibrio cholerae by inhibiting degradation of the transcription activator TcpP.Changing the surface of a virus shell fusion of an enzyme to polyoma VP1The Skp chaperone helps fold soluble proteins in vitro by inhibiting aggregation.The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane.Substrate oscillations boost recombinant protein release from Escherichia coli.The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization.Comparison of the cytoplasmic and periplasmic production of reteplase in Escherichia coli.Enhancing functional expression of Heterologous Burkholderia lipase in Escherichia coli.Display of aggregation-prone ligand binding domain of human PPAR gamma on surface of bacteriophage lambdaA dimeric bispecific miniantibody combines two specificities with avidity
P2860
Q28354278-4B55FFCE-613A-499D-91AF-9711CF2B7407Q30155439-438D4A09-53EB-4DC9-90CA-37030248F439Q30164981-A3AA0041-5B9A-4AEB-A758-2500772AD934Q30377057-C8C23F07-88E0-4FFA-89FD-75978EB3F744Q30763075-0E09C31A-571C-4DF0-A3F0-74FC50C951C6Q30854397-00787482-EAE4-463B-905F-FB6FA13FCE8CQ30856459-5E4B2EA6-2658-4300-B4BF-8B6D2D28EA3BQ30882235-785A0546-D986-4F51-9BB9-5F11A61EF612Q31144549-2F4E426E-02FF-4B5C-AB3E-E060FC08EE16Q31727669-ABFD74F8-433F-4759-B481-3C442171448BQ33293045-4FD1CBD1-BFB5-471F-B936-402FEBD93A5EQ33529299-4FAC6174-5179-4439-AAAD-6FC3F1EC6BB7Q33855793-3563E7E2-7017-4E0E-822D-11E2F5E9B823Q34032165-94192F75-FD32-423D-93EF-BC70F8F7F818Q34253218-E30DE889-287D-4690-BB7D-6C43BFA064F4Q35852647-67F351E8-05C4-443F-B684-393A99F1FF1FQ36174616-D15A6478-F994-4853-A6CD-533BA0ACFBDFQ36519376-2C7FA2FF-15AE-4A58-9CA7-174F916F8B15Q37097393-74E7EE13-1FE3-47F9-A664-76ADC1619BC3Q38020872-01A80CF6-ECE0-4AEE-8E57-CA30228DE9E3Q38126016-1CDEFAEC-1D83-436D-899B-B717A15FE56CQ38328990-FD7237D7-4999-40B5-B0C8-82C6E1638C7BQ38940176-D3B27BED-E1EB-4FEA-B38A-6FEECAAB9FF2Q39505348-7A6CC0A5-3C3A-4866-86FC-91A9874D9DECQ39680818-D6D53FEB-26E7-4D64-A1E8-ECF566F26CF6Q40497455-3E03E927-A545-4135-87CC-1E8363B06E4FQ40534708-3C492BFA-B28E-4440-94FD-1A5D87ABA900Q40906492-CA7B0908-BF99-441F-A7F5-0AEE1073CA87Q42662047-3D3ED3F0-5139-4997-A05B-4CCF1453F1EEQ43559987-F4D06BBF-CEFE-45F0-863C-78637FBED922Q43779297-1C0B55CF-1BEE-4093-B8C6-4A1CE5836290Q47723207-0754EE6A-F700-4705-B9A8-B40636486445Q50907239-C0E95A84-78F2-4159-981B-712A321187C4Q54380537-939D762C-B94E-4366-ACF5-FA8C12C423E8Q56894683-3A871487-057E-4B7C-A335-62B297A28E84Q57840051-FC63D24F-04BD-40F6-83DB-C23BF43A291E
P2860
Selection for a periplasmic factor improving phage display and functional periplasmic expression.
description
1998 nî lūn-bûn
@nan
1998 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Selection for a periplasmic fa ...... tional periplasmic expression.
@ast
Selection for a periplasmic fa ...... tional periplasmic expression.
@en
type
label
Selection for a periplasmic fa ...... tional periplasmic expression.
@ast
Selection for a periplasmic fa ...... tional periplasmic expression.
@en
prefLabel
Selection for a periplasmic fa ...... tional periplasmic expression.
@ast
Selection for a periplasmic fa ...... tional periplasmic expression.
@en
P2860
P356
P1433
P1476
Selection for a periplasmic fa ...... tional periplasmic expression.
@en
P2093
Bothmann H
Plückthun A
P2860
P2888
P304
P356
10.1038/NBT0498-376
P577
1998-04-01T00:00:00Z
P5875
P6179
1028625315