Engineering antibody fragments to fold in the absence of disulfide bonds. - Wikidata - awgldk - TriplyDB

Engineering antibody fragments to fold in the absence of disulfide bonds.

Engineering antibody fragments to fold in the absence of disulfide bonds.

http://www.wikidata.org/entity/Q33403805

about

Protein aggregation profile of the bacterial cytosol.Bacterial display in combinatorial protein engineering.Exploiting cross-reactivity to neutralize two different scorpion venoms with one single chain antibody fragment Strain engineering for improved expression of recombinant proteins in bacteria Construction of polyomavirus-derived pseudotype virus-like particles displaying a functionally active neutralizing antibody against hepatitis B virus surface antigen.Recombinant antibodies: engineering and production in yeast and bacterial hosts.Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.GFP-SCFV: expression and possible applications as a tool for experimental investigations of atherosclerosis.Exploration of broadly neutralizing antibody fragments produced in bacteria for the control of HIV.Continuous directed evolution of proteins with improved soluble expression

P2860

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P2860

Engineering antibody fragments to fold in the absence of disulfide bonds.

http://www.wikidata.org/entity/Q33403805

description

2009 nî lūn-bûn

@nan

2009 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Engineering antibody fragments to fold in the absence of disulfide bonds.

@ast

Engineering antibody fragments to fold in the absence of disulfide bonds.

@en

type

label

Engineering antibody fragments to fold in the absence of disulfide bonds.

@ast

Engineering antibody fragments to fold in the absence of disulfide bonds.

@en

prefLabel

Engineering antibody fragments to fold in the absence of disulfide bonds.

@ast

Engineering antibody fragments to fold in the absence of disulfide bonds.

@en

P1433

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P2860

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P1433

Protein Science

P1476

Engineering antibody fragments to fold in the absence of disulfide bonds.

@en

P2093

Brent L Iverson

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

Clinton E Leysath

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

Ki Jun Jeong

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

Min Jeong Seo

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

P2860

Protein thiol modifications visualized in vivo

Functional intracellular antibody fragments do not require invariant intra-domain disulfide bonds

Selection of antibodies for intracellular function using a two-hybrid in vivo system.

Evolution of highly active enzymes by homology-independent recombination.

Direct in vivo screening of intrabody libraries constructed on a highly stable single-chain framework.

Isolation and expression of recombinant antibody fragments to the biological warfare pathogen Brucella melitensis.

Tailoring in vitro evolution for protein affinity or stability.

A semi-synthetic repertoire of intrinsically stable antibody fragments derived from a single-framework scaffold.

Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries.

Direct phage to intrabody screening (DPIS): demonstration by isolation of cytosolic intrabodies against the TES1 site of Epstein Barr virus latent membrane protein 1 (LMP1) that block NF-kappaB transactivation.

P304

259-267

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

P31

scholarly article

P356

10.1002/PRO.31

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P433

2

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P478

18

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P50

George Georgiou

Andrew D Ellington

P577

2009-02-01T00:00:00Z

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23957721

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19177559

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P921

P932

2708069

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