Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Protein science : a publication of the Protein Society - 1 Feb 2009

Seo Min Jeong, Jeong Ki Jun, Leysath Clinton E, Ellington Andrew D, Iverson Brent L, Georgiou George

Abstract excerpt

Disulfide bonds play a critical role in the stabilization of the immunoglobulin beta-sandwich sandwich. Under reducing conditions, such as those that prevail in the cytoplasm, disulfide bonds do not normally form and as a result most antibodies expressed in that compartment (intrabodies) accumulate in a misfolded and inactive state. We have developed a simple method for the quantitative isolation of antibody...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antigens, Bacterial
Share to Bacterial Toxins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Directed Molecular Evolution

Share to Disulfides

Share to Gene Library

Share to Immunoglobulin Variable Region

Share to Protein Disulfide-Isomerases

Share to Protein Engineering

Source

Open in PubMed Open full text

Identifiers

PMID: 19177559
DOI: 10.1002/pro.31
PMCID: PMC2708069

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Engineering antibody fragments to fold in the absence of disulfide bonds.PMID 19177559Read ↗

The disulfide bonds in antibody variable domains: effects on stability, folding in vitro, and functional expression in Escherichia coli.Semantic proximity Read ↗

Disulfide-compatible phage-assisted continuous evolution in the periplasmic spaceSemantic proximity Read ↗

Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.Semantic proximity Read ↗

Efficient isolation of soluble intracellular single-chain antibodies using the twin-arginine translocation machinery.Semantic proximity Read ↗

Engineered pathways for correct disulfide bond oxidation.Semantic proximity Read ↗

Toward Antibody Production in Genome-Minimized Bacillus subtilis StrainsSemantic proximity Read ↗

Engineering antibodies by yeast displaySemantic proximity Read ↗

Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions.Semantic proximity Read ↗

An engineered pathway for the formation of protein disulfide bonds.Semantic proximity Read ↗

Design of an alternate antibody fragment format that can be produced in the cytoplasm of Escherichia coliSemantic proximity Read ↗

Efficient expression of full-length antibodies in the cytoplasm of engineered bacteriaSemantic proximity Read ↗

Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.