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 stability into Escherichia coli secreted Fabs leads to increased functional expression.

Protein engineering, design & selection : PEDS - 1 Jul 2006

Demarest Stephen J, Chen Gang, Kimmel Bruce E, Gustafson David, Wu Jane, Salbato Jared, Poland John, Elia Marikka, Tan Xuqiu, Wong Ken, Short Jay, Hansen Geneviève

Abstract excerpt

The recombinant expression of immunoglobulin domains, Fabs and scFvs in particular, in Escherichia coli can vary significantly from antibody to antibody. We hypothesized that poor Fab expression is often linked to poor intrinsic stability. To investigate this further, we applied a novel approach...

Read the complete abstract on PubMed

Topics

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

Share to Immunoglobulin Fab Fragments
Share to Immunoglobulin G

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immunoglobulin Variable Region

Share to Pattern Recognition, Automated

Share to Peptide Library

Share to Protein Denaturation

Share to Protein Engineering

Share to Thermodynamics

Source

Identifiers

PMID: 16672248
DOI: 10.1093/protein/gzl016

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-16672248-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Engineering stability into Escherichia coli secreted Fabs leads to increased functional expression.PMID 16672248Read ↗

Increased Fab thermoresistance via VH-targeted directed evolution.Semantic proximity Read ↗

Optimizing antibody expression by using the naturally occurring framework diversity in a live bacterial antibody display system.Semantic proximity Read ↗

Stability engineering of scFvs for the development of bispecific and multivalent antibodies.Semantic proximity Read ↗

Contributions of the complementarity determining regions to the thermal stability of a single-domain antibody.Semantic proximity Read ↗

Rational design approach to improve the solubility of the β-sandwich domain 1 of a thermophilic protein.Semantic proximity Read ↗

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

Rapid screening platform for stabilization of scFvs in Escherichia coli.Semantic proximity Read ↗

Stable mammalian serum albumins designed for bacterial expressionSemantic proximity Read ↗

An in vivo platform to select and evolve aggregation-resistant proteins.Semantic proximity Read ↗

Directed evolution of human heavy chain variable domain (VH) using in vivo protein fitness filter.Semantic proximity Read ↗

A systemic approach to identifying sequence frameworks that decrease mAb production in a transient Chinese hamster ovary cell expression system.Semantic proximity Read ↗

In vitro evolution of a hyperstable Gbeta1 variant.Semantic proximity Read ↗

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