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

A scFv antibody mutant isolated in a genetic screen for improved export via the twin arginine transporter pathway exhibits faster folding.

Journal of molecular biology - 8 Jun 2007

Ribnicky Brian, Van Blarcom Thomas, Georgiou George

Abstract excerpt

Proteins destined for export across the cytoplasmic membrane via the post-translational Sec-dependent route have to be maintained in a largely unfolded state within the cytoplasm. In sharp contrast, only proteins that have folded into a native-like state within the cytoplasm are competent for export via the twin arginine translocation (Tat) pathway. Proteins that contain disulfide bonds, such as scFv antibody...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Cytoplasm
Share to Disulfides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Techniques

Share to Immunoglobulin Fragments

Share to Immunoglobulin Variable Region

Share to Oxygen

Share to Protein Denaturation

Source

Open in PubMed Open full text

Identifiers

PMID: 17462668
DOI: 10.1016/j.jmb.2007.03.068
PMCID: PMC1995598

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A scFv antibody mutant isolated in a genetic screen for improved export via the twin arginine transporter pathway exhibits faster folding.PMID 17462668Read ↗

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

Isolation of trans-acting genes that enhance soluble expression of scFv antibodies in the E. coli cytoplasm by lambda phage display.Semantic proximity Read ↗

Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway.Semantic proximity Read ↗

Laboratory evolution of fast-folding green fluorescent protein using secretory pathway quality control.Semantic proximity Read ↗

Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones.Semantic proximity Read ↗

Endoplasmic Reticulum-Targeted Subunit Toxins Provide a New Approach to Rescue Misfolded Mutant Proteins and Revert Cell Models of Genetic Diseases.Semantic proximity Read ↗

Proofreading of substrate structure by the Twin-Arginine Translocase is highly dependent on substrate conformational flexibility but surprisingly tolerant of surface charge and hydrophobicity changes.Semantic proximity Read ↗

Twin-arginine translocase mutations that suppress folding quality control and permit export of misfolded substrate proteins.Semantic proximity Read ↗

Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli.Semantic proximity Read ↗

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

Versatile selection technology for intracellular protein-protein interactions mediated by a unique bacterial hitchhiker transport mechanism.Semantic proximity Read ↗

Optimisation of a novel method for the production of single-span membrane proteins in <i>Escherichia coli</i>Semantic proximity Read ↗

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