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

Probing a protein–protein interaction by in vitro evolution

9 May 2006

Abstract excerpt

In this study, we used in vitro protein evolution with ribosome and phage display to optimize the affinity of a human IL-13-neutralizing antibody, a therapeutic candidate for the treatment of asthma, >150-fold to 81 pM by using affinity-driven stringency selections. Simultaneously, the antibody potency to inhibit IL-13-dependent proliferation in a cell-based functional assay increased 345-fold to an IC50 of 229...

Read the complete abstract on PubMed

Topics

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

Share to Monoclonal and Polyclonal Antibodies Research
Share to RNA and protein synthesis mechanisms
Share to vaccines and immunoinformatics approaches

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 16684878
DOI: 10.1073/pnas.0602341103

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Probing a protein–protein interaction by in vitro evolutionPMID 16684878Read ↗

In vitro evolution of antibody affinity via insertional scanning mutagenesis of an entire antibody variable regionSemantic proximity Read ↗

<i>In vitro</i> Evolution of Antibody Affinity via Insertional Mutagenesis Scanning of an Entire Antibody Variable RegionSemantic proximity Read ↗

Protein Engineering by Combined Computational and In Vitro Evolution Approaches.Semantic proximity Read ↗

Directed in vitro evolution and crystallographic analysis of a peptide-binding single chain antibody fragment (scFv) with low picomolar affinity.Semantic proximity Read ↗

Tailoring in vitro evolution for protein affinity or stability.Semantic proximity Read ↗

Ribosome display for rapid protein evolution by consecutive rounds of mutation and selection.Semantic proximity Read ↗

Directed evolution of a G protein-coupled receptor for expression, stability, and binding selectivity.Semantic proximity Read ↗

Engineering Proteins by Combining Deep Mutational Scanning and Yeast Display.Semantic proximity Read ↗

Ribosome Display: A Potent Display Technology used for Selecting and Evolving Specific Binders with Desired PropertiesSemantic proximity Read ↗

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

Harnessing phage and ribosome display for antibody optimisation.Semantic proximity Read ↗

Effective Optimization of Antibody Affinity by Phage Display Integrated with High-Throughput DNA Synthesis and Sequencing TechnologiesSemantic proximity Read ↗

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