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 two-step selection approach for the identification of ligand-binding determinants in cytokine receptors.

Analytical biochemistry - 15 Mar 1999

Friedrich K, Wietek S, Lischke A, Wellbrock C, Kreitman R J, Pastan I, Sebald W

Abstract excerpt

We have developed a novel cell-based method for the isolation and selection of mutant cytokine receptors with defects in ligand binding and applied it to the human interleukin-4 receptor. The experimental procedure is based upon the functional heterologous expression of receptor mutants in eukaryotic cells followed by a two-step selection procedure. Positive selection for cells that express receptor variants is...

Read the complete abstract on PubMed

Topics

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

Share to Cell Division
Share to Dimerization
Share to Immunotoxins

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

Share to Interleukin-4

Share to Ligands

Share to Receptors, Cytokine

Share to Receptors, Interleukin-4

Share to Recombinant Fusion Proteins

Source

Identifiers

PMID: 10075806
DOI: 10.1006/abio.1998.3078

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

A two-step selection approach for the identification of ligand-binding determinants in cytokine receptors.PMID 10075806Read ↗

IL-4 receptor mutations.Semantic proximity Read ↗

Insights into Cytokine–Receptor Interactions from Cytokine EngineeringSemantic proximity Read ↗

Activating mutations in cytokine receptors: implications for receptor function and role in disease.Semantic proximity Read ↗

Conversion of human interleukin-4 into a high affinity antagonist by a single amino acid replacement.Semantic proximity Read ↗

Usage of activating mutations in the analysis of cytokine signal transduction pathways.Semantic proximity Read ↗

Novel protein engineering strategy for creating highly receptor-selective mutant TNFs.Semantic proximity Read ↗

Affinity maturation of leukemia inhibitory factor and conversion to potent antagonists of signaling.Semantic proximity Read ↗

Selection of Leptin Surrogates by a General Phenotypic Screening Method for Receptor Agonists.Semantic proximity Read ↗

Characterization of T Cell Receptors Engineered for High Affinity Against Toxic Shock Syndrome Toxin-1Semantic proximity Read ↗

Reversal of antigen-dependent signaling by two mutations in antibody/receptor chimera: implication of inverse agonism in cytokine receptor superfamily.Semantic proximity Read ↗

Phenotypic knockout of the high-affinity human interleukin 2 receptor by intracellular single-chain antibodies against the alpha subunit of the receptor.Semantic proximity Read ↗

Species-specific agonist/antagonist activities of human interleukin-4 variants suggest distinct ligand binding properties of human and murine common receptor gamma chain.Semantic proximity Read ↗

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