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

Enhancement of cell type specificity by quantitative modulation of a chimeric ligand.

The Journal of biological chemistry - 28 Mar 2008

Cironi Pablo, Swinburne Ian A, Silver Pamela A

Abstract excerpt

Evolution modulates the quantitative characteristics of protein interactions and often uses combinations of weak interactions to achieve a particular specificity. We addressed how quantitative optimization might be used in the design of multidomain proteins, using a chimera containing epidermal growth factor (EGF) as a cell targeting element and interferon-alpha-2a (IFNalpha-2a) to initiate signal transduction....

Read the complete abstract on PubMed

Topics

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

Share to Cell Physiological Phenomena
Share to Epidermal Growth Factor

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

Share to Interferon-alpha

Share to Interferon alpha-2

Share to Ligands

Share to Protein Engineering

Share to Sensitivity and Specificity

Share to STAT1 Transcription Factor

Source

Open in PubMed Open full text

Identifiers

PMID: 18230610
DOI: 10.1074/jbc.M708502200
PMCID: PMC2417160

Genes

EGF
IFNAR2

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

Enhancement of cell type specificity by quantitative modulation of a chimeric ligand.PMID 18230610Read ↗

Inquiring into the differential action of interferons (IFNs): an IFN-alpha2 mutant with enhanced affinity to IFNAR1 is functionally similar to IFN-beta.Semantic proximity Read ↗

Systematic Mutational Mapping of Sites on Human Interferon-β-1a That Are Important for Receptor Binding and Functional ActivitySemantic proximity Read ↗

An interferon alpha2 mutant optimized by phage display for IFNAR1 binding confers specifically enhanced antitumor activities.Semantic proximity Read ↗

Differences in Activity between α and β Type I Interferons Explored by Mutational AnalysisSemantic proximity Read ↗

Cytokine Activation by Antibody Fragments Targeted to Cytokine-Receptor Signaling Complexes.Semantic proximity Read ↗

Differential receptor subunit affinities of type I interferons govern differential signal activation.Semantic proximity Read ↗

Interleukin-2 activity can be fine tuned with engineered receptor signaling clamps.Semantic proximity Read ↗

Shared receptor components but distinct complexes for alpha and beta interferons.Semantic proximity Read ↗

Targeted mutations in IFNα2 improve its antiviral activity against various virusesSemantic proximity Read ↗

Ligand-Induced Association of the Type I Interferon Receptor ComponentsSemantic proximity Read ↗

Exploiting a natural conformational switch to engineer an interleukin-2 'superkine'.Semantic proximity Read ↗

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

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