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 single amino acid difference between human and monkey interleukin (IL)-1beta dictates effective binding to soluble type II IL-1 receptor.

The Journal of biological chemistry - 6 Dec 2002

Smith Dirk E, Ketchem Randal R, Moore Heather, Anderson Zachary, Renshaw Blair R, Friend Della J, Sims John E

Abstract excerpt

Soluble type II interleukin (IL)-1 receptor (sIL1R-II) binds human IL-1beta with high affinity and neutralizes its activity. Recombinant sIL1R-II is considered a potentially useful anti-IL-1 therapeutic, and preclinical studies have been undertaken with this molecule in primates. To better understand the cytokine-receptor interactions occurring in this nonhuman context, monkey IL-1 and IL1R-II were cloned, and...

Read the complete abstract on PubMed

Topics

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

Share to Binding, Competitive
Share to COS Cells

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

Share to Cytokines

Share to DNA, Complementary

Share to Dose-Response Relationship, Drug

Share to Interleukin-1

Share to Macaca fascicularis

Share to Receptors, Interleukin-1

Source

Identifiers

PMID: 12356774
DOI: 10.1074/jbc.M206636200

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 single amino acid difference between human and monkey interleukin (IL)-1beta dictates effective binding to soluble type II IL-1 receptor.PMID 12356774Read ↗

Structural biology of the IL‐1 superfamily: Key cytokines in the regulation of immune and inflammatory responsesSemantic proximity Read ↗

Inhibiting protein-protein interactions: a model for antagonist design.Semantic proximity Read ↗

Cloning and Characterization of an Alternatively Processed Human Type II Interleukin-1 Receptor mRNASemantic proximity Read ↗

Optimization of IL-1Ra Structure to Achieve a Smaller Protein with a Higher Affinity to its ReceptorSemantic proximity Read ↗

Generation and characterization of a human monoclonal autoantibody that acts as a high affinity interleukin-1 alpha specific inhibitor.Semantic proximity Read ↗

Inhibitory activity of IL-1 receptor antagonist depends on the balance between binding capacity for IL-1 receptor type 1 and IL-1 receptor type II.Semantic proximity Read ↗

Identification, Cloning, and Characterization of a Novel Soluble Receptor That Binds IL-22 and Neutralizes Its ActivitySemantic proximity Read ↗

Crystal structure of human cytomegalovirus IL-10 bound to soluble human IL-10R1Semantic proximity Read ↗

Molecular construction and optimization of anti-human IL-1α/β dual variable domain immunoglobulin (DVD-Ig<sup>TM</sup>) moleculesSemantic proximity Read ↗

Direct binding to integrins and loss of disulfide linkage in interleukin-1β (IL-1β) are involved in the agonistic action of IL-1β.Semantic proximity Read ↗

Structure and function of chicken interleukin-1 beta mutants: uncoupling of receptor binding and in vivo biological activity.Semantic proximity Read ↗

A point mutation uncouples human interleukin-1 beta biological activity and receptor binding.Semantic proximity Read ↗

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