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 dominant negative inhibitor indicates that monocyte chemoattractant protein 1 functions as a dimer.

Molecular and cellular biology - 1 Sept 1995

Zhang Y, Rollins B J

Abstract excerpt

Monocyte chemoattractant protein 1 (MCP-1) is a member of the chemokine family of proinflammatory cytokines, all of which share a high degree of amino acid sequence similarity. Aberrant expression of chemokines occurs in a variety of diseases that have an inflammatory component, such as atherosclerosis. Although structural analyses indicate that chemokines form homodimers, there is controversy about whether...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Cytokines
Share to Dose-Response Relationship, Drug

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

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Binding

Share to Protein Conformation

Share to Sequence Deletion

Source

Open in PubMed Open full text

Identifiers

PMID: 7651403
DOI: 10.1128/MCB.15.9.4851
PMCID: PMC230730

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 dominant negative inhibitor indicates that monocyte chemoattractant protein 1 functions as a dimer.PMID 7651403Read ↗

The C terminus of mouse monocyte chemoattractant protein 1 (MCP1) mediates MCP1 dimerization while blocking its chemotactic potency.Semantic proximity Read ↗

Monomeric and Dimeric CXCL8 Are Both Essential for In Vivo Neutrophil RecruitmentSemantic proximity Read ↗

Identification of the glycosaminoglycan binding site of the CC chemokine, MCP-1: implications for structure and function in vivo.Semantic proximity Read ↗

Interleukin 8 dimerization as a mechanism for regulation of neutrophil adherence-dependent oxidant production.Semantic proximity Read ↗

Hetero-oligomerization of CCR2, CCR5, and CXCR4 and the Protean Effects of “Selective” AntagonistsSemantic proximity Read ↗

Mapping of MCP-1 functional domains by peptide analysis and site-directed mutagenesis.Semantic proximity Read ↗

Mechanisms regulating chemokine receptor activitySemantic proximity Read ↗

Activation of the human c‐kit product by ligand‐induced dimerization mediates circular actin reorganization and chemotaxis.Semantic proximity Read ↗

Site-directed mutagenesis of the CC chemokine binding protein 35K-Fc reveals residues essential for activity and mutations that increase the potency of CC chemokine blockade.Semantic proximity Read ↗

Interference with heparin binding and oligomerization creates a novel anti-inflammatory strategy targeting the chemokine system.Semantic proximity Read ↗

Site-directed mutagenesis of monocyte chemoattractant protein-1 identifies two regions of the polypeptide essential for biological activitySemantic proximity Read ↗

Heterocomplexes between the Atypical Chemokine MIF and the CXC-Motif Chemokine CXCL4L1 Regulate Inflammation and Thrombus FormationSemantic proximity Read ↗

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