Evidence map›Paper›PMID 23415099›Full record

ReviewProgress in molecular biology and translational science2013

Chemokine receptor oligomerization and allostery.

Bryan Stephens, Tracy M Handel

Abstract readReview
In one paragraph

Review in Progress in molecular biology and translational science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
13.4field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Structural insights into CXCR4 modulation and oligomerization.Nature structural & molecular biology · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Advanced fluorescence microscopy reveals disruption of dynamic CXCR4 dimerization by subpocket-specific inverse agonists.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Review
  15. Article
  16. CCR5 is a required signaling receptor for macrophage expression of inflammatory genes in response to viral double-stranded RNA.American journal of physiology. Regulatory, integrative and comparative physiology · 2019
    Article
  17. Article
  18. Review
  19. Reprogramming G protein coupled receptor structure and function.Current opinion in structural biology · 2018
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Bryan StephensSkaggs School of Pharmacy and Pharmaceutical Science, University of California, San Diego, La Jolla, California, USA.
Tracy M Handel
University of California San Diego · US

Funding

GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008326 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1989 to 2020
$7.5M
Structure, Dynamics and Activation Mechanisms of Chemokine ReceptorsU01GM094612 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHANCE, MARK R · 2010 to 2014
$4.5M
Engineering Chemokine Receptor Signaling Complexes In VitroR01GM081763 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HANDEL, TRACY M · 2009 to 2011
$935k
NIGMS NIH HHS R01 GM081763NIGMS NIH HHS R01GM081763NIGMS NIH HHS T32 GM007752NIGMS NIH HHS T32GM007752NIGMS NIH HHS T32 GM008326NIGMS NIH HHS U01 GM094612NIGMS NIH HHS U01GM094612
6 · The paper itself

Abstract

Oligomerization of chemokine receptors has been reported to influence many aspects of receptor function through allosteric communication between receptor protomers. Allosteric interactions within chemokine receptor hetero-oligomers have been shown to cause negative cooperativity in the binding of chemokines and to inhibit receptor activation in the case of some receptor pairs. Other receptor pairs can cause enhanced signaling and even activate entirely new, hetero-oligomer-specific signaling complexes and responses downstream of receptor activation. Many mechanisms contribute to these effects including direct allosteric coupling between the receptors, G protein-mediated allostery, G protein stealing, ligand sequestration, and recruitment of new intracellular proteins by exposing unique binding interfaces on the oligomerized receptors. These effects present both challenges as well as exciting opportunities for drug discovery. One of the most difficult challenges will involve determining if and when hetero-oligomers versus homomeric receptors are involved in specific disease states.

Indexed as

Protein MultimerizationAllosteric RegulationAnimalsHumansLigandsModels, MolecularProtein BindingReceptors, ChemokineLigandsReceptors, Chemokine

Identifiers

PMID23415099
PMCPMC4072031
OpenAlexW2258056590

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.