Evidence map›Paper›PMID 21827949›Full record

ArticleStructure (London, England : 1993)2011

Oligomeric structure of the chemokine CCL5/RANTES from NMR, MS, and SAXS data.

Xu Wang, Caroline Watson, Joshua S Sharp, Tracy M Handel, James H Prestegard

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

53 citing papers in PubMed, 87 citations in OpenAlex.

  1. Review
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  5. Article
  6. Review
  7. Heterodimers Are an Integral Component of Chemokine Signaling Repertoire.International journal of molecular sciences · 2023
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. N-terminal Backbone Pairing Shifts in CCL5-International journal of molecular sciences · 2020
    Article
  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

5 authors at 2 institutions in 1 country.

Xu WangComplex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, USA.
Caroline Watson
Joshua S Sharp
Tracy M Handel
James H Prestegard
University of Georgia · USUniversity of Montana · US

Funding

ZINC DEFICIENCY &PROTEIN EXPRESSION IN RAT OLFACTORY BULBSP41RR005351 · NCRR · UNIVERSITY OF GEORGIA (UGA) · PI VENOT, ANDRE · 1989 to 2011
$18.4M
TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI LIVE, DAVID H · 2012 to 2019
$14.5M
STRUCTURE OF MACROPHAGE CHEMOTACTIC ACTIVATING PROTEINSR01AI037113 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HANDEL, TRACY M · 1995 to 2015
$5.2M
Structural Interactions of Bacterial Adhesin with GlycosaminoglycansR00GM088483 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI WANG, XU · 2011 to 2013
$696k
Structural Interactions of Bacterial Adhesin with GlycosaminoglycansK99GM088483 · NIGMS · UNIVERSITY OF GEORGIA · PI WANG, XU · 2009 to 2010
$105k
NCRR NIH HHS P41 RR005351NCRR NIH HHS P41-RR005351NIAID NIH HHS R01 AI037113NIAID NIH HHS R01AI37113NIGMS NIH HHS K99 GM088483NIGMS NIH HHS K99GM088483NIGMS NIH HHS P41 GM103390NIGMS NIH HHS R00 GM088483
6 · The paper itself

Abstract

CCL5 (RANTES) is a proinflammatory chemokine known to activate leukocytes through its receptor, CCR5. Although the monomeric form of CCL5 is sufficient to cause cell migration in vitro, CCL5's propensity for aggregation is essential for migration in vivo, T cell activation and apoptosis, and HIV entry into cells. However, there is currently no structural information on CCL5 oligomers larger than the canonical CC chemokine dimer. In this study the solution structure of a CCL5 oligomer was investigated using an integrated approach, including NMR residual dipolar couplings to determine allowed relative orientations of the component monomers, SAXS to restrict overall shape, and hydroxyl radical footprinting and NMR cross-saturation experiments to identify interface residues. The resulting model of the CCL5 oligomer provides a basis for explaining the disaggregating effect of E66 and E26 mutations and suggests mechanisms by which glycosaminoglycan binding may promote oligomer formation and facilitate cell migration in vivo.

Indexed as

Chemokine CCL5HumansHydroxyl RadicalMagnetic Resonance SpectroscopyMass SpectrometryModels, MolecularMultiprotein ComplexesProtein Interaction Domains and MotifsProtein Structure, QuaternaryProtein Structure, TertiaryScattering, Small AngleX-Ray DiffractionCCL5 protein, humanChemokine CCL5Hydroxyl RadicalMultiprotein Complexes

Identifiers

PMID21827949
PMCPMC3159919
OpenAlexW1969973543

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.