Evidence map›Paper›PMID 28368308›Full record

ArticleInternational journal of molecular sciences2017

Chemokine CXCL7 Heterodimers: Structural Insights, CXCR2 Receptor Function, and Glycosaminoglycan Interactions.

Aaron J Brown, Prem Raj B Joseph, Kirti V Sawant, Krishna Rajarathnam

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

25 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Bioinformatic Analysis of the CXCR2 Ligands in Cancer Processes.International journal of molecular sciences · 2023
    Article
  8. Heterodimers Are an Integral Component of Chemokine Signaling Repertoire.International journal of molecular sciences · 2023
    Review
  9. Review
  10. Article
  11. International journal of molecular sciences · 2022
    Review
  12. Review
  13. The marriage of chemokines and galectins as functional heterodimers.Cellular and molecular life sciences : CMLS · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Review
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

4 authors at 1 institution in 1 country.

Aaron J BrownDepartment of Biochemistry and Molecular Biology, and Sealy Center for Structural Biology and Molecular Biophysics, The University of Texas Medical Branch, Galveston, TX 77555, USA. aj3brown@utmb.edu.
Prem Raj B JosephDepartment of Biochemistry and Molecular Biology, and Sealy Center for Structural Biology and Molecular Biophysics, The University of Texas Medical Branch, Galveston, TX 77555, USA. pbjoseph@utmb.edu.
Kirti V SawantDepartment of Biochemistry and Molecular Biology, and Sealy Center for Structural Biology and Molecular Biophysics, The University of Texas Medical Branch, Galveston, TX 77555, USA. kisawant@utmb.edu.
Krishna RajarathnamDepartment of Biochemistry and Molecular Biology, and Sealy Center for Structural Biology and Molecular Biophysics, The University of Texas Medical Branch, Galveston, TX 77555, USA. krrajara@utmb.edu.
The University of Texas Medical Branch at Galveston · US

Funding

HOUSTON AREA MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008280 · NIGMS · RICE UNIVERSITY · PI WENSEL, THEODORE G · 1988 to 2023
$8.0M
NIGMS NIH HHS T32 GM008280
6 · The paper itself

Abstract

Chemokines mediate diverse fundamental biological processes, including combating infection. Multiple chemokines are expressed at the site of infection; thus chemokine synergy by heterodimer formation may play a role in determining function. Chemokine function involves interactions with G-protein-coupled receptors and sulfated glycosaminoglycans (GAG). However, very little is known regarding heterodimer structural features and receptor and GAG interactions. Solution nuclear magnetic resonance (NMR) and molecular dynamics characterization of platelet-derived chemokine CXCL7 heterodimerization with chemokines CXCL1, CXCL4, and CXCL8 indicated that packing interactions promote CXCL7-CXCL1 and CXCL7-CXCL4 heterodimers, and electrostatic repulsive interactions disfavor the CXCL7-CXCL8 heterodimer. As characterizing the native heterodimer is challenging due to interference from monomers and homodimers, we engineered a "trapped" disulfide-linked CXCL7-CXCL1 heterodimer. NMR and modeling studies indicated that GAG heparin binding to the heterodimer is distinctly different from the CXCL7 monomer and that the GAG-bound heterodimer is unlikely to bind the receptor. Interestingly, the trapped heterodimer was highly active in a Ca

Indexed as

Molecular Dynamics SimulationProtein DomainsProtein MultimerizationAmino Acid Sequencebeta-ThromboglobulinBinding SitesCalciumChemokine CXCL1GlycosaminoglycansHeparinHL-60 CellsHumansInterleukin-8KineticsMagnetic Resonance SpectroscopyOligosaccharidesbeta-ThromboglobulinCalciumChemokine CXCL1CXCL1 protein, humanGlycosaminoglycansHeparinInterleukin-8OligosaccharidesPlatelet Factor 4PPBP protein, humanchemokineCXCL7CXCR2glycosaminoglycanheparinheterodimerNMR

Identifiers

PMID28368308
PMCPMC5412333
OpenAlexW2605103134

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.