Evidence map›Paper›PMID 31455633›Full record

ArticleThe Journal of biological chemistry2019

Structural basis of chemokine interactions with heparan sulfate, chondroitin sulfate, and dermatan sulfate.

Krishna Mohan Sepuru, Krishna Rajarathnam

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 47 citations in OpenAlex.

  1. SpyCEP dismantles neutrophil immunity via disorder-driven chemokine remodeling and GAG targeting.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  13. NMR Methods for Characterization of Glycosaminoglycan-Chemokine Interactions.Methods in molecular biology (Clifton, N.J.) · 2023
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  17. International journal of molecular sciences · 2022
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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.

Krishna Mohan SepuruDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas 77555-1055.ORCID 0000-0002-3675-6294
Krishna RajarathnamDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas 77555-1055 krrajara@utmb.edu.ORCID 0000-0002-0077-700X
The University of Texas Medical Branch at Galveston · US

Funding

Therapeutic assessment of synthetic heparin sulfates in transplantation modelsP01HL107152 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI DESAI, UMESH RAMANLAL · 2011 to 2017
$15.8M
Chemokine Synergy and Neutrophil FunctionR21AI124681 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI RAJARATHNAM, KRISHNA · 2016 to 2017
$426k
NHLBI NIH HHS P01 HL107152NIAID NIH HHS R21 AI124681
6 · The paper itself

Abstract

Chemokines play diverse roles in human pathophysiology, ranging from trafficking leukocytes and immunosurveillance to the regulation of metabolism and neural function. Chemokine function is intimately coupled to binding tissue glycosaminoglycans (GAGs), heparan sulfate (HS), chondroitin sulfate (CS), and dermatan sulfate (DS). Currently, very little is known about how the structural features and sequences of a given chemokine, the structure and sulfation pattern of a given GAG, and structural differences among GAGs and among chemokines impact binding interactions. In this study, we used solution NMR spectroscopy to characterize the binding interactions of two related neutrophil-activating chemokines, CXCL1 and CXCL5, with HS, CS, and DS. For both chemokines, the dimer bound all three GAGs with higher affinity than did the monomer, and affinities of the chemokines for CS and DS were lower than for HS. NMR-based structural models reveal diverse binding geometries and show that the binding surfaces for each of the three GAGs were different between the two chemokines. However, a given chemokine had similar binding interactions with CS and DS that were different from HS. Considering the fact that CXCL1 and CXCL5 activate the same CXCR2 receptor, we conclude that GAG interactions play a role in determining the nature of chemokine gradients, levels of free chemokine available for receptor activation, how chemokines bind their receptors, and that differences in these interactions determine chemokine-specific function.

Indexed as

ChemokinesChondroitin SulfatesDermatan SulfateHeparan SulfateModels, MolecularProtein BindingProton Magnetic Resonance SpectroscopyChemokinesChondroitin SulfatesDermatan SulfateHeparan Sulfatechemokinechondroitin sulfatedermatan sulfateglycosaminoglycanheparan sulfatenuclear magnetic resonance (NMR)

Identifiers

PMID31455633
PMCPMC6816105
OpenAlexW2970343933

What OpenQuestion holds

Textmetadata
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.