Evidence map›Paper›PMID 21873605›Full record

ArticleGlycobiology2012

Characterization of the interaction of interleukin-8 with hyaluronan, chondroitin sulfate, dermatan sulfate and their sulfated derivatives by spectroscopy and molecular modeling.

Annelie Pichert, Sergey A Samsonov, Stephan Theisgen, Lars Thomas, Lars Baumann, Jürgen Schiller, Annette G Beck-Sickinger, Daniel Huster, M Teresa Pisabarro

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

59 citing papers in PubMed, 132 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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  17. Modeling Protein-Glycosaminoglycan Complexes: Does the Size Matter?Journal of chemical information and modeling · 2021
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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

9 authors at 2 institutions in 1 country.

Annelie PichertInstitute of Medical Physics and Biophysics, University of Leipzig, Härtelstr. 16-18, D-04107 Leipzig, Germany.
Sergey A Samsonov
Stephan Theisgen
Lars Thomas
Lars Baumann
Jürgen Schiller
Annette G Beck-Sickinger
Daniel Huster
M Teresa Pisabarro
Leipzig University · DETU Dresden · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interactions between glycosaminoglycans (GAGs), important components of the extracellular matrix, and proteins such as growth factors and chemokines play critical roles in cellular regulation processes. Therefore, the design of GAG derivatives for the development of innovative materials with bio-like properties in terms of their interaction with regulatory proteins is of great interest for tissue engineering and regenerative medicine. Previous work on the chemokine interleukin-8 (IL-8) has focused on its interaction with heparin and heparan sulfate, which regulate chemokine function. However, the extracellular matrix contains other GAGs, such as hyaluronic acid (HA), dermatan sulfate (DS) and chondroitin sulfate (CS), which have so far not been characterized in terms of their distinct molecular recognition properties towards IL-8 in relation to their length and sulfation patterns. NMR and molecular modeling have been in great part the methods of choice to study the structural and recognition properties of GAGs and their protein complexes. However, separately these methods have challenges to cope with the high degree of similarity and flexibility that GAGs exhibit. In this work, we combine fluorescence spectroscopy, NMR experiments, docking and molecular dynamics simulations to study the configurational and recognition properties of IL-8 towards a series of HA and CS derivatives and DS. We analyze the effects of GAG length and sulfation patterns in binding strength and specificity, and the influence of GAG binding on IL-8 dimer formation. Our results highlight the importance of combining experimental and theoretical approaches to obtain a better understanding of the molecular recognition properties of GAG-protein systems.

Indexed as

Molecular Dynamics SimulationAmino Acid MotifsBinding SitesCarbohydrate ConformationChondroitin SulfatesDermatan SulfateHumansHyaluronic AcidHydrogen BondingInterleukin-8Magnetic Resonance SpectroscopyProtein BindingProtein MultimerizationSpectrometry, FluorescenceThermodynamicsTitrimetryChondroitin SulfatesDermatan SulfateHyaluronic AcidInterleukin-8

Identifiers

PMID21873605
PMCPMC3230280
OpenAlexW2164401552

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.