Evidence map›Paper›PMID 30845788›Full record

ReviewMolecules (Basel, Switzerland)2019

Cross-Species Analysis of Glycosaminoglycan Binding Proteins Reveals Some Animal Models Are "More Equal" than Others.

Eric D Boittier, Neha S Gandhi, Vito Ferro, Deirdre R Coombe

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Article
  2. Heterodimers Are an Integral Component of Chemokine Signaling Repertoire.International journal of molecular sciences · 2023
    Review
  3. Review
  4. RHAMM Is a Multifunctional Protein That Regulates Cancer Progression.International journal of molecular sciences · 2021
    Review
  5. Review
  6. Introduction to the Molecules Special Edition Entitled 'Molecules (Basel, Switzerland) · 2019
    Article
  7. Review
  8. Rationale for the Role of Heparin and Related GAG Antithrombotics in COVID-19 Infection.Clinical and applied thrombosis/hemostasis : official journal of the International Academy of Clinical and Applied Thrombosis/Hemostasis
    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.

Eric D BoittierSchool of Chemistry and Molecular Biosciences, the University of Queensland, Brisbane, QLD 4072, Australia. eric.boittier@uq.net.au.ORCID 0000-0002-9611-1017
Neha S GandhiSchool of Mathematical Sciences and Institute for Health and Biomedical Innovation, Faculty of Science and Engineering, Queensland University of Technology, Brisbane, QLD 4000, Australia. neha.gandhi@qut.edu.au.ORCID 0000-0003-3119-6731
Vito FerroSchool of Chemistry and Molecular Biosciences, the University of Queensland, Brisbane, QLD 4072, Australia. v.ferro@uq.edu.au.ORCID 0000-0003-3306-2550
Deirdre R CoombeSchool of Pharmacy and Biomedical Sciences, Curtin Health Innovation Research Institute, Faculty of Health Sciences, Curtin University, Perth, WA 6102, Australia. d.coombe@curtin.edu.au.

Funding

Australian Research Council DP170104431Queensland University of Technology Not applicable
6 · The paper itself

Abstract

Glycosaminoglycan (GAG) mimetics are synthetic or semi-synthetic analogues of heparin or heparan sulfate, which are designed to interact with GAG binding sites on proteins. The preclinical stages of drug development rely on efficacy and toxicity assessment in animals and aim to apply these findings to clinical studies. However, such data may not always reflect the human situation possibly because the GAG binding site on the protein ligand in animals and humans could differ. Possible inter-species differences in the GAG-binding sites on antithrombin III, heparanase, and chemokines of the CCL and CXCL families were examined by sequence alignments, molecular modelling and assessment of surface electrostatic potentials to determine if one species of laboratory animal is likely to result in more clinically relevant data than another. For each protein, current understanding of GAG binding is reviewed from a protein structure and function perspective. This combinatorial analysis shows chemokine dimers and oligomers can present different GAG binding surfaces for the same target protein, whereas a cleft-like GAG binding site will differently influence the types of GAG structures that bind and the species preferable for preclinical work. Such analyses will allow an informed choice of animal(s) for preclinical studies of GAG mimetic drugs.

Indexed as

Models, MolecularAmino AcidsAmino Acid SequenceAnimalsBinding SitesGlycosaminoglycansHumansMembrane ProteinsModels, AnimalProtein BindingProtein ConformationAmino AcidsGlycosaminoglycansMembrane Proteinsantithrombinchemokineseotaxinglycosaminoglycansheparin binding proteinsIL-8molecular modelling

Identifiers

PMID30845788
PMCPMC6429508

What OpenQuestion holds

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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.