ReviewBritish journal of pharmacology2009
Therapeutically targeting protein-glycan interactions.
Review in British journal of pharmacology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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.
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.
Who cites it
22 citing papers in PubMed, 51 citations in OpenAlex.
- Lipoprotein(a) in Residual Cardiovascular Risk: Measurement Challenges, Assay Standardisation, and Clinical Implications.International journal of general medicine · 2026Review
- Plant lectins as prospective antiviral biomolecules in the search for COVID-19 eradication strategies.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022Review
- Inhibition of renal fibrosis with a human CXCL9-derived glycosaminoglycan-binding peptide.Clinical & translational immunology · 2022Article
- Na/K-ATPase beta1-subunit associates with neuronal growth regulator 1 (NEGR1) to participate in intercellular interactions.BMB reports · 2021Article
- Targeting Versican as a Potential Immunotherapeutic Strategy in the Treatment of Cancer.Frontiers in oncology · 2021Review
- Glycosaminoglycan-Protein Interactions and Their Roles in Human Disease.Frontiers in molecular biosciences · 2021Review
- Targeting Chemokine-Glycosaminoglycan Interactions to Inhibit Inflammation.Frontiers in immunology · 2020Review
- A quantitative, high-throughput method identifies protein-glycan interactions via mass spectrometry.Communications biology · 2019Article
- The Identification of Macrophage-enriched Glycoproteins Using Glycoproteomics.Molecular & cellular proteomics : MCP · 2017Article
- CXCL9-Derived Peptides Differentially Inhibit Neutrophil MigrationFrontiers in immunology · 2017Article
- Marine lectins and their medicinal applications.Applied microbiology and biotechnology · 2015Review
- Heparin/Heparan sulfate proteoglycans glycomic interactome in angiogenesis: biological implications and therapeutical use.Molecules (Basel, Switzerland) · 2015Review
- Synthesis and cell-selective antitumor properties of amino acid conjugated tumor-associated carbohydrate antigen-coated gold nanoparticles.Carbohydrate research · 2015Article
- Glycomic profiling of carcinoembryonic antigen isolated from human tumor tissue.Clinical proteomics · 2015Article
- Characterizing carbohydrate-protein interactions by nuclear magnetic resonance spectroscopy.Biopolymers · 2013Article
- Designing CXCL8-based decoy proteins with strong anti-inflammatory activity in vivo.Bioscience reports · 2013Article
- Structure-based design of decoy chemokines as a way to explore the pharmacological potential of glycosaminoglycans.British journal of pharmacology · 2012Review
- Touch of chemokines.Frontiers in immunology · 2012Article
- A glycobiology review: carbohydrates, lectins and implications in cancer therapeutics.Acta histochemica · 2011Review
- Simultaneous analysis of glycosylated and sialylated prostate-specific antigen revealing differential distribution of glycosylated prostate-specific antigen isoforms in prostate cancer tissues.Analytical chemistry · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosylation is the most common form of post-translational modifications by which oligosaccharide side chains are covalently attached to specific residues of the core protein. Especially O-linked glycan structures like the glycosaminoglycans were found to contribute significantly to many (patho-)biological processes like inflammation, coagulation, cancer and viral infections. Glycans exert their function by interacting with proteins thereby changing the structure of the interacting proteins and consequently modulating their function. Given the complex nature of cell-surface and extracellular matrix glycan structures, this therapeutic site has been neglected for a long time, the only exception being the antithrombin III-glycan interaction which has been successfully targeted by unfractionated and low-molecular weight heparins for many decades. Due to the recent breakthrough in the '-ome' sciences, among them proteomics and glycomics, protein-glycan interactions became more amenable for therapeutic approaches so that novel inhibitors of this interaction are currently in preclinical and clinical studies. An overview of current approaches, their advantages and disadvantages, is given and the promising potential of pharmacologically interfering with protein-glycan interactions is highlighted here.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.