ReviewMetallomics : integrated biometal science2018
Influence of zinc on glycosaminoglycan neutralisation during coagulation.
Review in Metallomics : integrated biometal science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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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.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Binding properties of marine sulfated glycans to coagulation (co)-factors using surface plasmon resonance spectroscopy.Scientific reports · 2026Article
- Inhibition Effects and Mechanism Study of rAj-HRP30, a Recombinant Histidine-Rich Peptide fromInternational journal of molecular sciences · 2025Article
- Heavy metal pollution and ischemic stroke: multimechanistic pathogenesis and countermeasures.Frontiers in public health · 2025Review
- Association of Metal Cations with the Anti-PF4/Heparin Antibody Response in Heparin-Induced Thrombocytopenia.Cardiovascular toxicology · 2024Article
- Association of Metal Cations with the Anti-PF4/Heparin Antibody Response in Heparin-Induced Thrombocytopenia.Research square · 2024Article
- Clays and Wound Healing.Materials (Basel, Switzerland) · 2024Review
- ZnInternational journal of molecular sciences · 2023Article
- Strategies for Therapeutic Amelioration of Aberrant Plasma ZnInternational journal of molecular sciences · 2022Review
- An NMR relaxometry approach for quantitative investigation of the transchelation of gadolinium ions from GBCAs to a competing macromolecular chelator.Scientific reports · 2021Article
- Albumin-mediated alteration of plasma zinc speciation by fatty acids modulates blood clotting in type-2 diabetes.Chemical science · 2021Article
- Elucidation of Cellular Contributions to Heparin-Induced Thrombocytopenia Using Omic Approaches.Frontiers in pharmacology · 2021Review
- Coagulatory Defects in Type-1 and Type-2 Diabetes.International journal of molecular sciences · 2019Review
- Zinc Homeostasis in Platelet-Related Diseases.International journal of molecular sciences · 2019Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Heparan sulfate (HS), dermatan sulfate (DS) and heparin are glycosaminoglycans (GAGs) that serve as key natural and pharmacological anticoagulants. During normal clotting such agents require to be inactivated or neutralised. Several proteins have been reported to facilitate their neutralisation, which reside in platelet α-granules and are released following platelet activation. These include histidine-rich-glycoprotein (HRG), fibrinogen and high-molecular-weight kininogen (HMWK). Zinc ions (Zn2+) are also present in α-granules at a high concentration and participate in the propagation of coagulation by influencing the binding of neutralising proteins to GAGs. Zn2+ in many cases increases the affinity of these proteins to GAGs, and is thus an important regulator of GAG neutralisation and haemostasis. Binding of Zn2+ to HRG, HMWK and fibrinogen is mediated predominantly through coordination to histidine residues but the mechanisms by which Zn2+ increases the affinity of the proteins for GAGs are not yet completely clear. Here we will review current knowledge of how Zn2+ binds to and influences the neutralisation of GAGs and describe the importance of this process in both normal and pathogenic clotting.
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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.