ArticleJournal of pharmaceutical sciences2017
Structural Analysis of Heparin-Derived 3-O-Sulfated Tetrasaccharides: Antithrombin Binding Site Variants.
Article in Journal of pharmaceutical sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed, 56 citations in OpenAlex.
- Non-anticoagulant heparins: glycan-mediated immune modulation and therapeutic applications.Frontiers in immunology · 2026Review
- RNA-binding protein PTBP1 mediates HSV-1 attachment and infection through regulation of heparan sulfate 3-O-sulfotransferase gene expression.Cell & bioscience · 2025Article
- UtilizingAmerican journal of physiology. Cell physiology · 2025Review
- Cloning, expression, and characterization of a heparinase III coupled with heparinase I for enzymatic depolymerization of heparin.World journal of microbiology & biotechnology · 2024Article
- Synthesis of bioengineered heparin chemically and biologically similar to porcine-derived products and convertible to low MW heparin.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Regulatory T cells use heparanase to access IL-2 bound to extracellular matrix in inflamed tissue.Nature communications · 2024Article
- Trauma promotes heparan sulfate modifications and cleavage that disrupt homeostatic gene expression in microvascular endothelial cells.Frontiers in cell and developmental biology · 2024Article
- Increased 3-Science advances · 2023Article
- Glycosaminoglycans from the StarfishMarine drugs · 2023Article
- Investigation of the pharmacokinetic properties of synthetic heparan sulfate oligosaccharides.Glycobiology · 2023Article
- [Advances in heparin structural analysis by chromatography technologies].Se pu = Chinese journal of chromatography · 2023Review
- Non-anticoagulant heparin derivatives for COVID-19 treatment.International journal of biological macromolecules · 2023Review
- Chemoenzymatic synthesis of sulfur-linked sugar polymers as heparanase inhibitors.Nature communications · 2022Article
- Emerging chemical and biochemical tools for studying 3-American journal of physiology. Cell physiology · 2022Review
- Analysis of 3-Analytical chemistry · 2022Article
- Glycosylation of SARS-CoV-2: structural and functional insights.Analytical and bioanalytical chemistry · 2021Review
- The 3-Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Chemical O-sulfation of N-sulfoheparosan: a route to rare N-sulfo-3-O-sulfoglucosamine and 2-O-sulfoglucuronic acid.Glycoconjugate journal · 2020Article
- Filter-entrapment enrichment pull-down assay for glycosaminoglycan structural characterization and protein interaction.Carbohydrate polymers · 2020Article
- Structural characterization of a clinically described heparin-like substance in plasma causing bleeding.Carbohydrate polymers · 2020Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Heparin is a polysaccharide that is widely used as an anticoagulant drug. The mechanism for heparin's anticoagulant activity is primarily through its interaction with a serine protease inhibitor, antithrombin III (AT), that enhances its ability to inactivate blood coagulation serine proteases, including thrombin (factor IIa) and factor Xa. The AT-binding site in the heparin is one of the most well-studied carbohydrate-protein binding sites and its structure is the basis for the synthesis of the heparin pentasaccharide drug, fondaparinux. Despite our understanding of the structural requirements for the heparin pentasaccharide AT-binding site, there is a lack of data on the natural variability of these binding sites in heparins extracted from animal tissues. The present work provides a detailed study on the structural variants of the tetrasaccharide fragments of this binding site afforded following treatment of a heparin with heparin lyase II. The 5 most commonly observed tetrasaccharide fragments of the AT-binding site are fully characterized, and a method for their quantification in heparin and low-molecular-weight heparin products is described.
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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.