ArticleJournal of medicinal chemistry2011
Heparin mapping using heparin lyases and the generation of a novel low molecular weight heparin.
Article in Journal of medicinal chemistry, 2011. 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.
- Switching mechanism from AR to EGFR signaling via 3-O-sulfated heparan sulfate in castration-resistant prostate cancer.Scientific reports · 2023Article
- Biotechnologically produced chitosans with nonrandom acetylation patterns differ from conventional chitosans in properties and activities.Nature communications · 2022Article
- Influence of saccharide modifications on heparin lyase III substrate specificities.Glycobiology · 2022Article
- The 3-Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Enzyme immobilization offers a robust tool to scale up the production of longer, diverse, natural glycosaminoglycan oligosaccharides.Glycobiology · 2020Article
- Synthesis of 3-Biochemistry · 2020Article
- Heparanase as an Additional Tool for Detecting Structural Peculiarities of Heparin Oligosaccharides.Molecules (Basel, Switzerland) · 2019Article
- Sources, Extraction and Biomedical Properties of Polysaccharides.Foods (Basel, Switzerland) · 2019Review
- Specificity and action pattern of heparanase Bp, a β-glucuronidase from Burkholderia pseudomallei.Glycobiology · 2019Article
- Recombinant Heparin-New Opportunities.Frontiers in medicine · 2018Review
- Bioactive polysaccharides from natural resources including Chinese medicinal herbs on tissue repair.Chinese medicine · 2018Review
- Structural Analysis of Heparin-Derived 3-O-Sulfated Tetrasaccharides: Antithrombin Binding Site Variants.Journal of pharmaceutical sciences · 2017Article
- Analysis of heparin oligosaccharides by capillary electrophoresis-negative-ion electrospray ionization mass spectrometry.Analytical and bioanalytical chemistry · 2017Article
- Bioengineered heparins and heparan sulfates.Advanced drug delivery reviews · 2016Review
- GlycCompSoft: Software for Automated Comparison of Low Molecular Weight Heparins Using Top-Down LC/MS Data.PloS one · 2016Article
- Bottom-up low molecular weight heparin analysis using liquid chromatography-Fourier transform mass spectrometry for extensive characterization.Analytical chemistry · 2014Article
- Analysis of 3-O-sulfo group-containing heparin tetrasaccharides in heparin by liquid chromatography-mass spectrometry.Analytical biochemistry · 2014Article
- Structure and activity of a new low-molecular-weight heparin produced by enzymatic ultrafiltration.Journal of pharmaceutical sciences · 2014Article
- Molecular engineering of glycosaminoglycan chemistry for biomolecule delivery.Acta biomaterialia · 2014Review
- Bioengineering murine mastocytoma cells to produce anticoagulant heparin.Glycobiology · 2014Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Seven pharmaceutical heparins were investigated by oligosaccharide mapping by digestion with heparin lyase 1, 2, or 3, followed by high performance liquid chromatography analysis. The structure of one of the prepared mapping standards, ΔUA-Gal-Gal-Xyl-O-CH(2)CONHCH(2)COOH (where ΔUA is 4-deoxy-α-l-threo-hex-4-eno-pyranosyluronic acid, Gal is β-d-galactpyranose, and Xyl is β-d-xylopyranose) released from the linkage region using either heparin lyase 2 or heparin lyase 3 digestion, is reported for the first time. A size-dependent susceptibility of site cleaved by heparin lyase 3 was also observed. Heparin lyase 3 acts on the undersulfated domains of the heparin chain and does not cleave the linkages within heparin's antithrombin III binding site. Thus, a novel low molecular weight heparin (LMWH) is afforded on heparin lyase 3 digestion of heparin due to this unique substrate specificity, which has anticoagulant activity comparable to that of currently available LMWH.
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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.