Evidence map›Paper›PMID 32718661›Full record

ArticleCarbohydrate polymers2020

Filter-entrapment enrichment pull-down assay for glycosaminoglycan structural characterization and protein interaction.

Yanlei Yu, Fuming Zhang, Gina Renois-Predelus, I Jonathan Amster, Robert J Linhardt

Open access · greenAbstract read
In one paragraph

Article in Carbohydrate polymers, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 30% of its field
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

4 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. [Annual review of capillary electrophoresis technology in 2020].Se pu = Chinese journal of chromatography · 2021
    Article
  4. 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

5 authors at 2 institutions in 1 country.

Yanlei YuDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA.
Fuming ZhangDepartment of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA.
Gina Renois-PredelusDepartment of Chemistry, University of Georgia, Athens, GA, 30602, USA.
I Jonathan AmsterDepartment of Chemistry, University of Georgia, Athens, GA, 30602, USA.
Robert J LinhardtDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA; Department of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA; Department of Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA; Department of Biomedical Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA. Electronic address: linhar@rpi.edu.
Rensselaer Polytechnic Institute · USUniversity of Georgia · US

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
The role ofglycosaminoglycan N-sulfation in glomerular biology/pathobiologyR01DK111958 · NIDDK · LOUISIANA STATE UNIV HSC SHREVEPORT · PI MCCARTHY, KEVIN JOHN · 2017 to 2021
$2.6M
An Automated Platform for the CE-MS Analysis of GlycosaminoglycansU01CA231074 · NCI · UNIVERSITY OF GEORGIA · PI AMSTER, I JONATHAN · 2018 to 2020
$895k
NCI NIH HHS U01 CA231074NIDDK NIH HHS R01 DK111958NIGMS NIH HHS P41 GM103390
6 · The paper itself

Abstract

Heparins are the most pharmaceutically important polysaccharides. These heparin-based anticoagulant/antithrombotic agents include unfractionated heparins, low molecular weight heparins (LMWHs) and ultralow molecular weight heparins (ULMWHs). Heparins exhibit their pharmacological and biological activities through interaction with heparin-binding proteins. The prototypical heparin-binding protein is antithrombin III (AT), responsible for heparin's anticoagulant/antithrombotic activity. This study describes a filter-trapping method to isolate the chains in enoxaparin, a LMWH, which bind to AT. We demonstrate this method using the ULMWH, fondaparinux, which consists of a single well defined AT binding site. The interacting chains of enoxaparin are then characterized by activity assays, top-down liquid chromatography-mass spectrometry, and capillary zone electrophoresis mass spectrometry. This filter-trapping assay is an improvement over affinity chromatography for isolating heparin chains interacting with heparin binding proteins.

Indexed as

AnticoagulantsAntithrombin IIIBinding SitesChromatography, AffinityChromatography, LiquidElectrophoresis, CapillaryEnoxaparinFibrinolytic AgentsFondaparinuxHeparin LyaseHumansMass SpectrometryMolecular WeightProtein BindingAnticoagulantsAntithrombin IIIEnoxaparinFibrinolytic AgentsFondaparinuxHeparin LyaseSERPINC1 protein, humanAntithrombin IIICapillary electrophoresisFilter trappingHeparinHeparin-binding proteinsMass spectrometry

Identifiers

PMID32718661
PMCPMC7387750
OpenAlexW3034950779

What OpenQuestion holds

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LicenceTDM
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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.