Evidence map›Paper›PMID 20345121›Full record

ArticleBiochemistry2010

Screening for anticoagulant heparan sulfate octasaccharides and fine structure characterization using tandem mass spectrometry.

Hicham Naimy, Nancy Leymarie, Joseph Zaia

Abstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.5field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Glycosaminoglycan glycomics using mass spectrometry.Molecular & cellular proteomics : MCP · 2013
    Review
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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

3 authors at 1 institution in 1 country.

Hicham NaimyDepartment of Biochemistry, Boston University School of Medicine, 670 Albany Street, Boston, Massachusetts 02118, USA.
Nancy Leymarie
Joseph Zaia
Boston University · US

Funding

XI INTERNATIONAL SYMPOSIUM ON AMYLOIDOSISP41RR010888 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 1996 to 2011
$18.6M
Mass Spectrometry Resource for Biology and MedicineP41GM104603 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2017
$10.4M
Post-biosynthetic Remodeling of Heparan SulfateR01HL098950 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 2010 to 2013
$1.6M
LTQ MASS SPECTROMETER: STRUCTURAL BIOLOGYS10RR020946 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 2006 to 2006
$497k
NCRR NIH HHS P41 RR010888NCRR NIH HHS P41RR10888NCRR NIH HHS S10 RR020946NCRR NIH HHS S10RR020946NHLBI NIH HHS R01 HL098950NIGMS NIH HHS P41 GM104603
6 · The paper itself

Abstract

Heparan sulfate (HS) is a sulfated glycosaminoglycan located on the surface and extracellular matrix of mammalian cells. HS is constituted of highly N-sulfated domains (NS domains) interrupted by lower sulfation domains. The arrangement of these domains dictates the function of HS which is mainly involved in binding proteins and regulating their biological activities. Heparin, a heparan sulfate analogue present in mast cells, resembles the NS domains of HS but lacks the alternating high and low sulfation architecture. Because the NS domains that range up to hexadecasaccharide in size are the main protein binders, heparin has been used as a model for HS in protein binding studies. Heparan sulfate, however, is the more physiologically relevant modulator of growth factor-receptor interactions. In this work, liquid chromatography and mass spectrometry (LC-MS) were used to compare the compositions of affinity-purified heparin and HS octasaccharides with anticoagulant activities versus library octasaccharides. The fine structures of the biologically active HS compositions were then compared against those of library octasaccharides using low-energy collision-induced dissociation tandem mass spectrometry. This approach confirmed isomeric enrichment of these compositions and, most importantly, produces ions diagnostic of their biological activity.

Indexed as

AnimalsAnticoagulantsAntithrombin IIIChromatography, LiquidFactor XaHeparan SulfateHydrolysisIntestinal MucosaOligosaccharidesSwineTandem Mass SpectrometryAnticoagulantsAntithrombin IIIFactor XaHeparan SulfateOligosaccharides

Identifiers

PMID20345121
PMCPMC3251171
OpenAlexW1997798905

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.