Evidence map›Paper›PMID 28589488›Full record

ArticleJournal of the American Society for Mass Spectrometry2017

Negative Electron Transfer Dissociation Sequencing of Increasingly Sulfated Glycosaminoglycan Oligosaccharides on an Orbitrap Mass Spectrometer.

Franklin E Leach, Nicholas M Riley, Michael S Westphall, Joshua J Coon, I Jonathan Amster

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 54 citations in OpenAlex.

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  13. Analysis of the Glycosaminoglycan Chains of Proteoglycans.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2021
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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

5 authors at 3 institutions in 1 country.

Franklin E LeachDepartment of Chemistry, University of Georgia, Athens, GA, USA.
Nicholas M RileyGenome Center of Wisconsin, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Michael S WestphallGenome Center of Wisconsin, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Joshua J CoonGenome Center of Wisconsin, University of Wisconsin-Madison, Madison, WI, 53706, USA.
I Jonathan AmsterDepartment of Chemistry, University of Georgia, Athens, GA, USA. jamster@uga.edu.ORCID 0000-0001-7523-5144
Energy Center of Wisconsin · USUniversity of Georgia · USMorgridge Institute for Research · US

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI LIVE, DAVID H · 2012 to 2019
$14.5M
Structure, Function and Regulation of the ProteomeR35GM118110 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI COON, JOSHUA J · 2016 to 2025
$9.1M
Purchase of a Thermo Fisher Scientific LTQ Orbitrap XL Mass SpectrometerS10RR028859 · NCRR · UNIVERSITY OF GEORGIA · PI AMSTER, I JONATHAN · 2011 to 2011
$832k
Rapid Sequencing of Sulfated Glycans By CE-MS/MSR21HL136271 · NHLBI · UNIVERSITY OF GEORGIA · PI AMSTER, I JONATHAN · 2016 to 2017
$611k
Activated-Ion Negative Electron Transfer Dissociation For High-Throughput GlycoproteomicsR21GM118341 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI COON, JOSHUA J · 2015 to 2016
$581k
Uniting Mass Spectrometry and Glycoscience to Investigate Cancer BiologyF99CA212454 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI RILEY, NICHOLAS M · 2016 to 2017
$65k
NCI NIH HHS F99 CA212454NCRR NIH HHS S10 RR028859NHLBI NIH HHS R21 HL136271NIGMS NIH HHS P41 GM103390NIGMS NIH HHS R21 GM118341NIGMS NIH HHS R35 GM118110
6 · The paper itself

Abstract

The structural characterization of sulfated glycosaminoglycan (GAG) carbohydrates remains an important target for analytical chemists attributable to challenges introduced by the natural complexity of these mixtures and the defined need for molecular-level details to elucidate biological structure-function relationships. Tandem mass spectrometry has proven to be the most powerful technique for this purpose. Previously, electron detachment dissociation (EDD), in comparison to other methods of ion activation, has been shown to provide the largest number of useful cleavages for de novo sequencing of GAG oligosaccharides, but such experiments are restricted to Fourier transform ion cyclotron resonance mass spectrometers (FTICR-MS). Negative electron transfer dissociation (NETD) provides similar fragmentation results, and can be achieved on any mass spectrometry platform that is designed to accommodate ion-ion reactions. Here, we examine for the first time the effectiveness of NETD-Orbitrap mass spectrometry for the structural analysis of GAG oligosaccharides. Compounds ranging in size from tetrasaccharides to decasaccharides were dissociated by NETD, producing both glycosidic and cross-ring cleavages that enabled the location of sulfate modifications. The highly-sulfated, heparin-like synthetic GAG, Arixtra

Indexed as

GlycosaminoglycanNETDOrbitrapSulfated carbohydrateTandem mass spectrometry

Identifiers

PMID28589488
PMCPMC5711533
OpenAlexW2622082039

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.