Evidence map›Paper›PMID 27604268›Full record

ArticleAnalytical and bioanalytical chemistry2017

Enhancing glycan isomer separations with metal ions and positive and negative polarity ion mobility spectrometry-mass spectrometry analyses.

Xueyun Zheng, Xing Zhang, Nathaniel S Schocker, Ryan S Renslow, Daniel J Orton, Jamal Khamsi, Roger A Ashmus, Igor C Almeida, Keqi Tang, Catherine E Costello and 3 more

Abstract read
In one paragraph

Article in Analytical and bioanalytical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
–field-weighted citation impact
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

40 citing papers in PubMed.

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  16. Evaluation ofJournal of chemical information and modeling · 2019
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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

13 authors.

Xueyun ZhengEarth and Biological Sciences Directorate, Pacific Northwest National Laboratory, 902 Battelle Blvd, P.O. Box 999, MSIN K8-98, Richland, WA, 99352, USA.
Xing ZhangSkaggs School of Pharmacy and Pharmaceutical Sciences, Anschutz Medical Campus, University of Colorado, 1380 Lawrence Street, Denver, CO, 80204, USA.
Nathaniel S SchockerDepartment of Chemistry and Border Biomedical Research Center, University of Texas at El Paso, 500 West University Avenue, El Paso, TX, 79968, USA.
Ryan S RenslowEarth and Biological Sciences Directorate, Pacific Northwest National Laboratory, 902 Battelle Blvd, P.O. Box 999, MSIN K8-98, Richland, WA, 99352, USA.
Daniel J OrtonEarth and Biological Sciences Directorate, Pacific Northwest National Laboratory, 902 Battelle Blvd, P.O. Box 999, MSIN K8-98, Richland, WA, 99352, USA.
Jamal KhamsiDepartment of Chemistry and Border Biomedical Research Center, University of Texas at El Paso, 500 West University Avenue, El Paso, TX, 79968, USA.
Roger A AshmusDepartment of Chemistry and Border Biomedical Research Center, University of Texas at El Paso, 500 West University Avenue, El Paso, TX, 79968, USA.
Igor C AlmeidaDepartment of Biological Sciences and Border Biomedical Research Center, University of Texas at El Paso, 500 West University Avenue, El Paso, TX, 79968, USA.
Keqi TangEarth and Biological Sciences Directorate, Pacific Northwest National Laboratory, 902 Battelle Blvd, P.O. Box 999, MSIN K8-98, Richland, WA, 99352, USA.
Catherine E CostelloCenter for Biomedical Mass Spectrometry, Boston University School of Medicine, 670 Albany Street, Boston, MA, 02118, USA.
Richard D SmithEarth and Biological Sciences Directorate, Pacific Northwest National Laboratory, 902 Battelle Blvd, P.O. Box 999, MSIN K8-98, Richland, WA, 99352, USA.
Katja MichaelDepartment of Chemistry and Border Biomedical Research Center, University of Texas at El Paso, 500 West University Avenue, El Paso, TX, 79968, USA. kmichael@utep.edu.
Erin S BakerEarth and Biological Sciences Directorate, Pacific Northwest National Laboratory, 902 Battelle Blvd, P.O. Box 999, MSIN K8-98, Richland, WA, 99352, USA. erin.baker@pnnl.gov.

Funding

Equipment Supplement Request for a Research Resource for Ultra-sensitive High Throughput ProteomicsP41GM103493 · NIGMS · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2012 to 2022
$22.6M
TCCG12MD007592 · NIMHD · UNIVERSITY OF TEXAS EL PASO · PI KIRKEN, ROBERT A. · 2012 to 2018
$19.4M
Mass Spectrometry Resource for Biology and MedicineP41GM104603 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2017
$10.4M
Platform Providing Increased Throughput, Sensitivity and Specificity for MetaboloR01ES022190 · NIEHS · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI BAKER, ERIN S · 2012 to 2016
$2.2M
A hybrid IMS-MS platform for ultrasensitive and high resolution glycan analysisR21CA199744 · NCI · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI TANG, KEQI · 2015 to 2016
$607k
Synthetic neoglycopeptides as Chagas disease vaccineR21AI115451 · NIAID · UNIVERSITY OF TEXAS EL PASO · PI ALMEIDA, IGOR C · 2015 to 2016
$423k
Synthesis of immunogenic glycolipopeptides for the development of vaccines for ChR21AI079618 · NIAID · UNIVERSITY OF TEXAS EL PASO · PI MICHAEL, KATJA · 2009 to 2010
$373k
NCI NIH HHS R21 CA199744NIAID NIH HHS R21 AI079618NIAID NIH HHS R21 AI115451NIEHS NIH HHS R01 ES022190NIGMS NIH HHS P41 GM103493NIGMS NIH HHS P41 GM104603NIMHD NIH HHS G12 MD007592
6 · The paper itself

Abstract

Glycomics has become an increasingly important field of research since glycans play critical roles in biology processes ranging from molecular recognition and signaling to cellular communication. Glycans often conjugate with other biomolecules, such as proteins and lipids, and alter their properties and functions, so glycan characterization is essential for understanding the effects they have on cellular systems. However, the analysis of glycans is extremely difficult due to their complexity and structural diversity (i.e., the number and identity of monomer units, and configuration of their glycosidic linkages and connectivities). In this work, we coupled ion mobility spectrometry with mass spectrometry (IMS-MS) to characterize glycan standards and biologically important isomers of synthetic αGal-containing O-glycans including glycotopes of the protozoan parasite Trypanosoma cruzi, which is the causative agent of Chagas disease. IMS-MS results showed significant differences for the glycan structural isomers when analyzed in positive and negative polarity and complexed with different metal cations. These results suggest that specific metal ions or ion polarities could be used to target and baseline separate glycan isomers of interest with IMS-MS. Graphical abstract Glycan isomers, such as fructose and glucose, show distinct separations in positive and negative ion mode.

Indexed as

Ion Mobility SpectrometryMass SpectrometryChemistry Techniques, AnalyticalIonsIsomerismMetalsPolysaccharidesIonsMetalsPolysaccharidesGlycansIon mobility spectrometryIsomersMass spectrometryO-Glycans

Identifiers

PMID27604268
PMCPMC5434874

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Registered trials

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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.