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Identification of Sialic Acid Linkages on Intact Glycopeptides via Differential Chemical Modification Using IntactGIG-HILIC

Overview of attention for article published in Journal of the American Society for Mass Spectrometry, April 2018
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Title
Identification of Sialic Acid Linkages on Intact Glycopeptides via Differential Chemical Modification Using IntactGIG-HILIC
Published in
Journal of the American Society for Mass Spectrometry, April 2018
DOI 10.1007/s13361-018-1931-0
Pubmed ID
Authors

Shuang Yang, Wells W. Wu, Rong-Fong Shen, Marshall Bern, John Cipollo

Abstract

Mass spectrometric analysis of intact glycopeptides can reveal detailed information about glycosite, glycan structural features, and their heterogeneity. Sialyl glycopeptides can be positively, negatively, or neutrally charged depending on pH of their buffer solution and ionization conditions. To detect sialoglycopeptides, a negative-ion mode mass spectrometry may be applied with a minimal loss of sialic acids, although the positively charged or neutral glycopeptides may be excluded. Alternatively, the sialyl glycopeptides can be identified using positive-ion mode analysis by doping a high concentration of sodium salts to the analytes. Although manipulation of unmodified sialoglycopeptides can be useful for analysis of samples, less than optimal ionization, facile loss of sialyl and unfavorable ionization of accompanying non-sialyl peptides make such strategies suboptimal. Currently available chemical derivatization methods, while stabilizing for sialic acid, mask sialic acid linkage configuration. Here, we report the development of a novel approach to neutralize sialic acids via sequentially chemical modification that also reveals their linkage configuration, often an important determinant in biological function. This method utilizes several components to facilitate glycopeptide identification. These include the following: solid phase derivatization, enhanced ionization of sialoglycopeptides, differentiation of sialic acid linkage, and enrichment of the modified glycopeptides by hydrophilic interaction liquid chromatography. This technology can be used as a tool for quantitative analysis of protein sialylation in diseases with determination of sialic acid linkage configuration. Graphical Abstract ᅟ.

Twitter Demographics

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Mendeley readers

The data shown below were compiled from readership statistics for 4 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 4 100%

Demographic breakdown

Readers by professional status Count As %
Other 1 25%
Student > Postgraduate 1 25%
Researcher 1 25%
Unspecified 1 25%
Readers by discipline Count As %
Unspecified 1 25%
Biochemistry, Genetics and Molecular Biology 1 25%
Computer Science 1 25%
Agricultural and Biological Sciences 1 25%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 24 April 2018.
All research outputs
#8,058,611
of 12,846,518 outputs
Outputs from Journal of the American Society for Mass Spectrometry
#1,387
of 2,231 outputs
Outputs of similar age
#163,061
of 271,475 outputs
Outputs of similar age from Journal of the American Society for Mass Spectrometry
#25
of 63 outputs
Altmetric has tracked 12,846,518 research outputs across all sources so far. This one is in the 23rd percentile – i.e., 23% of other outputs scored the same or lower than it.
So far Altmetric has tracked 2,231 research outputs from this source. They receive a mean Attention Score of 2.8. This one is in the 33rd percentile – i.e., 33% of its peers scored the same or lower than it.
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We're also able to compare this research output to 63 others from the same source and published within six weeks on either side of this one. This one is in the 44th percentile – i.e., 44% of its contemporaries scored the same or lower than it.