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Identification of Poly-N-Acetyllactosamine-Carrying Glycoproteins from HL-60 Human Promyelocytic Leukemia Cells Using a Site-Specific Glycome Analysis Method, Glyco-RIDGE

Overview of attention for article published in Journal of the American Society for Mass Spectrometry, April 2018
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  • In the top 25% of all research outputs scored by Altmetric
  • Good Attention Score compared to outputs of the same age (74th percentile)
  • High Attention Score compared to outputs of the same age and source (84th percentile)

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Title
Identification of Poly-N-Acetyllactosamine-Carrying Glycoproteins from HL-60 Human Promyelocytic Leukemia Cells Using a Site-Specific Glycome Analysis Method, Glyco-RIDGE
Published in
Journal of the American Society for Mass Spectrometry, April 2018
DOI 10.1007/s13361-018-1938-6
Pubmed ID
Authors

Akira Togayachi, Azusa Tomioka, Mika Fujita, Masako Sukegawa, Erika Noro, Daisuke Takakura, Michiyo Miyazaki, Toshihide Shikanai, Hisashi Narimatsu, Hiroyuki Kaji

Abstract

To elucidate the relationship between the protein function and the diversity and heterogeneity of glycans conjugated to the protein, glycosylation sites, glycan variation, and glycan proportions at each site of the glycoprotein must be analyzed. Glycopeptide-based structural analysis technology using mass spectrometry has been developed; however, complicated analyses of complex spectra obtained by multistage fragmentation are necessary, and sensitivity and throughput of the analyses are low. Therefore, we developed a liquid chromatography/mass spectrometry (MS)-based glycopeptide analysis method to reveal the site-specific glycome (Glycan heterogeneity-based Relational IDentification of Glycopeptide signals on Elution profile, Glyco-RIDGE). This method used accurate masses and retention times of glycopeptides, without requiring MS2, and could be applied to complex mixtures. To increase the number of identified peptide, fractionation of sample glycopeptides for reduction of sample complexity is required. Therefore, in this study, glycopeptides were fractionated into four fractions by hydrophilic interaction chromatography, and each fraction was analyzed using the Glyco-RIDGE method. As a result, many glycopeptides having long glycans were enriched in the highest hydrophilic fraction. Based on the monosaccharide composition, these glycans were thought to be poly-N-acetyllactosamine (polylactosamine [pLN]), and 31 pLN-carrier proteins were identified in HL-60 cells. Gene ontology enrichment analysis revealed that pLN carriers included many molecules related to signal transduction, receptors, and cell adhesion. Thus, these findings provided important insights into the analysis of the glycoproteome using our novel Glyco-RIDGE method. Graphical Abstract ᅟ.

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The data shown below were collected from the profiles of 2 X users who shared this research output. Click here to find out more about how the information was compiled.
Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 22 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 22 100%

Demographic breakdown

Readers by professional status Count As %
Other 3 14%
Student > Ph. D. Student 3 14%
Researcher 3 14%
Student > Postgraduate 2 9%
Student > Bachelor 1 5%
Other 2 9%
Unknown 8 36%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 3 14%
Medicine and Dentistry 2 9%
Agricultural and Biological Sciences 2 9%
Unspecified 1 5%
Pharmacology, Toxicology and Pharmaceutical Science 1 5%
Other 4 18%
Unknown 9 41%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 8. 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 05 July 2022.
All research outputs
#4,762,265
of 25,382,440 outputs
Outputs from Journal of the American Society for Mass Spectrometry
#438
of 3,835 outputs
Outputs of similar age
#86,273
of 340,931 outputs
Outputs of similar age from Journal of the American Society for Mass Spectrometry
#12
of 85 outputs
Altmetric has tracked 25,382,440 research outputs across all sources so far. Compared to these this one has done well and is in the 81st percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 3,835 research outputs from this source. They receive a mean Attention Score of 3.8. This one has done well, scoring higher than 88% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 340,931 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 74% of its contemporaries.
We're also able to compare this research output to 85 others from the same source and published within six weeks on either side of this one. This one has done well, scoring higher than 84% of its contemporaries.