↓ Skip to main content

Analysis of Congenital Disorder of Glycosylation-Id in a Yeast Model System Shows Diverse Site-Specific Under-glycosylation of Glycoproteins

Overview of attention for article published in Journal of Proteome Research, October 2012
Altmetric Badge

About this Attention Score

  • In the top 25% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (95th percentile)
  • High Attention Score compared to outputs of the same age and source (97th percentile)

Mentioned by

news
3 news outlets
twitter
2 X users

Citations

dimensions_citation
45 Dimensions

Readers on

mendeley
29 Mendeley
You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output. Click here to find out more.
Title
Analysis of Congenital Disorder of Glycosylation-Id in a Yeast Model System Shows Diverse Site-Specific Under-glycosylation of Glycoproteins
Published in
Journal of Proteome Research, October 2012
DOI 10.1021/pr300599f
Pubmed ID
Authors

Ulla-Maja Bailey, Muhammad Fairuz Jamaluddin, Benjamin L. Schulz

Abstract

Asparagine-linked glycosylation is a common post-translational modification of proteins in eukaryotes. Mutations in the human ALG3 gene cause changed levels and altered glycan structures on mature glycoproteins and are the cause of a severe congenital disorder of glycosylation (CDG-Id). Diverse glycoproteins are also under-glycosylated in Saccharomyces cerevisae alg3 mutants. Here we analyzed site-specific glycosylation occupancy in this yeast model system using peptide-N-glycosidase F to label glycosylation sites with an asparagine-aspartate conversion that creates a new endoproteinase AspN cleavage site, followed by proteolytic digestion, and detection of peptides and glycopeptides by LC-ESI-MS/MS. We used this analytical method to identify and measure site-specific glycosylation occupancy in alg3 mutant and wild type yeast strains. We found decreased site-specific N-glycosylation occupancy in the alg3 knockout strain preferentially at Asn-Xaa-Ser sequences located in secondary structural elements, features previously associated with poor glycosylation efficiency. Furthermore, we identified 26 previously experimentally unverified glycosylation sites. Our results provide insights into the underlying mechanisms of disease in CDG-Id, and our methodology will be useful in site-specific glycosylation analysis in many model systems and clinical applications.

X Demographics

X Demographics

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 29 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 29 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 7 24%
Student > Ph. D. Student 6 21%
Student > Master 5 17%
Student > Postgraduate 3 10%
Student > Doctoral Student 1 3%
Other 1 3%
Unknown 6 21%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 10 34%
Agricultural and Biological Sciences 8 28%
Veterinary Science and Veterinary Medicine 1 3%
Pharmacology, Toxicology and Pharmaceutical Science 1 3%
Arts and Humanities 1 3%
Other 2 7%
Unknown 6 21%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 27. 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 17 August 2015.
All research outputs
#1,210,966
of 22,681,577 outputs
Outputs from Journal of Proteome Research
#157
of 6,006 outputs
Outputs of similar age
#7,725
of 174,267 outputs
Outputs of similar age from Journal of Proteome Research
#3
of 121 outputs
Altmetric has tracked 22,681,577 research outputs across all sources so far. Compared to these this one has done particularly well and is in the 94th percentile: it's in the top 10% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 6,006 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 6.2. This one has done particularly well, scoring higher than 97% 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 174,267 tracked outputs that were published within six weeks on either side of this one in any source. This one has done particularly well, scoring higher than 95% of its contemporaries.
We're also able to compare this research output to 121 others from the same source and published within six weeks on either side of this one. This one has done particularly well, scoring higher than 97% of its contemporaries.