Evidence map›Paper›PMID 22261724›Full record

ArticleMolecular & cellular proteomics : MCP2012

Mapping yeast N-glycosites with isotopically recoded glycans.

Mark A Breidenbach, Krishnan K Palaniappan, Austin A Pitcher, Carolyn R Bertozzi

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
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  3. Article
  4. Article
  5. Article
  6. Article
  7. Chemical Glycoproteomics.Chemical reviews · 2016
    Review
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  10. Review
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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

4 authors at 2 institutions in 1 country.

Mark A BreidenbachDepartment of Chemistry, Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA.
Krishnan K Palaniappan
Austin A Pitcher
Carolyn R Bertozzi
University of California, Berkeley · USHoward Hughes Medical Institute · US

Funding

Studies of Protein GlycosylationR01GM066047 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERTOZZI, CAROLYN · 2002 to 2014
$3.8M
Howard Hughes Medical InstituteNCI NIH HHS PC080659NIGMS NIH HHS GM066047NIGMS NIH HHS R01 GM066047
6 · The paper itself

Abstract

Asparagine-linked glycosylation is a common post-translational modification of proteins; in addition to participating in key macromolecular interactions, N-glycans contribute to protein folding, trafficking, and stability. Despite their importance, few N-glycosites have been experimentally mapped in the Saccharomyces cerevisiae proteome. Factors including glycan heterogeneity, low abundance, and low occupancy can complicate site mapping. Here, we report a novel mass spectrometry-based strategy for detection of N-glycosites in the yeast proteome. Our method imparts N-glycopeptide mass envelopes with a pattern that is computationally distinguishable from background ions. Isotopic recoding is achieved via metabolic incorporation of a defined mixture of N-acetylglucosamine isotopologs into N-glycans. Peptides bearing the recoded envelopes are specifically targeted for fragmentation, facilitating high confidence site mapping. This strategy requires no chemical modification of the N-glycans or stringent sample enrichment. Further, enzymatically simplified N-glycans are preserved on peptides. Using this approach, we identify 133 N-glycosites spanning 58 proteins, nearly doubling the number of experimentally observed N-glycosites in the yeast proteome.

Indexed as

AcetylglucosamineAmino Acid MotifsAmino Acid SequenceConsensus SequenceGlycosylationIsotope LabelingMolecular Sequence DataPeptide FragmentsPeptide MappingPolysaccharidesProtein Processing, Post-TranslationalProteomeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAcetylglucosaminePeptide FragmentsPolysaccharidesProteomeSaccharomyces cerevisiae Proteins

Identifiers

PMID22261724
PMCPMC3433913
OpenAlexW2066363606

What OpenQuestion holds

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LicenceCC BY-NC
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.