Evidence map›Paper›PMID 23820512›Full record

ArticleMolecular & cellular proteomics : MCP2013

The GlycoFilter: a simple and comprehensive sample preparation platform for proteomics, N-glycomics and glycosylation site assignment.

Hui Zhou, John W Froehlich, Andrew C Briscoe, Richard S Lee

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

15 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Direct Analysis of NativeJournal of the American Society for Mass Spectrometry · 2020
    Article
  4. Article
  5. Article
  6. Clinical proteomics · 2019
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
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.

Hui ZhouDepartment of Urology and The Proteomics Center, Boston Children's Hospital and Harvard Medical School, Boston, Massachusetts 02115.
John W Froehlich
Andrew C Briscoe
Richard S Lee
Boston Children's Hospital · USHarvard University · US

Funding

Early Validation of Urinary Biomarkers of Renal ObstructionR01DK096238 · NIDDK · BOSTON CHILDREN'S HOSPITAL · PI LEE, RICHARD SANG-YONG · 2013 to 2017
$1.3M
The effect of congenital renal obstruction on the urinary proteome in infantsK08DK077836 · NIDDK · BOSTON CHILDREN'S HOSPITAL · PI LEE, RICHARD SANG-YONG · 2007 to 2011
$755k
NIDDK NIH HHS DK077836NIDDK NIH HHS DK077836S1NIDDK NIH HHS K08 DK077836NIDDK NIH HHS R01 DK096238
6 · The paper itself

Abstract

Current strategies to study N-glycoproteins in complex samples are often discrete, focusing on either N-glycans or N-glycosites enriched by sugar-based techniques. In this study we report a simple and rapid sample preparation platform, the GlycoFilter, which allows a comprehensive characterization of N-glycans, N-glycosites, and proteins in a single workflow. Both PNGase F catalyzed de-N-glycosylation and trypsin digestions are accelerated by microwave irradiation and performed sequentially in a single spin filter. Both N-glycans and peptides (including de-N-glycosylated peptides) are separately collected by filtration. The condition to effectively collect complex and heterogeneous N-glycans was established on model glycoproteins, bovine ribonuclease B, bovine fetuin, and human serum IgG. With this platform, the N-glycome, N-glycoproteome and proteome of human urine and plasma were characterized. Overall, a total of 865 and 295 N-glycosites were identified from three pairs of urine and plasma samples, respectively. Many sites were defined unambiguously as partially occupied by the detection of their nonsugar-modified peptides (128 from urine and 61 from plasma), demonstrating that partial occupancy of N-glycosylation occurs frequently. Given the likely high prevalence and variability of partial occupancy, glycoprotein quantification based exclusively on deglycosylated peptides may lead to inaccurate quantification.

Indexed as

AnimalsCattleChromatography, LiquidFetuinsGlycomicsGlycoproteinsGlycosylationHumansImmunoglobulin GPolysaccharidesProteomicsRibonucleasesTandem Mass SpectrometryFetuinsGlycoproteinsImmunoglobulin GPolysaccharidesribonuclease BRibonucleases

Identifiers

PMID23820512
PMCPMC3790305
OpenAlexW2133883131

What OpenQuestion holds

Textmetadata
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.