Evidence map›Paper›PMID 22843980›Full record

ReviewBriefings in bioinformatics2013

Automated glycopeptide analysis--review of current state and future directions.

David C Dallas, William F Martin, Serenus Hua, J Bruce German

Abstract readReview
In one paragraph

Review in Briefings in bioinformatics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Why Glycosylation Matters in Building a Better Flu Vaccine.Molecular & cellular proteomics : MCP · 2019
    Review
  5. Proteomics, Glycomics, and Glycoproteomics of Matrisome Molecules.Molecular & cellular proteomics : MCP · 2019
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Chemical Glycoproteomics.Chemical reviews · 2016
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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.

David C DallasUniversity of California, Davis, Davis, CA 95616, USA.
William F Martin
Serenus Hua
J Bruce German

Funding

Training Program in Biomolecular TechnologyT32GM008799 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI LEACH, J. KENT · 2002 to 2016
$2.4M
NIGMS NIH HHS 2-T3-GM08799
6 · The paper itself

Abstract

Glycosylation of proteins is involved in immune defense, cell-cell adhesion, cellular recognition and pathogen binding and is one of the most common and complex post-translational modifications. Science is still struggling to assign detailed mechanisms and functions to this form of conjugation. Even the structural analysis of glycoproteins-glycoproteomics-remains in its infancy due to the scarcity of high-throughput analytical platforms capable of determining glycopeptide composition and structure, especially platforms for complex biological mixtures. Glycopeptide composition and structure can be determined with high mass-accuracy mass spectrometry, particularly when combined with chromatographic separation, but the sheer volume of generated data necessitates computational software for interpretation. This review discusses the current state of glycopeptide assignment software-advances made to date and issues that remain to be addressed. The various software and algorithms developed so far provide important insights into glycoproteomics. However, there is currently no freely available software that can analyze spectral data in batch and unambiguously determine glycopeptide compositions for N- and O-linked glycopeptides from relevant biological sources such as human milk and serum. Few programs are capable of aiding in structural determination of the glycan component. To significantly advance the field of glycoproteomics, analytical software and algorithms are required that: (i) solve for both N- and O-linked glycopeptide compositions, structures and glycosites in biological mixtures; (ii) are high-throughput and process data in batches; (iii) can interpret mass spectral data from a variety of sources and (iv) are open source and freely available.

Indexed as

AutomationChromatography, LiquidGlycopeptidesHigh-Throughput Screening AssaysProteomicsSoftwareTandem Mass SpectrometryGlycopeptidesbioinformaticsglycopeptideglycopeptidomicsglycoproteomicsN-linkedO-linked

Identifiers

PMID22843980
PMCPMC3659302

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.