Evidence map›Paper›PMID 22239659›Full record

ArticleJournal of proteome research2012

Semi-automated identification of N-Glycopeptides by hydrophilic interaction chromatography, nano-reverse-phase LC-MS/MS, and glycan database search.

Petr Pompach, Kevin B Chandler, Renny Lan, Nathan Edwards, Radoslav Goldman

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
6.3field-weighted citation impact, top 3% 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

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 102 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021
    Review
  6. Article
  7. Article
  8. Databases and Bioinformatic Tools for Glycobiology and Glycoproteomics.International journal of molecular sciences · 2020
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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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

5 authors at 2 institutions in 1 country.

Petr PompachDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University , 3970 Reservoir Road NW, Washington, DC 20057-1465, United States.
Kevin B Chandler
Renny Lan
Nathan Edwards
Radoslav Goldman
Georgetown University · USGeorgetown University Medical Center · US

Funding

Tissue Culture Shared ResourceP30CA051008 · NCI · GEORGETOWN UNIVERSITY · PI STEPHEN W BYERS · 1990 to 2026
$71.5M
Glycans in Hepatocellular CarcinomaR01CA135069 · NCI · GEORGETOWN UNIVERSITY · PI GOLDMAN, RADOSLAV · 2009 to 2019
$4.1M
Proteomic Analysis of Serum in Liver CancerR01CA115625 · NCI · GEORGETOWN UNIVERSITY · PI GOLDMAN, RADOSLAV · 2007 to 2010
$1.4M
NCI NIH HHS CA135069NCI NIH HHS P30 CA051008NCI NIH HHS P30 CA51008NCI NIH HHS R01 CA115625NCI NIH HHS R01 CA135069
6 · The paper itself

Abstract

Glycoproteins fulfill many indispensable biological functions, and changes in protein glycosylation have been observed in various diseases. Improved analytical methods are needed to allow a complete characterization of this complex and common post-translational modification. In this study, we present a workflow for the analysis of the microheterogeneity of N-glycoproteins that couples hydrophilic interaction and nanoreverse-phase C18 chromatography to tandem QTOF mass spectrometric analysis. A glycan database search program, GlycoPeptideSearch, was developed to match N-glycopeptide MS/MS spectra with the glycopeptides comprised of a glycan drawn from the GlycomeDB glycan structure database and a peptide from a user-specified set of potentially glycosylated peptides. Application of the workflow to human haptoglobin and hemopexin, two microheterogeneous N-glycoproteins, identified a total of 57 distinct site-specific glycoforms in the case of haptoglobin and 14 site-specific glycoforms of hemopexin. Using glycan oxonium ions and peptide-characteristic glycopeptide fragment ions and by collapsing topologically redundant glycans, the search software was able to make unique N-glycopeptide assignments for 51% of assigned spectra, with the remaining assignments primarily representing isobaric topological rearrangements. The optimized workflow, coupled with GlycoPeptideSearch, is expected to make high-throughput semiautomated glycopeptide identification feasible for a wide range of users.

Indexed as

SoftwareAmino Acid SequenceCarbohydrate SequenceChromatography, Reverse-PhaseDatabases, ProteinGlycoproteinsHaptoglobinsHemopexinHumansHydrophobic and Hydrophilic InteractionsMolecular Sequence DataPeptide FragmentsPeptide MappingPolysaccharidesProtein IsoformsProteolysisGlycoproteinsHaptoglobinsHemopexinPeptide FragmentsPolysaccharidesProtein Isoforms

Identifiers

PMID22239659
PMCPMC3292689
OpenAlexW2013044141

What OpenQuestion holds

Textmetadata
LicenceTDM
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.