Evidence map›Paper›PMID 23494309›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2013

N-glycomic and N-glycoproteomic studies in the social amoebae.

Christa L Feasley, Alba Hykollari, Katharina Paschinger, Iain B H Wilson, Christopher M West

Open access · greenAbstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

12 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. CRISPR/Cas9 and glycomics tools forThe Journal of biological chemistry · 2019
    Article
  5. Article
  6. Article
  7. 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 1 institution in 1 country.

Christa L FeasleyDepartment of Biochemistry and Molecular Biology, Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
Alba Hykollari
Katharina Paschinger
Iain B H Wilson
Christopher M West
University of Oklahoma Health Sciences Center · US

Funding

Transfer of 5R01GM037539 - 22 CYTOSOLIC PROLINE HYDROXYLATION AND GLYCOSYLATIONR01GM037539 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI WEST, CHRISTOPHER M. · 1986 to 2016
$4.4M
Glycoregulation of Skp1 in the cytoplasm and nucleusR01GM084383 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI BLADER, IRA J, WEST, CHRISTOPHER M. · 2009 to 2018
$2.9M
Austrian Science Fund FWF P 19615NIGMS NIH HHS R01 GM037539NIGMS NIH HHS R01-GM037539NIGMS NIH HHS R01 GM084383NIGMS NIH HHS R01-GM084383
6 · The paper itself

Abstract

N-glycans modify the great majority of all secreted and plasma membrane proteins, which themselves constitute one-third to one-half of the proteome. The ultimate definition of the glycoproteome would be the identification of all the N-glycans attached to all the modified asparaginyl sites of all the proteins, but glycosylation heterogeneity makes this an unachievable goal. However, mass spectrometry in combination with other methods does have the power to deeply mine the N-glycome of Dictyostelium, and characterize glycan profiles at individual sites of glycoproteins. Recent studies from our laboratories using mass spectrometry-based methods have confirmed basic precepts of the N-glycome based on prior classical methods using radiotracer methods, and have extended the scope of glycan diversity and the distribution of glycan types across specific glycoprotein attachment sites. The protocols described here simplify studies of the N-glycome and -glycoproteome, which should prove useful for interpreting mutant phenotypes, conducting interstrain and interspecies comparisons, and investigating glycan functions in glycoproteins of interest.

Indexed as

Carbohydrate SequenceChromatography, High Pressure LiquidDictyosteliumGlycoproteinsGlycosylationMolecular Sequence DataPeptide FragmentsPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidasePolysaccharidesProtein Processing, Post-TranslationalProteomicsProtozoan ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem Mass SpectrometryGlycoproteinsPeptide FragmentsPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidasePolysaccharidesProtozoan Proteins

Identifiers

PMID23494309
PMCPMC4060149
OpenAlexW1781425196

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.