Evidence map›Paper›PMID 30257876›Full record

ArticleMolecular & cellular proteomics : MCP2019

Deciphering Protein Glycosylation by Computational Integration of On-chip Profiling, Glycan-array Data, and Mass Spectrometry.

Zachary Klamer, Peter Hsueh, David Ayala-Talavera, Brian Haab

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2019. 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
–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

12 citing papers in PubMed.

  1. Article
  2. Metabolomics andCommunications biology · 2024
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Phospho-regulation of mitotic spindle assembly.Cytoskeleton (Hoboken, N.J.) · 2020
    Review
  10. Review
  11. Article
  12. Review
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.

Zachary KlamerFrom the Van Andel Research Institute, 333 Bostwick NE, Grand Rapids, MI 49503.
Peter HsuehFrom the Van Andel Research Institute, 333 Bostwick NE, Grand Rapids, MI 49503.
David Ayala-TalaveraFrom the Van Andel Research Institute, 333 Bostwick NE, Grand Rapids, MI 49503.
Brian HaabFrom the Van Andel Research Institute, 333 Bostwick NE, Grand Rapids, MI 49503. Electronic address: Brian.haab@vai.org.

Funding

Detection of Pre-Invasive Pancreatic Cysts Using Protein and Glycan BiomarkersU01CA152653 · NCI · VAN ANDEL RESEARCH INSTITUTE · PI ALLEN, PETER J, BRAND, RANDALL · 2010 to 2021
$5.8M
Subpopulations of Pancreatic Cancer Cells Defined by Glycan MarkersU01CA226158 · NCI · VAN ANDEL RESEARCH INSTITUTE · PI BRAND, RANDALL, HAAB, BRIAN B. · 2019 to 2023
$3.2M
Targeted Glycomics and Affinity Reagents for Cancer Biomarker DevelopmentU01CA168896 · NCI · VAN ANDEL RESEARCH INSTITUTE · PI HAAB, BRIAN B. · 2012 to 2016
$2.3M
Comprehensive Glycoproteomic Tool Development for Cancer BiomarkersR42GM112750 · NIGMS · PROTEIN METRICS, LLC · PI BERN, MARSHALL WAYNE · 2017 to 2019
$947k
Orbitrap Fusion Tribrid Mass SpectrometerS10OD018530 · OD · UNIVERSITY OF GEORGIA · PI AZADI, PARASTOO · 2014 to 2014
$750k
Comprehensive Glycoproteomic Tool Development for Cancer BiomarkersR41GM112750 · NIGMS · PROTEIN METRICS, LLC · PI BECKER, CHRISTOPHER H, HAAB, BRIAN B. · 2014 to 2015
$686k
On-chip Glycan Analysis of Clinical SpecimensR21AI129872 · NIAID · VAN ANDEL RESEARCH INSTITUTE · PI HAAB, BRIAN B. · 2016 to 2017
$631k
NCI NIH HHS U01 CA152653NCI NIH HHS U01 CA168896NCI NIH HHS U01 CA226158NIAID NIH HHS R21 AI129872NIGMS NIH HHS R41 GM112750NIGMS NIH HHS R42 GM112750NIH HHS S10 OD018530
6 · The paper itself

Abstract

The difficulty in uncovering detailed information about protein glycosylation stems from the complexity of glycans and the large amount of material needed for the experiments. Here we report a method that gives information on the isomeric variants of glycans in a format compatible with analyzing low-abundance proteins. On-chip glycan modification and probing (on-chip gmap) uses sequential and parallel rounds of exoglycosidase cleavage and lectin profiling of microspots of proteins, together with algorithms that incorporate glycan-array analyses and information from mass spectrometry, when available, to computationally interpret the data. In tests on control proteins with simple or complex glycosylation, on-chip gmap accurately characterized the relative proportions of core types and terminal features of glycans. Subterminal features (monosaccharides and linkages under a terminal monosaccharide) were accurately probed using a rationally designed sequence of lectin and exoglycosidase incubations. The integration of mass information further improved accuracy in each case. An alternative use of on-chip gmap was to complement the mass spectrometry analysis of detached glycans by specifying the isomers that comprise the glycans identified by mass spectrometry. On-chip gmap provides the potential for detailed studies of glycosylation in a format compatible with clinical specimens or other low-abundance sources.

Indexed as

AlgorithmsAnimalsCattleComputational BiologyFetuinsGlycosylationHumansMass SpectrometryPolysaccharidesProtein Array AnalysisTransferrinFetuinsPolysaccharidesTransferrinBioinformaticsExoglycosidaseGlycoproteomicsGlycosidaseGlycosylationMicro ArraysProtein Array

Identifiers

PMID30257876
PMCPMC6317472

What OpenQuestion holds

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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.