Evidence map›Paper›PMID 38726698›Full record

ReviewJournal of mass spectrometry : JMS2024

Glycoproteomics: Charting new territory in mass spectrometry and glycobiology.

Stacy A Malaker

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Journal of mass spectrometry : JMS, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
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  10. Article
  11. 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

1 author.

Stacy A MalakerDepartment of Chemistry, Yale University, New Haven, Connecticut, USA.ORCID https://orcid.org/0000-0003-2382-5067

Funding

Toward understanding the role of altered glycosylation in cancerR35GM147039 · NIGMS · YALE UNIVERSITY · PI Stacy Alyse Malaker · 2022 to 2026
$2.0M
NIGMS NIH HHS R35 GM147039NIGMS NIH HHS R35-GM147039
6 · The paper itself

Abstract

Glycosylation is an incredibly common and diverse post-translational modification that contributes widely to cellular health and disease. Mass spectrometry is the premier technique to study glycoproteins; however, glycoproteomics has lagged behind traditional proteomics due to the challenges associated with studying glycosylation. For instance, glycans dissociate by collision-based fragmentation, thus necessitating electron-based fragmentation for site-localization. The vast glycan heterogeneity leads to lower overall abundance of each glycopeptide, and often, ion suppression is observed. One of the biggest issues facing glycoproteomics is the lack of reliable software for analysis, which necessitates manual validation and serves as a massive bottleneck in data processing. Here, I will discuss each of these challenges and some ways in which the field is attempting to address them, along with perspectives on how I believe we should move forward.

Indexed as

GlycomicsGlycoproteinsMass SpectrometryProteomicsAnimalsGlycopeptidesGlycosylationHumansPolysaccharidesProtein Processing, Post-TranslationalSoftwareGlycopeptidesGlycoproteinsPolysaccharidesbioinformaticsglycobiologyglycoproteomicsion suppressionpeptide fragmentation

Identifiers

PMID38726698
PMCPMC13229594

What OpenQuestion holds

Textmetadata
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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.