Evidence map›Paper›PMID 33908007›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Site-Specific O-Glycosylation Analysis by Liquid Chromatography-Mass Spectrometry with Electron-Transfer/Higher-Energy Collisional Dissociation.

Noritaka Hashii, Junya Suzuki

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021
    Review
  3. 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

2 authors at 1 institution in 1 country.

Noritaka HashiiDivision of Biological Chemistry and Biologicals, National Institute of Health Sciences, Kawasaki, Kanagawa, Japan. hashii@nihs.go.jp.
Junya SuzukiDivision of Biological Chemistry and Biologicals, National Institute of Health Sciences, Kawasaki, Kanagawa, Japan.
National Institute of Health Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

O-glycosylation is a major post-translational modification of proteins. Accurate and detailed analysis to reveal O-glycosylation patterns at each site (site-specific O-glycosylation analysis) is essential to deeply understand glycoprotein function. Recent reports also demonstrated that unintended O-glycosylation occurs on therapeutic fusion glycoproteins; therefore, it is increasingly important to perform detailed and exhaustive O-glycosylation analysis during the development of therapeutic glycoproteins. Here, we describe a method of in-depth site-specific O-glycosylation analysis by liquid chromatography-mass spectrometry using electron-transfer/higher-energy collisional dissociation (EThcD) and database analysis.

Indexed as

Chromatography, Reverse-PhaseProtein Processing, Post-TranslationalTandem Mass SpectrometryGlycoproteinsGlycosylationResearch DesignWorkflowGlycoproteinsDatabase searchElectron-transfer/higher-energy collisional dissociationLiquid chromatography–mass spectrometryO-Glycosylation

Identifiers

PMID33908007
OpenAlexW3159194080

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.