Evidence map›Paper›PMID 35388686›Full record

ArticleAnalytical chemistry2022

Analysis of Viral Spike Protein N-Glycosylation Using Ultraviolet Photodissociation Mass Spectrometry.

Edwin E Escobar, Shuaishuai Wang, Rupanjan Goswami, Michael B Lanzillotti, Lei Li, Jason S McLellan, Jennifer S Brodbelt

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

8 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. UnravelingAnalytical chemistry · 2024
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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

7 authors at 2 institutions in 1 country.

Edwin E EscobarDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.
Shuaishuai WangDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas 78712, United States.ORCID 0000-0002-8346-9159
Rupanjan GoswamiPREMIER Biosoft, San Francisco, California 94131, United States.
Michael B LanzillottiDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.
Lei LiDepartment of Chemistry, Georgia State University, Atlanta, Georgia 30303, United States.ORCID 0000-0002-1146-0761
Jason S McLellanDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas 78712, United States.
Jennifer S BrodbeltDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.ORCID 0000-0003-3207-0217
The University of Texas at Austin · USGeorgia State University · US

Funding

Ultraviolet Photodissociation Mass Spectrometry for Characterization of Biological MoleculesR35GM139658 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2021 to 2025
$2.9M
UVPD Mass Spectrometry of Protein ComplexesR01GM121714 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2017 to 2020
$1.4M
Advancing Ultraviolet Photodissociation Mass Spectrometry for Precision Mapping of Protein GlycosylationF31GM140595 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI ESCOBAR, EDWIN E · 2021 to 2022
$66k
NIGMS NIH HHS F31 GM140595NIGMS NIH HHS R01 GM121714NIGMS NIH HHS R35 GM139658
6 · The paper itself

Abstract

Characterization of protein glycosylation by tandem mass spectrometry remains challenging owing to the vast diversity of oligosaccharides bound to proteins, the variation in monosaccharide linkage patterns, and the lability of the linkage between the glycan and protein. Here, we have adapted an HCD-triggered-ultraviolet photodissociation (UVPD) approach for the simultaneous localization of glycosites and full characterization of both glycan compositions and intersaccharide linkages, the latter provided by extensive cross-ring cleavages enabled by UVPD. The method is applied to study glycan compositions based on analysis of glycopeptides from proteolytic digestion of recombinant human coronaviruse spike proteins from SARS-CoV-2 and HKU1. UVPD reveals unique intersaccharide linkage information and is leveraged to localize N-linked glycoforms with confidence.

Indexed as

COVID-19Viral ProteinsGlycosylationHumansPolysaccharidesSARS-CoV-2Spike Glycoprotein, CoronavirusTandem Mass SpectrometryUltraviolet RaysPolysaccharidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Viral Proteins

Identifiers

PMID35388686
PMCPMC9272412
OpenAlexW4224239452

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.