Evidence map›Paper›PMID 35945033›Full record

ArticleRapid communications in mass spectrometry : RCM2022

PNGase H + variant from Rudaea cellulosilytica with improved deglycosylation efficiency for rapid analysis of eukaryotic N-glycans and hydrogen deuterium exchange mass spectrometry analysis of glycoproteins.

Rui-Rui Guo, Tian-Chan Zhang, Thomas Ole Tandrup Lambert, Ting Wang, Josef Voglmeir, Kasper D Rand, Li Liu

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Rapid communications in mass spectrometry : RCM, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

5 citing papers in PubMed, 13 citations in OpenAlex.

  1. PNGaseL fromRoyal Society open science · 2025
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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 2 countries.

Rui-Rui GuoGlycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, China.
Tian-Chan ZhangGlycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, China.
Thomas Ole Tandrup LambertProtein Analysis Group, Department of Pharmacy, University of Copenhagen, Copenhagen, Denmark.
Ting WangGlycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, China.
Josef VoglmeirGlycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, China.ORCID https://orcid.org/0000-0002-4096-4926
Kasper D RandProtein Analysis Group, Department of Pharmacy, University of Copenhagen, Copenhagen, Denmark.ORCID https://orcid.org/0000-0002-6337-5489
Li LiuGlycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, China.ORCID https://orcid.org/0000-0002-2178-9237
Nanjing Agricultural University · CNUniversity of Copenhagen · DK

Funding

100 Foreign Talents Plan JSB2014012H2020 European Research Council 101003052National Natural Science Foundation of China 31471703National Natural Science Foundation of China 31671854National Natural Science Foundation of China 31871754National Natural Science Foundation of China 31871793
6 · The paper itself

Abstract

The analysis of glycoproteins and the comparison of protein N-glycosylation from different eukaryotic origins require unbiased and robust analytical workflows. The structural and functional analysis of vertebrate protein N-glycosylation currently depends extensively on bacterial peptide-N4-(N-acetyl-β-glucosaminyl) asparagine amidases (PNGases), which are indispensable enzymatic tools in releasing asparagine-linked oligosaccharides (N-glycans) from glycoproteins. So far, only limited PNGase candidates are available for N-glycans analysis, and particularly the analysis of plant and invertebrate N-glycans is hampered by the lack of suitable PNGases. Furthermore, liquid chromatography-mass spectrometry (LC-MS) workflows, such as hydrogen deuterium exchange mass spectrometry (HDX-MS), require a highly efficient enzymatic release of N-glycans at low pH values to facilitate the comprehensive structural analysis of glycoproteins. Herein, we describe a previously unstudied superacidic bacterial N-glycanase (PNGase H

Indexed as

AsparagineHydrogen Deuterium Exchange-Mass SpectrometryAmidohydrolasesAnimalsDeuterium Exchange MeasurementDisulfidesEukaryotaGammaproteobacteriaGlycoproteinsHorseradish PeroxidaseLactoferrinMiceOligosaccharidesPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidasePolysaccharidesSoilAmidohydrolasesAsparagineDisulfidesGlycoproteinsHorseradish PeroxidaseLactoferrinOligosaccharidesPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidasePolysaccharidesSoil

Identifiers

PMID35945033
PMCPMC9541014
OpenAlexW4292458069

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.