Evidence map›Paper›PMID 34138841›Full record

ArticlePLoS biology2021

Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea.

Stefan Schulze, Friedhelm Pfeiffer, Benjamin A Garcia, Mechthild Pohlschroder

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

20 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
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  7. Journal of bacteriology · 2025
    Review
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  9. Review
  10. Studying the long-term adaptation ofFrontiers in microbiology · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Viruses · 2022
    Article
  18. Article
  19. Review
  20. Article
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 at 2 institutions in 2 countries.

Stefan SchulzeDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America.ORCID 0000-0002-4771-7987
Friedhelm PfeifferComputational Biology Group, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0003-4691-3246
Benjamin A GarciaEpigenetics Institute, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America.
Mechthild PohlschroderDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America.ORCID 0000-0001-7729-1342
University of Pennsylvania · USMax Planck Institute of Biochemistry · DE

Funding

Shared Resources Core 2: Quantitative Proteomics CoreP01CA196539 · NCI · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2015 to 2024
$17.6M
Viral modulation of epitranscriptomic mechanismsR01AI118891 · NIAID · WASHINGTON UNIVERSITY · PI GARCIA, BENJAMIN A, WEITZMAN, MATTHEW D. · 2015 to 2025
$5.4M
NCI NIH HHS P01 CA196539NIAID NIH HHS R01 AI118891
6 · The paper itself

Abstract

Glycosylation is one of the most complex posttranslational protein modifications. Its importance has been established not only for eukaryotes but also for a variety of prokaryotic cellular processes, such as biofilm formation, motility, and mating. However, comprehensive glycoproteomic analyses are largely missing in prokaryotes. Here, we extend the phenotypic characterization of N-glycosylation pathway mutants in Haloferax volcanii and provide a detailed glycoproteome for this model archaeon through the mass spectrometric analysis of intact glycopeptides. Using in-depth glycoproteomic datasets generated for the wild-type (WT) and mutant strains as well as a reanalysis of datasets within the Archaeal Proteome Project (ArcPP), we identify the largest archaeal glycoproteome described so far. We further show that different N-glycosylation pathways can modify the same glycosites under the same culture conditions. The extent and complexity of the Hfx. volcanii N-glycoproteome revealed here provide new insights into the roles of N-glycosylation in archaeal cell biology.

Indexed as

Amino Acid SequenceArchaeal ProteinsBiological AssayCell ShapeDatabases, ProteinGlycopeptidesGlycoproteinsGlycosylationHaloferax volcaniiMutationPhenotypePhylogenyProteomicsSodium ChlorideArchaeal ProteinsGlycopeptidesGlycoproteinsSodium Chloride

Identifiers

PMID34138841
PMCPMC8241124
OpenAlexW3167093271

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.