Evidence map›Paper›PMID 33087899›Full record

ReviewNature reviews. Molecular cell biology2020

Global view of human protein glycosylation pathways and functions.

Katrine T Schjoldager, Yoshiki Narimatsu, Hiren J Joshi, Henrik Clausen

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 701 papers.

0numbers the graph read from it
0cells of the map it votes in
701citing papers in PubMed
45.1field-weighted citation impact, top 1% 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

701 citing papers in PubMed, 1,238 citations in OpenAlex.

  1. Discovery of a secretedGut microbes · 2026
    Article
  2. Article
  3. Review
  4. Reading sugars cell by cell.Nature chemical biology · 2026
    Article
  5. Review
  6. Article
  7. Protein O-Glycosylation Shapes Lymphatic Endothelia and Lymph Node Macrophage Populations.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  8. Article
  9. Article
  10. Unraveling the Glycosylation Machinery ofInternational journal of molecular sciences · 2026
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. Article

641 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Katrine T SchjoldagerCenter for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.ORCID http://orcid.org/0000-0002-8592-6763
Yoshiki NarimatsuCenter for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.ORCID http://orcid.org/0000-0003-1428-5695
Hiren J JoshiCenter for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark. joshi@sund.ku.dk.ORCID http://orcid.org/0000-0002-8192-2829
Henrik ClausenCenter for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark. hclau@sund.ku.dk.ORCID http://orcid.org/0000-0002-0915-5055
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation is the most abundant and diverse form of post-translational modification of proteins that is common to all eukaryotic cells. Enzymatic glycosylation of proteins involves a complex metabolic network and different types of glycosylation pathways that orchestrate enormous amplification of the proteome in producing diversity of proteoforms and its biological functions. The tremendous structural diversity of glycans attached to proteins poses analytical challenges that limit exploration of specific functions of glycosylation. Major advances in quantitative transcriptomics, proteomics and nuclease-based gene editing are now opening new global ways to explore protein glycosylation through analysing and targeting enzymes involved in glycosylation processes. In silico models predicting cellular glycosylation capacities and glycosylation outcomes are emerging, and refined maps of the glycosylation pathways facilitate genetic approaches to address functions of the vast glycoproteome. These approaches apply commonly available cell biology tools, and we predict that use of (single-cell) transcriptomics, genetic screens, genetic engineering of cellular glycosylation capacities and custom design of glycoprotein therapeutics are advancements that will ignite wider integration of glycosylation in general cell biology.

Indexed as

Carbohydrate MetabolismGlycoproteinsGlycosylationHumansMetabolic Networks and PathwaysPolysaccharidesProtein Processing, Post-TranslationalProteomeGlycoproteinsPolysaccharidesProteome

Identifiers

PMID33087899
OpenAlexW3094407181

What Socratic 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 Socratic graph.