Evidence map›Paper›PMID 30958118›Full record

ReviewOpen biology2019

Structures and functions of invertebrate glycosylation.

Feifei Zhu, Dong Li, Keping Chen

Abstract readReview
In one paragraph

Review in Open biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Novel Lectins fromACS omega · 2025
    Article
  2. Ly6CCell reports · 2024
    Article
  3. Article
  4. Article
  5. In Silico Analysis of aPathogens (Basel, Switzerland) · 2023
    Article
  6. Article
  7. Article
  8. Review
  9. Frontiers in cellular and infection microbiology · 2022
    Article
  10. Article
  11. Expanding the Chondroitin Sulfate Glycoproteome - But How Far?Frontiers in cell and developmental biology · 2021
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Global Transcription Profiles ofFrontiers in veterinary science · 2020
    Article
  18. 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

3 authors.

Feifei Zhu1 Institute of Life Sciences, Jiangsu University , Zhenjiang 212013 , People's Republic of China.
Dong Li1 Institute of Life Sciences, Jiangsu University , Zhenjiang 212013 , People's Republic of China.
Keping Chen1 Institute of Life Sciences, Jiangsu University , Zhenjiang 212013 , People's Republic of China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation refers to the covalent attachment of sugar residues to a protein or lipid, and the biological importance of this modification has been widely recognized. While glycosylation in mammals is being extensively investigated, lower level animals such as invertebrates have not been adequately interrogated for their glycosylation. The rich diversity of invertebrate species, the increased database of sequenced invertebrate genomes and the time and cost efficiency of raising and experimenting on these species have enabled a handful of the species to become excellent model organisms, which have been successfully used as tools for probing various biologically interesting problems. Investigation on invertebrate glycosylation, especially on model organisms, not only expands the structural and functional knowledgebase, but also can facilitate deeper understanding on the biological functions of glycosylation in higher organisms. Here, we reviewed the research advances in invertebrate glycosylation, including N- and O-glycosylation, glycosphingolipids and glycosaminoglycans. The aspects of glycan biosynthesis, structures and functions are discussed, with a focus on the model organisms Drosophila and Caenorhabditis. Analytical strategies for the glycans and glycoconjugates are also summarized.

Indexed as

AnimalsCaenorhabditis elegansDrosophila melanogasterGlycoconjugatesGlycosaminoglycansGlycosphingolipidsGlycosylationInvertebratesPolysaccharidesSpecies SpecificityGlycoconjugatesGlycosaminoglycansGlycosphingolipidsPolysaccharidesglycan profilingglycoconjugatesglycosylationinvertebratestructure and function

Identifiers

PMID30958118
PMCPMC6367135

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.