Evidence map›Paper›PMID 12824488›Full record

ArticleProtein science : a publication of the Protein Society2003

Three monophyletic superfamilies account for the majority of the known glycosyltransferases.

Jing Liu, Arcady Mushegian

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

96 citing papers in PubMed, 232 citations in OpenAlex.

  1. From a single C-mannose to multiple C-mannosyltransferases.The Journal of biological chemistry · 2026
    Review
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  5. 3-D substructure search by transitive closure in AlphaFold database.Protein science : a publication of the Protein Society · 2025
    Article
  6. O-Glycosyltransferase GenePlants (Basel, Switzerland) · 2024
    Article
  7. Article
  8. Structure of the priming arabinosyltransferase AftA required for AG biosynthesis ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Article
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  15. Review
  16. Large Clostridial Toxins: Mechanisms and Roles in Disease.Microbiology and molecular biology reviews : MMBR · 2021
    Review
  17. Review
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  19. Review
  20. Article

36 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

2 authors at 1 institution in 1 country.

Jing LiuStowers Institute for Medical Research, 1000 E. 50th Street, Kansas City, MO 64110, USA.
Arcady Mushegian
Stowers Institute for Medical Research · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sixty-five families of glycosyltransferases (EC 2.4.x.y) have been recognized on the basis of high-sequence similarity to a founding member with experimentally demonstrated enzymatic activity. Although distant sequence relationships between some of these families have been reported, the natural history of glycosyltransferases is poorly understood. We used iterative searches of sequence databases, motif extraction, structural comparison, and analysis of completely sequenced genomes to track the origins of modern-type glycosyltransferases. We show that >75% of recognized glycosyltransferase families belong to one of only three monophyletic superfamilies of proteins, namely, (1) a recently described GPGTF/GT-B superfamily; (2) a nucleoside-diphosphosugar transferase (GT-A) superfamily, which is characterized by a DxD sequence signature and also includes nucleotidyltransferases; and (3) a GT-C superfamily of integral membrane glycosyltransferases with a modified DxD signature in the first extracellular loop. Several developmental regulators in Metazoans, including Fringe and Egghead homologs, belong to the second superfamily. Interestingly, Tout-velu/Exostosin family of developmental proteins found in all multicellular eukaryotes, contains separate domains belonging to the first and the second superfamilies, explaining multiple glycosyltransferase activities in one protein.

Indexed as

Multigene FamilyAmino Acid SequenceConserved SequenceDatabases, ProteinEvolution, MolecularGlycosyltransferasesMolecular Sequence DataNucleotidyltransferasesPhylogenyProtein FoldingProtein Structure, SecondarySequence AlignmentStatistics as TopicGlycosyltransferasesNucleotidyltransferases

Identifiers

PMID12824488
PMCPMC2323934
OpenAlexW2095529535

What OpenQuestion 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 OpenQuestion graph.