Evidence map›Paper›PMID 28810664›Full record

ReviewGlycobiology2017

Bacterial phosphoglycosyl transferases: initiators of glycan biosynthesis at the membrane interface.

Vinita Lukose, Marthe T C Walvoort, Barbara Imperiali

Abstract readReview
In one paragraph

Review in Glycobiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Article
  2. Glycoconjugate diversification inbioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Proteome-wide bioinformatic annotation and functional validation of the monotopic phosphoglycosyl transferase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Microorganisms · 2024
    Article
  12. Three-component systems represent a common pathway for extracytoplasmic addition of pentofuranose sugars into bacterial glycans.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. A New Face of the Old Gene: Deletion of theInternational journal of molecular sciences · 2023
    Article
  19. Article
  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

3 authors.

Vinita LukoseDepartments of Chemistry and Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Marthe T C WalvoortStratingh Institute for Chemistry, University of Groningen, 9747 AG Groningen, The Netherlands.
Barbara ImperialiDepartments of Chemistry and Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

Funding

SPECIFICITY IN CO- AND POST-TRANSLATIONAL MODIFICATIONR01GM039334 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALLEN, KAREN N., IMPERIALI, BARBARA · 1993 to 2025
$8.0M
NIGMS NIH HHS R01 GM039334
6 · The paper itself

Abstract

Phosphoglycosyl transferases (PGTs) initiate the biosynthesis of both essential and virulence-associated bacterial glycoconjugates including lipopolysaccharide, peptidoglycan and glycoproteins. PGTs catalyze the transfer of a phosphosugar moiety from a nucleoside diphosphate sugar to a polyprenol phosphate, to form a membrane-bound polyprenol diphosphosugar product. PGTs are integral membrane proteins, which include between 1 and 11 predicted transmembrane domains. Despite this variation, common motifs have been identified in PGT families through bioinformatics and mutagenesis studies. Bacterial PGTs represent important antibacterial and virulence targets due to their significant role in initiating the biosynthesis of key bacterial glycoconjugates. Considerable effort has gone into mechanistic and inhibition studies for this class of enzymes, both of which depend on reliable, high-throughput assays for easy quantification of activity. This review summarizes recent advances made in the characterization of this challenging but important class of enzymes.

Indexed as

Gene Expression Regulation, BacterialCarbohydrate MetabolismCell MembraneConserved SequenceEnzyme InhibitorsEscherichia coliEscherichia coli ProteinsGlycoconjugatesHexosyltransferasesHigh-Throughput Screening AssaysKineticsProtein DomainsSubstrate SpecificityEnzyme InhibitorsEscherichia coli ProteinsGlycoconjugatesHexosyltransferasesglycan biosynthesismembrane proteinphosphoglycosyl transferase

Identifiers

PMID28810664
PMCPMC5881778

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.