Evidence map›Paper›PMID 20017480›Full record

ArticleJournal of the American Chemical Society2010

The role of the substrate lipid in processive glycan polymerization by the peptidoglycan glycosyltransferases.

Deborah L Perlstein, Tsung-Shing Andrew Wang, Emma H Doud, Daniel Kahne, Suzanne Walker

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

26 citing papers in PubMed, 53 citations in OpenAlex.

  1. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Activities and regulation of peptidoglycan synthases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. The molecular origins of chiral growth in walled cells.Current opinion in microbiology · 2012
    Review
  18. 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

5 authors at 1 institution in 1 country.

Deborah L PerlsteinDepartment of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
Tsung-Shing Andrew Wang
Emma H Doud
Daniel Kahne
Suzanne Walker
Harvard University · US

Funding

Mechanism and Inhibition of Enzymes that Assemble Bacterial Cell WallR01GM076710 · NIGMS · HARVARD MEDICAL SCHOOL · PI WALKER, SUZANNE · 2007 to 2019
$5.9M
Finding the overlookes transglycosylases in cell wall biosynthesisF32GM078845 · NIGMS · HARVARD MEDICAL SCHOOL · PI PERLSTEIN, DEBORAH L · 2007 to 2008
$96k
NIGMS NIH HHS F32 GM078845NIGMS NIH HHS GM076710NIGMS NIH HHS R01 GM076710
6 · The paper itself

Abstract

The peptidoglycan glycosyltransferases (PGTs) catalyze the processive polymerization of a C55 lipid-linked disaccharide (Lipid II) to form peptidoglycan, the main component of the bacterial cell wall. Our ability to understand this reaction has been limited due to challenges identifying the appropriate substrate analogues to selectively interrogate the donor (the elongating strand) and acceptor (Lipid II) sites. To address this problem, we have developed an assay using synthetic substrates that can discriminate between the donor and acceptor sites of the PGTs. We have shown that each site has a distinct lipid length preference. We have also established that processive polymerization depends on the length of the lipid attached to the donor.

Indexed as

Lipid MetabolismAquifoliaceaeElectrophoresis, Polyacrylamide GelLipidsPeptidoglycan GlycosyltransferasePolymersPolysaccharidesLipidsPeptidoglycan GlycosyltransferasePolymersPolysaccharides

Identifiers

PMID20017480
PMCPMC2830065
OpenAlexW2057006564

What OpenQuestion holds

Textmetadata
LicenceTDM
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.