Evidence map›Paper›PMID 30237166›Full record

ArticleThe Journal of biological chemistry2018

A partial reconstitution implicates DltD in catalyzing lipoteichoic acid d-alanylation.

B McKay Wood, John P Santa Maria, Leigh M Matano, Christopher R Vickery, Suzanne Walker

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

37 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. ThemBio · 2025
    Article
  4. Article
  5. D-Serine Can Modify the Wall Teichoic Acid of MRSA via theInternational journal of molecular sciences · 2025
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Deletion ofFrontiers in cellular and infection microbiology · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  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.

B McKay WoodFrom the Department of Microbiology, Harvard Medical School, Boston, Massachusetts 02115.
John P Santa MariaFrom the Department of Microbiology, Harvard Medical School, Boston, Massachusetts 02115.
Leigh M MatanoFrom the Department of Microbiology, Harvard Medical School, Boston, Massachusetts 02115.
Christopher R VickeryFrom the Department of Microbiology, Harvard Medical School, Boston, Massachusetts 02115.
Suzanne WalkerFrom the Department of Microbiology, Harvard Medical School, Boston, Massachusetts 02115. Electronic address: suzanne_walker@hms.harvard.edu.
Harvard University · US

Funding

Technical Mother Machine CoreP01AI083214 · NIAID · SCHEPENS EYE RESEARCH INSTITUTE · PI Michael S Gilmore · 2009 to 2026
$39.4M
Identifying and validating new antibiotic targets in cell wall synthesis pathwaysR01AI099144 · NIAID · HARVARD MEDICAL SCHOOL · PI BERNHARDT, THOMAS G, WALKER, SUZANNE · 2012 to 2016
$4.3M
Molecular Basis for Activity by Membrane Bound O-AcyltransferasesR21AI119892 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI MARMORSTEIN, RONEN · 2016 to 2017
$465k
NIAID NIH HHS P01 AI083214NIAID NIH HHS R01 AI099144NIAID NIH HHS R21 AI119892
6 · The paper itself

Abstract

Modifications to the Gram-positive bacterial cell wall play important roles in antibiotic resistance and pathogenesis, but the pathway for the d-alanylation of teichoic acids (DLT pathway), a ubiquitous modification, is poorly understood. The d-alanylation machinery includes two membrane proteins of unclear function, DltB and DltD, which are somehow involved in transfer of d-alanine from a carrier protein inside the cell to teichoic acids on the cell surface. Here, we probed the role of DltD in the human pathogen

Indexed as

AlanineAmino Acid SubstitutionBacterial ProteinsCarbon-Oxygen LigasesCarrier ProteinsEnzyme AssaysHistidineKineticsLipopolysaccharidesMembrane Transport ProteinsMutagenesis, Site-DirectedMutationSerineStaphylococcus aureusTeichoic AcidsThiolester HydrolasesAlaninealanyl-lipoteichoic acidBacterial ProteinsCarbon-Oxygen LigasesCarrier ProteinsD-alanyl carrier protein, bacteriaDltB protein, StaphylococcusDltD protein, bacteriaHistidineLipopolysaccharideslipoteichoic acidMembrane Transport ProteinsSerineTeichoic AcidsThiolester Hydrolasesacyltransferasecell wallDltBDLT pathwayMBOATmembrane proteinpathway reconstitutionStaphylococcus aureus (S. aureus)teichoic acid

Identifiers

PMID30237166
PMCPMC6240853
OpenAlexW2890948890

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.