Evidence map›Paper›PMID 31597040›Full record

ArticleACS infectious diseases2019

Phylogenetic and Biochemical Analyses of Mycobacterial l,d-Transpeptidases Reveal a Distinct Enzyme Class That Is Preferentially Acylated by Meropenem.

Trevor A Zandi, Robert L Marshburn, Paige K Stateler, Leighanne A Brammer Basta

Abstract readLetter
In one paragraph

Article in ACS infectious diseases, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Activity Profiling of Mycobacterial L,D-Transpeptidases.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Peptidoglycan LD-Transpeptidases.Antibiotics (Basel, Switzerland) · 2025
    Review
  5. Oral β-lactam combinations are effectiveMicrobiology spectrum · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Competing off-loading mechanisms of meropenem from an l,d-transpeptidase reduce antibiotic effectiveness.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Frontiers in immunology · 2021
    Article
  15. Article
  16. Article
  17. 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

4 authors at 2 institutions in 1 country.

Trevor A ZandiDepartment of Biophysics , Johns Hopkins University , 3400 N. Charles Street , Baltimore , Maryland 21218 , United States.
Robert L MarshburnChemistry Department , United States Naval Academy , 572M Holloway Road , Annapolis , Maryland 21402 , United States.
Paige K StatelerChemistry Department , United States Naval Academy , 572M Holloway Road , Annapolis , Maryland 21402 , United States.
Leighanne A Brammer BastaChemistry Department , United States Naval Academy , 572M Holloway Road , Annapolis , Maryland 21402 , United States.ORCID 0000-0002-4121-5505
United States Naval Academy · USJohns Hopkins University · US

Funding

PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Program of Molecular BiophysicsT32GM135131 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Karen G. Fleming · 2020 to 2026
$5.4M
Development of novel penems for drug-resistant tuberculosisR01AI137329 · NIAID · JOHNS HOPKINS UNIVERSITY · PI NUERMBERGER, ERIC L, TOWNSEND, CRAIG ARTHUR · 2018 to 2022
$3.9M
NIAID NIH HHS R01 AI137329NIGMS NIH HHS T32 GM008403NIGMS NIH HHS T32 GM135131
6 · The paper itself

Abstract

The genomes of diverse mycobacterial species encode multiple proteins with the canonical l,d-transpeptidase (Ldt) sequence motif. The reason for this apparent redundancy is not well understood, but evidence suggests paralogous Ldts may serve niche roles in maintaining and/or remodeling mycobacterial peptidoglycan. We examined 323 mycobacterial Ldts and determined these enzymes cluster into six clades. We identified a variably represented yet distinct Ldt class (class 6) containing

Indexed as

AcylationAmino Acid MotifsAnti-Bacterial AgentsCatalytic DomainEvolution, MolecularMeropenemModels, MolecularMultigene FamilyMycobacteriumPeptidyl TransferasesPhylogenySequence Homology, Amino AcidAnti-Bacterial AgentsMeropenemPeptidyl TransferasescarbapenemLdtl,d-transpeptidaseMycobacterium smegmatisMycobacterium tuberculosispeptidoglycan

Identifiers

PMID31597040
PMCPMC6910976
OpenAlexW2979699655

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.