Evidence map›Paper›PMID 31974163›Full record

ReviewThe Journal of biological chemistry2020

Uncovering the activities, biological roles, and regulation of bacterial cell wall hydrolases and tailoring enzymes.

Truc Do, Julia E Page, Suzanne Walker

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
13.3field-weighted citation impact, top 1% 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

66 citing papers in PubMed, 118 citations in OpenAlex.

  1. mBio · 2026
    Article
  2. Article
  3. Review
  4. bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Bacterial extracellular vesicles target different bacterial species, impairing cell division and diminishing their pathogenicity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Review

6 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

3 authors at 1 institution in 1 country.

Truc DoDepartment of Microbiology, Harvard Medical School, Boston, Massachusetts 02115.
Julia E PageDepartment of Microbiology, Harvard Medical School, Boston, Massachusetts 02115.
Suzanne WalkerDepartment of Microbiology, Harvard Medical School, Boston, Massachusetts 02115. Electronic address: suzanne_walker@hms.harvard.edu.
Harvard University · US

Funding

Medical Scientist Training ProgramT32GM007753 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WALENSKY, LOREN DAVID · 1985 to 2021
$50.0M
Mechanism and Inhibition of Enzymes that Assemble Bacterial Cell WallR01GM076710 · NIGMS · HARVARD MEDICAL SCHOOL · PI WALKER, SUZANNE · 2007 to 2019
$5.9M
Discovery and characterization of new bacterial cell wall targets and inhibitors to treat resistant infectionsR01AI148752 · NIAID · HARVARD MEDICAL SCHOOL · PI Daniel Kahne, Suzanne Walker · 2020 to 2026
$5.5M
NIAID NIH HHS R01 AI148752NIGMS NIH HHS R01 GM076710NIGMS NIH HHS T32 GM007753
6 · The paper itself

Abstract

Bacteria account for 1000-fold more biomass than humans. They vary widely in shape and size. The morphological diversity of bacteria is due largely to the different peptidoglycan-based cell wall structures that encase bacterial cells. Although the basic structure of peptidoglycan is highly conserved, consisting of long glycan strands that are cross-linked by short peptide chains, the mature cell wall is chemically diverse. Peptidoglycan hydrolases and cell wall-tailoring enzymes that regulate glycan strand length, the degree of cross-linking, and the addition of other modifications to peptidoglycan are central in determining the final architecture of the bacterial cell wall. Historically, it has been difficult to biochemically characterize these enzymes that act on peptidoglycan because suitable peptidoglycan substrates were inaccessible. In this review, we discuss fundamental aspects of bacterial cell wall synthesis, describe the regulation and diverse biochemical and functional activities of peptidoglycan hydrolases, and highlight recently developed methods to make and label defined peptidoglycan substrates. We also review how access to these substrates has now enabled biochemical studies that deepen our understanding of how bacterial cell wall enzymes cooperate to build a mature cell wall. Such improved understanding is critical to the development of new antibiotics that disrupt cell wall biogenesis, a process essential to the survival of bacteria.

Indexed as

BacteriaBacterial ProteinsCell WallN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanProtein Structure, TertiaryStaphylococcus aureusSubstrate SpecificityBacterial ProteinsN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanacetyltransferaseantibiotic developmentantibioticscell wall biochemistryhydrolaseLipid IILytR-CpsA-Psr ligasesO-acetyltransferasepeptidoglycanpeptidoglycan hydrolasepeptidoglycan hydrolase regulatorsteichoic acid

Identifiers

PMID31974163
PMCPMC7062177
OpenAlexW3001299653

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.