Evidence map›Paper›PMID 28644060›Full record

ReviewCritical reviews in biochemistry and molecular biology2017

Lytic transglycosylases: concinnity in concision of the bacterial cell wall.

David A Dik, Daniel R Marous, Jed F Fisher, Shahriar Mobashery

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
11.2field-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

108 citing papers in PubMed, 179 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structural Insights into MltC fromJournal of microbiology and biotechnology · 2026
    Article
  7. Review
  8. A Concise Route to Orthogonally Protected Bulgecinine.The Journal of organic chemistry · 2026
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. The interplay betweenInfection and immunity · 2025
    Article
  19. Article
  20. Article

48 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

4 authors at 1 institution in 1 country.

David A Dika Department of Chemistry and Biochemistry , University of Notre Dame , Notre Dame , IN , USA.ORCID 0000-0002-4700-3837
Daniel R Marousa Department of Chemistry and Biochemistry , University of Notre Dame , Notre Dame , IN , USA.
Jed F Fishera Department of Chemistry and Biochemistry , University of Notre Dame , Notre Dame , IN , USA.
Shahriar Mobasherya Department of Chemistry and Biochemistry , University of Notre Dame , Notre Dame , IN , USA.
University of Notre Dame · US

Funding

Penicillin-Binding Proteins, Mechanism and InhibitionR01GM061629 · NIGMS · WAYNE STATE UNIVERSITY · PI MOBASHERY, SHAHRIAR · 2001 to 2018
$5.1M
Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
NIGMS NIH HHS R01 GM061629NIGMS NIH HHS T32 GM075762
6 · The paper itself

Abstract

The lytic transglycosylases (LTs) are bacterial enzymes that catalyze the non-hydrolytic cleavage of the peptidoglycan structures of the bacterial cell wall. They are not catalysts of glycan synthesis as might be surmised from their name. Notwithstanding the seemingly mundane reaction catalyzed by the LTs, their lytic reactions serve bacteria for a series of astonishingly diverse purposes. These purposes include cell-wall synthesis, remodeling, and degradation; for the detection of cell-wall-acting antibiotics; for the expression of the mechanism of cell-wall-acting antibiotics; for the insertion of secretion systems and flagellar assemblies into the cell wall; as a virulence mechanism during infection by certain Gram-negative bacteria; and in the sporulation and germination of Gram-positive spores. Significant advances in the mechanistic understanding of each of these processes have coincided with the successive discovery of new LTs structures. In this review, we provide a systematic perspective on what is known on the structure-function correlations for the LTs, while simultaneously identifying numerous opportunities for the future study of these enigmatic enzymes.

Indexed as

BacteriaBacterial ProteinsCell WallGlycosyltransferasesPeptidoglycanBacterial ProteinsGlycosyltransferasesPeptidoglycanAmpCAmpRbacteriacell-wall recyclingLytic transglycosylasemuropeptidepeptidoglycansecretion system

Identifiers

PMID28644060
PMCPMC6102726
OpenAlexW2680788573

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.