Evidence map›Paper›PMID 8626282›Full record

ArticleJournal of bacteriology1996

An autolysin ring associated with cell separation of Staphylococcus aureus.

S Yamada, M Sugai, H Komatsuzawa, S Nakashima, T Oshida, A Matsumoto, H Suginaka

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 1996. 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
3.3field-weighted citation impact, top 7% 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, 203 citations in OpenAlex.

  1. Article
  2. A novel polysaccharide in the envelope ofJournal of bacteriology · 2025
    Article
  3. Article
  4. Autolysin-mediated peptidoglycan hydrolysis is required for the surface display ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Review
  6. Review
  7. Inhibition ofMicrobiology (Reading, England) · 2022
    Article
  8. Article
  9. Non-deacetylated poly-Frontiers in microbiology · 2022
    Article
  10. Understanding tolerance to cell wall-active antibiotics.Annals of the New York Academy of Sciences · 2021
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. 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

7 authors at 1 institution in 1 country.

S YamadaDepartment of Microbiology, Kawasaki Medical School, Okayama, Japan.
M Sugai
H Komatsuzawa
S Nakashima
T Oshida
A Matsumoto
H Suginaka
Kawasaki Medical School · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

atl is a newly discovered autolysin gene in Staphylococcus aureus. The gene product, ATL, is a unique, bifunctional protein that has an amidase domain and a glucosaminidase domain. It undergoes proteolytic processing to generate two extracellular peptidoglycan hydrolases, a 59-kDa endo-beta-N-acetylglucosaminidase and a 62-kDa N-acetylmuramyl-L-alanine amidase. It has been suggested that these enzymes are involved in the separation of daughter cells after cell division. We recently demonstrated that atl gene products are cell associated (unpublished data). The cell surface localization of the atl gene products was investigated by immunoelectron microscopy using anti-62-kDa N-acetylmuramyl-L-alanine amidase or anti-51-kDa endo-beta-N-acetylglucosaminidase immunoglobulin G. Protein A-gold particles reacting with the antigen-antibody complex were found to form a ring structure on the cell surface at the septal region for the next cell division site. Electron microscopic examination of an ultrathin section of the preembedded sample revealed preferential distribution of the gold particles at the presumptive sites for cell separation where the new septa had not been completed. The distribution of the gold particles on the surface of protoplast cells and the association of the gold particles with fibrous materials extending from the cells suggested that some atl gene products were associated with a cellular component extending from the cell membrane, such as lipoteichoic acid. The formation of a ring structure of atl gene products may be required for efficient partitioning of daughter cells after cell division.

Indexed as

Cell CompartmentationAcetylglucosaminidaseCell DivisionGoldMicroscopy, ImmunoelectronModels, BiologicalN-Acetylmuramoyl-L-alanine AmidaseStaphylococcus aureusAcetylglucosaminidaseGoldN-Acetylmuramoyl-L-alanine Amidase

Identifiers

PMID8626282
PMCPMC177839
OpenAlexW2168611643

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.