Evidence map›Paper›PMID 23030422›Full record

ReviewFuture microbiology2012

Bacteriophage endolysins as novel antimicrobials.

Mathias Schmelcher, David M Donovan, Martin J Loessner

Open access · greenAbstract readReview
In one paragraph

Review in Future microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 430 papers.

0numbers the graph read from it
0cells of the map it votes in
430citing papers in PubMed
22.1field-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

430 citing papers in PubMed, 776 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Domain shuffling of endolysin LysKB317 to controlBiotechnology reports (Amsterdam, Netherlands) · 2026
    Article
  6. Article
  7. Phage as a prospective arsenal against superbugs.Molecular biology reports · 2026
    Review
  8. Review
  9. Article
  10. Recombinant Expression and Activity Analysis of aCurrent issues in molecular biology · 2026
    Article
  11. Article
  12. Review
  13. Review
  14. Enhancing the Antibacterial Activity of Endolysin againstJournal of microbiology and biotechnology · 2026
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Review

370 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 2 institutions in 2 countries.

Mathias SchmelcherInstitute of Food, Nutrition & Health, ETH Zurich, Schmelzbergstrasse 7, 8092 Zurich, Switzerland.
David M Donovan
Martin J Loessner
ETH Zurich · CHAgricultural Research Service · US

Funding

Triple action chimera: eradication of nasal S. aureus by cell wall hydrolasesR01AI075077 · NIAID · U.S. AGRICULTURAL RESEARCH CENTER · PI DONOVAN, DAVID MATTHEW · 2008 to 2010
$697k
NIAID NIH HHS 1R01AI075077-01A1NIAID NIH HHS R01 AI075077
6 · The paper itself

Abstract

Endolysins are enzymes used by bacteriophages at the end of their replication cycle to degrade the peptidoglycan of the bacterial host from within, resulting in cell lysis and release of progeny virions. Due to the absence of an outer membrane in the Gram-positive bacterial cell wall, endolysins can access the peptidoglycan and destroy these organisms when applied externally, making them interesting antimicrobial candidates, particularly in light of increasing bacterial drug resistance. This article reviews the modular structure of these enzymes, in which cell wall binding and catalytic functions are separated, as well as their mechanism of action, lytic activity and potential as antimicrobials. It particularly focuses on molecular engineering as a means of optimizing endolysins for specific applications, highlights new developments that may render these proteins active against Gram-negative and intracellular pathogens and summarizes the most recent applications of endolysins in the fields of medicine, food safety, agriculture and biotechnology.

Indexed as

Anti-Infective AgentsBacteriophagesBinding SitesBiological ProductsEndopeptidasesGenetic EngineeringAnti-Infective AgentsBiological ProductsendolysinEndopeptidases

Identifiers

PMID23030422
PMCPMC3563964
OpenAlexW2153843103

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.