Evidence map›Paper›PMID 38203699›Full record

ArticleInternational journal of molecular sciences2023

Cellular and Enzymatic Determinants Impacting the Exolytic Action of an Anti-Staphylococcal Enzybiotic.

Ana Gouveia, Daniela Pinto, Jorge M B Vítor, Carlos São-José

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Domain shuffling of endolysin LysKB317 to controlBiotechnology reports (Amsterdam, Netherlands) · 2026
    Article
  2. Article
  3. Article
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.

Ana GouveiaPhage Biology Research and Infection Control (PhaBRIC), Research Institute for Medicines (iMed.ULisboa), Faculdade de Farmácia, Universidade de Lisboa, Av. Prof. Gama Pinto, 1649-003 Lisboa, Portugal.ORCID 0000-0002-4989-6472
Daniela PintoPhage Biology Research and Infection Control (PhaBRIC), Research Institute for Medicines (iMed.ULisboa), Faculdade de Farmácia, Universidade de Lisboa, Av. Prof. Gama Pinto, 1649-003 Lisboa, Portugal.ORCID 0000-0002-2405-8755
Jorge M B VítorPathogen Genome Bioinformatics and Computational Biology, Research Institute for Medicines (iMed.ULisboa), Faculdade de Farmácia, Universidade de Lisboa, Av. Prof. Gama Pinto, 1649-003 Lisboa, Portugal.ORCID 0000-0001-6486-3444
Carlos São-JoséPhage Biology Research and Infection Control (PhaBRIC), Research Institute for Medicines (iMed.ULisboa), Faculdade de Farmácia, Universidade de Lisboa, Av. Prof. Gama Pinto, 1649-003 Lisboa, Portugal.ORCID 0000-0002-4890-9446
University of Lisbon · PT

Funding

FCT - Fundação para a Ciência e a Tecnologia, I.P. UIDB/04138/2020, UIDP/04138/2020, PTDC/EMD-EMD/28109/2017, 2020.05606.BD
6 · The paper itself

Abstract

Bacteriophage endolysins are bacteriolytic enzymes that have been explored as potential weapons to fight antibiotic-resistant bacteria. Despite several studies support the application of endolysins as enzybiotics, detailed knowledge on cellular and enzymatic factors affecting their lytic activity is still missing. The bacterial membrane proton motive force (PMF) and certain cell wall glycopolymers of Gram-positive bacteria have been implicated in some tolerance to endolysins. Here, we studied how the anti-staphylococcal endolysin Lys11, a modular enzyme with two catalytic domains (peptidase and amidase) and a cell binding domain (CBD

Indexed as

Peptide HydrolasesStaphylococcusAmidohydrolasesAnti-Bacterial AgentsBacteriolysisAmidohydrolasesAnti-Bacterial AgentsPeptide Hydrolasesantibiotic resistancecell wallendolysinenzybioticlysinmembrane potentialpeptidoglycan hydrolaseproton motive forceStaphylococcus aureuswall teichoic acids

Identifiers

PMID38203699
PMCPMC10778630
OpenAlexW4390467367

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.