ArticleACS infectious diseases2023
Understanding the Molecular Basis for Homodimer Formation of the Pneumococcal Endolysin Cpl-1.
Article in ACS infectious diseases, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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.
The trial behind it
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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- Enzymatic property and stabilization mechanism of LysBT1, a novel polyextremotolerant endolysin with a C-terminal S-layer homology domain.Applied and environmental microbiology · 2025Article
- Agents Targeting the Bacterial Cell Wall as Tools to Combat Gram-Positive Pathogens.Molecules (Basel, Switzerland) · 2024Review
- Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
The rise of multi-drug-resistant bacteria that cannot be treated with traditional antibiotics has prompted the search for alternatives to combat bacterial infections. Endolysins, which are bacteriophage-derived peptidoglycan hydrolases, are attractive tools in this fight. Several studies have already demonstrated the efficacy of endolysins in targeting bacterial infections. Endolysins encoded by bacteriophages that infect Gram-positive bacteria typically possess an N-terminal catalytic domain and a C-terminal cell-wall binding domain (CWBD). In this study, we have uncovered the molecular mechanisms that underlie formation of a homodimer of Cpl-1, an endolysin that targets
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