- ORCID iD
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0000-0002-6856-5863
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From design to function : an automation-enabled pipeline for the development of precision lysin therapeutics
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- Journal Article
- A1
- open access
Diversity, structure-function relationships and evolution of cell wall-binding domains of staphylococcal phage endolysins
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PhaLP 2.0 : a community-oriented database and portal for phage lysin research with new tailored computational tools and metagenomic data
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‘Exquisite specificity’, if the context allows : endolysin evolution is a contingent outcome of phage-host molecular landscapes
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Dissecting the unknown specificity of cell wall-binding domains of phage endolysins
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Lessons learned from a systematic structural-functional characterization of cell wall binding domains (CBDs) from phage endolysins
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- Journal Article
- A1
- open access
You get what you test for : the killing effect of phage lysins is highly dependent on buffer tonicity and ionic strength
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Structural and functional diversity of staphylococcal cell wall binding domains
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Structural and functional diversity of cell wall binding domains in staphylococcal endolysins
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Exploring PhaLP, an open source portal for Phage Lytic Proteins, to engineer modular enzybiotics against vancomycin-resistant Enterococcus faecalis