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Staphylococcal Phage 2638A endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain secondary translational start site.
- Published in:
- Applied Microbiology & Biotechnology, 2013, v. 97, n. 8, p. 3449, doi. 10.1007/s00253-012-4252-4
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- Article
Triple-acting Lytic Enzyme Treatment of Drug-Resistant and Intracellular Staphylococcus aureus.
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- Scientific Reports, 2016, p. 25063, doi. 10.1038/srep25063
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- Article
Optimized production of a biologically active Clostridium perfringens glycosyl hydrolase phage endolysin PlyCP41 in plants using virus-based systemic expression.
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- BMC Biotechnology, 2019, v. 19, n. 1, p. 1, doi. 10.1186/s12896-019-0594-7
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- Article
Resolving the database sequence discrepancies for the Staphylococcus aureus bacteriophage φ11 amidase.
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- Journal of Basic Microbiology, 2008, v. 48, n. 1, p. 48, doi. 10.1002/jobm.200700179
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- Article
A Chimeric LysK-Lysostaphin Fusion Enzyme Lysing Staphylococcus aureus Cells: a Study of Both Kinetics of Inactivation and Specifics of Interaction with Anionic Polymers.
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- Applied Biochemistry & Biotechnology, 2016, v. 180, n. 3, p. 544, doi. 10.1007/s12010-016-2115-7
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- Article
Evolutionarily distinct bacteriophage endolysins featuring conserved peptidoglycan cleavage sites protect mice from MRSA infection.
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- Journal of Antimicrobial Chemotherapy (JAC), 2015, v. 70, n. 5, p. 1453, doi. 10.1093/jac/dku552
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- Article