A Chimeric LysK-Lysostaphin Fusion Enzyme Lysing Staphylococcus aureus Cells: a Study of Both Kinetics of Inactivation and Specifics of Interaction with Anionic Polymers

Bacteriophage phi11 lysin: Physicochemical characterization and comparison with phage phi80α lysin

(2015) Lyubov Y. Filatova et al.   ENZYME AND MICROBIAL TECHNOLOGY

Physicochemical characterization of the staphylolytic LysK enzyme in complexes with polycationic polymers as a potent antimicrobial

(2013) Lyubov Y. Filatova et al.   BIOCHIMIE

The Phage Lytic Proteins from the Staphylococcus aureus Bacteriophage vB_SauS-phiIPLA88 Display Multiple Active Catalytic Domains and Do Not Trigger Staphylococcal Resistance

(2013) Lorena Rodríguez-Rubio et al.   PLoS One

Bacteriophage endolysins as novel antimicrobials

(2012) Mathias Schmelcher et al.   Future Microbiology

X-ray crystal structure of the streptococcal specific phage lysin PlyC

(2012) S. McGowan et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Lysostaphin-functionalized cellulose fibers with antistaphylococcal activity for wound healing applications

(2011) Jianjun Miao et al.   BIOMATERIALS

Water Soluble Polymers for Pharmaceutical Applications

(2011) Veeran Gowda Kadajji et al.   Polymers

LysK, the enzyme lysing Staphylococcus aureus cells: Specific kinetic features and approaches towards stabilization

(2010) Lyubov Yu. Filatova et al.   BIOCHIMIE

Phage Lysin LysK Can Be Truncated to Its CHAP Domain and Retain Lytic Activity against Live Antibiotic-Resistant Staphylococci

(2008) M. Horgan et al.   APPLIED AND ENVIRONMENTAL MICROBIOLOGY

The phage K lytic enzyme LysK and lysostaphin act synergistically to kill MRSA

(2008) Stephen C. Becker et al.   FEMS MICROBIOLOGY LETTERS