S. C. Becker

发表

Chimeric Phage Lysins Act Synergistically with Lysostaphin To Kill Mastitis-Causing Staphylococcus aureus in Murine Mammary Glands

M. Schmelcher, D. Donovan, M. Camp, 2012, Applied and Environmental Microbiology.

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

N. Klyachko, D. Donovan, L. Filatova, 2010, Biochimie.

LysK CHAP endopeptidase domain is required for lysis of live staphylococcal cells.

D. Donovan, David M Donovan, J. Baker, 2009, FEMS microbiology letters.

Triple-acting Lytic Enzyme Treatment of Drug-Resistant and Intracellular Staphylococcus aureus

K. Doran, M. Schmelcher, I. Marriott, 2016, Scientific Reports.

Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain.

D. Donovan, J. Foster-Frey, Stephen C. Becker, 2009, Gene.

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

D. Donovan, J. Foster-Frey, S. C. Becker, 2008, FEMS microbiology letters.

Evolutionarily distinct bacteriophage endolysins featuring conserved peptidoglycan cleavage sites protect mice from MRSA infection.

M. Loessner, M. Schmelcher, M. Eugster, 2015, The Journal of antimicrobial chemotherapy.

Staphylococcal Phage 2638A endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain secondary translational start site

M. Schmelcher, D. Donovan, N. Shishkova, 2012, Applied Microbiology and Biotechnology.

Author ' s personal copy Differentially conserved staphylococcal SH 3 b _ 5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain

D. Donovan, J. Foster-Frey, Stephen C. Becker, 2009 .

Staphylococcal Phage 2638A endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain secondary translational start site

M. Schmelcher, D. Donovan, N. Shishkova, 2013, Applied Microbiology and Biotechnology.

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

N. Klyachko, D. Donovan, L. Filatova, 2016, Applied Biochemistry and Biotechnology.

An investigation of the structure and function of antistaphylococcal endolysins using kinetic methods

L. Filatova, N. Klyachko, A. Kabanov, 2014, Moscow University Chemistry Bulletin.

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

A. Kabanov, N. Klyachko, Dmitry Lebedev, 2013, Biochimie.

Lysostaphin: molecular changes that preserve staphylolytic activity

D. Kerr, D. Donovan, A. Powell, 2011 .

AntimicrobiALs Peptidoglycan hydrolase enzyme fusions for treating multi-drug resistant pathogens

J. Baker, S. Dong, D. Pritchard, 2022 .

Lytic activity of the staphylolytic Twort phage endolysin CHAP domain is enhanced by the SH3b cell wall binding domain.

D. Donovan, O. Korobova, Nina Schischkova, 2015, FEMS microbiology letters.

Functional characterization of the competence protein DprA/Smf in Escherichia coli.

C. Vandenbroucke-Grauls, W. Bitter, G. J. Barcak, 2006, FEMS microbiology letters.

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

N. Klyachko, D. Donovan, L. Filatova, 2010, Biochimie.