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United States Department of Agriculture

Agricultural Research Service

Stephen Charles Becker
Animal Biosciences and Biotechnology Laboratory
Biological Science Lab Technician

Phone: n/a
Room 124

BLDG 230 BARC-EAST
10300 BALTIMORE AVENUE
BELTSVILLE, MD, 20705


Publications (Clicking on the reprint icon Reprint Icon will take you to the publication reprint.)
Triple-acting antimicrobial treatment for drug-resistant and intracellular Staphylococcus aureus. - (Abstract Only) - (21-May-14)
Triple-acting antimicrobial treatment for drug-resistant and intracellular Staphylococcus aureus - (Abstract Only) - (28-Apr-14)
Sperm-mediated transgenesis in chicken using a PiggyBac transposon system - (Abstract Only) - (11-Apr-14)
Triple-acting antimicrobial treatment for drug-resistant and intracellular Staphylococcus aureus - (Abstract Only) - (01-Apr-14)
Sperm-mediated transgenesis in chicken using a PiggyBac transposon system - (Abstract Only) - (20-Mar-14)
Triple-acting Peptidoglycan hydrolase treatment for drug-resistant and intracellular Staphylococcus aureus - (Abstract Only) - (18-Mar-14)
An investigation of the structure and function of antistaphylococcal endolysins using kinetic methods - (Other)
Filatova, L., Donovan, D.M., Becker, S.C., Kabanov, A., Klyachko, N.L. 2014. An investigation of the structure and function of antistaphylococcal endolysins using kinetic methods. Moscow University Chemistry Bulletin. Vol. 69, No.3, pp.107-111.
Staphylococcal phage 2638a endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain cryptic translational start site. - (Peer Reviewed Journal)
Abaev, I., Foster Frey, J.A., Korobova, O., Shishkova, N., Kopylov, P., Pyramchuk, S., Schmelcher, M., Becker, S.C., Donovan, D.M. 2013. Staphylococcal phage 2638a endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain cryptic translational start site. Applied and Environmental Microbiology. 97(8):3449-3456.
Chimeric phage lysins act synergistically with lysostaphin to kill mastitis causing staphylococcus aureus in murine mammary glands - (Peer Reviewed Journal)
Schmelcher, M., Powell, A.M., Becker, S.C., Camp, M.J., Donovan, D.M. 2012. Chimeric phage lysins act synergistically with lysostaphin to kill mastitis causing staphylococcus aureus in murine mammary glands. Applied and Environmental Microbiology. 78(7):2297-305.
Lysostaphin: molecular changes that preserve staphylolytic activity. - (Proceedings) - (20-Feb-11)
LysK, the enzyme lysing Staphylococcus aureus cells: specific kinetic features and approaches towards stabilization - (Review Article)
Filatova, L.Y., Becker, S.C., Donovan, D.M., Gladilin, A.K., Klyachko, N.L. 2010. LysK, the enzyme lysing Staphylococcus aureus cells: specific kinetic features and approaches towards stabilization. Biochimie. 92(5):507-13.
Engineering Antimicrobials Refractory to Resistance - (Abstract Only)
Becker, S.C., Pohl, C.S., Mohammadi, H., Schmelcher, M., Foster Frey, J.A., Lease, R.A., Don, S., Baker, J.R., Pritchard, D.G., Donovan, D.M. 2009. Engineering Antimicrobials Refractory to Resistance. Evergreen International Phage Meeting.
Peptidoglycan hydrolase fusion to protein transduction domains kill intracellular staphylococci. - (Abstract Only)
Becker, S.C., Foster Frey, J.A., Willard, R.R., Lease, R.A., Almeida, R., Marriott, I., Dong, S., Baker, J.R., Pritchard, D.G., Donovan, D.M. 2009. Peptidoglycan hydrolase fusion to protein transduction domains kill intracellular staphylococci. Evergreen International Phage Meeting.
Peptidoglycan Hydrolases for Control of Mastitis Pathogens - (Abstract Only)
Schmelcher, M., Becker, S.C., Foster Frey, J.A., Donovan, D.M. 2009. Peptidoglycan Hydrolases for Control of Mastitis Pathogens. Evergreen International Phage Meeting.
Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain. - (Peer Reviewed Journal)
Becker, S.C., Foster-Frey, J., Stodola, A.J., Anacker, D., Donovan, D.M., 2009. Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer identical staphylolytic activity to a streptococcal prophage endolysin lytic domain. FEMS Immunology and Medical Microbiology. 443(1-2):32-41.
Antimicrobials for staphylococcal pathogens that are refractory to resistance development - (Abstract Only)
Becker, S.C., Foster Frey, J.A., Willard, R.R., Lease, R.A., Almeida, R., Marriott, I., Dong, S., Pritchard, D.G., Donovan, D.M. 2009. Antimicrobials for staphylococcal pathogens that are refractory to resistance development. International Symposium on Antimicrobial Peptides.
Antimicrobials for mastitis causing pathogens that are refractory to resistance development - (Abstract Only)
Becker, S.C., Don, S., Baker, J.R., Foster Frey, J.A., Pritchard, D.G., Donovan, D.M. 2009. Antimicrobials for mastitis causing pathogens that are refractory to resistance development. BARC Poster Day.
Peptidoglycan hydrolase enzyme fusions are uniquely suited for treating multi-drug resistant pathogens - (Review Article)
Donovan, D.M., Becker, S.C., Dong, S., Baker, J.R., Foster Frey, J.A., Pritchard, D.G. 2009. Peptidoglycan hydrolase enzyme fusions are uniquely suited for treating multi-drug resistant pathogens. Biotech International 21(2):6-10.
LysK CHAP endopeptidase domain is required for lysis of live staphylococcal cells. - (Peer Reviewed Journal)
Becker, S.C., Don, S., Baker, J.R., Foster Frey, J.A., Pritchard, D.G., Donovan, D.M. 2009. LysK CHAP endopeptidase domain is required for lysis of live staphylococcal cells. FEMS Microbiology Letter. 294(1):52-60.
SH3b Cell wall binding domains can enhance anti-staphylococcal activity of endolysin lytic domains. - (Abstract Only) - (10-Jul-08)
Engineering Antimicrobials that are Refractory to Resistance Development. - (Abstract Only)
Donovan, D.M., Becker, S.C. 2009. Engineering Antimicrobials that are Refractory to Resistance Development. Meeting Abstract.
Engineering MRSA antimicrobials that are refractory to resistance development - (Abstract Only)
Becker, S.C., Donovan, D.M., Foster Frey, J.A. 2008. Engineering MRSA antimicrobials that are refractory to resistance development. BARC Poster Day.
Last Modified: 11/20/2014
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