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United States Department of Agriculture

Agricultural Research Service

Related Topics

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

Phone:
Fax:
Room 124

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


Publications (Clicking on the reprint icon Reprint Icon will take you to the publication reprint.)
A chimeric LysK-lysostaphin fusion enzyme lysing Staphylococcus aureus cells: a study of both kinetics of inactivation and specifics of interaction with anionic polymers -
Filatova, L.Y., Donovan, D.M., Ishnazarova, N., Foster Frey, J.A., Becker, S.C., Pugachev, V.G., Dmitrieva, N.F., Klyachko, N.L. 2016. A chimeric LysK-lysostaphin fusion enzyme lysing Staphylococcus aureus cells: A study of both kinetics of inactivation and specifics of interaction with anionic polymers. Enzyme and Microbial Technology. doi: 10.1007/s12010-016-2115-7.
Evolutionarily distinct bacteriophage endolysins featuring conserved peptidoglycan cleavage sites protect mice from MRSA infection -
Schmelcher, M., Shen, Y., Nelson, D.C., Eugster, M.R., Eichenseher, F., Hanke, D.C., Loessner, M.J., Dong, S., Pritchard, D.G., Lee, J.C., Becker, S.C., Donovan, D.M. 2015. Evolutionarily distinct bacteriophage endolysins featuring conserved peptidoglycan cleavage sites protect mice from MRSA infection. Antimicrobial Chemotherapy. 70(5):1453-1465.
Lytic activity of the staphylolytic Twort phage endolysin CHAP domain is enhanced by the SH3b cell wall binding domain -
Becker, S.C., Korobova, O., Schischkova, N., Kopylov, P., Donovan, D.M., Abaev, I. 2014. Lytic activity of the staphylolytic Twort phage endolysin CHAP domain is enhanced by the SH3b cell wall binding domain. FEMS Microbiology Letters. 362(1):1-8.
Triple-acting antimicrobial treatment for drug-resistant and intracellular Staphylococcus aureus. -
Triple-acting antimicrobial treatment for drug-resistant and intracellular Staphylococcus aureus -
Sperm-mediated transgenesis in chicken using a PiggyBac transposon system -
Quansah, E., Long, J.A., Donovan, D.M., Becker, S.C., Telugu, B., Foster Frey, J.A., Urwin, N. 2014. Sperm-mediated transgenesis in chicken using a PiggyBac transposon system. BARC Poster Day. BARC Poster Day.
Triple-acting antimicrobial treatment for drug-resistant and intracellular Staphylococcus aureus -
Sperm-mediated transgenesis in chicken using a PiggyBac transposon system -
Quansah, E., Long, J.A., Donovan, D.M., Becker, S.C., Telugu, B., Foster Frey, J.A., Urwin, N. 2014. Sperm-mediated transgenesis in chicken using a PiggyBac transposon system. Poultry Science Association Meeting Abstract. BARC Poster Day.
Triple-acting Peptidoglycan hydrolase treatment for drug-resistant and intracellular Staphylococcus aureus -
An investigation of the structure and function of antistaphylococcal endolysins using kinetic methods -
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. 69(3):107-111.
Staphylococcal phage 2638a endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain cryptic translational start site. -
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 -
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. -
LysK, the enzyme lysing Staphylococcus aureus cells: specific kinetic features and approaches towards stabilization -
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 -
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. -
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 -
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. -
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 -
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 -
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 -
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. -
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. -
Engineering Antimicrobials that are Refractory to Resistance Development. -
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 -
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: 5/2/2016
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