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Volumn 36, Issue 3, 2018, Pages 624-640

Synthetic biology of modular endolysins

Author keywords

clinical trials; Domain swapping; Endolysin; Engineering; Enzybiotics; Fusions; Mutagenesis; Truncation

Indexed keywords

BIOTECHNOLOGY; ENGINEERING; FUSION REACTIONS; MUTAGENESIS;

EID: 85040007747     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2017.12.009     Document Type: Review
Times cited : (134)

References (182)
  • 1
    • 84976477315 scopus 로고    scopus 로고
    • T4 lysozyme fused with cellulose-binding module for antimicrobial cellulosic wound dressing materials
    • Abouhmad, A., Mamo, G., Dishisha, T., Amin, M.A., Hatti-Kaul, R., T4 lysozyme fused with cellulose-binding module for antimicrobial cellulosic wound dressing materials. J. Appl. Microbiol. 121 (2016), 115–125, 10.1111/jam.13146.
    • (2016) J. Appl. Microbiol. , vol.121 , pp. 115-125
    • Abouhmad, A.1    Mamo, G.2    Dishisha, T.3    Amin, M.A.4    Hatti-Kaul, R.5
  • 2
    • 85019074849 scopus 로고    scopus 로고
    • Immobilization to positively charged cellulose nanocrystals enhances the antibacterial activity and stability of hen egg white and T4 lysozyme
    • Abouhmad, A., Dishisha, T., Amin, M.A., Hatti-Kaul, R., Immobilization to positively charged cellulose nanocrystals enhances the antibacterial activity and stability of hen egg white and T4 lysozyme. Biomacromolecules 18 (2017), 1600–1608, 10.1021/acs.biomac.7b00219.
    • (2017) Biomacromolecules , vol.18 , pp. 1600-1608
    • Abouhmad, A.1    Dishisha, T.2    Amin, M.A.3    Hatti-Kaul, R.4
  • 4
    • 84966340446 scopus 로고    scopus 로고
    • Biocontrol and rapid detection of food-borne pathogens using bacteriophages and endolysins
    • Bai, J., Kim, Y.-T., Ryu, S., Lee, J.-H., Biocontrol and rapid detection of food-borne pathogens using bacteriophages and endolysins. Front. Microbiol., 7, 2016, 474, 10.3389/fmicb.2016.00474.
    • (2016) Front. Microbiol. , vol.7
    • Bai, J.1    Kim, Y.-T.2    Ryu, S.3    Lee, J.-H.4
  • 5
    • 77952183463 scopus 로고    scopus 로고
    • Lysostaphin: a staphylococcal bacteriolysin with potential clinical applications
    • Bastos, M. do C. de F., Coutinho, B.G., Coelho, M.L.V., Lysostaphin: a staphylococcal bacteriolysin with potential clinical applications. Pharmaceuticals (Basel) 3 (2010), 1139–1161, 10.3390/ph3041139.
    • (2010) Pharmaceuticals (Basel) , vol.3 , pp. 1139-1161
    • Bastos, M.D.C.D.F.1    Coutinho, B.G.2    Coelho, M.L.V.3
  • 6
    • 84919782024 scopus 로고    scopus 로고
    • Triggered release of bacteriophage K from agarose/hyaluronan hydrogel matrixes by Staphylococcus aureus virulence factors
    • Bean, J.E., Alves, D.R., Laabei, M., Esteban, P.P., Thet, N.T., Enright, M.C., Jenkins, A.T.A., Triggered release of bacteriophage K from agarose/hyaluronan hydrogel matrixes by Staphylococcus aureus virulence factors. Chem. Mater. 26 (2014), 7201–7208, 10.1021/cm503974g.
    • (2014) Chem. Mater. , vol.26 , pp. 7201-7208
    • Bean, J.E.1    Alves, D.R.2    Laabei, M.3    Esteban, P.P.4    Thet, N.T.5    Enright, M.C.6    Jenkins, A.T.A.7
  • 7
    • 51349140468 scopus 로고    scopus 로고
    • The phage K lytic enzyme LysK and lysostaphin act synergistically to kill MRSA
    • Becker, S.C., Foster-Frey, J., Donovan, D.M., The phage K lytic enzyme LysK and lysostaphin act synergistically to kill MRSA. FEMS Microbiol. Lett. 287 (2008), 185–191, 10.1111/j.1574-6968.2008.01308.x.
    • (2008) FEMS Microbiol. Lett. , vol.287 , pp. 185-191
    • Becker, S.C.1    Foster-Frey, J.2    Donovan, D.M.3
  • 8
    • 67549109077 scopus 로고    scopus 로고
    • 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., Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain. Gene 443 (2009), 32–41, 10.1016/j.gene.2009.04.023.
    • (2009) Gene , vol.443 , pp. 32-41
    • Becker, S.C.1    Foster-Frey, J.2    Stodola, A.J.3    Anacker, D.4    Donovan, D.M.5
  • 10
    • 84983070108 scopus 로고    scopus 로고
    • PL3 amidase, a tailor-made lysin constructed by domain shuffling with potent killing activity against pneumococci and related species
    • Blázquez, B., Fresco-Taboada, A., Iglesias-Bexiga, M., Menéndez, M., García, P., PL3 amidase, a tailor-made lysin constructed by domain shuffling with potent killing activity against pneumococci and related species. Front. Microbiol., 7, 2016, 1156, 10.3389/fmicb.2016.01156.
    • (2016) Front. Microbiol. , vol.7 , pp. 1156
    • Blázquez, B.1    Fresco-Taboada, A.2    Iglesias-Bexiga, M.3    Menéndez, M.4    García, P.5
  • 11
    • 84926179791 scopus 로고    scopus 로고
    • Breaking barriers: expansion of the use of endolysins as novel antibacterials against Gram-negative bacteria
    • Briers, Y., Lavigne, R., Breaking barriers: expansion of the use of endolysins as novel antibacterials against Gram-negative bacteria. Future Microbiol 10 (2015), 377–390, 10.2217/fmb.15.8.
    • (2015) Future Microbiol , vol.10 , pp. 377-390
    • Briers, Y.1    Lavigne, R.2
  • 12
    • 34547897398 scopus 로고    scopus 로고
    • Muralytic activity and modular structure of the endolysins of Pseudomonas Aeruginosa bacteriophages phiKZ and EL
    • Briers, Y., Volckaert, G., Cornelissen, A., Lagaert, S., Michiels, C.W., Hertveldt, K., Lavigne, R., Muralytic activity and modular structure of the endolysins of Pseudomonas Aeruginosa bacteriophages phiKZ and EL. Mol. Microbiol. 65 (2007), 1334–1344, 10.1111/j.1365-2958.2007.05870.x.
    • (2007) Mol. Microbiol. , vol.65 , pp. 1334-1344
    • Briers, Y.1    Volckaert, G.2    Cornelissen, A.3    Lagaert, S.4    Michiels, C.W.5    Hertveldt, K.6    Lavigne, R.7
  • 13
    • 38849130696 scopus 로고    scopus 로고
    • Analysis of outer membrane permeability of Pseudomonas aeruginosa and bactericidal activity of endolysins KZ144 and EL188 under high hydrostatic pressure
    • Briers, Y., Cornelissen, A., Aertsen, A., Hertveldt, K., Michiels, C.W., Volckaert, G., Lavigne, R., Analysis of outer membrane permeability of Pseudomonas aeruginosa and bactericidal activity of endolysins KZ144 and EL188 under high hydrostatic pressure. FEMS Microbiol. Lett. 280 (2008), 113–119, 10.1111/j.1574-6968.2007.01051.x.
    • (2008) FEMS Microbiol. Lett. , vol.280 , pp. 113-119
    • Briers, Y.1    Cornelissen, A.2    Aertsen, A.3    Hertveldt, K.4    Michiels, C.W.5    Volckaert, G.6    Lavigne, R.7
  • 17
    • 85046833193 scopus 로고    scopus 로고
    • Results of the First In Human Study of Lysin CF-301 Evaluating the Safety, Tolerability and Pharmacokinetic Profile in Healthy Volunteers
    • ([ Document]. 26th ECCMID, April 9)
    • Cassino, C., Murphy, M.G., Boyle, J., Rotolo, J., Wittekind, M., Results of the First In Human Study of Lysin CF-301 Evaluating the Safety, Tolerability and Pharmacokinetic Profile in Healthy Volunteers. 2016 ([WWW Document]. 26th ECCMID, April 9).
    • (2016)
    • Cassino, C.1    Murphy, M.G.2    Boyle, J.3    Rotolo, J.4    Wittekind, M.5
  • 18
    • 85008230646 scopus 로고    scopus 로고
    • Endolysin LysSA97 is synergistic with carvacrol in controlling Staphylococcus aureus in foods
    • Chang, Y., Yoon, H., Kang, D.-H., Chang, P.-S., Ryu, S., Endolysin LysSA97 is synergistic with carvacrol in controlling Staphylococcus aureus in foods. Int. J. Food Microbiol. 244 (2017), 19–26, 10.1016/j.ijfoodmicro.2016.12.007.
    • (2017) Int. J. Food Microbiol. , vol.244 , pp. 19-26
    • Chang, Y.1    Yoon, H.2    Kang, D.-H.3    Chang, P.-S.4    Ryu, S.5
  • 19
    • 85046835785 scopus 로고    scopus 로고
    • Preclinical Studies of Anti-Staphylococcal Ectolysin P128 for Potential Systemic Hypersensitivity and Evaluation of Efficacy in Staphylococcus aureus Bacteremia with Renal Abscesses in Rats
    • Document ASM Microbe (June)
    • Channabasappa, S., Chikkamadaiah, R., Durgaiah, M., Hariharan, S., Joshi, A., Kumar, S., Maheshwari, U., Nandish, P., Sriram, B., Vijayan, A., Keelara, S., Preclinical Studies of Anti-Staphylococcal Ectolysin P128 for Potential Systemic Hypersensitivity and Evaluation of Efficacy in Staphylococcus aureus Bacteremia with Renal Abscesses in Rats. WWW Document, 2017, ASM Microbe (June).
    • (2017)
    • Channabasappa, S.1    Chikkamadaiah, R.2    Durgaiah, M.3    Hariharan, S.4    Joshi, A.5    Kumar, S.6    Maheshwari, U.7    Nandish, P.8    Sriram, B.9    Vijayan, A.10    Keelara, S.11
  • 20
    • 34247598409 scopus 로고    scopus 로고
    • Mutagenesis of a bacteriophage lytic enzyme PlyGBS significantly increases its antibacterial activity against group B streptococci
    • Cheng, Q., Fischetti, V.A., Mutagenesis of a bacteriophage lytic enzyme PlyGBS significantly increases its antibacterial activity against group B streptococci. Appl. Microbiol. Biotechnol. 74 (2007), 1284–1291, 10.1007/s00253-006-0771-1.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 1284-1291
    • Cheng, Q.1    Fischetti, V.A.2
  • 21
    • 0031805819 scopus 로고    scopus 로고
    • Lysostaphin treatment of experimental methicillin-resistant Staphylococcus aureus aortic valve endocarditis
    • Climo, M.W., Patron, R.L., Goldstein, B.P., Archer, G.L., Lysostaphin treatment of experimental methicillin-resistant Staphylococcus aureus aortic valve endocarditis. Antimicrob. Agents Chemother. 42 (1998), 1355–1360.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1355-1360
    • Climo, M.W.1    Patron, R.L.2    Goldstein, B.P.3    Archer, G.L.4
  • 22
    • 0035040527 scopus 로고    scopus 로고
    • Mechanism and suppression of lysostaphin resistance in oxacillin-resistant Staphylococcus aureus
    • Climo, M.W., Ehlert, K., Archer, G.L., Mechanism and suppression of lysostaphin resistance in oxacillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 45 (2001), 1431–1437, 10.1128/AAC.45.5.1431-1437.2001.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1431-1437
    • Climo, M.W.1    Ehlert, K.2    Archer, G.L.3
  • 23
    • 0027204227 scopus 로고
    • Interchange of functional domains switches enzyme specificity: construction of a chimeric pneumococcal-clostridial cell wall lytic enzyme
    • Croux, C., Ronda, C., López, R., García, J.L., Interchange of functional domains switches enzyme specificity: construction of a chimeric pneumococcal-clostridial cell wall lytic enzyme. Mol. Microbiol. 9 (1993), 1019–1025.
    • (1993) Mol. Microbiol. , vol.9 , pp. 1019-1025
    • Croux, C.1    Ronda, C.2    López, R.3    García, J.L.4
  • 25
    • 77950126213 scopus 로고    scopus 로고
    • Synergism between a novel chimeric lysin and oxacillin protects against infection by methicillin-resistant Staphylococcus aureus
    • Daniel, A., Euler, C., Collin, M., Chahales, P., Gorelick, K.J., Fischetti, V.A., Synergism between a novel chimeric lysin and oxacillin protects against infection by methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 54 (2010), 1603–1612, 10.1128/AAC.01625-09.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 1603-1612
    • Daniel, A.1    Euler, C.2    Collin, M.3    Chahales, P.4    Gorelick, K.J.5    Fischetti, V.A.6
  • 27
    • 0028961002 scopus 로고
    • The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus
    • DeHart, H.P., Heath, H.E., Heath, L.S., LeBlanc, P.A., Sloan, G.L., The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus. Appl. Environ. Microbiol. 61 (1995), 1475–1479.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1475-1479
    • DeHart, H.P.1    Heath, H.E.2    Heath, L.S.3    LeBlanc, P.A.4    Sloan, G.L.5
  • 28
    • 0025186362 scopus 로고
    • Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes
    • Díaz, E., López, R., García, J.L., Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes. Proc. Natl. Acad. Sci. U. S. A. 87 (1990), 8125–8129.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 8125-8129
    • Díaz, E.1    López, R.2    García, J.L.3
  • 29
    • 0025949202 scopus 로고
    • Chimeric pneumococcal cell wall lytic enzymes reveal important physiological and evolutionary traits
    • Díaz, E., López, R., García, J.L., Chimeric pneumococcal cell wall lytic enzymes reveal important physiological and evolutionary traits. J. Biol. Chem. 266 (1991), 5464–5471.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5464-5471
    • Díaz, E.1    López, R.2    García, J.L.3
  • 30
    • 84885913953 scopus 로고    scopus 로고
    • Improving the lethal effect of cpl-7, a pneumococcal phage lysozyme with broad bactericidal activity, by inverting the net charge of its cell wall-binding module
    • Díez-Martínez, R., de Paz, H.D., de Paz, H., Bustamante, N., García, E., Menéndez, M., García, P., Improving the lethal effect of cpl-7, a pneumococcal phage lysozyme with broad bactericidal activity, by inverting the net charge of its cell wall-binding module. Antimicrob. Agents Chemother. 57 (2013), 5355–5365, 10.1128/AAC.01372-13.
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 5355-5365
    • Díez-Martínez, R.1    de Paz, H.D.2    de Paz, H.3    Bustamante, N.4    García, E.5    Menéndez, M.6    García, P.7
  • 32
    • 14744269239 scopus 로고    scopus 로고
    • Synergistic killing of Streptococcus pneumoniae with the bacteriophage lytic enzyme Cpl-1 and penicillin or gentamicin depends on the level of penicillin resistance
    • Djurkovic, S., Loeffler, J.M., Fischetti, V.A., Synergistic killing of Streptococcus pneumoniae with the bacteriophage lytic enzyme Cpl-1 and penicillin or gentamicin depends on the level of penicillin resistance. Antimicrob. Agents Chemother. 49 (2005), 1225–1228, 10.1128/AAC.49.3.1225-1228.2005.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 1225-1228
    • Djurkovic, S.1    Loeffler, J.M.2    Fischetti, V.A.3
  • 34
    • 84923529521 scopus 로고    scopus 로고
    • Construction of a chimeric lysin Ply187N-V12C with extended lytic activity against staphylococci and streptococci
    • Dong, Q., Wang, J., Yang, H., Wei, C., Yu, J., Zhang, Y., Huang, Y., Zhang, X.-E., Wei, H., Construction of a chimeric lysin Ply187N-V12C with extended lytic activity against staphylococci and streptococci. Microb. Biotechnol. 8 (2015), 210–220, 10.1111/1751-7915.12166.
    • (2015) Microb. Biotechnol. , vol.8 , pp. 210-220
    • Dong, Q.1    Wang, J.2    Yang, H.3    Wei, C.4    Yu, J.5    Zhang, Y.6    Huang, Y.7    Zhang, X.-E.8    Wei, H.9
  • 35
    • 84951335015 scopus 로고    scopus 로고
    • Fighting sinus-derived Staphylococcus Aureus biofilms in vitro with a bacteriophage-derived muralytic enzyme
    • Drilling, A.J., Cooksley, C., Chan, C., Wormald, P.-J., Vreugde, S., Fighting sinus-derived Staphylococcus Aureus biofilms in vitro with a bacteriophage-derived muralytic enzyme. Int. Forum Allergy Rhinol. 6 (2016), 349–355, 10.1002/alr.21680.
    • (2016) Int. Forum Allergy Rhinol. , vol.6 , pp. 349-355
    • Drilling, A.J.1    Cooksley, C.2    Chan, C.3    Wormald, P.-J.4    Vreugde, S.5
  • 36
    • 27644534839 scopus 로고    scopus 로고
    • Therapeutic effects of bacteriophage Cpl-1 lysin against Streptococcus pneumoniae endocarditis in rats
    • Entenza, J.M., Loeffler, J.M., Grandgirard, D., Fischetti, V.A., Moreillon, P., Therapeutic effects of bacteriophage Cpl-1 lysin against Streptococcus pneumoniae endocarditis in rats. Antimicrob. Agents Chemother. 49 (2005), 4789–4792, 10.1128/AAC.49.11.4789-4792.2005.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 4789-4792
    • Entenza, J.M.1    Loeffler, J.M.2    Grandgirard, D.3    Fischetti, V.A.4    Moreillon, P.5
  • 37
    • 84926642568 scopus 로고    scopus 로고
    • Antibiotics and bacterial resistance in the 21st century
    • Fair, R.J., Tor, Y., Antibiotics and bacterial resistance in the 21st century. Perspect. Medicin. Chem. 6 (2014), 25–64, 10.4137/PMC.S14459.
    • (2014) Perspect. Medicin. Chem. , vol.6 , pp. 25-64
    • Fair, R.J.1    Tor, Y.2
  • 40
    • 85018177137 scopus 로고    scopus 로고
    • Downregulation of autolysin-encoding genes by phage-derived lytic proteins inhibits biofilm formation in Staphylococcus aureus
    • Fernández, L., González, S., Campelo, A.B., Martínez, B., Rodríguez, A., García, P., Downregulation of autolysin-encoding genes by phage-derived lytic proteins inhibits biofilm formation in Staphylococcus aureus. Antimicrob. Agents Chemother., 61, 2017, e02724-16, 10.1128/AAC.02724-16.
    • (2017) Antimicrob. Agents Chemother. , vol.61 , pp. e02724-16
    • Fernández, L.1    González, S.2    Campelo, A.B.3    Martínez, B.4    Rodríguez, A.5    García, P.6
  • 41
    • 84881147266 scopus 로고    scopus 로고
    • Physicochemical characterization of the staphylolytic LysK enzyme in complexes with polycationic polymers as a potent antimicrobial
    • Filatova, L.Y., Donovan, D.M., Becker, S.C., Lebedev, D.N., Priyma, A.D., Koudriachova, H.V., Kabanov, A.V., Klyachko, N.L., Physicochemical characterization of the staphylolytic LysK enzyme in complexes with polycationic polymers as a potent antimicrobial. Biochimie 95 (2013), 1689–1696, 10.1016/j.biochi.2013.04.013.
    • (2013) Biochimie , vol.95 , pp. 1689-1696
    • Filatova, L.Y.1    Donovan, D.M.2    Becker, S.C.3    Lebedev, D.N.4    Priyma, A.D.5    Koudriachova, H.V.6    Kabanov, A.V.7    Klyachko, N.L.8
  • 43
    • 0037903426 scopus 로고    scopus 로고
    • Novel method to control pathogenic bacteria on human mucous membranes
    • Fischetti, V.A., Novel method to control pathogenic bacteria on human mucous membranes. Ann. N. Y. Acad. Sci. 987 (2003), 207–214, 10.1111/j.1749-6632.2003.tb06050.x.
    • (2003) Ann. N. Y. Acad. Sci. , vol.987 , pp. 207-214
    • Fischetti, V.A.1
  • 44
    • 24944587206 scopus 로고    scopus 로고
    • Bacteriophage lytic enzymes: novel anti-infectives
    • Fischetti, V.A., Bacteriophage lytic enzymes: novel anti-infectives. Trends Microbiol. 13 (2005), 491–496, 10.1016/j.tim.2005.08.007.
    • (2005) Trends Microbiol. , vol.13 , pp. 491-496
    • Fischetti, V.A.1
  • 45
    • 77955557492 scopus 로고    scopus 로고
    • Bacteriophage endolysins: a novel anti-infective to control Gram-positive pathogens
    • Fischetti, V.A., Bacteriophage endolysins: a novel anti-infective to control Gram-positive pathogens. Int. J. Med. Microbiol. 300 (2010), 357–362, 10.1016/j.ijmm.2010.04.002.
    • (2010) Int. J. Med. Microbiol. , vol.300 , pp. 357-362
    • Fischetti, V.A.1
  • 46
    • 84896728759 scopus 로고    scopus 로고
    • Expression and delivery of an endolysin to combat Clostridium perfringens
    • Gervasi, T., Horn, N., Wegmann, U., Dugo, G., Narbad, A., Mayer, M.J., Expression and delivery of an endolysin to combat Clostridium perfringens. Appl. Microbiol. Biotechnol. 98 (2014), 2495–2505, 10.1007/s00253-013-5128-y.
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , pp. 2495-2505
    • Gervasi, T.1    Horn, N.2    Wegmann, U.3    Dugo, G.4    Narbad, A.5    Mayer, M.J.6
  • 47
    • 84921664578 scopus 로고    scopus 로고
    • Application of Lactobacillus johnsonii expressing phage endolysin for control of Clostridium perfringens
    • Gervasi, T., Lo Curto, R., Minniti, E., Narbad, A., Mayer, M.J., Application of Lactobacillus johnsonii expressing phage endolysin for control of Clostridium perfringens. Lett. Appl. Microbiol. 59 (2014), 355–361, 10.1111/lam.12298.
    • (2014) Lett. Appl. Microbiol. , vol.59 , pp. 355-361
    • Gervasi, T.1    Lo Curto, R.2    Minniti, E.3    Narbad, A.4    Mayer, M.J.5
  • 48
    • 85046842905 scopus 로고    scopus 로고
    • Population pharmacokinetic-pharmacodynamic assessment of cardiac safety endpoints for CF-301, a first-in-class antibacterial lysin
    • WWW Document (June 3)
    • Ghahramani, P., Khariton, T., Jones, S., Murphy, J., Boyle, G., Jandourek, A., Cassino, C., Population pharmacokinetic-pharmacodynamic assessment of cardiac safety endpoints for CF-301, a first-in-class antibacterial lysin. WWW Document ASM Microbe, 2017 (June 3) https://www.contrafect.com/news/posters-and-presentations.
    • (2017) ASM Microbe
    • Ghahramani, P.1    Khariton, T.2    Jones, S.3    Murphy, J.4    Boyle, G.5    Jandourek, A.6    Cassino, C.7
  • 49
    • 84877859662 scopus 로고    scopus 로고
    • Novel bacteriophage lysin with broad lytic activity protects against mixed infection by Streptococcus pyogenes and methicillin-resistant Staphylococcus aureus
    • Gilmer, D.B., Schmitz, J.E., Euler, C.W., Fischetti, V.A., Novel bacteriophage lysin with broad lytic activity protects against mixed infection by Streptococcus pyogenes and methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 57 (2013), 2743–2750, 10.1128/AAC.02526-12.
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 2743-2750
    • Gilmer, D.B.1    Schmitz, J.E.2    Euler, C.W.3    Fischetti, V.A.4
  • 50
    • 43949128054 scopus 로고    scopus 로고
    • Phage lytic enzyme Cpl-1 for antibacterial therapy in experimental pneumococcal meningitis
    • Grandgirard, D., Loeffler, J.M., Fischetti, V.A., Leib, S.L., Phage lytic enzyme Cpl-1 for antibacterial therapy in experimental pneumococcal meningitis. J. Infect. Dis. 197 (2008), 1519–1522, 10.1086/587942.
    • (2008) J. Infect. Dis. , vol.197 , pp. 1519-1522
    • Grandgirard, D.1    Loeffler, J.M.2    Fischetti, V.A.3    Leib, S.L.4
  • 51
    • 33749005403 scopus 로고    scopus 로고
    • Staphylococcus aureus mutants with increased lysostaphin resistance
    • Grundling, A., Missiakas, D.M., Schneewind, O., Staphylococcus aureus mutants with increased lysostaphin resistance. J. Bacteriol. 188 (2006), 6286–6297, 10.1128/JB.00457-06.
    • (2006) J. Bacteriol. , vol.188 , pp. 6286-6297
    • Grundling, A.1    Missiakas, D.M.2    Schneewind, O.3
  • 52
    • 78650865739 scopus 로고    scopus 로고
    • LysGH15, a novel bacteriophage lysin, protects a murine bacteremia model efficiently against lethal methicillin-resistant Staphylococcus aureus infection
    • Gu, J., Xu, W., Lei, L., Huang, J., Feng, X., Sun, C., Du, C., Zuo, J., Li, Y., Du, T., Li, L., Han, W., LysGH15, a novel bacteriophage lysin, protects a murine bacteremia model efficiently against lethal methicillin-resistant Staphylococcus aureus infection. J. Clin. Microbiol. 49 (2011), 111–117, 10.1128/JCM.01144-10.
    • (2011) J. Clin. Microbiol. , vol.49 , pp. 111-117
    • Gu, J.1    Xu, W.2    Lei, L.3    Huang, J.4    Feng, X.5    Sun, C.6    Du, C.7    Zuo, J.8    Li, Y.9    Du, T.10    Li, L.11    Han, W.12
  • 54
    • 84929942884 scopus 로고    scopus 로고
    • Effective removal of staphylococcal biofilms by the endolysin LysH5
    • Gutiérrez, D., Ruas-Madiedo, P., Martínez, B., Rodríguez, A., García, P., Effective removal of staphylococcal biofilms by the endolysin LysH5. PLoS One, 9, 2014, e107307, 10.1371/journal.pone.0107307.
    • (2014) PLoS One , vol.9 , pp. e107307
    • Gutiérrez, D.1    Ruas-Madiedo, P.2    Martínez, B.3    Rodríguez, A.4    García, P.5
  • 55
    • 85027555232 scopus 로고    scopus 로고
    • A novel chimeric endolysin with antibacterial activity against methicillin-resistant Staphylococcus aureus
    • Haddad Kashani, H., Fahimi, H., Dasteh Goli, Y., Moniri, R., A novel chimeric endolysin with antibacterial activity against methicillin-resistant Staphylococcus aureus. Front. Cell. Infect. Microbiol., 7, 2017, 290, 10.3389/fcimb.2017.00290.
    • (2017) Front. Cell. Infect. Microbiol. , vol.7 , pp. 290
    • Haddad Kashani, H.1    Fahimi, H.2    Dasteh Goli, Y.3    Moniri, R.4
  • 56
    • 34548039230 scopus 로고    scopus 로고
    • Application of bacteriophages for detection and control of foodborne pathogens
    • Hagens, S., Loessner, M.J., Application of bacteriophages for detection and control of foodborne pathogens. Appl. Microbiol. Biotechnol. 76 (2007), 513–519, 10.1007/s00253-007-1031-8.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 513-519
    • Hagens, S.1    Loessner, M.J.2
  • 57
    • 84999143036 scopus 로고    scopus 로고
    • Thermally triggered release of the bacteriophage endolysin CHAPK and the bacteriocin lysostaphin for the control of methicillin resistant Staphylococcus aureus (MRSA)
    • Hathaway, H., Ajuebor, J., Stephens, L., Coffey, A., Potter, U., Sutton, J.M., Jenkins, A.T.A., Thermally triggered release of the bacteriophage endolysin CHAPK and the bacteriocin lysostaphin for the control of methicillin resistant Staphylococcus aureus (MRSA). J. Control. Release 245 (2017), 108–115, 10.1016/j.jconrel.2016.11.030.
    • (2017) J. Control. Release , vol.245 , pp. 108-115
    • Hathaway, H.1    Ajuebor, J.2    Stephens, L.3    Coffey, A.4    Potter, U.5    Sutton, J.M.6    Jenkins, A.T.A.7
  • 58
    • 85021143778 scopus 로고    scopus 로고
    • Recent advances in therapeutic delivery systems of bacteriophage and bacteriophage-encoded endolysins
    • Hathaway, H., Milo, S., Sutton, J.M., Jenkins, T.A., Recent advances in therapeutic delivery systems of bacteriophage and bacteriophage-encoded endolysins. Ther. Deliv. 8 (2017), 543–556, 10.4155/tde-2017-0040.
    • (2017) Ther. Deliv. , vol.8 , pp. 543-556
    • Hathaway, H.1    Milo, S.2    Sutton, J.M.3    Jenkins, T.A.4
  • 59
    • 0033514996 scopus 로고    scopus 로고
    • Evolutionary relationships among diverse bacteriophages and prophages: all the world's a phage
    • Hendrix, R.W., Smith, M.C.M., Burns, R.N., Ford, M.E., Hatfull, G.F., Evolutionary relationships among diverse bacteriophages and prophages: all the world's a phage. Evolution (N. Y). 96 (1999), 2192–2197.
    • (1999) Evolution (N. Y). , vol.96 , pp. 2192-2197
    • Hendrix, R.W.1    Smith, M.C.M.2    Burns, R.N.3    Ford, M.E.4    Hatfull, G.F.5
  • 60
    • 84873734989 scopus 로고    scopus 로고
    • A new screening method for the directed evolution of thermostable bacteriolytic enzymes
    • Heselpoth, R.D., Nelson, D.C., A new screening method for the directed evolution of thermostable bacteriolytic enzymes. J. Vis. Exp., 2012, 10.3791/4216.
    • (2012) J. Vis. Exp.
    • Heselpoth, R.D.1    Nelson, D.C.2
  • 61
    • 84946125376 scopus 로고    scopus 로고
    • Increasing the stability of the bacteriophage endolysin PlyC using rationale-based FoldX computational modeling
    • Heselpoth, R.D., Yin, Y., Moult, J., Nelson, D.C., Increasing the stability of the bacteriophage endolysin PlyC using rationale-based FoldX computational modeling. Protein Eng. Des. Sel. 28 (2015), 85–92, 10.1093/protein/gzv004.
    • (2015) Protein Eng. Des. Sel. , vol.28 , pp. 85-92
    • Heselpoth, R.D.1    Yin, Y.2    Moult, J.3    Nelson, D.C.4
  • 62
    • 59649128479 scopus 로고    scopus 로고
    • Phage lysin LysK can be truncated to its CHAP domain and retain lytic activity against live antibiotic-resistant staphylococci
    • Horgan, M., O'Flynn, G., Garry, J., Cooney, J., Coffey, A., Fitzgerald, G.F., Ross, R.P., McAuliffe, O., Phage lysin LysK can be truncated to its CHAP domain and retain lytic activity against live antibiotic-resistant staphylococci. Appl. Environ. Microbiol. 75 (2009), 872–874, 10.1128/AEM.01831-08.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 872-874
    • Horgan, M.1    O'Flynn, G.2    Garry, J.3    Cooney, J.4    Coffey, A.5    Fitzgerald, G.F.6    Ross, R.P.7    McAuliffe, O.8
  • 63
    • 84923864536 scopus 로고    scopus 로고
    • Antibacterial properties of Acinetobacter baumanniiphage Abp1 endolysin (PlyAB1)
    • Huang, G., Shen, X., Gong, Y., Dong, Z., Zhao, X., Shen, W., Wang, J., Hu, F., Peng, Y., Antibacterial properties of Acinetobacter baumanniiphage Abp1 endolysin (PlyAB1). BMC Infect. Dis., 14, 2014, 681, 10.1186/s12879-014-0681-2.
    • (2014) BMC Infect. Dis. , vol.14 , pp. 681
    • Huang, G.1    Shen, X.2    Gong, Y.3    Dong, Z.4    Zhao, X.5    Shen, W.6    Wang, J.7    Hu, F.8    Peng, Y.9
  • 64
    • 10744225724 scopus 로고    scopus 로고
    • Phage lytic enzymes as therapy for antibiotic-resistant Streptococcus pneumoniae infection in a murine sepsis model
    • Jado, I., López, R., García, E., Fenoll, A., Casal, J., García, P., Network, Spanish Pneumococcal Infection Study, Phage lytic enzymes as therapy for antibiotic-resistant Streptococcus pneumoniae infection in a murine sepsis model. J. Antimicrob. Chemother. 52 (2003), 967–973, 10.1093/jac/dkg485.
    • (2003) J. Antimicrob. Chemother. , vol.52 , pp. 967-973
    • Jado, I.1    López, R.2    García, E.3    Fenoll, A.4    Casal, J.5    García, P.6    Network, S.P.I.S.7
  • 65
    • 84987834838 scopus 로고    scopus 로고
    • LytM fusion with SH3b-like domain expands its activity to physiological conditions
    • Jagielska, E., Chojnacka, O., Sabała, I., LytM fusion with SH3b-like domain expands its activity to physiological conditions. Microb. Drug Resist. 22 (2016), 461–469, 10.1089/mdr.2016.0053.
    • (2016) Microb. Drug Resist. , vol.22 , pp. 461-469
    • Jagielska, E.1    Chojnacka, O.2    Sabała, I.3
  • 66
    • 85046842265 scopus 로고    scopus 로고
    • Long term immunology results of a phase 1 placebo controlled dose escalating study to examine the safety of CF-301 in human volunteers [WWW document]
    • Jandourek, A., Boyle, J., Cassino, C., Wittekind, M., Kirby, H., Long term immunology results of a phase 1 placebo controlled dose escalating study to examine the safety of CF-301 in human volunteers [WWW document]. 27th ECCMID, April 22, 2017.
    • (2017) 27th ECCMID, April 22
    • Jandourek, A.1    Boyle, J.2    Cassino, C.3    Wittekind, M.4    Kirby, H.5
  • 67
    • 85046863024 scopus 로고    scopus 로고
    • Inflammatory markers in a phase 1 placebo controlled dose escalating study of intravenous doses of CF-301 in human subjects [WWW document]
    • Jandourek, A., Boyle, J., Murphy, G., Cassino, C., Inflammatory markers in a phase 1 placebo controlled dose escalating study of intravenous doses of CF-301 in human subjects [WWW document]. ASM Microbe, June 2, 2017.
    • (2017) ASM Microbe, June 2
    • Jandourek, A.1    Boyle, J.2    Murphy, G.3    Cassino, C.4
  • 68
    • 85025145415 scopus 로고    scopus 로고
    • Repurposing a two-component system-based biosensor for the killing of Vibrio cholerae
    • Jayaraman, P., Holowko, M.B., Yeoh, J.W., Lim, S., Poh, C.L., Repurposing a two-component system-based biosensor for the killing of Vibrio cholerae. ACS Synth. Biol. 6 (2017), 1403–1415, 10.1021/acssynbio.7b00058.
    • (2017) ACS Synth. Biol. , vol.6 , pp. 1403-1415
    • Jayaraman, P.1    Holowko, M.B.2    Yeoh, J.W.3    Lim, S.4    Poh, C.L.5
  • 70
  • 72
    • 84896993913 scopus 로고    scopus 로고
    • Preclinical safety evaluation of intravenously administered SAL200 containing the recombinant phage endolysin SAL-1 as a pharmaceutical ingredient
    • Jun, S.Y., Jung, G.M., Yoon, S.J., Choi, Y.-J., Koh, W.S., Moon, K.S., Kang, S.H., Preclinical safety evaluation of intravenously administered SAL200 containing the recombinant phage endolysin SAL-1 as a pharmaceutical ingredient. Antimicrob. Agents Chemother. 58 (2014), 2084–2088, 10.1128/AAC.02232-13.
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 2084-2088
    • Jun, S.Y.1    Jung, G.M.2    Yoon, S.J.3    Choi, Y.-J.4    Koh, W.S.5    Moon, K.S.6    Kang, S.H.7
  • 73
    • 84985019767 scopus 로고    scopus 로고
    • Pharmacokinetics of the phage endolysin-based candidate drug SAL200 in monkeys and its appropriate intravenous dosing period
    • Jun, S.Y., Jung, G.M., Yoon, S.J., Youm, S.Y., Han, H.-Y., Lee, J.-H., Kang, S.H., Pharmacokinetics of the phage endolysin-based candidate drug SAL200 in monkeys and its appropriate intravenous dosing period. Clin. Exp. Pharmacol. Physiol. 43 (2016), 1013–1016, 10.1111/1440-1681.12613.
    • (2016) Clin. Exp. Pharmacol. Physiol. , vol.43 , pp. 1013-1016
    • Jun, S.Y.1    Jung, G.M.2    Yoon, S.J.3    Youm, S.Y.4    Han, H.-Y.5    Lee, J.-H.6    Kang, S.H.7
  • 74
    • 85019709674 scopus 로고    scopus 로고
    • Pharmacokinetics and tolerance of the phage endolysin-based candidate drug SAL200 after a single intravenous administration among healthy volunteers
    • Jun, S.Y., Jang, I.J., Yoon, S., Jang, K., Yu, K.-S., Cho, J.Y., Seong, M.-W., Jung, G.M., Yoon, S.J., Kang, S.H., Pharmacokinetics and tolerance of the phage endolysin-based candidate drug SAL200 after a single intravenous administration among healthy volunteers. Antimicrob. Agents Chemother., 61, 2017, e02629-16, 10.1128/AAC.02629-16.
    • (2017) Antimicrob. Agents Chemother. , vol.61 , pp. e02629-16
    • Jun, S.Y.1    Jang, I.J.2    Yoon, S.3    Jang, K.4    Yu, K.-S.5    Cho, J.Y.6    Seong, M.-W.7    Jung, G.M.8    Yoon, S.J.9    Kang, S.H.10
  • 76
    • 84925356373 scopus 로고    scopus 로고
    • Bacteriophage PBC1 and its endolysin as an antimicrobial agent against Bacillus cereus
    • Kong, M., Ryu, S., Bacteriophage PBC1 and its endolysin as an antimicrobial agent against Bacillus cereus. Appl. Environ. Microbiol. 81 (2015), 2274–2283, 10.1128/AEM.03485-14.
    • (2015) Appl. Environ. Microbiol. , vol.81 , pp. 2274-2283
    • Kong, M.1    Ryu, S.2
  • 77
    • 84938970534 scopus 로고    scopus 로고
    • A novel and highly specific phage endolysin cell wall binding domain for detection of Bacillus cereus
    • Kong, M., Sim, J., Kang, T., Nguyen, H.H., Park, H.K., Chung, B.H., Ryu, S., A novel and highly specific phage endolysin cell wall binding domain for detection of Bacillus cereus. Eur. Biophys. J. 44 (2015), 437–446, 10.1007/s00249-015-1044-7.
    • (2015) Eur. Biophys. J. , vol.44 , pp. 437-446
    • Kong, M.1    Sim, J.2    Kang, T.3    Nguyen, H.H.4    Park, H.K.5    Chung, B.H.6    Ryu, S.7
  • 78
    • 85018381939 scopus 로고    scopus 로고
    • Lateral flow assay-based bacterial detection using engineered cell wall binding domains of a phage endolysin
    • Kong, M., Shin, J.H., Heu, S., Park, J.-K., Ryu, S., Lateral flow assay-based bacterial detection using engineered cell wall binding domains of a phage endolysin. Biosens. Bioelectron. 96 (2017), 173–177, 10.1016/j.bios.2017.05.010.
    • (2017) Biosens. Bioelectron. , vol.96 , pp. 173-177
    • Kong, M.1    Shin, J.H.2    Heu, S.3    Park, J.-K.4    Ryu, S.5
  • 79
    • 33947396809 scopus 로고    scopus 로고
    • Use of high-affinity cell wall-binding domains of bacteriophage endolysins for immobilization and separation of bacterial cells
    • Kretzer, J.W., Lehmann, R., Schmelcher, M., Banz, M., Kim, K.-P., Korn, C., Loessner, M.J., Use of high-affinity cell wall-binding domains of bacteriophage endolysins for immobilization and separation of bacterial cells. Appl. Environ. Microbiol. 73 (2007), 1992–2000, 10.1128/AEM.02402-06.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 1992-2000
    • Kretzer, J.W.1    Lehmann, R.2    Schmelcher, M.3    Banz, M.4    Kim, K.-P.5    Korn, C.6    Loessner, M.J.7
  • 80
    • 33846623697 scopus 로고    scopus 로고
    • Lysostaphin-resistant variants of Staphylococcus aureus demonstrate reduced fitness in vitro and in vivo
    • Kusuma, C., Jadanova, A., Chanturiya, T., Kokai-Kun, J.F., Lysostaphin-resistant variants of Staphylococcus aureus demonstrate reduced fitness in vitro and in vivo. Antimicrob. Agents Chemother. 51 (2007), 475–482, 10.1128/AAC.00786-06.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 475-482
    • Kusuma, C.1    Jadanova, A.2    Chanturiya, T.3    Kokai-Kun, J.F.4
  • 81
    • 79954652277 scopus 로고    scopus 로고
    • Antibacterial activity of Acinetobacter baumannii phage ϕAB2 endolysin (LysAB2) against both Gram-positive and Gram-negative bacteria
    • Lai, M.-J., Lin, N.-T., Hu, A., Soo, P.-C., Chen, L.-K., Chen, L.-H., Chang, K.-C., Antibacterial activity of Acinetobacter baumannii phage ϕAB2 endolysin (LysAB2) against both Gram-positive and Gram-negative bacteria. Appl. Microbiol. Biotechnol. 90 (2011), 529–539, 10.1007/s00253-011-3104-y.
    • (2011) Appl. Microbiol. Biotechnol. , vol.90 , pp. 529-539
    • Lai, M.-J.1    Lin, N.-T.2    Hu, A.3    Soo, P.-C.4    Chen, L.-K.5    Chen, L.-H.6    Chang, K.-C.7
  • 82
    • 84880302580 scopus 로고    scopus 로고
    • Identification and characterisation of the putative phage-related endolysins through full genome sequence analysis in Acinetobacter baumannii ATCC 17978
    • Lai, M.-J., Soo, P.-C., Lin, N.-T., Hu, A., Chen, Y.-J., Chen, L.-K., Chang, K.-C., Identification and characterisation of the putative phage-related endolysins through full genome sequence analysis in Acinetobacter baumannii ATCC 17978. Int. J. Antimicrob. Agents 42 (2013), 141–148, 10.1016/j.ijantimicag.2013.04.022.
    • (2013) Int. J. Antimicrob. Agents , vol.42 , pp. 141-148
    • Lai, M.-J.1    Soo, P.-C.2    Lin, N.-T.3    Hu, A.4    Chen, Y.-J.5    Chen, L.-K.6    Chang, K.-C.7
  • 83
    • 84902603132 scopus 로고    scopus 로고
    • Exogenous lytic activity of SPN9CC endolysin against gram-negative bacteria
    • Lim, J.-A., Shin, H., Heu, S., Ryu, S., Exogenous lytic activity of SPN9CC endolysin against gram-negative bacteria. J. Microbiol. Biotechnol. 24 (2014), 803–811, 10.4014/jmb.1403.03035.
    • (2014) J. Microbiol. Biotechnol. , vol.24 , pp. 803-811
    • Lim, J.-A.1    Shin, H.2    Heu, S.3    Ryu, S.4
  • 84
    • 84876415152 scopus 로고    scopus 로고
    • Cell-mediated killing of Listeria monocytogenes by leucocin C producing Escherichia coli
    • Liu, S., Takala, T.M., Wan, X., Reunanen, J., Saris, P.E.J., Cell-mediated killing of Listeria monocytogenes by leucocin C producing Escherichia coli. Microbiol. Res. 168 (2013), 300–304, 10.1016/j.micres.2012.11.011.
    • (2013) Microbiol. Res. , vol.168 , pp. 300-304
    • Liu, S.1    Takala, T.M.2    Wan, X.3    Reunanen, J.4    Saris, P.E.J.5
  • 85
    • 84926617213 scopus 로고    scopus 로고
    • Attachment of Escherichia coli to Listeria monocytogenes for Pediocin-Mediated Killing
    • Liu, S., Takala, T.M., Reunanen, J., Saris, O., Saris, P.E.J., Attachment of Escherichia coli to Listeria monocytogenes for Pediocin-Mediated Killing. Curr. Microbiol. 70 (2015), 195–198, 10.1007/s00284-014-0703-8.
    • (2015) Curr. Microbiol. , vol.70 , pp. 195-198
    • Liu, S.1    Takala, T.M.2    Reunanen, J.3    Saris, O.4    Saris, P.E.J.5
  • 86
    • 0037224191 scopus 로고    scopus 로고
    • Synergistic lethal effect of a combination of phage lytic enzymes with different activities on penicillin-sensitive and -resistant Streptococcus pneumoniae strains
    • Loeffler, J.M., Fischetti, V.A., Synergistic lethal effect of a combination of phage lytic enzymes with different activities on penicillin-sensitive and -resistant Streptococcus pneumoniae strains. Antimicrob. Agents Chemother. 47 (2003), 375–377.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 375-377
    • Loeffler, J.M.1    Fischetti, V.A.2
  • 87
    • 85046834039 scopus 로고    scopus 로고
    • Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase
    • Loeffler, J.M., Nelson, D., Fischetti, V.A., Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase. Science, 80, 2001, 294.
    • (2001) Science , vol.80 , pp. 294
    • Loeffler, J.M.1    Nelson, D.2    Fischetti, V.A.3
  • 88
    • 0242286566 scopus 로고    scopus 로고
    • Phage lytic enzyme Cpl-1 as a novel antimicrobial for pneumococcal bacteremia
    • Loeffler, J.M., Djurkovic, S., Fischetti, V.A., Phage lytic enzyme Cpl-1 as a novel antimicrobial for pneumococcal bacteremia. Infect. Immun. 71 (2003), 6199–6204.
    • (2003) Infect. Immun. , vol.71 , pp. 6199-6204
    • Loeffler, J.M.1    Djurkovic, S.2    Fischetti, V.A.3
  • 89
    • 0036231904 scopus 로고    scopus 로고
    • C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates
    • Loessner, M.J., Kramer, K., Ebel, F., Scherer, S., C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates. Mol. Microbiol. 44 (2002), 335–349.
    • (2002) Mol. Microbiol. , vol.44 , pp. 335-349
    • Loessner, M.J.1    Kramer, K.2    Ebel, F.3    Scherer, S.4
  • 90
    • 84901256994 scopus 로고    scopus 로고
    • A highly active and negatively charged streptococcus pyogenes lysin with a rare D-alanyl-L-alanine endopeptidase activity protects mice against streptococcal bacteremia
    • Lood, R., Raz, A., Molina, H., Euler, C.W., Fischetti, V.A., A highly active and negatively charged streptococcus pyogenes lysin with a rare D-alanyl-L-alanine endopeptidase activity protects mice against streptococcal bacteremia. Antimicrob. Agents Chemother. 58 (2014), 3073–3084, 10.1128/AAC.00115-14.
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 3073-3084
    • Lood, R.1    Raz, A.2    Molina, H.3    Euler, C.W.4    Fischetti, V.A.5
  • 91
    • 84928910762 scopus 로고    scopus 로고
    • Novel phage lysin capable of killing the multidrug-resistant gram-negative bacterium Acinetobacter baumannii in a mouse bacteremia model
    • Lood, R., Winer, B.Y., Pelzek, A.J., Díez-Martínez, R., Thandar, M., Euler, C.W., Schuch, R., Fischetti, V.A., Novel phage lysin capable of killing the multidrug-resistant gram-negative bacterium Acinetobacter baumannii in a mouse bacteremia model. Antimicrob. Agents Chemother. 59 (2015), 1983–1991, 10.1128/AAC.04641-14.
    • (2015) Antimicrob. Agents Chemother. , vol.59 , pp. 1983-1991
    • Lood, R.1    Winer, B.Y.2    Pelzek, A.J.3    Díez-Martínez, R.4    Thandar, M.5    Euler, C.W.6    Schuch, R.7    Fischetti, V.A.8
  • 92
    • 80053201228 scopus 로고    scopus 로고
    • Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins
    • Low, L.Y., Yang, C., Perego, M., Osterman, A., Liddington, R., Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins. J. Biol. Chem. 286 (2011), 34391–34403, 10.1074/jbc.M111.244160.
    • (2011) J. Biol. Chem. , vol.286 , pp. 34391-34403
    • Low, L.Y.1    Yang, C.2    Perego, M.3    Osterman, A.4    Liddington, R.5
  • 93
    • 85008512224 scopus 로고    scopus 로고
    • Past, present, and future of antibacterial economics: increasing bacterial resistance, limited antibiotic pipeline, and societal implications
    • Luepke, K.H., Suda, K.J., Boucher, H., Russo, R.L., Bonney, M.W., Hunt, T.D., Mohr, J.F., Past, present, and future of antibacterial economics: increasing bacterial resistance, limited antibiotic pipeline, and societal implications. Pharmacother. J. Hum. Pharmacol. Drug Ther. 37 (2017), 71–84, 10.1002/phar.1868.
    • (2017) Pharmacother. J. Hum. Pharmacol. Drug Ther. , vol.37 , pp. 71-84
    • Luepke, K.H.1    Suda, K.J.2    Boucher, H.3    Russo, R.L.4    Bonney, M.W.5    Hunt, T.D.6    Mohr, J.F.7
  • 94
    • 84870158000 scopus 로고    scopus 로고
    • Using a bacteriocin structure to engineer a phage lysin that targets Yersinia pestis
    • Lukacik, P., Barnard, T.J., Buchanan, S.K., Using a bacteriocin structure to engineer a phage lysin that targets Yersinia pestis. Biochem. Soc. Trans., 40(6), 2012, 1503, 10.1042/BST20120209.
    • (2012) Biochem. Soc. Trans. , vol.40 , Issue.6 , pp. 1503
    • Lukacik, P.1    Barnard, T.J.2    Buchanan, S.K.3
  • 96
    • 85046884197 scopus 로고    scopus 로고
    • Topical Applications - LYSANDO AG [WWW Document]
    • Lysando, Topical Applications - LYSANDO AG [WWW Document]. 2017.
    • (2017)
    • Lysando1
  • 97
    • 85004045015 scopus 로고    scopus 로고
    • Enhancement of the direct antimicrobial activity of Lysep3 against Escherichia coli by inserting cationic peptides into its C terminus
    • Ma, Q., Guo, Z., Gao, C., Zhu, R., Wang, S., Yu, L., Qin, W., Xia, X., Gu, J., Yan, G., Lei, L., Enhancement of the direct antimicrobial activity of Lysep3 against Escherichia coli by inserting cationic peptides into its C terminus. Antonie Van Leeuwenhoek 110 (2017), 347–355, 10.1007/s10482-016-0806-2.
    • (2017) Antonie Van Leeuwenhoek , vol.110 , pp. 347-355
    • Ma, Q.1    Guo, Z.2    Gao, C.3    Zhu, R.4    Wang, S.5    Yu, L.6    Qin, W.7    Xia, X.8    Gu, J.9    Yan, G.10    Lei, L.11
  • 99
    • 57349146775 scopus 로고    scopus 로고
    • Antimicrobial activity of a chimeric enzybiotic towards Staphylococcus aureus
    • Manoharadas, S., Witte, A., Bläsi, U., Antimicrobial activity of a chimeric enzybiotic towards Staphylococcus aureus. J. Biotechnol. 139 (2009), 118–123, 10.1016/j.jbiotec.2008.09.003.
    • (2009) J. Biotechnol. , vol.139 , pp. 118-123
    • Manoharadas, S.1    Witte, A.2    Bläsi, U.3
  • 100
    • 84876308417 scopus 로고    scopus 로고
    • Chimeric Ply187 endolysin kills Staphylococcus aureus more effectively than the parental enzyme
    • Mao, J., Schmelcher, M., Harty, W.J., Foster-Frey, J., Donovan, D.M., Chimeric Ply187 endolysin kills Staphylococcus aureus more effectively than the parental enzyme. FEMS Microbiol. Lett. 342 (2013), 30–36, 10.1111/1574-6968.12104.
    • (2013) FEMS Microbiol. Lett. , vol.342 , pp. 30-36
    • Mao, J.1    Schmelcher, M.2    Harty, W.J.3    Foster-Frey, J.4    Donovan, D.M.5
  • 101
    • 80053609598 scopus 로고    scopus 로고
    • Structure-based modification of a Clostridium difficile-targeting endolysin affects activity and host range
    • Mayer, M.J., Garefalaki, V., Spoerl, R., Narbad, A., Meijers, R., Structure-based modification of a Clostridium difficile-targeting endolysin affects activity and host range. J. Bacteriol. 193 (2011), 5477–5486, 10.1128/JB.00439-11.
    • (2011) J. Bacteriol. , vol.193 , pp. 5477-5486
    • Mayer, M.J.1    Garefalaki, V.2    Spoerl, R.3    Narbad, A.4    Meijers, R.5
  • 102
    • 84886292840 scopus 로고    scopus 로고
    • Stimuli-responsive nanocarriers for drug delivery
    • Mura, S., Nicolas, J., Couvreur, P., Stimuli-responsive nanocarriers for drug delivery. Nat. Mater. 12 (2013), 991–1003, 10.1038/nmat3776.
    • (2013) Nat. Mater. , vol.12 , pp. 991-1003
    • Mura, S.1    Nicolas, J.2    Couvreur, P.3
  • 103
    • 84996565674 scopus 로고    scopus 로고
    • Antibiofilm activity and synergistic inhibition of Staphylococcus aureus biofilms by bactericidal protein P128 in combination with antibiotics
    • Nair, S., Desai, S., Poonacha, N., Vipra, A., Sharma, U., Antibiofilm activity and synergistic inhibition of Staphylococcus aureus biofilms by bactericidal protein P128 in combination with antibiotics. Antimicrob. Agents Chemother. 60 (2016), 7280–7289, 10.1128/AAC.01118-16.
    • (2016) Antimicrob. Agents Chemother. , vol.60 , pp. 7280-7289
    • Nair, S.1    Desai, S.2    Poonacha, N.3    Vipra, A.4    Sharma, U.5
  • 104
    • 0036141647 scopus 로고    scopus 로고
    • Modulation of release of proinflammatory bacterial compounds by antibacterials: potential impact on course of inflammation and outcome in sepsis and meningitis
    • Nau, R., Eiffert, H., Modulation of release of proinflammatory bacterial compounds by antibacterials: potential impact on course of inflammation and outcome in sepsis and meningitis. Clin. Microbiol. Rev. 15 (2002), 95–110, 10.1128/CMR.15.1.95-110.2002.
    • (2002) Clin. Microbiol. Rev. , vol.15 , pp. 95-110
    • Nau, R.1    Eiffert, H.2
  • 105
    • 84930832473 scopus 로고    scopus 로고
    • Antimicrobial Resistance: Tackling a Crisis for the Health and Wealth of Nations The Review on Antimicrobial Resistance Chaired
    • Neill, J.O., Antimicrobial Resistance: Tackling a Crisis for the Health and Wealth of Nations The Review on Antimicrobial Resistance Chaired. 2014.
    • (2014)
    • Neill, J.O.1
  • 106
    • 0035957329 scopus 로고    scopus 로고
    • Prevention and elimination of upper respiratory colonization of mice by group A streptococci by using a bacteriophage lytic enzyme
    • Nelson, D., Loomis, L., Fischetti, V.A., Prevention and elimination of upper respiratory colonization of mice by group A streptococci by using a bacteriophage lytic enzyme. Proc. Natl. Acad. Sci. U. S. A. 98 (2001), 4107–4112, 10.1073/pnas.061038398.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 4107-4112
    • Nelson, D.1    Loomis, L.2    Fischetti, V.A.3
  • 108
    • 84887476185 scopus 로고    scopus 로고
    • In vitro characterization of PlySK1249, a novel phage lysin, and assessment of its antibacterial activity in a mouse model of Streptococcus agalactiae bacteremia
    • Oechslin, F., Daraspe, J., Giddey, M., Moreillon, P., Resch, G., In vitro characterization of PlySK1249, a novel phage lysin, and assessment of its antibacterial activity in a mouse model of Streptococcus agalactiae bacteremia. Antimicrob. Agents Chemother. 57 (2013), 6276–6283, 10.1128/AAC.01701-13.
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 6276-6283
    • Oechslin, F.1    Daraspe, J.2    Giddey, M.3    Moreillon, P.4    Resch, G.5
  • 109
    • 85046859427 scopus 로고    scopus 로고
    • The Sub-MIC Effect of Lysin CF-301 on Staphylococcus aureus (S. aureus) [ Document]. ASM Microbe, June 2.
    • Oh, J., Schuch, R., 2017. The Sub-MIC Effect of Lysin CF-301 on Staphylococcus aureus (S. aureus) [WWW Document]. ASM Microbe, June 2.
    • (2017)
    • Oh, J.1    Schuch, R.2
  • 111
    • 84988927829 scopus 로고    scopus 로고
    • Characterization and genome sequencing of a Citrobacter freundii phage CfP1 harboring a lysin active against multidrug-resistant isolates
    • Oliveira, H., Pinto, G., Oliveira, A., Oliveira, C., Faustino, M.A., Briers, Y., Domingues, L., Azeredo, J., Characterization and genome sequencing of a Citrobacter freundii phage CfP1 harboring a lysin active against multidrug-resistant isolates. Appl. Microbiol. Biotechnol. 100 (2016), 10543–10553, 10.1007/s00253-016-7858-0.
    • (2016) Appl. Microbiol. Biotechnol. , vol.100 , pp. 10543-10553
    • Oliveira, H.1    Pinto, G.2    Oliveira, A.3    Oliveira, C.4    Faustino, M.A.5    Briers, Y.6    Domingues, L.7    Azeredo, J.8
  • 112
    • 84962129551 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-gram-negative bacterial activity
    • Oliveira, H., Vilas Boas, D., Mesnage, S., Kluskens, L.D., Lavigne, R., Sillankorva, S., Secundo, F., Azeredo, J., Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-gram-negative bacterial activity. Front. Microbiol., 7, 2016, 208, 10.3389/fmicb.2016.00208.
    • (2016) Front. Microbiol. , vol.7 , pp. 208
    • Oliveira, H.1    Vilas Boas, D.2    Mesnage, S.3    Kluskens, L.D.4    Lavigne, R.5    Sillankorva, S.6    Secundo, F.7    Azeredo, J.8
  • 113
    • 3843065569 scopus 로고    scopus 로고
    • Bacillus amyloliquefaciens phage endolysin can enhance permeability of Pseudomonas aeruginosa outer membrane and induce cell lysis
    • Orito, Y., Morita, M., Hori, K., Unno, H., Tanji, Y., Bacillus amyloliquefaciens phage endolysin can enhance permeability of Pseudomonas aeruginosa outer membrane and induce cell lysis. Appl. Microbiol. Biotechnol. 65 (2004), 105–109, 10.1007/s00253-003-1522-1 https://link.springer.com/article/10.1007/s00253-003-1522-1.
    • (2004) Appl. Microbiol. Biotechnol. , vol.65 , pp. 105-109
    • Orito, Y.1    Morita, M.2    Hori, K.3    Unno, H.4    Tanji, Y.5
  • 114
    • 84937639167 scopus 로고    scopus 로고
    • Discovery of novel S. aureus autolysins and molecular engineering to enhance bacteriolytic activity
    • Osipovitch, D.C., Therrien, S., Griswold, K.E., Discovery of novel S. aureus autolysins and molecular engineering to enhance bacteriolytic activity. Appl. Microbiol. Biotechnol. 99 (2015), 6315–6326, 10.1007/s00253-015-6443-2.
    • (2015) Appl. Microbiol. Biotechnol. , vol.99 , pp. 6315-6326
    • Osipovitch, D.C.1    Therrien, S.2    Griswold, K.E.3
  • 115
    • 78751697614 scopus 로고    scopus 로고
    • A novel chimeric lysin shows superiority to mupirocin for skin decolonization of methicillin-resistant and -sensitive Staphylococcus aureus strains
    • Pastagia, M., Euler, C., Chahales, P., Fuentes-Duculan, J., Krueger, J.G., Fischetti, V.A., A novel chimeric lysin shows superiority to mupirocin for skin decolonization of methicillin-resistant and -sensitive Staphylococcus aureus strains. Antimicrob. Agents Chemother. 55 (2011), 738–744, 10.1128/AAC.00890-10.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 738-744
    • Pastagia, M.1    Euler, C.2    Chahales, P.3    Fuentes-Duculan, J.4    Krueger, J.G.5    Fischetti, V.A.6
  • 116
    • 84863613709 scopus 로고    scopus 로고
    • Structural and mechanistic studies of pesticin, a bacterial homolog of phage lysozymes
    • Patzer, S.I., Albrecht, R., Braun, V., Zeth, K., Structural and mechanistic studies of pesticin, a bacterial homolog of phage lysozymes. J. Biol. Chem. 287 (2012), 23381–23396, 10.1074/jbc.M112.362913.
    • (2012) J. Biol. Chem. , vol.287 , pp. 23381-23396
    • Patzer, S.I.1    Albrecht, R.2    Braun, V.3    Zeth, K.4
  • 118
  • 119
    • 85026363454 scopus 로고    scopus 로고
    • Efficient killing of planktonic and biofilm embedded coagulase-negative staphylococci by bactericidal protein P128
    • AAC.00457-17
    • Poonacha, N., Nair, S., Desai, S., Tuppad, D., Hiremath, D., Mohan, T., Vipra, A., Sharma, U., Efficient killing of planktonic and biofilm embedded coagulase-negative staphylococci by bactericidal protein P128. Antimicrob. Agents Chemother. 61:8 (2017), e00457–17 AAC.00457-17 https://doi.org/10.1128/AAC.00457-17.
    • (2017) Antimicrob. Agents Chemother. , vol.61 , Issue.8 , pp. e00457-17
    • Poonacha, N.1    Nair, S.2    Desai, S.3    Tuppad, D.4    Hiremath, D.5    Mohan, T.6    Vipra, A.7    Sharma, U.8
  • 121
    • 36649027884 scopus 로고    scopus 로고
    • LambdaSa1 and LambdaSa2 prophage lysins of Streptococcus agalactiae
    • https://doi.org/10.1128/AEM.01783-07
    • Pritchard, D.G., Dong, S., Kirk, M.C., Cartee, R.T., Baker, J.R., LambdaSa1 and LambdaSa2 prophage lysins of Streptococcus agalactiae. Appl. Environ. Microbiol. 73 (2007), 7150–7154 http://aem.asm.org/content/73/22/7150.full https://doi.org/10.1128/AEM.01783-07.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 7150-7154
    • Pritchard, D.G.1    Dong, S.2    Kirk, M.C.3    Cartee, R.T.4    Baker, J.R.5
  • 123
    • 85018310882 scopus 로고    scopus 로고
    • Lysibodies are IgG Fc fusions with lysin binding domains targeting Staphylococcus aureus wall carbohydrates for effective phagocytosis
    • Raz, A., Serrano, A., Lawson, C., Thaker, M., Alston, T., Bournazos, S., Ravetch, J.V., Fischetti, V.A., Lysibodies are IgG Fc fusions with lysin binding domains targeting Staphylococcus aureus wall carbohydrates for effective phagocytosis. Proc. Natl. Acad. Sci. U. S. A. 114 (2017), 4781–4786, 10.1073/pnas.1619249114.
    • (2017) Proc. Natl. Acad. Sci. U. S. A. , vol.114 , pp. 4781-4786
    • Raz, A.1    Serrano, A.2    Lawson, C.3    Thaker, M.4    Alston, T.5    Bournazos, S.6    Ravetch, J.V.7    Fischetti, V.A.8
  • 124
    • 80255133188 scopus 로고    scopus 로고
    • A stable phage lysin (Cpl-1) dimer with increased antipneumococcal activity and decreased plasma clearance
    • Resch, G., Moreillon, P., Fischetti, V.A., A stable phage lysin (Cpl-1) dimer with increased antipneumococcal activity and decreased plasma clearance. Int. J. Antimicrob. Agents 38 (2011), 516–521, 10.1016/j.ijantimicag.2011.08.009.
    • (2011) Int. J. Antimicrob. Agents , vol.38 , pp. 516-521
    • Resch, G.1    Moreillon, P.2    Fischetti, V.A.3
  • 125
    • 84863507788 scopus 로고    scopus 로고
    • PEGylating a bacteriophage endolysin inhibits its bactericidal activity
    • Resch, G., Moreillon, P., Fischetti, V.A., PEGylating a bacteriophage endolysin inhibits its bactericidal activity. AMB Express, 1, 2011, 29, 10.1186/2191-0855-1-29.
    • (2011) AMB Express , vol.1 , pp. 29
    • Resch, G.1    Moreillon, P.2    Fischetti, V.A.3
  • 126
    • 84947506478 scopus 로고    scopus 로고
    • Antimicrobial bacteriophage-derived proteins and therapeutic applications
    • Roach, D.R., Donovan, D.M., Antimicrobial bacteriophage-derived proteins and therapeutic applications. Bacteriophage, 5, 2015, e1062590, 10.1080/21597081.2015.1062590.
    • (2015) Bacteriophage , vol.5 , pp. e1062590
    • Roach, D.R.1    Donovan, D.M.2
  • 127
    • 84861148398 scopus 로고    scopus 로고
    • Enhanced staphylolytic activity of the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 HydH5 virion-associated peptidoglycan hydrolase: fusions, deletions, and synergy with LysH5
    • Rodríguez-Rubio, L., Martínez, B., Rodríguez, A., Donovan, D.M., García, P., Enhanced staphylolytic activity of the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 HydH5 virion-associated peptidoglycan hydrolase: fusions, deletions, and synergy with LysH5. Appl. Environ. Microbiol. 78 (2012), 2241–2248, 10.1128/AEM.07621-11.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 2241-2248
    • Rodríguez-Rubio, L.1    Martínez, B.2    Rodríguez, A.3    Donovan, D.M.4    García, P.5
  • 128
    • 84872841566 scopus 로고    scopus 로고
    • Potential of the virion-associated peptidoglycan hydrolase HydH5 and its derivative fusion proteins in milk biopreservation
    • Rodríguez-Rubio, L., Martínez, B., Donovan, D.M., García, P., Rodríguez, A., Potential of the virion-associated peptidoglycan hydrolase HydH5 and its derivative fusion proteins in milk biopreservation. PLoS One, 8, 2013, e54828, 10.1371/journal.pone.0054828.
    • (2013) PLoS One , vol.8 , pp. e54828
    • Rodríguez-Rubio, L.1    Martínez, B.2    Donovan, D.M.3    García, P.4    Rodríguez, A.5
  • 130
    • 85046867848 scopus 로고    scopus 로고
    • PK-PD Driver of Efficacy for CF-301, a Novel Anti-Staphylococcal Lysin: Implications for Human Target Dose [ Document]. ASM Microbe, June 18.
    • Rotolo, J.A., Ramirez, R.A., Schuch, R., Machacek, M., Khariton, T., Ghahramani, P., Wittekind, M., 2016. PK-PD Driver of Efficacy for CF-301, a Novel Anti-Staphylococcal Lysin: Implications for Human Target Dose [WWW Document]. ASM Microbe, June 18.
    • (2016)
    • Rotolo, J.A.1    Ramirez, R.A.2    Schuch, R.3    Machacek, M.4    Khariton, T.5    Ghahramani, P.6    Wittekind, M.7
  • 132
    • 85041608574 scopus 로고    scopus 로고
    • Inhibitory and bactericidal effect of Artilysin® Art-175 against colistin- resistant mcr-1-positive Escherichia coli isolates
    • Schirmeier, E., Zimmermann, P., Hofmann, V., Biebl, M., Gerstmans, H., Maervoet, V.E., Briers, Y., Inhibitory and bactericidal effect of Artilysin® Art-175 against colistin- resistant mcr-1-positive Escherichia coli isolates. Int. J. Antimicrob. Agents, 2017, 10.1016/j.ijantimicag.2017.08.027.
    • (2017) Int. J. Antimicrob. Agents
    • Schirmeier, E.1    Zimmermann, P.2    Hofmann, V.3    Biebl, M.4    Gerstmans, H.5    Maervoet, V.E.6    Briers, Y.7
  • 133
    • 84949975789 scopus 로고    scopus 로고
    • Bacteriophage endolysins: applications for food safety
    • Schmelcher, M., Loessner, M.J., Bacteriophage endolysins: applications for food safety. Curr. Opin. Biotechnol. 37 (2016), 76–87, 10.1016/j.copbio.2015.10.005.
    • (2016) Curr. Opin. Biotechnol. , vol.37 , pp. 76-87
    • Schmelcher, M.1    Loessner, M.J.2
  • 134
    • 77956573488 scopus 로고    scopus 로고
    • Rapid multiplex detection and differentiation of Listeria cells by use of fluorescent phage endolysin cell wall binding domains
    • Schmelcher, M., Shabarova, T., Eugster, M.R., Eichenseher, F., Tchang, V.S., Banz, M., Loessner, M.J., Rapid multiplex detection and differentiation of Listeria cells by use of fluorescent phage endolysin cell wall binding domains. Appl. Environ. Microbiol. 76 (2010), 5745–5756, 10.1128/AEM.00801-10.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 5745-5756
    • Schmelcher, M.1    Shabarova, T.2    Eugster, M.R.3    Eichenseher, F.4    Tchang, V.S.5    Banz, M.6    Loessner, M.J.7
  • 135
    • 84860389171 scopus 로고    scopus 로고
    • Domain shuffling and module engineering of Listeria phage endolysins for enhanced lytic activity and binding affinity
    • Schmelcher, M., Tchang, V.S., Loessner, M.J., Domain shuffling and module engineering of Listeria phage endolysins for enhanced lytic activity and binding affinity. Microb. Biotechnol. 4 (2011), 651–662, 10.1111/j.1751-7915.2011.00263.x.
    • (2011) Microb. Biotechnol. , vol.4 , pp. 651-662
    • Schmelcher, M.1    Tchang, V.S.2    Loessner, M.J.3
  • 136
    • 84867073569 scopus 로고    scopus 로고
    • Bacteriophage endolysins as novel antimicrobials
    • Schmelcher, M., Donovan, D.M., Loessner, M.J., Bacteriophage endolysins as novel antimicrobials. Future Microbiol 7 (2012), 1147–1171, 10.2217/fmb.12.97.
    • (2012) Future Microbiol , vol.7 , pp. 1147-1171
    • Schmelcher, M.1    Donovan, D.M.2    Loessner, M.J.3
  • 137
    • 84861123085 scopus 로고    scopus 로고
    • 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., Chimeric phage lysins act synergistically with lysostaphin to kill mastitis-causing Staphylococcus aureus in murine mammary glands. Appl. Environ. Microbiol. 78 (2012), 2297–2305, 10.1128/AEM.07050-11.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 2297-2305
    • Schmelcher, M.1    Powell, A.M.2    Becker, S.C.3    Camp, M.J.4    Donovan, D.M.5
  • 138
    • 84941994476 scopus 로고    scopus 로고
    • Synergistic streptococcal phage λSA2 and B30 endolysins kill streptococci in cow milk and in a mouse model of mastitis
    • Schmelcher, M., Powell, A.M., Camp, M.J., Pohl, C.S., Donovan, D.M., Synergistic streptococcal phage λSA2 and B30 endolysins kill streptococci in cow milk and in a mouse model of mastitis. Appl. Microbiol. Biotechnol. 99 (2015), 8475–8486, 10.1007/s00253-015-6579-0.
    • (2015) Appl. Microbiol. Biotechnol. , vol.99 , pp. 8475-8486
    • Schmelcher, M.1    Powell, A.M.2    Camp, M.J.3    Pohl, C.S.4    Donovan, D.M.5
  • 140
    • 85046844416 scopus 로고    scopus 로고
    • Post-antibiotic Effects of Lysin CF-301 Against Staphylococcus aureus in Human Serum [ Document]. ASM Microbe, June 20.
    • Schuch, R., 2016. Post-antibiotic Effects of Lysin CF-301 Against Staphylococcus aureus in Human Serum [WWW Document]. ASM Microbe, June 20.
    • (2016)
    • Schuch, R.1
  • 141
    • 0037158695 scopus 로고    scopus 로고
    • A bacteriolytic agent that detects and kills Bacillus anthracis
    • Schuch, R., Nelson, D., Fischetti, V.A., A bacteriolytic agent that detects and kills Bacillus anthracis. Nature 418 (2002), 884–889, 10.1038/nature01026.
    • (2002) Nature , vol.418 , pp. 884-889
    • Schuch, R.1    Nelson, D.2    Fischetti, V.A.3
  • 142
    • 84988422106 scopus 로고    scopus 로고
    • In vitro study of the antibacterial effect of the bacteriophage T5 thermostable endolysin on Escherichia coli cells
    • Shavrina, M.S., Zimin, A.A., Molochkov, N.V., Chernyshov, S.V., Machulin, A.V., Mikoulinskaia, G.V., In vitro study of the antibacterial effect of the bacteriophage T5 thermostable endolysin on Escherichia coli cells. J. Appl. Microbiol. 121 (2016), 1282–1290, 10.1111/jam.13251.
    • (2016) J. Appl. Microbiol. , vol.121 , pp. 1282-1290
    • Shavrina, M.S.1    Zimin, A.A.2    Molochkov, N.V.3    Chernyshov, S.V.4    Machulin, A.V.5    Mikoulinskaia, G.V.6
  • 143
    • 0029906313 scopus 로고    scopus 로고
    • Analysis of the catalytic domain of the lysin of the lactococcal bacteriophage Tuc2009 by chimeric gene assembling
    • Sheehan, M.M., García, J.L., López, R., García, P., Analysis of the catalytic domain of the lysin of the lactococcal bacteriophage Tuc2009 by chimeric gene assembling. FEMS Microbiol. Lett. 140 (1996), 23–28.
    • (1996) FEMS Microbiol. Lett. , vol.140 , pp. 23-28
    • Sheehan, M.M.1    García, J.L.2    López, R.3    García, P.4
  • 144
    • 0030824227 scopus 로고    scopus 로고
    • The lytic enzyme of the pneumococcal phage Dp-1: a chimeric lysin of intergeneric origin
    • Sheehan, M.M., García, J.L., López, R., García, P., The lytic enzyme of the pneumococcal phage Dp-1: a chimeric lysin of intergeneric origin. Mol. Microbiol. 25 (1997), 717–725, 10.1046/j.1365-2958.1997.5101880.x.
    • (1997) Mol. Microbiol. , vol.25 , pp. 717-725
    • Sheehan, M.M.1    García, J.L.2    López, R.3    García, P.4
  • 147
    • 80055002173 scopus 로고    scopus 로고
    • Specific detection of Campylobacter jejuni using the bacteriophage NCTC 12673 receptor binding protein as a probe
    • Singh, A., Arutyunov, D., McDermott, M.T., Szymanski, C.M., Evoy, S., Specific detection of Campylobacter jejuni using the bacteriophage NCTC 12673 receptor binding protein as a probe. Analyst, 136, 2011, 4780, 10.1039/c1an15547d.
    • (2011) Analyst , vol.136 , pp. 4780
    • Singh, A.1    Arutyunov, D.2    McDermott, M.T.3    Szymanski, C.M.4    Evoy, S.5
  • 148
    • 84863678359 scopus 로고    scopus 로고
    • Bacteriophage based probes for pathogen detection
    • Singh, A., Arutyunov, D., Szymanski, C.M., Evoy, S., Bacteriophage based probes for pathogen detection. Analyst, 137, 2012, 3405, 10.1039/c2an35371g.
    • (2012) Analyst , vol.137 , pp. 3405
    • Singh, A.1    Arutyunov, D.2    Szymanski, C.M.3    Evoy, S.4
  • 149
    • 84905403715 scopus 로고    scopus 로고
    • Intravitreal injection of the chimeric phage endolysin Ply187 protects mice from Staphylococcus aureus endophthalmitis
    • Singh, P.K., Donovan, D.M., Kumar, A., Intravitreal injection of the chimeric phage endolysin Ply187 protects mice from Staphylococcus aureus endophthalmitis. Antimicrob. Agents Chemother. 58 (2014), 4621–4629, 10.1128/AAC.00126-14.
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 4621-4629
    • Singh, P.K.1    Donovan, D.M.2    Kumar, A.3
  • 150
    • 49849102138 scopus 로고    scopus 로고
    • Towards on-site pathogen detection using antibody-based sensors
    • Skottrup, P.D., Nicolaisen, M., Justesen, A.F., Towards on-site pathogen detection using antibody-based sensors. Biosens. Bioelectron. 24 (2008), 339–348, 10.1016/j.bios.2008.06.045.
    • (2008) Biosens. Bioelectron. , vol.24 , pp. 339-348
    • Skottrup, P.D.1    Nicolaisen, M.2    Justesen, A.F.3
  • 151
    • 85046834281 scopus 로고    scopus 로고
    • Pharmacokinetics and efficacy of ectolysin P128 in a mouse model of systemic Methicillin Resistant Staphylococcus aureus (MRSA) infection [ Document]. ASM Microbe, June.
    • Sriram, B., Channabasappa, S., Chikkamadaiah, R., Durgaiah, M., Hariharan, S., Jayaraman, R., Kumar, S., Maheshwari, U., Nandish, P., 2017. Pharmacokinetics and efficacy of ectolysin P128 in a mouse model of systemic Methicillin Resistant Staphylococcus aureus (MRSA) infection [WWW Document]. ASM Microbe, June.
    • (2017)
    • Sriram, B.1    Channabasappa, S.2    Chikkamadaiah, R.3    Durgaiah, M.4    Hariharan, S.5    Jayaraman, R.6    Kumar, S.7    Maheshwari, U.8    Nandish, P.9
  • 154
    • 84964910629 scopus 로고    scopus 로고
    • Novel engineered peptides of a phage lysin as effective antimicrobials against multidrug-resistant acinetobacter Baumannii
    • Thandar, M., Lood, R., Winer, B.Y., Deutsch, D.R., Euler, C.W., Fischetti, V.A., Novel engineered peptides of a phage lysin as effective antimicrobials against multidrug-resistant acinetobacter Baumannii. Antimicrob. Agents Chemother. 60 (2016), 2671–2679, 10.1128/AAC.02972-15.
    • (2016) Antimicrob. Agents Chemother. , vol.60 , pp. 2671-2679
    • Thandar, M.1    Lood, R.2    Winer, B.Y.3    Deutsch, D.R.4    Euler, C.W.5    Fischetti, V.A.6
  • 155
    • 84992691719 scopus 로고    scopus 로고
    • Enhanced antibacterial activity of Acinetobacter baumannii bacteriophage ØABP-01 endolysin (LysABP-01) in combination with colistin
    • Thummeepak, R., Kitti, T., Kunthalert, D., Sitthisak, S., Enhanced antibacterial activity of Acinetobacter baumannii bacteriophage ØABP-01 endolysin (LysABP-01) in combination with colistin. Front. Microbiol., 7, 2016, 1402, 10.3389/fmicb.2016.01402.
    • (2016) Front. Microbiol. , vol.7
    • Thummeepak, R.1    Kitti, T.2    Kunthalert, D.3    Sitthisak, S.4
  • 156
    • 84870502596 scopus 로고    scopus 로고
    • A bacteriophage endolysin-based electrochemical impedance biosensor for the rapid detection of Listeria cells
    • Tolba, M., Ahmed, M.U., Tlili, C., Eichenseher, F., Loessner, M.J., Zourob, M., A bacteriophage endolysin-based electrochemical impedance biosensor for the rapid detection of Listeria cells. Analyst, 137, 2012, 5749, 10.1039/c2an35988j.
    • (2012) Analyst , vol.137 , pp. 5749
    • Tolba, M.1    Ahmed, M.U.2    Tlili, C.3    Eichenseher, F.4    Loessner, M.J.5    Zourob, M.6
  • 157
    • 85108124687 scopus 로고    scopus 로고
    • Successful treatment of chronic Staphylococcus aureus-related dermatoses with the topical endolysin staphefekt SA.100: a report of 3 cases
    • Totté, J.E.E., van Doorn, M.B., Pasmans, S.G.M.A., Successful treatment of chronic Staphylococcus aureus-related dermatoses with the topical endolysin staphefekt SA.100: a report of 3 cases. Case Rep. Dermatol. 9 (2017), 19–25, 10.1159/000473872.
    • (2017) Case Rep. Dermatol. , vol.9 , pp. 19-25
    • Totté, J.E.E.1    van Doorn, M.B.2    Pasmans, S.G.M.A.3
  • 158
    • 85015961490 scopus 로고    scopus 로고
    • Identification of peptidoglycan hydrolase constructs with synergistic staphylolytic activity in cow milk
    • (AEM.03445-16)
    • Verbree, C.T., Dätwyler, S.M., Meile, S., Eichenseher, F., Donovan, D.M., Loessner, M.J., Schmelcher, M., Identification of peptidoglycan hydrolase constructs with synergistic staphylolytic activity in cow milk. Appl. Environ. Microbiol. 83:7 (2017), e03445–16, 10.1128/AEM.03445-16 (AEM.03445-16).
    • (2017) Appl. Environ. Microbiol. , vol.83 , Issue.7 , pp. e03445-16
    • Verbree, C.T.1    Dätwyler, S.M.2    Meile, S.3    Eichenseher, F.4    Donovan, D.M.5    Loessner, M.J.6    Schmelcher, M.7
  • 159
    • 85034018109 scopus 로고    scopus 로고
    • Retraction for Verbree et al., “Identification of peptidoglycan hydrolase constructs with synergistic Staphylolytic activity in cow's milk.”
    • Verbree, C.T., Dätwyler, S.M., Meile, S., Eichenseher, F., Donovan, D.M., Loessner, M.J., Schmelcher, M., Retraction for Verbree et al., “Identification of peptidoglycan hydrolase constructs with synergistic Staphylolytic activity in cow's milk.”. Appl. Environ. Microbiol. 83 (2017), e02100–17, 10.1128/AEM.02100-17.
    • (2017) Appl. Environ. Microbiol. , vol.83 , pp. e02100-17
    • Verbree, C.T.1    Dätwyler, S.M.2    Meile, S.3    Eichenseher, F.4    Donovan, D.M.5    Loessner, M.J.6    Schmelcher, M.7
  • 161
    • 77956395636 scopus 로고    scopus 로고
    • Evaluation of paramagnetic beads coated with recombinant Listeria phage endolysin–derived cell-wall-binding domain proteins for separation of Listeria monocytogenes from raw milk in combination with culture-based and real-time polymerase cha
    • Walcher, G., Stessl, B., Wagner, M., Eichenseher, F., Loessner, M.J., Hein, I., Evaluation of paramagnetic beads coated with recombinant Listeria phage endolysin–derived cell-wall-binding domain proteins for separation of Listeria monocytogenes from raw milk in combination with culture-based and real-time polymerase cha. Foodborne Pathog. Dis. 7 (2010), 1019–1024, 10.1089/fpd.2009.0475.
    • (2010) Foodborne Pathog. Dis. , vol.7 , pp. 1019-1024
    • Walcher, G.1    Stessl, B.2    Wagner, M.3    Eichenseher, F.4    Loessner, M.J.5    Hein, I.6
  • 162
    • 84870749535 scopus 로고    scopus 로고
    • Characterization of modular bacteriophage endolysins from Myoviridae phages OBP, 201φ2-1 and PVP-SE1
    • Walmagh, M., Briers, Y., Santos, S.B. dos, Azeredo, J., Lavigne, R., Characterization of modular bacteriophage endolysins from Myoviridae phages OBP, 201φ2-1 and PVP-SE1. PLoS One, 7, 2012, e36991, 10.1371/journal.pone.0036991.
    • (2012) PLoS One , vol.7
    • Walmagh, M.1    Briers, Y.2    Santos, S.B.D.3    Azeredo, J.4    Lavigne, R.5
  • 163
    • 84870749535 scopus 로고    scopus 로고
    • Characterization of modular bacteriophage endolysins from Myoviridae phages OBP, 201phi2-1 and PVP-SE1
    • Walmagh, M., Briers, Y., Santos, S.B. dos, Azeredo, J., Lavigne, R., dos Santos, S.B., Azeredo, J., Lavigne, R., Characterization of modular bacteriophage endolysins from Myoviridae phages OBP, 201phi2-1 and PVP-SE1. PLoS One, 7, 2012, e36991, 10.1371/journal.pone.0036991.
    • (2012) PLoS One , vol.7
    • Walmagh, M.1    Briers, Y.2    Santos, S.B.D.3    Azeredo, J.4    Lavigne, R.5    dos Santos, S.B.6    Azeredo, J.7    Lavigne, R.8
  • 165
    • 0037311091 scopus 로고    scopus 로고
    • Improved pharmacokinetics and reduced antibody reactivity of lysostaphin conjugated to polyethylene glycol
    • Walsh, S., Shah, A., Mond, J., Improved pharmacokinetics and reduced antibody reactivity of lysostaphin conjugated to polyethylene glycol. Antimicrob. Agents Chemother. 47 (2003), 554–558, 10.1128/aac.47.2.554-558.2003.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 554-558
    • Walsh, S.1    Shah, A.2    Mond, J.3
  • 166
    • 85010755048 scopus 로고    scopus 로고
    • The antibacterial activity of E. coli bacteriophage lysin lysep3 is enhanced by fusing the Bacillus amyloliquefaciens bacteriophage endolysin binding domain D8 to the C-terminal region
    • Wang, S., Gu, J., Lv, M., Guo, Z., Yan, G., Yu, L., Du, C., Feng, X., Han, W., Sun, C., Lei, L., The antibacterial activity of E. coli bacteriophage lysin lysep3 is enhanced by fusing the Bacillus amyloliquefaciens bacteriophage endolysin binding domain D8 to the C-terminal region. J. Microbiol. 55 (2017), 403–408, 10.1007/s12275-017-6431-6.
    • (2017) J. Microbiol. , vol.55 , pp. 403-408
    • Wang, S.1    Gu, J.2    Lv, M.3    Guo, Z.4    Yan, G.5    Yu, L.6    Du, C.7    Feng, X.8    Han, W.9    Sun, C.10    Lei, L.11
  • 167
    • 84901809320 scopus 로고    scopus 로고
    • Antimicrobial Resistance: Global Report on Surveillance 2014
    • WHO
    • WHO, Antimicrobial Resistance: Global Report on Surveillance 2014. 2016, WHO.
    • (2016)
    • WHO1
  • 168
    • 84973594579 scopus 로고    scopus 로고
    • Cell wall hydrolases and antibiotics: exploiting synergy to create efficacious new antimicrobial treatments
    • Wittekind, M., Schuch, R., Cell wall hydrolases and antibiotics: exploiting synergy to create efficacious new antimicrobial treatments. Curr. Opin. Microbiol. 33 (2016), 18–24, 10.1016/j.mib.2016.05.006.
    • (2016) Curr. Opin. Microbiol. , vol.33 , pp. 18-24
    • Wittekind, M.1    Schuch, R.2
  • 171
    • 84866333863 scopus 로고    scopus 로고
    • Existence of separate domains in lysin PlyG for recognizing Bacillus anthracis spores and vegetative cells
    • Yang, H., Wang, D.-B., Dong, Q., Zhang, Z., Cui, Z., Deng, J., Yu, J., Zhang, X.-E., Wei, H., Existence of separate domains in lysin PlyG for recognizing Bacillus anthracis spores and vegetative cells. Antimicrob. Agents Chemother. 56 (2012), 5031–5039, 10.1128/AAC.00891-12.
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 5031-5039
    • Yang, H.1    Wang, D.-B.2    Dong, Q.3    Zhang, Z.4    Cui, Z.5    Deng, J.6    Yu, J.7    Zhang, X.-E.8    Wei, H.9
  • 172
    • 84987849551 scopus 로고    scopus 로고
    • Engineered bacteriophage lysins as novel anti-infectives
    • Yang, H., Yu, J., Wei, H., Engineered bacteriophage lysins as novel anti-infectives. Front. Microbiol., 5, 2014, 542, 10.3389/fmicb.2014.00542.
    • (2014) Front. Microbiol. , vol.5 , pp. 542
    • Yang, H.1    Yu, J.2    Wei, H.3
  • 173
    • 84891543534 scopus 로고    scopus 로고
    • Novel chimeric lysin with high-level antimicrobial activity against methicillin-resistant Staphylococcus aureus in vitro and in vivo
    • Yang, H., Zhang, Y., Yu, J., Huang, Y., Zhang, X.-E., Wei, H., Novel chimeric lysin with high-level antimicrobial activity against methicillin-resistant Staphylococcus aureus in vitro and in vivo. Antimicrob. Agents Chemother. 58 (2014), 536–542, 10.1128/AAC.01793-13.
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 536-542
    • Yang, H.1    Zhang, Y.2    Yu, J.3    Huang, Y.4    Zhang, X.-E.5    Wei, H.6
  • 174
    • 84948396142 scopus 로고    scopus 로고
    • A chimeolysin with extended-spectrum streptococcal host range found by an induced lysis-based rapid screening method
    • Yang, H., Linden, S.B., Wang, J., Yu, J., Nelson, D.C., Wei, H., A chimeolysin with extended-spectrum streptococcal host range found by an induced lysis-based rapid screening method. Sci. Rep., 5, 2015, 17257, 10.1038/srep17257.
    • (2015) Sci. Rep. , vol.5 , pp. 17257
    • Yang, H.1    Linden, S.B.2    Wang, J.3    Yu, J.4    Nelson, D.C.5    Wei, H.6
  • 175
    • 84954237133 scopus 로고    scopus 로고
    • Antibacterial activity of a novel peptide-modified lysin against Acinetobacter baumannii and Pseudomonas aeruginosa
    • Yang, H., Wang, M., Yu, J., Wei, H., Antibacterial activity of a novel peptide-modified lysin against Acinetobacter baumannii and Pseudomonas aeruginosa. Front. Microbiol., 6, 2015, 1471, 10.3389/fmicb.2015.01471.
    • (2015) Front. Microbiol. , vol.6 , pp. 1471
    • Yang, H.1    Wang, M.2    Yu, J.3    Wei, H.4
  • 176
    • 84996598379 scopus 로고    scopus 로고
    • Antibiofilm activities of a novel chimeolysin against Streptococcus mutans under physiological and cariogenic conditions
    • Yang, H., Bi, Y., Shang, X., Wang, M., Linden, S.B., Li, Y., Li, Y., Nelson, D.C., Wei, H., Antibiofilm activities of a novel chimeolysin against Streptococcus mutans under physiological and cariogenic conditions. Antimicrob. Agents Chemother. 60 (2016), 7436–7443, 10.1128/AAC.01872-16.
    • (2016) Antimicrob. Agents Chemother. , vol.60 , pp. 7436-7443
    • Yang, H.1    Bi, Y.2    Shang, X.3    Wang, M.4    Linden, S.B.5    Li, Y.6    Li, Y.7    Nelson, D.C.8    Wei, H.9
  • 177
    • 85008957040 scopus 로고    scopus 로고
    • A novel chimeric lysin with robust antibacterial activity against planktonic and biofilm methicillin-resistant Staphylococcus aureus
    • Yang, H., Zhang, H., Wang, J., Yu, J., Wei, H., A novel chimeric lysin with robust antibacterial activity against planktonic and biofilm methicillin-resistant Staphylococcus aureus. Sci. Rep., 7, 2017, 40182, 10.1038/srep40182.
    • (2017) Sci. Rep. , vol.7 , pp. 40182
    • Yang, H.1    Zhang, H.2    Wang, J.3    Yu, J.4    Wei, H.5
  • 178
    • 3042856527 scopus 로고    scopus 로고
    • Identification of a broadly active phage lytic enzyme with lethal activity against antibiotic-resistant Enterococcus faecalis and Enterococcus faecium
    • Yoong, P., Schuch, R., Nelson, D., Fischetti, V.A., Identification of a broadly active phage lytic enzyme with lethal activity against antibiotic-resistant Enterococcus faecalis and Enterococcus faecium. J. Bacteriol. 186 (2004), 4808–4812, 10.1128/JB.186.14.4808-4812.2004.
    • (2004) J. Bacteriol. , vol.186 , pp. 4808-4812
    • Yoong, P.1    Schuch, R.2    Nelson, D.3    Fischetti, V.A.4
  • 179
    • 84943247438 scopus 로고    scopus 로고
    • Sensitive and rapid detection of staphylococcus aureus in milk via cell binding domain of lysin
    • Yu, J., Zhang, Y., Zhang, Y., Li, H., Yang, H., Wei, H., Sensitive and rapid detection of staphylococcus aureus in milk via cell binding domain of lysin. Biosens. Bioelectron. 77 (2016), 366–371, 10.1016/j.bios.2015.09.058.
    • (2016) Biosens. Bioelectron. , vol.77 , pp. 366-371
    • Yu, J.1    Zhang, Y.2    Zhang, Y.3    Li, H.4    Yang, H.5    Wei, H.6
  • 181
    • 85013278144 scopus 로고    scopus 로고
    • The lytic activity of recombinant phage lysin LysKΔamidase against staphylococcal strains associated with bovine and human infections in the Jiangsu province of China
    • Zhou, Y., Zhang, H., Bao, H., Wang, X., Wang, R., The lytic activity of recombinant phage lysin LysKΔamidase against staphylococcal strains associated with bovine and human infections in the Jiangsu province of China. Res. Vet. Sci. 111 (2017), 113–119, 10.1016/j.rvsc.2017.02.011.
    • (2017) Res. Vet. Sci. , vol.111 , pp. 113-119
    • Zhou, Y.1    Zhang, H.2    Bao, H.3    Wang, X.4    Wang, R.5
  • 182
    • 0141926716 scopus 로고    scopus 로고
    • Genome and proteome of Listeria monocytogenes phage PSA: an unusual case for programmed + 1 translational frameshifting in structural protein synthesis
    • Zimmer, M., Sattelberger, E., Inman, R.B., Calendar, R., Loessner, M.J., Genome and proteome of Listeria monocytogenes phage PSA: an unusual case for programmed + 1 translational frameshifting in structural protein synthesis. Mol. Microbiol. 50 (2003), 303–317, 10.1046/j.1365-2958.2003.03684.x.
    • (2003) Mol. Microbiol. , vol.50 , pp. 303-317
    • Zimmer, M.1    Sattelberger, E.2    Inman, R.B.3    Calendar, R.4    Loessner, M.J.5


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