-
1
-
-
33645227952
-
Bacteriophage endolysins as a novel class of antibacterial agents
-
J. Borysowski, B. Weber-Dabrowska, and A. Górski Bacteriophage endolysins as a novel class of antibacterial agents Exp. Biol. Med. 231 2006 366 377
-
(2006)
Exp. Biol. Med.
, vol.231
, pp. 366-377
-
-
Borysowski, J.1
Weber-Dabrowska, B.2
Górski, A.3
-
2
-
-
84868663036
-
Turning a new phage
-
L. Gravitz Turning a new phage Nat. Med. 18 2012 1318 1320
-
(2012)
Nat. Med.
, vol.18
, pp. 1318-1320
-
-
Gravitz, L.1
-
3
-
-
24944587206
-
Bacteriophage lytic enzymes: Novel anti-infectives
-
V.A. Fischetti Bacteriophage lytic enzymes: novel anti-infectives Trends Microbiol. 13 2005 491 496
-
(2005)
Trends Microbiol.
, vol.13
, pp. 491-496
-
-
Fischetti, V.A.1
-
4
-
-
66749132773
-
Bacteriophage and their lysins for elimination of infectious bacteria
-
S. O'Flaherty, R.P. Ross, and A. Coffey Bacteriophage and their lysins for elimination of infectious bacteria FEMS Microbiol. Rev. 33 2009 801 819
-
(2009)
FEMS Microbiol. Rev.
, vol.33
, pp. 801-819
-
-
O'Flaherty, S.1
Ross, R.P.2
Coffey, A.3
-
5
-
-
77955557492
-
Bacteriophage endolysins: A novel anti-infective to control gram-positive pathogens
-
V.A. Fischetti Bacteriophage endolysins: a novel anti-infective to control gram-positive pathogens Int. J. Med. Microbiol. 300 2010 357 362
-
(2010)
Int. J. Med. Microbiol.
, vol.300
, pp. 357-362
-
-
Fischetti, V.A.1
-
7
-
-
33847633917
-
A standardized approach for accurate quantification of murein hydrolase activity in high-throughput assays
-
Y. Briers, R. Lavigne, G. Volckaert, and K. Hertveldt A standardized approach for accurate quantification of murein hydrolase activity in high-throughput assays J. Biochem. Biophys. Methods 70 2007 531 533
-
(2007)
J. Biochem. Biophys. Methods
, vol.70
, pp. 531-533
-
-
Briers, Y.1
Lavigne, R.2
Volckaert, G.3
Hertveldt, K.4
-
8
-
-
0017184389
-
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
-
M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
-
(1976)
Anal. Biochem.
, vol.72
, pp. 248-254
-
-
Bradford, M.1
-
9
-
-
0014949207
-
Cleavage of structural proteins during the assembly of the head of bacteriophage T4
-
U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
-
(1970)
Nature
, vol.227
, pp. 680-685
-
-
Laemmli, U.K.1
-
10
-
-
84915758273
-
-
posessing lytic activity, 2412243
-
V. Pugachev, O. Totmenina, V. Repin, N. Kljachko, and P. Levashov Strain of Salmonella Typhimurium Bacteriophage S-394 posessing lytic activity, 2412243 2009
-
(2009)
Strain of Salmonella Typhimurium Bacteriophage S-394
-
-
Pugachev, V.1
Totmenina, O.2
Repin, V.3
Kljachko, N.4
Levashov, P.5
-
11
-
-
70350437756
-
Position paper: The creation of a rational scheme for the nomenclature of viruses of bacteria and archaea
-
A.M. Kropinski, D. Prangishvili, and R. Lavigne Position paper: the creation of a rational scheme for the nomenclature of viruses of bacteria and archaea Environ. Microbiol. 11 2009 2775 2777
-
(2009)
Environ. Microbiol.
, vol.11
, pp. 2775-2777
-
-
Kropinski, A.M.1
Prangishvili, D.2
Lavigne, R.3
-
12
-
-
56649094151
-
Identication of host receptor and receptor-bindingmodule of a newly sequenced T5-like phage EPS7
-
J. Hong, K.-P. Kim, S. Heu, S.J. Lee, S. Adhya, and S. Ryu Identication of host receptor and receptor-bindingmodule of a newly sequenced T5-like phage EPS7 FEMS Microbiol. Lett. 289 2008 202 209
-
(2008)
FEMS Microbiol. Lett.
, vol.289
, pp. 202-209
-
-
Hong, J.1
Kim, K.-P.2
Heu, S.3
Lee, S.J.4
Adhya, S.5
Ryu, S.6
-
13
-
-
71949115542
-
Identification and characterization of the metal ion-dependent L-alanoyl-D-glutamate peptidase encoded by bacteriophage T5
-
G. Mikoulinskaia, I. Odinokova, A. Zimin, V. Lysanskaya, S. Feofanov, and O. Stepnaya Identification and characterization of the metal ion-dependent L-alanoyl-D-glutamate peptidase encoded by bacteriophage T5 FEBS J. 276 2009 7329 7342
-
(2009)
FEBS J.
, vol.276
, pp. 7329-7342
-
-
Mikoulinskaia, G.1
Odinokova, I.2
Zimin, A.3
Lysanskaya, V.4
Feofanov, S.5
Stepnaya, O.6
-
14
-
-
0014272375
-
Rapid fixed-time assay for penicillinase
-
M.G. Sargent Rapid fixed-time assay for penicillinase J. Bacteriol. 95 1968 1493 1494
-
(1968)
J. Bacteriol.
, vol.95
, pp. 1493-1494
-
-
Sargent, M.G.1
-
16
-
-
80055107985
-
Genomic and proteomic characterization of the broad-host-range Salmonella phage PVP-SE1: Creation of a new phage genus
-
S.B. Santos, A.M. Kropinski, P.-J. Ceyssens, H.-W. Ackermann, A. Villegas, and R. Lavigne Genomic and proteomic characterization of the broad-host-range Salmonella phage PVP-SE1: creation of a new phage genus J. Virol. 85 2011 11265 11273
-
(2011)
J. Virol.
, vol.85
, pp. 11265-11273
-
-
Santos, S.B.1
Kropinski, A.M.2
Ceyssens, P.-J.3
Ackermann, H.-W.4
Villegas, A.5
Lavigne, R.6
-
17
-
-
79551681153
-
Use of bacteriophage endolysin EL188 and outer membrane permeabilizers against pseudomonas aeruginosa
-
Y. Briers, M. Walmagh, and R. Lavigne Use of bacteriophage endolysin EL188 and outer membrane permeabilizers against pseudomonas aeruginosa J. Appl. Microbiol. 110 2011 778 785
-
(2011)
J. Appl. Microbiol.
, vol.110
, pp. 778-785
-
-
Briers, Y.1
Walmagh, M.2
Lavigne, R.3
-
19
-
-
22544471225
-
Bacteriophage endolysins - Current state of research and applications
-
M.J. Loessner Bacteriophage endolysins - current state of research and applications Curr. Opin. Microbiol. 8 2005 480 487
-
(2005)
Curr. Opin. Microbiol.
, vol.8
, pp. 480-487
-
-
Loessner, M.J.1
-
20
-
-
0026802197
-
Agents that increase the permeability of the outer membrane
-
M. Vaara Agents that increase the permeability of the outer membrane Microbiol. Rev. 56 1992 395 411
-
(1992)
Microbiol. Rev.
, vol.56
, pp. 395-411
-
-
Vaara, M.1
-
21
-
-
0035018312
-
CENTA as a chromogenic substrate for studying beta-lactamases
-
C. Bebrone, C. Moali, F. Mahy, S. Rival, J.D. Docquier, and G.M. Rossolini CENTA as a chromogenic substrate for studying beta-lactamases Antimicrob. Agents Chemother. 45 2001 1868 1871
-
(2001)
Antimicrob. Agents Chemother.
, vol.45
, pp. 1868-1871
-
-
Bebrone, C.1
Moali, C.2
Mahy, F.3
Rival, S.4
Docquier, J.D.5
Rossolini, G.M.6
-
23
-
-
34447550839
-
Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against gram-negative pathogens
-
J. Andrä, D. Monreal, G.M. de Tejada, C. Olak, G. Brezesinski, and S.S. Gomez Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against gram-negative pathogens J. Biol. Chem. 282 2007 14719 14728
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 14719-14728
-
-
Andrä, J.1
Monreal, D.2
De Tejada, G.M.3
Olak, C.4
Brezesinski, G.5
Gomez, S.S.6
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