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PhoP-phoQ

Miller, S.I. Kukral, A.M. Mekalanos, J.J. A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence. Proc. Natl. Acad. Sci. USA, 86, 5054-5058 (1989)... [Pg.462]

Kasahara, M. Nakata, A. Shinagawa, H. Molecular analysis of the Escherichia coli phoP-phoQ operon. J. BacterioL, 174, 492-498 (1992)... [Pg.465]

Guo, L., Lim, K.B., Gunn, J.S., Bainbridge, B., Darveau, R.P., Hackett, M., Miller, S.I. Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ. Science 276 (1997) 250-253. [Pg.23]

Kawasaki, K., Ernst, R.K., Miller, S.I. 3-O-deacylation of lipid A by PagL, a PhoP/PhoQ-regulated deacylase of Salmonella typhimurium, modulates signaling through Toll-like receptor 4. J Biol Chem 279 (2004) 20044-20048. [Pg.23]

Gunn, 1., Miller, S. PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance. 1 Bacteriol 178 (1996) 6857-6864. [Pg.117]

Hohmann, E., Oletta, C., Miller, S. Evaluation of a phoP/phoQ-deleted, aroA-deleted live oral Salmonella typhi vaccine strain in human volunteers. Vaccine 14 (1996) 19-24. [Pg.118]

Kato, A., Tanabe, H., Utsumi, R. Molecular characterization of the PhoP-PhoQ two-component system in Escherichia coli K-12 identification of extracellular Mg2+-responsive promoters. J Bacteriol 181 (1999) 5516-5520. [Pg.118]

Lejona, S., Aguirre, A., Cabeza, M., Garcia Vescovi, E., Soncini, F. Molecular characterization of the Mg2+-responsive PhoP-PhoQ regulon in Salmonella enterica. J Bacteriol 185 (2003) 6287-6294. [Pg.119]

McPhee, J., Bains, M., Winsor, G., Lewenza, S., Kwasnicka, A., Brazas, M., Brinkman, F., Hancock, R. Contribution of the PhoP-PhoQ and PmrA-PmrB two-component regulatory systems to Mg2-t-induced gene regulation in Pseudomonas aeruginosa. J Bacteriol 188 (2006) 3995-4006. [Pg.119]

Tierrez, A., Garcia-del Portillo, F. The Salmonella membrane protein IgaA modulates the activity of the RcsC-YojN-RcsB and PhoP-PhoQ regulons. J Bacteriol 186 (2004) 7481-7489. [Pg.121]

Trent, M., Pabich, W., Raetz, C., Miller, S. A PhoP/PhoQ-induced Lipase (PagL) that catalyzes 3-O-deacylation of lipid A precursors in membranes of Salmonella typhimurium. J Biol Chem 276 (2001a) 9083-9092. [Pg.121]

Macfarlane, E.L., Kwasnicka, A., Hancock, R.E. Role of Pseudomonas aeruginosa PhoP-phoQ in resistance to antimicrobial cationic peptides and aminoglycosides. Microbiology 146(Pt 10) (2000) 2543-2554. [Pg.252]

Macfarlane EL, Kwasnicka A, Ochs MM, Hancock RE. PhoP-PhoQ homologues in Pseudomonas aeruginosa regn-late expression of the outer-membrane protein OprH and polymyxin B resistance. Mol Microbiol 1999 34(2) 305-16. [Pg.2894]

DiPetrillo, M. D., Tibbetts, T., Kleanthous, H., Killeen, K. P. and Hohmann, E. L. 1999, Safety and immunogenicity of phoP/phoQ-deleted Salmonella typhi expressing Helicobacter pylori urease in adult volunteers. Vaccine, 18 449-459 Donahue, J. P., Israel, D. A., Torres, V. J., Necheva, A. S. and Miller, G. G. 2002, Inactivation of a Helicobacter pylori DNA methyltransferase alters dnaK operon expression following host-cell adherence. FEMS Microbiol.Lett., 208 295-301 Donati, M., Moreno, S., Stomi, E., Tucci, A., Poll, L., Mazzoni, C., Varoli, O., Sambri,... [Pg.334]

Figure 3. Other regulated acylation reactions involved in E. coli lipid A biosynthesis under special conditions. The reactions catalyzed by LpxP (formerly known as Ddg) [59] and LpxY (also known as PagP or CrcA) [51] are shown. LpxP is a cold induced protein which incorporates an unsaturated 16 carbon fatty acyl chain in place of the laurate normally incorporated by HtrB. LpxY, the expression of which is activated by the PhoP/PhoQ system [51], is an outer membrane protein that incorporates palmitate to make hepta-acylated lipid A. LpxY is capable of acylating lipid X, lipid IVa, and lipid A, as well as Kdo2-lipid IVa (as shown). The physiological substrate is probably lipid A, given that LpxY is an outer membrane protein. Figure 3. Other regulated acylation reactions involved in E. coli lipid A biosynthesis under special conditions. The reactions catalyzed by LpxP (formerly known as Ddg) [59] and LpxY (also known as PagP or CrcA) [51] are shown. LpxP is a cold induced protein which incorporates an unsaturated 16 carbon fatty acyl chain in place of the laurate normally incorporated by HtrB. LpxY, the expression of which is activated by the PhoP/PhoQ system [51], is an outer membrane protein that incorporates palmitate to make hepta-acylated lipid A. LpxY is capable of acylating lipid X, lipid IVa, and lipid A, as well as Kdo2-lipid IVa (as shown). The physiological substrate is probably lipid A, given that LpxY is an outer membrane protein.
Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ. Science 276, 250-253. [Pg.1563]

See other pages where PhoP-phoQ is mentioned: [Pg.124]    [Pg.447]    [Pg.454]    [Pg.14]    [Pg.16]    [Pg.16]    [Pg.17]    [Pg.18]    [Pg.19]    [Pg.101]    [Pg.108]    [Pg.109]   
See also in sourсe #XX -- [ Pg.124 ]

See also in sourсe #XX -- [ Pg.12 , Pg.14 , Pg.15 , Pg.16 , Pg.108 , Pg.109 ]



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