Authors:
Trent, MS
Ribeiro, AA
Lin, SH
Cotter, RJ
Raetz, CRH
Citation: Ms. Trent et al., An inner membrane enzyme in Salmonella and Escherichia coli that transfers4-amino-4-deoxy-L-arabinose to lipid A - Induction in polymyxin-resistant mutants and role of a novel lipid-linked donor, J BIOL CHEM, 276(46), 2001, pp. 43122-43131
Authors:
Trent, MS
Ribeiro, AA
Doerrler, WT
Lin, SH
Cotter, RJ
Raetz, CRH
Citation: Ms. Trent et al., Accumulation of a polyisoprene-linked amino sugar in polymyxin-resistant Salmonella typhimurium and Escherichia coli - Structural characterization and transfer to lipid A in the periplasm, J BIOL CHEM, 276(46), 2001, pp. 43132-43144
Authors:
Trent, MS
Pabich, W
Raetz, CRH
Miller, SI
Citation: Ms. Trent et al., A PhoP/PhoQ-induced lipase (PagL) that catalyzes 3-O-deacylation of lipid a precursors in membranes of Salmonella typhimurium, J BIOL CHEM, 276(12), 2001, pp. 9083-9092
Authors:
Worsham, LMS
Trent, MS
Earls, L
Jolly, C
Ernst-Fonberg, ML
Citation: Lms. Worsham et al., Insights into the catalytic mechanism of HlyC, the internal protein acyltransferase that activates Escherichia coli hemolysin toxin, BIOCHEM, 40(45), 2001, pp. 13607-13616
Authors:
Bishop, RE
Gibbons, HS
Guina, T
Trent, MS
Miller, SI
Raetz, CRH
Citation: Re. Bishop et al., Transfer of palmitate from phospholipids to lipid A in outer membranes of Gram-negative bacteria, EMBO J, 19(19), 2000, pp. 5071-5080
Citation: Ms. Trent et al., HlyC, the internal protein acyltransferase that activates hemolysin toxin:Roles of various conserved residues in enzymatic activity as probed by site-directed mutagenesis, BIOCHEM, 38(29), 1999, pp. 9541-9548
Citation: Ms. Trent et al., HlyC, the internal protein acyltransferase that activates hemolysin toxin:The role of conserved tyrosine and arginine residues in enzymatic activityas probed by chemical modification and site-directed mutagenesis, BIOCHEM, 38(27), 1999, pp. 8831-8838
Citation: Ms. Trent et al., HlyC, the internal protein acyltransferase that activates hemolysin toxin:Role of conserved histidine, serine, and cysteine residues in enzymatic activity as probed by chemical modification and site-directed mutagenesis, BIOCHEM, 38(11), 1999, pp. 3433-3439