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Pore formation, polymerization, hemolytic and leukotoxic effects of a new Enterobacter cloacae toxin neutralized by antiserum
(Elsevier Gmbh, 2005-04)
A new toxin of Enterobacter cloacae was purified and studied by SDS-PAGE electrophoresis with the purpose of investigating its ability to generate polymers and their molecular mass. Monomer of 13.3 kDa and structures of ...
Functional and Topological Studies with Trp-Containing Analogs of the Peptide StII(1-30) Derived From the N-Terminus of the Pore Forming Toxin Sticholysin II: Contribution to Understand its Orientation in Membrane
(Wiley-Blackwell, 2013-07-01)
Sticholysin II (St II) is the most potent cytolysin produced by the sea anemone Stichodactyla helianthus, exerting hemolytic activity via pore formation in membranes. The toxin's N-terminus contains an amphipathic alpha-helix ...
A pore-forming toxin enables Serratia a nonlytic egress from host cells
(Wiley Blackwell Publishing, Inc, 2016-08)
Several pathogens co-opt host intracellular compartments to survive and replicate, and they thereafter disperse progeny to prosper in a new niche. Little is known about strategies displayed by Serratia marcescens to defeat ...
Selective blockage of Serratia marcescens ShlA by nickel inhibits the pore-forming toxin-mediated phenotypes in eukaryotic cells
(Wiley Blackwell Publishing, Inc, 2019-05)
Serratia marcescens is an opportunistic pathogen with increasing incidence in clinical settings. This is mainly attributed to the timely expression of a wide diversity of virulence factors and intrinsic and acquired ...
Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II
(Wiley-Blackwell, 2006-01-01)
Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II
(Wiley-Blackwell, 2006-01-01)