Disulfide by design: a computational method for the rational design of disulfide bonds in proteins. Failed CTL/NK cell killing and cytokine hypersecretion are directly linked through prolonged synapse time. pH dependence of listeriolysin O aggregation and pore-forming ability. Bax assembly into rings and arcs in apoptotic mitochondria is linked to membrane pores. Defining the interaction of perforin with calcium and the phospholipid membrane. Monomer–monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins. Binding of perforin to membranes is sensitive to lipid spacing and not headgroup. Critical point fluctuations in supported lipid membranes. Calcium-dependent plasma membrane binding and cell lysis by perforin are mediated through its C2 domain: a critical role for aspartate residues 429, 435, 483, and 485 but not 491. Effects of MACPF/CDC proteins on lipid membranes. C., Mikelj, M., Dalla Serra, M., Froelich, C. Atomic force microscopy of membrane pore formation by cholesterol dependent cytolysins. Perforin forms transient pores on the target cell plasma membrane to facilitate rapid access of granzymes during killer cell attack. Human perforin employs different avenues to damage membranes. Perforin oligomers form arcs in cellular membranes: a locus for intracellular delivery of granzymes. Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC). Binding of human complement C8 to C9: role of the N-terminal modules in the C8α subunit. Conformational changes during pore formation by the perforin-related protein pleurotolysin. ![]() Structural basis of complement membrane attack complex formation. Structure of the poly-C9 component of the complement membrane attack complex. The structural basis for membrane binding and pore formation by lymphocyte perforin. Listeriolysin O membrane damaging activity involves arc formation and lineaction-implication for Listeria monocytogenes escape from phagocytic vacuole. Directly observing the lipid-dependent self-assembly and pore-forming mechanism of the cytolytic toxin listeriolysin O. Plasticity of listeriolysin O pores and its regulation by pH and unique histidine. Incomplete pneumolysin oligomers form membrane pores. ![]() Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin. ![]() Structural basis of pore formation by the bacterial toxin pneumolysin. The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation. ![]() Vertical collapse of a cytolysin prepore moves its transmembrane β-hairpins to the membrane. Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane β-sheet from a prepore intermediate. The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane β-hairpins. The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins. The membrane attack complex/perforin and cholesterol-dependent cytolysin (MACPF/CDC) superfamily of pore forming proteins. Giant MACPF/CDC pore forming toxins: a class of their own. Perforin and granzymes: function, dysfunction and human pathology.
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