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Staphylococcal Pore-Forming Toxins
2001Together with Pseudomonas aeruginosa and Escherichia coli, Staphylococcus aureus (S. aureus) is the most frequently isolated bacteria in routine hospital testing. Like the two other pathogens, S. aureus may synthesize numerous virulence factors, develop multiple resistances to antibiotics, and be responsible for numerous no-socomial infections.
G, Prévost +3 more
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Liposomes in the Study of Pore-Forming Toxins
2003Publisher Summary Liposomes are the most practical and useful model system to study the effects of pore-forming toxins (PFTs) and similar agents. Compared with other systems, such as bilayer lipid membranes BLMs, they may not provide the same level of molecular detail about some specific aspects of the interaction but certainly have the advantage of ...
DALLA SERRA M, MENESTRINA G
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Staphylococcus aureus Pore-Forming Toxins
2016Staphylococcus aureus (S. aureus) is a formidable foe equipped with an armamentarium of virulence factors to thwart host defenses and establish a successful infection. Among these virulence factors, S. aureus produces several potent secreted proteins that act as cytotoxins, predominant among them the beta-barrel pore-forming toxins.
Tamara, Reyes-Robles, Victor J, Torres
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Lysenin: A sphingomyelin specific pore-forming toxin
Biochimica et Biophysica Acta (BBA) - General Subjects, 2008Sphingomyelin is a major sphingolipid in mammalian cells. Recent results indicate that sphingomyelin is a reservoir of lipid second messengers, ceramide and sphingosine-1-phosphate. Sphingomyelin is also a major component of sphingolipid and cholesterol-rich membrane domains (lipid rafts).
Hidehiko, Shogomori +1 more
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Serratia Type Pore Forming Toxins
Current Protein & Peptide Science, 2000The Serratia marcescens hemolysin represents a new type of hemolysin and has been studied in great molecular detail with regard to structure, activation and secretion. It has nothing in common with the pore forming toxins of E. coli type (RTX toxins), the Staphylococcus aureus alpha-toxin or the thiol activated toxin of group A beta-hemolytic ...
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Cooperative Assembly of -Barrel Pore-Forming Toxins
Journal of Biochemistry, 2004Bacterial beta-barrel pore-forming toxins are secreted as water-soluble monomeric proteins and assemble into beta-barrel-shaped pores/channels through membranes of target cells, causing cell death and lysis. The pore assemblies that undergo various intermediate stages are symbolized by the association of multi-subunit structures in cells.
Vananh T, Nguyen, Yoshiyuki, Kamio
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Architecture of the pore forming toxin sticholysin I in membranes
Journal of Structural Biology, 2019Sticholysin I (StI) is a toxin produced by the sea anemone Stichodactyla helianthus and belonging to the actinoporins family. Upon binding to sphingomyelin-containing membranes StI forms oligomeric pores, thereby leading to cell death. According to recent controversial experimental evidences, the pore architecture of actinoporins is a debated topic ...
Yadira P, Hervis +8 more
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Pore-forming peptides and protein toxins
2003PART 1 PORE-FORMING PROTEINS Staphylococcal Bicomponent Leucotoxins, Mechanisms of Action, Impact on Cells and Contribution to Virulence, Gilles Prevost, Gianfranco Menestrina, Didier A. Colin, Sandra Werner, Stephen Bronner, Mauro Dalla Serra, Lamin Baba Moussa, Manual Coraiola, Alain Gravet, and Henri Monteil The Formulation of Ion-permeable Channels
G Menestrina +2 more
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The Sensing of Membrane Microdomains Based on Pore-Forming Toxins
Current Medicinal Chemistry, 2013Membrane rafts are transient and unstable membrane microdomains that are enriched in sphingolipids, cholesterol, and specific proteins. They are involved in intracellular trafficking, signal transduction, pathogen entry, and attachment of various ligands.
M, Skočaj +5 more
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The Family of Serratia Type Pore Forming Toxins
Current Protein & Peptide Science, 2005The Serratia marcescens hemolysin represents the prototype of a growing family of pore forming toxins. The available bacterial genome sequences reveal Serratia hemolysin homologues in additional species. However, only S. marcescens hemolysin has been studied in great molecular detail.
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