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Pore-Forming Toxins

2001
Pore-forming bacterial protein toxins: an overview * The cholesterol-dependent cytolysins * Aerolysin from aeromonas hydrophyla and related toxins * Staphylococcal pore-forming toxins * RTX toxin structure and function, a story of numerous anomalies and few analogies in toxin biology * Helicobacter pylori vacuolating cytotoxin: cell intoxication and ...
Menestrina G, Dalla Serra M
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Pore-forming toxins in Cnidaria

Seminars in Cell & Developmental Biology, 2017
The ancient phylum of Cnidaria contains many aquatic species with peculiar lifestyle. In order to survive, these organisms have evolved attack and defense mechanisms that are enabled by specialized cells and highly developed venoms. Pore-forming toxins are an important part of their venomous arsenal.
Marjetka, Podobnik, Gregor, Anderluh
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Epsilon toxin: a fascinating pore‐forming toxin

The FEBS Journal, 2011
Epsilon toxin (ETX) is produced by strains of Clostridium perfringens classified as type B or type D. ETX belongs to the heptameric β‐pore‐forming toxins including aerolysin and Clostridium septicum alpha toxin, which are characterized by the formation of a pore through the plasma membrane of eukaryotic cells consisting in a β‐barrel of 14 amphipatic β 
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Staphylococcus aureus Pore-Forming Toxins

2016
Staphylococcus 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, 2008
Sphingomyelin 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, 2000
The 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, 2004
Bacterial 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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Pore-forming toxins from pathogenic amoebae

Applied Microbiology and Biotechnology, 2014
Some amoeboid protozoans are facultative or obligate parasites in humans and bear an enormous cytotoxic potential that can result in severe destruction of host tissues and fatal diseases. Pathogenic amoebae produce soluble pore-forming polypeptides that bind to prokaryotic and eukaryotic target cell membranes and generate pores upon insertion and ...
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Liposomes in the Study of Pore-Forming Toxins

2003
Publisher 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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Pore-forming peptides and protein toxins

2003
PART 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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