Results 221 to 230 of about 33,056 (253)

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, M Dalla Serra, P Lazarovici   +2 more
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How Lipid Membranes Affect Pore Forming Toxin Activity

Accounts of Chemical Research, 2015
Pore forming toxins (PFTs) evolved to permeate the plasma membrane of target cells. This is achieved in a multistep mechanism that usually involves binding of soluble protein monomer to the lipid membrane, oligomerization at the plane of the membrane, and insertion of part of the polypeptide chain across the lipid membrane to form a conductive channel.
Nejc, Rojko, Gregor, Anderluh
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Pore-Forming Bacterial Protein Toxins: An Overview

2001
Among the ca. 325 protein toxins produced by gram-positive and gram-negative bacteria so far identified (Alouf 2000), at least 115 (35%) belong to the group of the so-called membrane-damaging toxins (MDTs). The most characteristic feature of these effectors is to damage or disrupt the cytoplasmic phospholipid bilayer membrane (7–9nm) of appropriate ...
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Activation induced by pore-forming bacterial toxins

Trends in Microbiology, 2001
Pore-forming bacterial toxins are considered to be the principal virulence factors contributing to severe inflammatory diseases in humans and animals. The pore-forming toxins are released from Gram-negative bacteria as soluble monomeric proteins, which then assemble into oligomeric pores on their target cell membranes.
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The Family of Serratia Type Pore Forming Toxins

Current Protein & Peptide Science, 2005
The 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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Biology and evolution of bacterial toxin–antitoxin systems

Nature Reviews Microbiology, 2022
Dukas Jurenas, Nathan Fraikin, Frédéric Goormaghtigh   +2 more
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