نتایج جستجو برای: Pore-forming toxin

تعداد نتایج: 200158  

Introduction: Chemotherapy has been restricted due to the high-dose side effects. In the present study, acceleration of the chemotherapeutic drug (5FU) entrance into MCF-7 cells has been explored by using a recombinant form of Fragaceatoxin C (FraC) pore-forming toxin. Methods: In this experimental study, the gene for FraC toxin was order from a commercial source and was sub-cloned into pET28a...

Journal: :The Journal of biological chemistry 1998
K H Krause M Fivaz A Monod F G van der Goot

Aerolysin is a pore-forming toxin that plays a key role in the pathogenesis of Aeromonas hydrophila infections. In this study, we have analyzed the effect of aerolysin on human granulocytes (HL-60 cells). Proaerolysin could bind to these cells, was processed into active aerolysin, and led to membrane depolarization, indicating that granulocytes are potential targets for this toxin. Fura-2 measu...

1998
Karl-Heinz Krause Marc Fivaz Antoinette Monod F. Gisou van der Goot

Aerolysin is a pore-forming toxin that plays a key role in the pathogenesis of Aeromonas hydrophila infections. In this study, we have analyzed the effect of aerolysin on human granulocytes (HL-60 cells). Proaerolysin could bind to these cells, was processed into active aerolysin, and led to membrane depolarization, indicating that granulocytes are potential targets for this toxin. Fura-2 measu...

Journal: :Biochimica et biophysica acta 2008
Hidehiko Shogomori Toshihide Kobayashi

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). Lysenin is a pore-forming toxin that specifically binds sphingomyelin. The binding of lysenin to sphingomy...

2015
Stephan Benke Daniel Roderer Bengt Wunderlich Daniel Nettels Rudi Glockshuber Benjamin Schuler

Pore-forming toxins are protein assemblies used by many organisms to disrupt the membranes of target cells. They are expressed as soluble monomers that assemble spontaneously into multimeric pores. However, owing to their complexity, the assembly processes have not been resolved in detail for any pore-forming toxin. To determine the assembly mechanism for the ring-shaped, homododecameric pore o...

2015
Y. Tanaka

Y. Tanaka and M. Yao (Hokkaido Univ.) Pathogenic bacteria express pore-forming toxins (PFTs) to attack host cells. PFTs are expressed as soluble monomeric proteins, which assemble to prepore oligomer on the target cells. After forming prepore, conformational change occurs, and then the pore is formed. Although the crystal structures of monomer and pore have been determined, the detailed mechani...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2004
Danielle L Huffman Laurence Abrami Roman Sasik Jacques Corbeil F Gisou van der Goot Raffi V Aroian

Cytolytic pore-forming toxins are important for the virulence of many disease-causing bacteria. How target cells molecularly respond to these toxins and whether or not they can mount a defense are poorly understood. By using microarrays, we demonstrate that the nematode Caenorhabditis elegans responds robustly to Cry5B, a member of the pore-forming Crystal toxin family made by Bacillus thuringi...

2013
Jessica Huyet Claire E. Naylor Christos G. Savva Maryse Gibert Michel R. Popoff Ajit K. Basak

Clostridium perfringens Delta toxin is one of the three hemolysin-like proteins produced by C. perfringens type C and possibly type B strains. One of the others, NetB, has been shown to be the major cause of Avian Nectrotic Enteritis, which following the reduction in use of antibiotics as growth promoters, has become an emerging disease of industrial poultry. Delta toxin itself is cytotoxic to ...

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