Opening of smaller toxin pores by lipid micelle formation
نویسندگان
چکیده
منابع مشابه
suppression of coke formation in thermal cracking by coke inhibitors
the main purpose of this research was to:1.develop a coking model for thermal cracking of naphtha.2.study coke inhibition methods using different coke inhibitors.developing a coking model in naphtha cracking reactors requires a suitable model of the thermal cracking reactor based on a reliable kinetic model.to obtain reliable results all these models shall be solved simultaneously.for this pu...
15 صفحه اولOpening closed pores
JCB • VOLUME 167 • NUMBER 6 • 2004 994 Opening closed pores closed mitosis may be less closed than was thought, based on results from Colin De Souza, Stephen Osmani, and colleagues (The Ohio State University, Columbus, OH). The authors find that a fungus opens nuclear pores during mitosis to permit diffusion into and out of the nucleus. Simple organisms may thus be viable model systems for the ...
متن کاملPore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures.
Pore formation in the target cell membranes is a common mechanism used by many toxins in order to kill cells. Among various described mechanisms, a toroidal pore concept was described recently in the course of action of small antimicrobial peptides. Here we provide evidence that such mechanism may be used also by larger toxins. Membrane-destabilizing effects of equinatoxin II, a sea anemone cyt...
متن کاملPersister-promoting bacterial toxin TisB produces anion-selective pores in planar lipid bilayers.
We studied membrane activity of the bacterial peptide TisB involved in persister cell formation. TisB and its analogs form multi-state ion-conductive pores in planar lipid bilayers with all states displaying similar anionic selectivity. TisB analogs differing by ±1 elementary charges show corresponding changes in selectivity. Probing TisB pores with poly-(ethylene glycol)s reveals only restrict...
متن کاملThe vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH.
Pathogenic strains of Helicobacter pylori secrete a cytotoxin, VacA, that in the presence of weak bases, causes osmotic swelling of acidic intracellular compartments enriched in markers for late endosomes and lysosomes. The molecular mechanisms by which VacA causes this vacuolation remain largely unknown. At neutral pH, VacA is predominantly a water-soluble dodecamer formed by two apposing hexa...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2020
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1921467117