Results 301 to 310 of about 987,804 (362)
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Anesthesiology Clinics of North America, 2006
Exposures to toxins are prevalent, frequently complicate surgical emergencies, and impact critical care. A fundamental understanding of pathophysiologic principles and management strategies is essential for the anesthesiologist frequently responsible for the acute care of patients who have toxicologic exposures. Given their pervasiveness and ability to
John E, Sather, Hossam, Tantawy
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Exposures to toxins are prevalent, frequently complicate surgical emergencies, and impact critical care. A fundamental understanding of pathophysiologic principles and management strategies is essential for the anesthesiologist frequently responsible for the acute care of patients who have toxicologic exposures. Given their pervasiveness and ability to
John E, Sather, Hossam, Tantawy
openaire +2 more sources
Toxins: Bacterial and Marine Toxins
Clinics in Laboratory Medicine, 2006The term toxin refers in a specific way to a toxic substance of biologic origin; that is, a true toxin is a poison produced by a living organism. The purpose of this article is to review some of the most potentially dangerous toxins of concern today. Mechanisms of action, routes of exposure, diagnostic tools, and treatment recommendations are addressed.
Matthew, Salzman +2 more
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Annual Review of Cell and Developmental Biology, 2003
▪ Abstract  Anthrax toxin consists of three nontoxic proteins that associate in binary or ternary combinations to form toxic complexes at the surface of mammalian cells. One of these proteins, protective antigen (PA), transports the other two, edema factor (EF) and lethal factor (LF), to the cytosol.
R John, Collier, John A T, Young
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▪ Abstract  Anthrax toxin consists of three nontoxic proteins that associate in binary or ternary combinations to form toxic complexes at the surface of mammalian cells. One of these proteins, protective antigen (PA), transports the other two, edema factor (EF) and lethal factor (LF), to the cytosol.
R John, Collier, John A T, Young
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Current Opinion in Structural Biology, 1995
Crystal structures of shiga and pertussis toxins have recently revealed a remarkable degree of structural homology among the members of the AB5 class of bacterial toxins. Other structures have provided a detailed view of the molecular basis of receptor binding specificity of cholera toxin, and of the heat-labile enterotoxin of Escherichia coli.
E A, Merritt, W G, Hol
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Crystal structures of shiga and pertussis toxins have recently revealed a remarkable degree of structural homology among the members of the AB5 class of bacterial toxins. Other structures have provided a detailed view of the molecular basis of receptor binding specificity of cholera toxin, and of the heat-labile enterotoxin of Escherichia coli.
E A, Merritt, W G, Hol
openaire +2 more sources