Structures of a synthetic antibody selected against and bound to the C-terminal domain of Clostridium perfringens enterotoxin. [PDF]
Ogbu CP +5 more
europepmc +1 more source
Cryo-EM structures of Clostridium perfringens enterotoxin bound to its human receptor, claudin-4. [PDF]
Rathnayake SS +3 more
europepmc +1 more source
Sporulation and enterotoxin regulation by sigma factors in Clostridium perfringens
Clostridium perfringens is a leading cause of food poisoning annually in the United States. Ingested C. perfringens vegetative cells respond to the acidic conditions of the stomach by initiating sporulation.
Harry, Kathryn Helene
core
Processing of <i>Clostridium perfringens</i> Enterotoxin by Intestinal Proteases. [PDF]
Shrestha A +4 more
europepmc +1 more source
Trans-Mediated, Cis-Inhibited Paradoxal Activity of <i>Clostridium perfringens</i> Enterotoxin (c-CPE) in Modulating Epithelial Permeability. [PDF]
Sanchez JM +10 more
europepmc +1 more source
The interaction of Clostridium perfringens enterotoxin with receptor claudins. [PDF]
Shrestha A, Uzal FA, McClane BA.
europepmc +1 more source
Role of Clostridium perfringens Enterotoxin on YAP Activation in Colonic Sessile Serrated Adenoma/ Polyps with Dysplasia. [PDF]
Fujiwara-Tani R +13 more
europepmc +1 more source
Choque séptico fulminante neonatal por Clostridium perfringens
Clostridium spp. es un bacilo grampositivos, anaerobio, formador de esporas y ampliamente distribuido en el ambiente. Las infecciones por Clostridium perfringens en neonatos son en extremo raras.
Naranjo-Bustamante, Natalí +4 more
core
Size-selective permeation-enhancing modulation of the tight junction by receptor-binding domains of <i>Clostridium perfringens</i> enterotoxin and <i>Clostridium perfringens</i> iota-toxin. [PDF]
Tachibana K +8 more
europepmc +1 more source
Bystander Host Cell Killing Effects of Clostridium perfringens Enterotoxin. [PDF]
Shrestha A +3 more
europepmc +1 more source

