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Alison D. O'Brien

Researcher at Uniformed Services University of the Health Sciences

Publications -  195
Citations -  19269

Alison D. O'Brien is an academic researcher from Uniformed Services University of the Health Sciences. The author has contributed to research in topics: Escherichia coli & Shiga toxin. The author has an hindex of 73, co-authored 194 publications receiving 18602 citations. Previous affiliations of Alison D. O'Brien include Albert Einstein College of Medicine & Bristol Royal Infirmary.

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Mutation of flgM attenuates virulence of Salmonella typhimurium, and mutation of fliA represses the attenuated phenotype.

TL;DR: Results demonstrate that flgM and fliA, two genes previously shown to regulate flagellar operons, are also involved in the regulation of expression of virulence of S. typhimurium and that this system may not be unique to the genus Salmonella.
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Purification and some properties of a Vero toxin from a human strain of Escherichia coli that is immunologically related to Shiga-like toxin II (VT2).

TL;DR: The purified toxin was cytotoxic to Vero cells, and showed lethal toxicity to mice when injected intraperitoneally, the LD50 being about 2.7 ng per mouse.
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Shiga-like toxin converting phage of enterohemorrhagic Escherichia coli strain 933

TL;DR: The present evidence demonstrates that strain 933 contains both the SLT-II converting phages like 933W and other sequences of DNA homologous with phage 933J that probably represent a defectiveSLT-I converting phage.
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In vivo formation of hybrid toxins comprising Shiga toxin and the Shiga-like toxins and role of the B subunit in localization and cytotoxic activity.

TL;DR: Differences in cytotoxin localization and host cell specificity were examined and the cytotoxic specificity and localization of the hybrid cytotoxins always corresponded to the activities of the native toxin possessing the same B subunit.
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Phase 1 Safety and Pharmacokinetic Study of Chimeric Murine-Human Monoclonal Antibody cαStx2 Administered Intravenously to Healthy Adult Volunteers

TL;DR: A chimeric mouse-human antibody that has neutralizing activity in a mouse model was produced and tested in healthy adult volunteers and was generally well tolerated, suggesting saturable elimination in HUS.