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Randall K. Holmes

Researcher at University of Colorado Denver

Publications -  168
Citations -  11717

Randall K. Holmes is an academic researcher from University of Colorado Denver. The author has contributed to research in topics: Cholera toxin & Escherichia coli. The author has an hindex of 59, co-authored 168 publications receiving 11348 citations. Previous affiliations of Randall K. Holmes include University of Colorado Boulder & Uniformed Services University of the Health Sciences.

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Shiga and Shiga-like toxins.

TL;DR: Although Shigella dysenteriae serotype 1 (Shiga) toxin was discovered more than 80 years ago and has long been recognized as one of the most potent bacterial toxins, early efforts to characterize its structure, biologic activity, genetics, role in pathogenesis, and other properties were hindered by difficulties in preparing pure toxin, obtaining appropriate immunologic reagents, and conducting genetic studies.
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Shiga-like toxin-converting phages from Escherichia coli strains that cause hemorrhagic colitis or infantile diarrhea

TL;DR: One of these phages and another Shiga-like toxin-converting phage from an Escherichia coli O26 isolate associated with infantile diarrhea were closely related in terms of morphology, virion polypeptides, DNA restriction fragments, lysogenic immunity, and heat stability, although a difference in host range was noted.
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Two toxin-converting phages from Escherichia coli O157:H7 strain 933 encode antigenically distinct toxins with similar biologic activities.

TL;DR: Findings indicate that E. coli produces two genetically related but antigenically distinct cytotoxins with similar biologic activities which are proposed to name Shiga-like toxins I and II.
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Nucleotide sequence analysis and comparison of the structural genes for Shiga-like toxin I and Shiga-like toxin II encoded by bacteriophages from Escherichia coli 933

TL;DR: The nucleotide sequence of the Shiga-like toxin type II (SLT-II) structural genes cloned from bacteriophage 933W of the enterohemorrhagic Escherichia coli O157:H7 strain 933 was determined and the regulation proposed for the SLT -II operon is similar to that previously proposed for SLT-I.
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Cloning and sequencing of a Shiga-like toxin type II variant from Escherichia coli strain responsible for edema disease of swine.

TL;DR: The hypothesis that SLT-IIv binds to a different cellular receptor than do other members of the Shiga toxin family but has a similar mode of intracellular action is supported.