Anthrax Toxin: Structure, Activity, and New Inhibitors |
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| Launch in standalone player | |
| Air date: | Monday, October 07, 2002, 9:00:00 AM |
| Category: | Special |
| Runtime: | 60 minutes |
| NLM Title: | Anthrax toxin : structure, activity, and new inhibitors [electronic resource] / R. John Collier. |
| Series: | Kinyoun lecture |
| Author: | Collier, R John. National Institutes of Health (U.S.) |
| Publisher: | [Bethesda, Md. : National Institutes of Health, 2002] |
| Other Title(s): | Kinyoun lecture |
| Abstract: | (CIT): Kinyoun Lecture. R. John Collier, Ph.D., Professor, Microbiology and Molecular Genetics, Harvard Medical School. Dr. Collier has devoted his career to understanding the molecular mechanisms by which bacteria cause disease. His research has elucidated the structures and modes of action of bacterial protein toxins, and he has applied this knowledge to develop novel approaches to treat and prevent diseases. Early in his career Collier discovered that diphtheria toxin (DT) inhibits protein synthesis by directly inactivating a eukaryotic polypeptide elongation factor (elongation factor-2) within the cytosol. Besides explaining the mode of action of DT, this represented the first demonstration that a bacterial protein toxin could breach a membrane protecting the mammalian cytosol from the extracellular milieu. This finding changed thinking about how protein toxins act. |
| Subjects: | Bacillus anthracis--pathogenicity Bacterial Toxins |
| Publication Types: | Government Publications |
| Rights: | This is a work of the United States Government. No copyright exists on this material. It may be disseminated freely. |
| NLM Classification: | QW 127.5.B2 |
| NLM ID: | 101267542 |
| CIT File ID: | 10345 |
| CIT Live ID: | 1766 |
| Permanent link: | http://videocast.nih.gov/launch.asp?10345 |