SMU Department of Biological Sciences
A picture is worth 1,000 words when it comes to understanding how things work, but 3D moving pictures are even better. That’s true for scientists trying to stop cancer by better understanding the proteins that make some chemotherapies unsuccessful. Now SMU biochemist John G. Wise at SMU has brought to life in a moving 3D computer model the structure of a key protein related to recurring cancers. Continue reading
Now biologists at Southern Methodist University, Dallas, report they have developed a new discovery tool that will help researchers better understand this deadly disease. Continue reading
They hope to find a compound that can be developed into a drug that re-enables chemotherapy after it fails to work against recurring cancer. Continue reading
In 1996 the introduction of “triple cocktail” drug therapy transformed AIDS from a death sentence into a manageable chronic disease. The drug regimen, also known as HAART for highly active antiretroviral treatment, involved treating patients with three or more classes of antiviral medicines.
But the virus fought back. It mutates easily, and the mutations caused resistance to first one and then another drug making up the cocktail. Unsettling reports of newly infected patients with the drug-resistant virus meant researchers needed to find new ways to fight HIV infection.
In his third-floor laboratory in Dedman Life Sciences Building, biologist Robert Harrod and his team are zeroing in on a new way to inhibit the virus that causes AIDS. They already have shown that their approach, which involves the rare genetic disorder Werner syndrome, works when the disorder’s enzyme defect is introduced into cells.
Now they are trying to find practical ways to use this pathway to inhibit the AIDS virus. The beauty of this approach is that the AIDS virus will not be able to mutate in a way that can defeat this treatment, says Harrod, associate professor in the Biological Sciences Department of Dedman College.
A professor in the Department of Biological Sciences, Vik’s research interests include protein structure and function, and the biochemistry of membrane-bound enzymes. His work focuses on key mechanisms of bioenergetics, the study of how living systems get and use the energy sources required to sustain life.