A team of researchers with the MRC Laboratory of Molecular Biology in the U.K. and Indiana University School of Medicine in the U.S. has determined the structure of tau filaments in patients with Pick’s disease. In their paper published in the journal Nature, the group describes the technique and technology they used to discover the shape of the folds in the brain and what they found.
Neurological diseases are often characterized by misfolded tau proteins in the brain that lead to the destruction of neurons. Prior research has led to the discovery that there are six tau protein shapes in the human brain, and all of them are essential for normal neuronal activity. For unknown reasons, these proteins sometimes fold improperly, which leads to a cascading effect in which more become misfolded—such cascades are referred to as filaments, and the cascading effect is what leads to degeneration of neurons, and in most patients, death from neurological disease. The researchers with this new effort have been working to determine the structure of the misfolds involved in such diseases, hoping to an understand why proteins misfold, and perhaps find a way to stop it from happening. Recently, they announced that they had determined the structure of tau filaments associated with Alzheimer’s disease. In this new effort, they have now done the same with Pick’s disease—a degenerative neurological disease that results in destruction of neurons in the frontal lobe.
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