Would Disrupting the Way Tau Proteins Copy Themselves Slow Alzheimer's Disease?

Reducing the speed of the already-slow replication process could be a new way to attack the disease. View in browser

Image credits: NIH Would Disrupting the Way Tau Proteins Copy Themselves Slow Alzheimer's Disease? Reducing the speed of the already-slow replication process could be a new way to attack the disease. Haley Weiss, Staff Writer November 4, 2021                                                                                                                                                                                   (Inside Science) -- The story of Alzheimer's disease at the cellular level is still in many ways a mystery. Among them is how the disease progresses within the brain, an oft-debated mystery that may finally have an answer thanks to a team of researchers at the University of Cambridge and Harvard Medical School. Several proteins that inflict the damage within the brain that we recognize as Alzheimer's play significant roles in this story. But none are thought to play a role as significant as the protein known as tau. In a healthy brain, tau helps microscopic structures within the brain's connection points remain straight and strong, but in a brain with Alzheimer's, tau forms twisted tangles that instead limit the flow of information and can cause cellular death. As tau tangles accumulate throughout the brain, the disease worsens. "For the past 15 years, here in Cambridge, we have been working together with collaborators in trying to answer what was, in principle, a very simple question. Namely: What was the mechanism of protein aggregation?" said Tuomas Knowles, a physical chemist and biophysicist at the University of Cambridge... Read more Copyright 2021 American Institute of Physics. Inside Science syndicates its articles, columns, blogs and videos to news organizations. To initiate syndication, or request permission to republish our content (on a one-time or continuing basis), please contact Inside Science at insidescience@aip.org. News organizations seeking permission to republish Inside Science content must fully credit Inside Science as the original source of the content, include the author byline, and republish the original, unaltered form (excluding content titles, headlines, or sub-headlines). The reprint format can be seen here. Copyright conditions and usage terms are subject to change at any time without consent or any type of prior notice. To unsubscribe from all future mailings from Inside Science please click here. To manage your email subscriptions please click here.

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