A new molecular tag discovered by scientists at The University of Texas M. D. Anderson Cancer Center may help doctors decide which breast cancer patients need more aggressive treatment and which can forego the potentially toxic course of chemotherapy.
Khandan Keyomarsi, Ph.D., associate professor in experimental radiation at M. D. Anderson, and her colleagues report in the November 14, 2002, issue of the New England Journal of Medicine that high levels of a protein called cyclin E are closely associated with aggressive, invasive breast cancer. The study, conducted with tissue samples of current or former breast cancer patients, appears to show that cyclin E is a much better predictor of patient outcome than any current predictive marker. However, says Keyomarsi, the study must be repeated with newly diagnosed patients to determine its true predictive value.
The ability to predict which breast cancer tumors will recur or spread throughout the body is an important aspect of breast cancer treatment, says Keyomarsi. Currently, the prognosis for women diagnosed with breast cancer is determined by whether tumor cells have spread to lymph nodes. But some women who have cancer cells in the lymph nodes never have a recurrence, while others whose cancer has not spread do have a recurrence. Yet many women, after discussions with their doctors, opt to undergo grueling chemotherapy in hopes of ensuring any rogue cancer cells that may be present are killed. If an accurate predictive marker were available, many women could be spared chemotherapy, she says.
Laura Sussman | EurekAlert!
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Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Hamburg and the European Molecular Biology Laboratory (EMBL) outstation in the city have developed a new method to watch biomolecules at work. This method dramatically simplifies starting enzymatic reactions by mixing a cocktail of small amounts of liquids with protein crystals. Determination of the protein structures at different times after mixing can be assembled into a time-lapse sequence that shows the molecular foundations of biology.
The functions of biomolecules are determined by their motions and structural changes. Yet it is a formidable challenge to understand these dynamic motions.
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Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Potsdam (both in Germany) and the University of Toronto (Canada) have pieced together a detailed time-lapse movie revealing all the major steps during the catalytic cycle of an enzyme. Surprisingly, the communication between the protein units is accomplished via a water-network akin to a string telephone. This communication is aligned with a ‘breathing’ motion, that is the expansion and contraction of the protein.
This time-lapse sequence of structures reveals dynamic motions as a fundamental element in the molecular foundations of biology.
Two research teams have succeeded simultaneously in measuring the long-sought Thorium nuclear transition, which enables extremely precise nuclear clocks. TU Wien (Vienna) is part of both teams.
If you want to build the most accurate clock in the world, you need something that "ticks" very fast and extremely precise. In an atomic clock, electrons are...
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