Researchers discover misfolded protein clumps common to dementia, Lou Gehrig’s disease

Scientists have identified a misfolded, or incorrectly formed, protein common to two devastating neurological diseases, frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS, also known as Lou Gehrig’s disease), according to a report in the Oct. 6, 2006, issue of Science. The findings suggest that certain forms of FTD, ALS and possibly other neurological diseases might share a common pathological process.
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A New Way of Looking at Molecular Motors

An innovative method of categorizing myosin—one of three molecular “motors” that produce movement within the cells of the body—has dramatically increased the amount of information available about these essential proteins. The studies lay the groundwork for development of treatments for conditions ranging from certain kinds of blindness and kidney disease to neurodegenerative disorders and parasitic diseases such as malaria.
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Structure of the protein essential for immortalizing cells and promoting cancer is determined

Scientists have determined the detailed structure of an essential piece of the telomerase enzyme, an important contributor to the vast majority of human cancers. Understanding the physical shape of the protein has led to a better understanding of how it acts to immortalize cells – and should help scientists design broadly effective cancer drugs.

3-dimensional structure of an essential domain of TERT (the telomerase catalytic protein subunit). Green highlights the groove that “anchors” the DNA near the end of the chromosome:

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