Structure of hnRNPDL-2 amyloid fibres obtained by cryoEM at 2.5 A resolution. The upper part shows the organisation of the protein with two nucleic acid binding domains in pink and a low-complexity ...
The tiny protein known as transthyretin can cause big problems in the body when it misfolds after secretion. While healthy transthyretin moves hormones through blood and spinal fluid, misfolded ...
Prof. Liu Cong from the Shanghai Institute of Organic Chemistry of the Chinese Academy of Sciences, along with collaborators, has revealed the high-resolution structures of amyloid fibrils directly ...
Researchers have developed a microscopy technique to visualize amyloid beta’s underlying structure, which could yield new insights into Alzheimer’s disease. As the prevalence of Alzheimer’s rises, ...
Amyloid fibrils appear in many neurodegenerative diseases, and scientists are eager to understand how they form and spread. But amyloids—clumped aggregations of misfolded proteins—can be difficult to ...
Amyloid-beta (A-beta) aggregates are tangles of proteins most notably associated with neurodegenerative diseases like Alzheimer's. Despite its constant stint in the limelight, however, researchers ...
Researchers have now proposed a molecular mechanism that links amyloid deposition in the aortic valve with degenerative calcification. They also theorize that other risk factors for CAVD, such as high ...
Piller is an investigative journalist for Science. In November 2022, Dennis Selkoe, a Harvard professor of neurologic diseases and among the most celebrated and prolific Alzheimer’s researchers, ...
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