Penn Medicine: Yeast Protein Breaks up Amyloid Fibrils and Disordered Protein Clumps In Different Ways

PHILADELPHIA — Several fatal brain disorders, including Parkinson's disease, are connected by the misfolding of specific proteins into disordered clumps and stable, insoluble fibrils called amyloid. Amyloid fibrils are hard to break up due to their stable, ordered structure. For example, a-synuclein forms amyloid fibrils that accumulate in Lewy Bodies in Parkinson's disease.

Karen Kreeger

Penn-Temple Team Discovers Gatekeeper for Maintaining Health of Cell Energy Source

PHILADELPHIA — Most healthy cells rely on a complicated process to produce the fuel ATP. Knowing how ATP is produced by the cell’s energy storehouse – the mitochondria -- is important for understanding a cell’s normal state, as well as what happens when things go wrong, for example in cancer, cardiovascular disease, neurodegeneration, and many rare disorders of the mitochondria.

Karen Kreeger

Institute of Medicine Elects Six New Members From Penn

PHILADELPHIA — Six professors from the University of Pennsylvania, representing four schools, have been elected members of the Institute of Medicine (IOM), one of the nation's highest honors in biomedicine.

Katherine Unger Baillie, Karen Kreeger

Composite Nanofibers Developed by Penn Scientists Next Chapter in Orthopaedic Biomaterials

Bioengineered replacements for tendons, ligaments, the meniscus of the knee, and other tissues require re-creation of the exquisite architecture of these tissues in three dimensions. These fibrous, collagen-based tissues located throughout the body have an ordered structure that gives them their robust ability to bear extreme mechanical loading.

Karen Kreeger