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Penn biochemist receives NIH New Innovator's Award

PHILADELPHIA - James Shorter, PhD, Assistant Professor of Biochemistry and Biophysics at the University of Pennsylvania School of Medicine, has been named an inaugural recipient of the 2007 NIH Director's New Innovator Award. This highly prestigious award totals $1.5 million in direct costs over five years to each of 29 investigators, many of whom are in the early stages of their careers. More than 2,100 applications were received for this extremely competitive program.

As a key component of the National Institutes of Health (NIH) Roadmap for Medical Research, the New Innovator Award program supports exceptionally creative early-career scientists who take highly innovative approaches to major challenges in biomedical research. Shorter will develop biochemical methods to combat diseases caused by nerve degeneration, such as Parkinsons, Alzheimers, and Huntingtons.

Novel ideas and new investigators are essential ingredients for scientific progress, and the creative scientists we recognize with NIH Directors Pioneer Awards and NIH Directors New Innovator Awards are well-positioned to make significantand potentially transformativediscoveries in a variety of areas, said NIH Director Elias A. Zerhouni, MD.

This award is an honor, and a relief, in a way, to now be able to focus on my research in a significant way, says Shorter. Shorters lab seeks to understand how cells prevent, reverse, or even promote the formation of amyloid and prion fibers, extremely stable protein aggregates implicated in many neurodegenerative diseases. He aims to test his ideas using a panel of proteins that are implicated in human disease to search for potential cures for these disorders.

When amyloid fibers grow and divide they can be infectious, and are then termed prions. Prion and amyloid formation are associated with some of the most devastating neurodegenerative diseases confronting humans, including Alzheimer's disease, Parkinson's disease, and variant Creutzfeldt-Jacob disease.

Cells have evolved a sophisticated machinery to alleviate amyloid and prion aggregates, but these biological safeguards can be breached, especially as organisms age, and the consequences are often fatal. Working in a yeast model, Shorter and colleagues employ biochemistry and genetics to understand how the interactions between amyloid proteins and other proteins can be manipulated to avoid pathogenic outcomes and promote beneficial outcomes.

Shorter received his PhD from the Imperial Cancer Research Fund at University College London in 2000 and moved to Penn from the Whitehead Institute in Boston in April 2007.


Contact: Karen Kreeger
University of Pennsylvania School of Medicine

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