The Scope E-Newsletter
From the Dean's Office
Defining GSM: What Is Your Story?
A New Cancer Institute Will Break Ground in July
Faculty Appreciation
Dr. Baljepally, Dr. Panella and Dr. Rasnake Are Recognized for Excellence
In the Spotlight
Researchers Take First Sub-Nanoscale Images of Huntington's Disease Protein
Medtronic Awards Grant to Study Possible BRONJ Prevention Treatment
Radiology Residents Pass Oral Board Exam; Dr. Hudson and Dr. Bradley Proctor
Dr. Terrell Receives Grant to Examine Nature Versus Nurture in Concussion
Faculty Discuss Hot Topics in the News
Visiting Professor Dr. Park Studies at Regional Forensic Center
Dr. Carlson Receives Prestigious Honor from His Alma Mater
Dr. Zite Wins Blue Ribbon Award
Radiology Residents Attend National Meetings
Dr. Hudson Elected as Exam Regional Advisor
Dr. Craft Provides Leadership on Anesthesiology Exams
Pathology Hosts Visiting Professor Dr. Robert Young
Dr. Burgiss Honored as Fellow in Telemedicine
News
Frontiers Magazine Features Centers of Excellence, Economic Impact
Reporting Hazards, Accidents and Near Misses
Portrait Services Now Available
Continuing Education
Heart, Lung, Vascular Update: Early Registration Ends August 26
Tumor Boards Now Certified for Credit
CME Courses at UTK Focus on EHR and Lean for Healthcare
Inaugural GI Cancer Conference Successful
Scholarly Activity
Residents and Fellows Present at UTGSM Research Days
Read all articles in this issue of The Scope
Researchers Take First Sub-Nanoscale Images of Huntington's Disease Protein
Researchers at the University of Tennessee Graduate School of Medicine and the Department of Energy's Oak Ridge National Laboratory have for the first time successfully characterized the earliest structural formation of the disease type of the protein that causes Huntington's disease. The incurable, hereditary neurological disorder is always fatal and affects one in 10,000 Americans.
Huntington's disease is caused by a renegade protein "huntingtin" that destroys neurons in areas of the brain concerned with the emotions, intellect and movement. All humans have the normal huntingtin protein, which is known to be essential to human life, although its true biological functions remain unclear.
Valerie Berthelier, PhD, Assistant Professor of Medicine and Director of Conformational Diseases and Therapeutics Research, and Christopher Stanley, PhD, a Shull Fellow in the Neutron Scattering Division at Oak Ridge National Laboratory, have used a small-angle neutron scattering instrument, called Bio-SANS, at ORNL's High Flux Isotope Reactor to explore the earliest aggregate species of protein that are believed to be the most toxic in causing Huntington's disease.
Dr. Stanley and Dr. Berthelier, in research published May 18 in Biophysical Journal, were able to determine the size and mass of the mutant protein structures—from the earliest small, spherical precursor species composed of two (dimers) and three (trimers) peptides—along the aggregation pathway to the development of the resulting, later-stage fibrils. They were also able to see inside the later-stage fibrils and determine their internal structure, which provides additional insight into how the peptides aggregate.
Now that they know the structures, the hope is to develop drugs that can counteract the toxic properties in the early stages, or dissuade them from taking the path to toxicity.
Read more about the process Dr. Stanley and Dr. Berthelier used to explore the toxic proteins in an article released by Bill Cabage with ORNL.
