Alternative conformations of amyloidogenic proteins govern their behavior
JW Kelly - Current opinion in structural biology, 1996 - Elsevier
JW Kelly
Current opinion in structural biology, 1996•ElsevierRecent publications strongly support the hypothesis that conformational changes in
amyloidogenic proteins lead to amyloid fibril formation and cause disease. Biophysical
studies on several amyloidogenic proteins provide insights into the conformational changes
required for fibrilogenesis. In addition, newly available moderate to high resolution structural
studies are bringing us closer to understanding the structure of amyloid.
amyloidogenic proteins lead to amyloid fibril formation and cause disease. Biophysical
studies on several amyloidogenic proteins provide insights into the conformational changes
required for fibrilogenesis. In addition, newly available moderate to high resolution structural
studies are bringing us closer to understanding the structure of amyloid.
Recent publications strongly support the hypothesis that conformational changes in amyloidogenic proteins lead to amyloid fibril formation and cause disease. Biophysical studies on several amyloidogenic proteins provide insights into the conformational changes required for fibrilogenesis. In addition, newly available moderate to high resolution structural studies are bringing us closer to understanding the structure of amyloid.
Elsevier