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Molecular Microbiology|March 18, 2014
Extracellular environment modulates the formation and propagation of particular amyloid structuresLaura Westergard, Heather L TrueMolecular Microbiology|March 29, 2014
Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilitiesLaura Westergard, Heather L TrueBiochimica Et Biophysica Acta|April 25, 2007
The cellular prion protein (PrP(C)): its physiological function and role in diseaseLaura Westergard, Heather M Christensen, David A HarrisThe Journal of Neuroscience : the Official Journal of the Society for Neuroscience|September 30, 2011
A nine amino acid domain is essential for mutant prion protein toxicityLaura Westergard, Jessie A Turnbaugh, David A HarrisThe Journal of Biological Chemistry|October 26, 2011
A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formationLaura Westergard, Jessie A Turnbaugh, David A HarrisPlos One|October 8, 2011
The N-terminal, polybasic region is critical for prion protein neuroprotective activityJessie A Turnbaugh, Laura Westergard, Ursula Unterberger, et al.Pageof 1