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BMC Biochemistry|March 28, 2008
Prion protein insertional mutations increase aggregation propensity but not fiber stabilityTejas Kalastavadi, Heather L TrueThe Journal of Biological Chemistry|May 6, 2010
Analysis of the [RNQ+] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagationTejas Kalastavadi, Heather L TruePrion|December 23, 2008
Insights into intragenic and extragenic effectors of prion propagation using chimeric prion proteinsHeather L True, Tejas Kalastavadi, Elizabeth M H TankTrends in Genetics : TIG|December 28, 2005
The battle of the fold: chaperones take on prionsHeather L TrueMolecular 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 TrueJournal of Molecular Biology|March 28, 2009
Heterologous prion interactions are altered by mutations in the prion protein Rnq1pJ Patrick Bardill, Heather L TrueMolecular Microbiology|July 26, 2014
Structural variants of yeast prions show conformer-specific requirements for chaperone activityKevin C Stein, Heather L TruePrion|November 5, 2011
The [RNQ+] prion: a model of both functional and pathological amyloidKevin C Stein, Heather L TruePlos Genetics|May 10, 2014
Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regionsKevin C Stein, Heather L TruePageof 4