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Heather L True

Showing results (1-10 of 39) with videos related to

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Trends in Genetics : TIG|December 28, 2005
The battle of the fold: chaperones take on prionsHeather L True
The 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 True
Molecular Microbiology|March 18, 2014
Extracellular environment modulates the formation and propagation of particular amyloid structuresLaura Westergard, Heather L True
Molecular Microbiology|March 29, 2014
Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilitiesLaura Westergard, Heather L True
BMC Biochemistry|March 28, 2008
Prion protein insertional mutations increase aggregation propensity but not fiber stabilityTejas Kalastavadi, Heather L True
Journal of Molecular Biology|March 28, 2009
Heterologous prion interactions are altered by mutations in the prion protein Rnq1pJ Patrick Bardill, Heather L True
Molecular Microbiology|July 26, 2014
Structural variants of yeast prions show conformer-specific requirements for chaperone activityKevin C Stein, Heather L True
Prion|November 5, 2011
The [RNQ+] prion: a model of both functional and pathological amyloidKevin C Stein, Heather L True
Plos Genetics|May 10, 2014
Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regionsKevin C Stein, Heather L True
Neuron|May 6, 2006
New insights into prion structure and toxicityDavid A Harris, Heather L True
Pageof 4

Showing results (1-10 of 39) with videos related to

Sort By:
Pageof 4
Trends in Genetics : TIG|December 28, 2005
The battle of the fold: chaperones take on prionsHeather L True
The 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 True
Molecular Microbiology|March 18, 2014
Extracellular environment modulates the formation and propagation of particular amyloid structuresLaura Westergard, Heather L True
Molecular Microbiology|March 29, 2014
Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilitiesLaura Westergard, Heather L True
BMC Biochemistry|March 28, 2008
Prion protein insertional mutations increase aggregation propensity but not fiber stabilityTejas Kalastavadi, Heather L True
Journal of Molecular Biology|March 28, 2009
Heterologous prion interactions are altered by mutations in the prion protein Rnq1pJ Patrick Bardill, Heather L True
Molecular Microbiology|July 26, 2014
Structural variants of yeast prions show conformer-specific requirements for chaperone activityKevin C Stein, Heather L True
Prion|November 5, 2011
The [RNQ+] prion: a model of both functional and pathological amyloidKevin C Stein, Heather L True
Plos Genetics|May 10, 2014
Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regionsKevin C Stein, Heather L True
Neuron|May 6, 2006
New insights into prion structure and toxicityDavid A Harris, Heather L True
Pageof 4