The True Lab

Department of Cell Biology & Physiology

Washington University School of Medicine

Selected Publications


  • Stein KC, True HL (2014). Prion strains and amyloid polymorphism influence phenotypic variation. PLoS Pathog. Sep 4;10(9):e1004328. doi:10.1371/journal.ppat.1004328
  • Stein KC, True HL (2014). Structural variants of yeast prions show conformer-specific requirements for chaperone activity. Mol Microbiol. Sep;93(6):1156-71. doi:10.1111/mmi.12725
  • Stein KC, Bengoechea R, Harms MB, Weihl CC, True HL (2014). Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers. J Biol Chem. Jul 25;289(30):21120-30.
  • Stein KC, True HL (2014). Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions. PLoS Genet. May 8;10(5):e1004337 doi:10.1371/journal.pgen.1004337
  • Westergard L, True HL (2014). Extracellular environment modulates the formation and propagation of particular amyloid structures. Mol Microbiol. May;92(4):698-715. doi:10.1111/mmi.12579
  • Westergard L, True HL (2014). Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities. Mol Microbiol. Apr;92(1):183-93. doi:10.1111/mmi.1254
  • Dulle JE, Stein KC, True HL (2014). Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation. PLoS ONE. Jan 23;9(1):e87521. doi:10.1371/journal.pone.0087521


  • Huang VJ, Stein KC, True HL (2013). Spontaneous variants of the [RNQ+] prion in yeast demonstrate the extensive conformational diversity possible with prion proteins. PLoS ONE. Oct 25;8(10):e79582. doi:10.1371/journal.pone.0079582
  • Dulle JE, Bouttenot RE, Underwood LA, True HL (2013). Soluble oligomers are sufficient for transmission of a yeast prion but do not confer phenotype. J Cell Biol. Oct 28;203(2):197-204. doi:10.1083/jcb.201307040
  • Dulle JE, True HL (2013). Low activity of select Hsp104 mutants is sufficient to propagate unstable prion variants. Prion. Sep 1;7(5):394-403. doi:10.4161/pri.26547


  • Stein KC, True HL (2011). The [RNQ+] prion: A model of both functional and pathological amyloid. Prion. Oct 1;5(4):291-98. doi:10.4161/pri.18213


  • Kalastavadi T, True HL (2010). Analysis of the [RNQ+] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagation. J Biol Chem. Jul 2;285(27):20748-55. doi:10.1074/jbc.M110.115303
  • Lancaster AK, Bardill JP, True HL, Masel J (2010). The spontaneous appearance rate of the yeast prion [PSI+] and its implications for the evolution of the evolvability properties of the [PSI+] system. Genetics. Feb;184(2)393-400. doi:10.1534/genetics.109.110213
  • Lin CA, Ellis SR, True HL (2010). The Sua5 protein is essential for normal translational regulation in yeast. Mol Cell Biol. Jan;30(1):354-63. doi:10.1128/MCB.00754-09


  • Bardill JP, Dulle JE, Fisher JR, True HL (2009). Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ+] prion. Prion. Jul;3(3):151-60.
  • Bardill JP and True HL (2009). Heterologous prion interactions are altered by mutations in the prion protein Rnq1p. J Mol Biol. May 8;388(3):583-96. doi:10.1016/j.jmb.2009.03.036
  • Strawn LA, Lin CA, Tank EM, Osman MM, Simpson SA, True HL (2009). Mutants of the Paf1 Complex Alter Phenotypic Expression of the Yeast Prion [PSI+]. Mol Biol Cell. Apr;20(8):2229-41. doi:10.1091/mbc.E08-08-0813
  • Tank EM, True HL (2009). Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates. PLoS Genet. Feb;5(2):e1000382. doi:10.1371/journal.pgen.1000382


  • True HL, Kalastavadi T, Tank EM (2008). Insights into intragenic and extragenic effectors of prion propagation using chimeric prion proteins. Prion. Apr;2(2):45-7.
  • Kalastavadi T, True HL (2008). Prion protein insertional mutations increase aggregation propensity but not fiber stability. BMC Biochem. Mar 17;9:7. doi:10.1186/1471-2091-9-7


  • Tank EM, Harris DA, Desai AA, True HL (2007). Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability. Mol Cell Biol.  Aug;27(15):5445-55. doi:10.1128/MCB.02127-06


  • Strawn LA, True HL (2006). Deletion of RNQ1 gene reveals novel functional relationship between divergently transcribed Bik1p/CLIP-170 and Sfi1p in spindle pole body separation. Curr Genet. Dec;50(6):347-66. doi:10.1007/s00294-006-0098-6
  • Harris DA, True HL (2006). New insights into prion structure and toxicity. Neuron. May 4;50(3):353-7. doi:10.1016/j.neuron.2006.04.020
  • True HL (2006). The battle of the fold: chaperones take on prions. Trends Genet. Feb;22(2):110-7. doi:10.1016/j.tig.2005.12.004