(†corresponding author, *equal author)


Cai X, Chen J, Xu H, Liu S, Jiang QX, Halfmann R†, and Chen ZJ†. (2014). Prion-like Polymerization Underlies Signal Transduction in Antiviral Immune Defense and Inflammasome Activation. Cell 156(6), 1207-1222.

Holmes DL, Lancaster AK, Lindquist S, and Halfmann R†. (2013). Heritable remodeling of yeast multicellularity by an environmentally responsive prion. Cell 153(1), 153-165.

Wang G, Wang X, Yu H, Wei S, Williams N, Holmes DL, Halfmann R, Naidoo J, Wang L, Li L, Chen S, Harran P, Lei X, Wang X. (2013). Small-molecule activation of the TRAIL receptor DR5 in human cancer cells. Nature Chemical Biology 9, 84–89.

Halfmann R†*, Wright J*, Alberti S, Lindquist S, Rexach M. (2012). Prion formation by a yeast GLFG nucleoporin. Prion 6(4).

Halfmann R*, Jarosz DF*, Jones SK, Chang A, Lancaster AK, Lindquist S. (2012). Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 482(7385), 363-8.

Halfmann, R.*, Alberti, S.*, Krishnan, R., Lyle, N., Pappu, R., Lindquist, S. (2011). Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins. Molecular Cell 43(1), 72-84.


O'Donnell, C.W., Waldispühl, J., Lis, M., Halfmann, R., Devadas, S., Lindquist, S., Berger, B. (2011). A method for probing the mutational landscape of amyloid structure. Bioinformatics 27(13):i34-42.

Halfmann, R., Lindquist, S. (2010). Epigenetics in the extreme: Prions and the inheritance of environmentally acquired traits. Science 330(6004), 629-32.

Alberti, S., Halfmann, R., and Lindquist, S. (2010). Biochemical, cell biological and genetic assays to analyze amyloid and prion aggregation in yeast. For: Guide to Yeast Genetics: Functional Genomics, Proteomics, and Other Systems Analysis, 2nd Ed. Methods in Enzymology 470, 709-731.

Halfmann, R., Alberti, S., Lindquist, S. (2010). Prions, protein homeostasis, and phenotypic diversity. Trends in Cell Biology 20, 125-33.

Alberti, S.*, Halfmann, R.*, King, O., Kapila, A., and Lindquist, S. (2009). A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137, 146-58.