Publications

Detecting and Characterizing Protein Self-Assembly in vivo by Flow Cytometry
Venkatesan S, Kandola TS, Rodriguez-Gama A, Box A, Halfmann R. J Vis Exp. 2019;149:e59577. doi: 59510.53791/59577.
Original Data

Structures of autoinhibited and polymerized forms of CARD9 reveal mechanisms of CARD9 and CARD11 activation
Holliday MJ, Witt A, Rodriguez Gama A, Walters BT, Arthur CP, Halfmann R, Rohou A, Dueber EC, Fairbrother WJ. Nat Commun. 2019;10:3070. doi: 10.1038/s41467-019-10953-z.
Original Data    

Quantifying nucleation in vivo reveals the physical basis of prion-like phase behavior.
Khan T, Kandola TS, Wu J, Venkatesan S, Ketter E, Lange JJ, Rodriguez Gama A, Box A, Unruh JR, Cook M, Halfmann R. (2018) Mol Cell 71:155-168.e157
Original Data

A self-perpetuating repressive state of a viral replication protein blocks superinfection by the same virus.
Zhang XF, Sun R, Guo Q, Zhang S, Meulia T, Halfmann R, Li D, Qu F. (2017) PLoS Pathogens 13(3): e1006253

A glass menagerie of low complexity sequences.
Halfmann R. (2016) Curr Opin Struct Biol. 38:9-16.

TGP, an extremely stable, non-aggregating fluorescent protein created by structure-guided surface engineering.
Close DW, Don Paul C, Langan PS, Wilce MC, Traore DA, Halfmann R, Rocha R, Waldo GS, Payne RJ, Rucker JB, and Prescott M. (2015) Proteins: Structure, Function and Bioinformatics 83(7), 1225-1237.

Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation.
Cai X, Chen J, Xu H, Liu S, Jiang Q, Halfmann R, and Chen ZJ. (2014) Cell 156(6), 1207-1222.

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

Small-molecule activation of the TRAIL receptor DR5 in human cancer cells.
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) Nature Chemical Biology 9, 84–89.

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

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

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

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

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

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis.
Halfmann R and Lindquist S. (2008). Journal of Visualized Experiments 17.

Chaperone-dependent amyloid assembly protects cells from prion toxicity.
Douglas P, Treusch S, Ren H, Halfmann R, Duennwald M, Lindquist S, and Cyr D. (2008).  Proc. Natl. Acad. Sci. USA 105, 7206-7211.