R. Krishnan

Structural insights into a yeast prion illuminate nucleation and strain diversity

S. Lindquist, R. Krishnan, 2005, Nature.

A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures

S. Lindquist, E. Lemke, A. Deniz, 2007, Proceedings of the National Academy of Sciences.

Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins.

Bonnie Berger, Susan Lindquist, Randal Halfmann, 2011, Molecular cell.

Remodeling Amyloid Fibers: Baker's Yeast Shows Us the Way.

R. Krishnan, E. Asp, M. Proschitsky, 2015, Chemistry & biology.

NPT088 reduces both amyloid-β and tau pathologies in transgenic mice

K. Gannon, E. Mufson, H. Dodiya, 2016, Alzheimer's & dementia.

The cellular prion protein mediates neurotoxic signalling of β‐sheet‐rich conformers independent of prion replication

S. Lindquist, R. Vabulas, H. Kretzschmar, 2011, The EMBO journal.

Stability and Inter-domain Interactions Modulate Amyloid Binding Activity of a General Amyloid Interaction Motif.

R. Krishnan, H. Tsubery, E. Asp, 2019, Journal of molecular biology.

Stability and Inte Interactions Mod Binding Activity Amyloid Interact

R. Krishnan, H. Tsubery, E. Asp, 2019 .

Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro.

S. Lindquist, S. M. Uptain, T. Outeiro, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Conserved features of intermediates in amyloid assembly determine their benign or toxic states

S. Lindquist, E. Lemke, A. Deniz, 2012, Proceedings of the National Academy of Sciences.

A bacteriophage capsid protein provides a general amyloid interaction motif (GAIM) that binds and remodels misfolded protein assemblies.

D. Kirschner, A. Hounslow, J. Waltho, 2014, Journal of molecular biology.

Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs

Andrew D. Steele, Martin L. Duennwald, J. King, 2008, Proceedings of the National Academy of Sciences.

Discovery, preclinical development, and clinical trial approach for npt088, a general amyloid interaction motif (GAIM)-immunoglobulin fusion

E. Masliah, K. Gannon, M. Grundman, 2015, Alzheimer's & Dementia.

GAIM fusions are therapeutic candidates for peripheral amyloidosis

S. Kennel, J. Wall, R. Krishnan, 2019, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.