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Susan Lindquist

Researcher at Massachusetts Institute of Technology

Publications -  443
Citations -  86482

Susan Lindquist is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Heat shock protein & Saccharomyces cerevisiae. The author has an hindex of 147, co-authored 440 publications receiving 81067 citations. Previous affiliations of Susan Lindquist include University of Illinois at Chicago & Howard Hughes Medical Institute.

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

TL;DR: This natural yeast prion samples two conformational states similar to those sampled by Aβ, and when assembly stalls at one of these two states, but not the other, it becomes extremely toxic.
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Chaperones as thermodynamic sensors of drug-target interactions reveal kinase inhibitor specificities in living cells.

TL;DR: The sensitivity of chaperones to the stability of client proteins is used for kinome-wide profiling of kinase inhibitors as mentioned in this paper, where chaperone sensitivity is used to identify the kinase inhibitor.
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Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation

TL;DR: In this article, a visually tractable prion model consisting of the Sup35 prion domain fused to GFP (PrD-GFP) and overexpressed it to achieve induction in many cells simultaneously was presented.
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Rapid selection of cyclic peptides that reduce alpha-synuclein toxicity in yeast and animal models.

TL;DR: This work describes the first expressed library of head-to-tail cyclic peptides in yeast, which specifically reduce the toxicity of human α-synuclein and prevents dopaminergic neuron loss in an established Caenorhabditis elegans Parkinson’s model.
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Regulation of HSP70 synthesis by messenger RNA degradation.

TL;DR: It is postulated that a mechanism for degrading hsp70 mRNA pre-exists in Drosophila cells, that it is inactivated by heat shock and that the reactivation of this mechanism that is responsible for hsp 70 repression during recovery is the same as that used by other unstable mRNAs.