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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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Patent

Compounds for treating infectious diseases

TL;DR: In this article, the authors provide compounds of Formula I, pharmaceutically acceptable salts thereof, and pharmaceutical compositions thereof for inhibiting fungal or parasitic growth, which are useful as inhibitors of glycosylphosphatidylinositol (GPI)-anchor biosynthesis.

Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP (prionyprotein structureyaggregationychaperone protein)

TL;DR: In this paper, the authors show that when purified Sup35 and Hsp104 are mixed, the circular dichroism (CD) spectrum differs from that predicted by the addition of the proteins' individual spectra, and the ATPase activity of Sup35 is inhibited.
Journal ArticleDOI

Persistent Activation of mRNA Translation by Transient Hsp90 Inhibition

TL;DR: This article showed that transient loss of heat shock protein 90 function can promote a nongenetic inheritance of a translational state affecting specific mRNAs, introducing a mechanism by which Hsp90 can promote phenotypic variation.
Book ChapterDOI

Yeast Cells as a Discovery Platform for Parkinson's Disease and other Protein Misfolding Diseases

TL;DR: This chapter explores yeast cells as a discovery platform for Parkinson's disease (PD) and finding genetic factors and chemical compounds that modify the toxicity of proteins that are prone to misfoldings and producing toxic gain-of-function phenotypes in man.

Chaperones as thermodynamic sensors of drug-target interactions reveal kinase inhibitor specificities in living cells

TL;DR: The method allows determination of target specificities of both ATP-competitive and allosteric inhibitors in the kinases' native cellular context in high throughput and is applicable to other chaperones and target classes by assaying HSP70/steroid hormone receptor and CDC37/kinase interactions, suggesting that chaperone interactions will have broad application in detecting drug-target interactions in vivo.