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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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α-Synuclein: Membrane Interactions and Toxicity in Parkinson's Disease

TL;DR: Evidence regarding α- Syn's normal interactions with membranes and regulation of synaptic vesicles as well as how overexpression of α-syn yields global cellular dysfunction are reviewed, and a model linking vesicle dynamics to toxicity is presented.
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Hsp104 Catalyzes Formation and Elimination of Self-Replicating Sup35 Prion Conformers

TL;DR: In vitro activities of the protein-remodeling factor Hsp104 catalyzed the formation of oligomeric intermediates that proved critical for the nucleation of Sup 35 fibrillization de novo and displayed a conformation common among amyloidogenic polypeptides and can explain [PSI+] inheritance patterns.
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The Parkinson's disease protein α-synuclein disrupts cellular Rab homeostasis

TL;DR: Yeast α-syn inhibits endoplasmic reticulum-to-Golgi vesicle trafficking, which is rescued by overexpression of a Rab GTPase that regulates ER→golgi trafficking, and the homologous Rab1 rescues α- syn toxicity in dopaminergic neuronal models of PD.
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Structural insights into a yeast prion illuminate nucleation and strain diversity

TL;DR: The nature of Sup35's cooperatively folded amyloid core is determined, and this information is used to investigate central questions in prion biology and have broad implications for other amyloids.
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A suite of Gateway cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae.

TL;DR: The resulting suite of 288 yeast Gateway vectors is based upon the two commonly used GPD and GAL1 promoter expression systems that enable expression of ORFs, either constitutively or under galactose‐inducible conditions.