S
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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Journal ArticleDOI
Inhibiting GPI Anchor Biosynthesis in Fungi Stresses the Endoplasmic Reticulum and Enhances Immunogenicity
Catherine A. McLellan,Luke Whitesell,Oliver D. King,Alex K. Lancaster,Ralph Mazitschek,Susan Lindquist +5 more
TL;DR: It is found that, unlike all three major classes of antifungals in current use, the direct antimicrobial activity of this compound results predominantly from its ability to induce overwhelming stress to the endoplasmic reticulum.
Book ChapterDOI
Yeast prion [psi +] and its determinant, Sup35p.
TL;DR: This chapter focuses on both in vivo and in vitro methods used to analyze [ PSI + ], the most extensively studied member of the amyloidogenic proteins group.
Journal ArticleDOI
Selective translation and degradation of heat-shock messenger RNAs in Drosophila.
Susan Lindquist,Robert Petersen +1 more
TL;DR: Current knowledge is reviewed of two cytoplasmic mechanisms employed during the response in the fruit fly Drosophila melanogaster that are very stable and accumulate in large numbers during heat shock.
Journal ArticleDOI
The role of calorie restriction and SIRT1 in prion-mediated neurodegeneration.
Danica Chen,Andrew D. Steele,Gregor Hutter,Joanne Bruno,Arvind Govindarajan,Erin J. Easlon,Su Ju Lin,Adriano Aguzzi,Susan Lindquist,Leonard Guarente +9 more
TL;DR: It is reported that the onset of prion disease is delayed by CR and in the SIRT1 KO mice fed ad libitum, suggesting a possible mechanism for the delayed onset of disease, as PrP levels are a critical determinant of how quickly mice succumb toPrion disease.
Journal ArticleDOI
Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities.
Heather Sadlish,Heike Rampelt,James Shorter,Renee D. Wegrzyn,Claes Andréasson,Susan Lindquist,Bernd Bukau +6 more
TL;DR: A chaperone-like activity of Sse1 that assists in stabilization of early folding intermediates of the Sup35 prion conformation is suggested.