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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Molecular population genetics and evolution of a prion-like protein in Saccharomyces cerevisiae.
TL;DR: The N domain of Sup35p is highly conserved in amino acid sequence and is highly biased in codon usage toward preferred codons, which concludes that Amino acid changes are under weak purifying selection based on a quantitative analysis of polymorphism and divergence.
Journal ArticleDOI
Developmentally regulated nuclear transport of transcription factors in drosophila embryos enable the heat shock response
Zhaohui Wang,Susan Lindquist +1 more
TL;DR: It is suggested that the potentiation of general and heat shock-specific transcription in Drosophila embryos is controlled by the developmentally programmed relocalization ofgeneral and heatshock- specific transcription factors.
Journal ArticleDOI
Transcriptional derepression of the Saccharomyces cerevisiae HSP26 gene during heat shock.
R E Susek,Susan Lindquist +1 more
TL;DR: It is proposed that basal repression and heat-induced depression of transcription play major roles in regulating the expression of HSP26, the small heat shock protein of Saccharomyces cerevisiae.
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
Susan Lindquist,Steve Henikoff +1 more
Prion Formation and Polyglutamine Aggregation Are Controlled by Two Classes of Genes
Anita L. Manogaran,Joo Y. Hong,Joan Hufana,Jens Tyedmers,Jens Tyedmers,Susan Lindquist,Susan W. Liebman +6 more
TL;DR: The effects of over 400 gene deletions on this de novo induction of [PSI +] suggest that prion formation and polyglutamine aggregation involve a multi-phase process that can be inhibited at different steps.