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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Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity.
Aaron D. Gitler,Alessandra Chesi,Melissa Geddie,Katherine E. Strathearn,Shusei Hamamichi,Kathryn J. Hill,Kim A. Caldwell,Guy A. Caldwell,Antony A. Cooper,Jean-Christophe Rochet,Susan Lindquist +10 more
TL;DR: Dopaminergic neuron loss caused by α-syn overexpression in animal and neuronal PD models is rescued by coexpression of PARK9, and yeast PARK9 helps to protect cells from manganese toxicity, revealing a connection between PD genetics and an environmental risk factor.
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The heat shock response is self-regulated at both the transcriptional and posttranscriptional levels
TL;DR: It is shown that production of HSP 70 (the major heat-induced protein in these cells) is quantitatively correlated with the degree of stress, and evidence is presented that indicates that the same quantity of H SP 70 is required to release the block in normal protein synthesis.
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Neurotoxicity and Neurodegeneration When PrP Accumulates in the Cytosol
TL;DR: A mechanism for converting wild-type PrP to a highly neurotoxic species that is distinct from the self-propagating PrPSc isoform is established and suggests a potential common framework for seemingly diverse PrP neurodegenerative disorders.
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RNA splicing is interrupted by heat shock and is rescued by heat shock protein synthesis
H. Joseph Yost,Susan Lindquist +1 more
TL;DR: It is suggested that the disruption of intron processing contributes to heat- induced lethality and developmental abnormalities and that one function of the heat shock proteins is to protect processing from heat-induced disruption.
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Thermotolerance in Saccharomyces cerevisiae: the Yin and Yang of trehalose
Mike A. Singer,Susan Lindquist +1 more
TL;DR: Work in yeast indicates that trehalose also promotes survival under conditions of extreme heat, by enabling proteins to retain their native conformation at elevated temperatures and suppressing the aggregation of denatured proteins.