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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Bridging high-throughput genetic and transcriptional data reveals cellular responses to alpha-synuclein toxicity
Esti Yeger-Lotem,Laura Riva,Linhui Julie Su,Aaron D. Gitler,Aaron D. Gitler,Anil G. Cashikar,Anil G. Cashikar,Oliver D. King,Oliver D. King,Pavan K. Auluck,Pavan K. Auluck,Melissa Geddie,Julie S. Valastyan,David R. Karger,Susan Lindquist,Ernest Fraenkel +15 more
TL;DR: An integrative approach is developed that bridges the gap between data using known molecular interactions, thus highlighting major response pathways responding to the toxicity of alpha-synuclein, a protein implicated in several neurodegenerative disorders including Parkinson's disease.
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Flanking sequences profoundly alter polyglutamine toxicity in yeast
TL;DR: Using a yeast model, this work finds that sequences flanking the polyQ region of human huntingtin exon I can convert a benign protein to a toxic species and vice versa, and observes that flanking sequences can direct polyQ misfolding to at least two morphologically distinct types of polyQ aggregates.
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A Chaperone Pathway in Protein Disaggregation HSP26 ALTERS THE NATURE OF PROTEIN AGGREGATES TO FACILITATE REACTIVATION BY HSP104
TL;DR: Hsp26 plays an important role in pathways that defend cells against environmental stress and the types of protein misfolding seen in neurodegenerative disease, and renders aggregates more accessible to Hsp104/Ssa1/Ydj1.
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Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
Jiyan Ma,Susan Lindquist +1 more
TL;DR: It is demonstrated that PrP can accumulate in the cytoplasm and is likely to enter this compartment through normal protein quality-control pathways, which has implications for pathogenesis.
Hsp90 and Environmental Stress Transform the Adaptive Value of Natural Genetic Variation
Daniel F. Jarosz,Susan Lindquist +1 more
TL;DR: By linking genetic variation to phenotypic variation via environmental stress, the Hsp90 protein-folding reservoir might promote both stasis and change, and the nature and adaptive value of HSp90-contingent traits remain uncertain.