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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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A network of protein interactions determines polyglutamine toxicity.

TL;DR: This work finds that amino acid sequences that modulate polyQ toxicity in cis can also do so in trans, and presents a paradigm for how a complex, dynamic interplay between intramolecular features of polyQ proteins and intermolecular factors in the cellular environment might determine the unique pathobiologies ofpolyQ expansion proteins.
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Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity

TL;DR: It is reported that for both Hsp104 and ClpB, mixtures of ATP and ATP-γS unexpectedly unleash activation, disaggregation and unfolding activities independent of cochaperones, and it is suggested that this versatility in reaction mechanism enables Clp B and Hsp 104 to reactivate the entire aggregated proteome after stress and enables Hsp105 to control prion inheritance.
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Intrinsically Disordered Proteins Drive Emergence and Inheritance of Biological Traits

TL;DR: The data establish a common type of protein-based inheritance through which intrinsically disordered proteins can drive the emergence of new traits and adaptive opportunities.
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A new method for manipulating transgenes: engineering heat tolerance in a complex, multicellular organism.

TL;DR: It is shown that manipulating the expression of a single hsp can be sufficient to improve the stress tolerance of a complex multicellular organism, and also that the role of the 70 kD heat-shock protein, Hsp 70, in thermotolerance is investigated.
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Intracellular localization of heat shock proteins in Drosophila

TL;DR: It is concluded that little (if any) heat shock protein becomes associated with mitochondria, despite the many lines of evidence linking the response to respiratory stress, and that their transport to the nucleus occurs very rapidly.