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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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Yeast reveal a "druggable" Rsp5/Nedd4 network that ameliorates α-synuclein toxicity in neurons.

TL;DR: Using unbiased phenotypic screens as an alternative to target-based approaches, NAB identifies a druggable node in the biology of α-syn that can correct multiple aspects of its underlying pathology, including dysfunctional endosomal and endoplasmic reticulum–to-Golgi vesicle trafficking.
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The role of heat-shock proteins in thermotolerance

TL;DR: The role of heat-shock proteins (hsps) in thermotolerance was examined in the budding yeast Saccharomyces cerevisiae and in the fruit fly Drosophila melanogaster, suggesting that the primary function of hsp 104 is to rescue proteins from denaturation rather than to degrade them once they have been denatured.
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Cdc37 is a molecular chaperone with specific functions in signal transduction.

TL;DR: In this article, the effect of Cdc37 on Hsp90 functions was examined and it was shown that Cdc 37 can compensate for Hspg0 in maintaining the activity of v-Src kinase but does not maintain the activation of the glucocorticoid receptor.
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Epigenetics in the Extreme: Prions and the Inheritance of Environmentally Acquired Traits

TL;DR: Prions are an unusual form of epigenetics: Their stable inheritance and complex phenotypes come about through protein folding rather than nucleic acid–associated changes.
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Potent inhibition of huntingtin aggregation and cytotoxicity by a disulfide bond-free single-domain intracellular antibody.

TL;DR: This is the first attempt to improve affinity in the absence of a disulfide bond to improve intrabody function and suggests a generally applicable approach to the development of effective intrabodies against other intracellular targets.