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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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Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers

TL;DR: Muralidharan et al. as mentioned in this paper showed that Plasmodium Hsp110 protein prevents aggregation of asparagine-rich proteins, thereby allowing the parasite to survive febrile episodes.
Journal ArticleDOI

Self-perpetuating changes in Sup35 protein conformation as a mechanism of heredity in yeast.

TL;DR: A mechanism exists to ensure replication of the conformational information that underlies protein-only inheritance, and is characterized by which the alternative conformation of Sup35 is adopted by an unstructured oilgomeric intermediate at the time of assembly.
Book ChapterDOI

Differential mRNA Stability: A Regulatory Strategy for Hsp70 Synthesis

TL;DR: Many organisms face the challenge of a changing environment and have developed the ability to mount transient responses in which subsets of genes appropriate to current conditions are activated for an appropriate time.

STITCHER: Dynamic assembly of likely amyloid and prion beta-structures from secondary structure predictions

TL;DR: A system of energetic rules that can be used to dynamically assemble discrete β‐strand pairs into complete amyloid β‐structures is devised, and STITCHER provides novel insight into the energetic basis of amyloids structure, provides accurate structure predictions, and can help guide future experimental studies.
Patent

Recombinant prion-like genes and proteins and materials and methods comprising same

TL;DR: The present paper as discussed by the authors provides polypeptides comprising a prion-aggregation domain and a second domain; polynucleotides encoding such poly-peptide; host cells transformed or transfected with such po-lynucleotide; and methods of making and using the foregoing.