Susan Lindquist

Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.

Susan L. Lindquist.

Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding.

Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein.

Hsp90 as a capacitor of phenotypic variation.

Analysis of prion factors in yeast.

Prions as protein-based genetic elements.

Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol.

Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol.

Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+].

Self-perpetuating structural states in biology, disease, and genetics.

Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition.

Hsp90 and chromatin: where is the link?

Prion protein gene polymorphisms in Saccharomyces cerevisiae.

Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein.

Yeast cells provide insight into alpha-synuclein biology and pathobiology.

A neuronal isoform of the aplysia CPEB has prion-like properties.

Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region.

The elongation of yeast prion fibers involves separable steps of association and conversion.

Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance.

Interactions among alpha-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease.

Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers.

Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits.

Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro.

Potent inhibition of huntingtin aggregation and cytotoxicity by a disulfide bond-free single-domain intracellular antibody.

Navigating the ClpB channel to solution.

A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104.

Prions as adaptive conduits of memory and inheritance.

Structural insights into a yeast prion illuminate nucleation and strain diversity.

Prion proteins: one surprise after another.

HSP90 and the chaperoning of cancer.

Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi.

Increase in activity during calorie restriction requires Sirt1.

Harnessing natural diversity to probe metabolic pathways.

Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal.

Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis.

Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models.

A network of protein interactions determines polyglutamine toxicity.

Flanking sequences profoundly alter polyglutamine toxicity in yeast.

Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities.

Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models.

Genetic architecture of Hsp90-dependent drug resistance.

Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity.

The power of automated high-resolution behavior analysis revealed by its application to mouse models of Huntington's and prion diseases.

A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures.

Prion recognition elements govern nucleation, strain specificity and species barriers.

A suite of Gateway cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae.

Phenotypic diversity and altered environmental plasticity in Arabidopsis thaliana with reduced Hsp90 levels.

Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis.

Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions.

Alternative assembly pathways of the amyloidogenic yeast prion determinant Sup35-NM.

Diminishing apoptosis by deletion of Bax or overexpression of Bcl-2 does not protect against infectious prion toxicity in vivo.

Illuminating aggregate heterogeneity in neurodegenerative disease.

Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104.

The Parkinson's disease protein alpha-synuclein disrupts cellular Rab homeostasis.

HSP90-buffered genetic variation is common in Arabidopsis thaliana.

HSP90 affects the expression of genetic variation and developmental stability in quantitative traits.

Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities.

Detection of compounds that rescue Rab1-synuclein toxicity.

A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity.

Chaperone-dependent amyloid assembly protects cells from prion toxicity.

Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs.

Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease.

Heat shock factor 1 regulates lifespan as distinct from disease onset in prion disease.

The role of calorie restriction and SIRT1 in prion-mediated neurodegeneration.

Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.

Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity.

Using yeast to understand protein folding diseases: an interview with Susan Lindquist by Kristin Kain.

Prion switching in response to environmental stress.

Lymphotoxin-dependent prion replication in inflammatory stromal cells of granulomas.

Evidence that alpha-synuclein does not inhibit phospholipase D.

The prion protein knockout mouse: a phenotype under challenge.

Prion pathogenesis is independent of caspase-12.

Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity.

Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease.

Bridging high-throughput genetic and transcriptional data reveals cellular responses to alpha-synuclein toxicity.

BETASCAN: probable beta-amyloids identified by pairwise probabilistic analysis.

Inhibiting the transcription factor HSF1 as an anticancer strategy.

A systematic survey identifies prions and illuminates sequence features of prionogenic proteins.

A nucleolar protein allows viability in the absence of the essential ER-residing molecular chaperone calnexin.

Motor mechanism for protein threading through Hsp104.

Amyloid deposits: protection against toxic protein species?

Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+].

Rapid selection of cyclic peptides that reduce alpha-synuclein toxicity in yeast and animal models.

Loss of Hsp70 exacerbates pathogenesis but not levels of fibrillar aggregates in a mouse model of Huntington's disease.

Spontaneous generation of prion infectivity in fatal familial insomnia knockin mice.

The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion.

A heritable switch in carbon source utilization driven by an unusual yeast prion.

Context-dependent perturbation of neural systems in transgenic mice expressing a cytosolic prion protein.

Context dependent neuroprotective properties of prion protein (PrP).

Compounds from an unbiased chemical screen reverse both ER-to-Golgi trafficking defects and mitochondrial dysfunction in Parkinson's disease models.

Prions, protein homeostasis, and phenotypic diversity.

Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation.

Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker's yeast?

Conversion of a yeast prion protein to an infectious form in bacteria.

α-Synuclein: membrane interactions and toxicity in Parkinson's disease.

HSP90 at the hub of protein homeostasis: emerging mechanistic insights.

Polyamine pathway contributes to the pathogenesis of Parkinson disease.

Biochemical, cell biological, and genetic assays to analyze amyloid and prion aggregation in yeast.

Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits.

Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms.

Three quite different things that matter to me.

Optical trapping with high forces reveals unexpected behaviors of prion fibrils.

Hsp90 and environmental stress transform the adaptive value of natural genetic variation.

Cyclin-G-associated kinase modifies α-synuclein expression levels and toxicity in Parkinson's disease: results from the GenePD Study.

Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB).

The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication.

A yeast model of FUS/TLS-dependent cytotoxicity.

ResponseNet: revealing signaling and regulatory networks linking genetic and transcriptomic screening data.

A flurry of folding problems: an interview with Susan Lindquist by Jane Gitschier.

Prion formation and polyglutamine aggregation are controlled by two classes of genes.

A method for probing the mutational landscape of amyloid structure.

Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins.

Generation of isogenic pluripotent stem cells differing exclusively at two early onset Parkinson point mutations.

Physical properties of polymorphic yeast prion amyloid fibers.

Piperazinyl quinolines as chemosensitizers to increase fluconazole susceptibility of Candida albicans clinical isolates.

TorsinA and the torsinA-interacting protein printor have no impact on endoplasmic reticulum stress or protein trafficking in yeast.

Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis.

Functional links between Aβ toxicity, endocytic trafficking, and Alzheimer's disease risk factors in yeast.

High levels of nuclear heat-shock factor 1 (HSF1) are associated with poor prognosis in breast cancer.

Using the Heat-Shock Response To Discover Anticancer Compounds that Target Protein Homeostasis.

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

QnAs with Susan L. Lindquist. Interviewed by Prashant Nair.

Different 8-Hydroxyquinolines Protect Models of TDP-43 Protein, α-Synuclein, and Polyglutamine Proteotoxicity through Distinct Mechanisms.

SIRT1 protects against α-synuclein aggregation by activating molecular chaperones.

Prions are a common mechanism for phenotypic inheritance in wild yeasts.