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Prions in yeast

Genetics (Austin), 2012-08, Vol.191 (4), p.1041-1072

2012

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The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion

Nature cell biology, 2009-03, Vol.11 (3), p.344-349

2009

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Respiration Enhances TDP-43 Toxicity, but TDP-43 Retains Some Toxicity in the Absence of Respiration

Journal of molecular biology, 2019-05, Vol.431 (10), p.2050-2059

2019

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Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis

PLoS genetics, 2017-05, Vol.13 (5), p.e1006805

2017

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Calcium-responsive transactivator (CREST) toxicity is rescued by loss of PBP1/ATXN2 function in a novel yeast proteinopathy model and in transgenic flies

PLoS genetics, 2019-08, Vol.15 (8), p.e1008308

2019

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Exploring the Basis of [PIN+] Variant Differences in [PSI+] Induction

Journal of molecular biology, 2013-09, Vol.425 (17), p.3046-3059

2013

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TDP-43 Toxicity in Yeast Is Associated with a Reduction in Autophagy, and Deletions of TIP41 and PBP1 Counteract These Effects

Viruses, 2022-10, Vol.14 (10), p.2264

2022

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Long non-coding RNA NEAT1_1 ameliorates TDP-43 toxicity in in vivo models of TDP-43 proteinopathy

RNA biology, 2021-11, Vol.18 (11), p.1546-1554

2021

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A Genetic Tool to Track Protein Aggregates and Control Prion Inheritance

Cell, 2017-11, Vol.171 (4), p.966-979.e18

2017

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Heterologous aggregates promote de novo prion appearance via more than one mechanism

PLoS genetics, 2015-01, Vol.11 (1), p.e1004814-e1004814

2015

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Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets

iScience, 2021-01, Vol.24 (1), p.102000-102000, Article 102000

2021

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Prion Induction by the Short-Lived, Stress-Induced Protein Lsb2 Is Regulated by Ubiquitination and Association with the Actin Cytoskeleton

Molecular cell, 2011-07, Vol.43 (2), p.242-252

2011

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Comment on Billant et al. p53, A Victim of the Prion Fashion. Cancers 2021, 13 , 269

Cancers, 2023-01, Vol.15 (1), p.309

2023

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

PLoS genetics, 2011-05, Vol.7 (5), p.e1001386

2011

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Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability

PLoS genetics, 2013-01, Vol.9 (1), p.e1003236-e1003236

2013

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Localization of HET-S to the Cell Periphery, Not to [Het-s] Aggregates, Is Associated with [Het-s]–HET-S Toxicity

Molecular and Cellular Biology, 2012-01, Vol.32 (1), p.139-153

2012

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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

Proceedings of the National Academy of Sciences - PNAS, 2004-08, Vol.101 (35), p.12934-12939

2004

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Interactions among Prions and Prion "Strains" in Yeast

Proceedings of the National Academy of Sciences - PNAS, 2002-12, Vol.99 (suppl_4), p.16392-16399

2002

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Overexpression of a conserved HSP40 chaperone reduces toxicity of several neurodegenerative disease proteins

Prion, 2018-01, Vol.12 (1), p.16-22

2018

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Protein folding: sticky N17 speeds huntingtin pile-up

Nature chemical biology, 2010-01, Vol.6 (1), p.7

2010

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Visualization of Aggregation of the Rnq1 Prion Domain and Cross-seeding Interactions with Sup35NM

The Journal of biological chemistry, 2007-01, Vol.282 (3), p.1779-1787

2007

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A Non-Q/N-Rich Prion Domain of a Foreign Prion, [Het-s], Can Propagate as a Prion in Yeast

Molecular cell, 2007-07, Vol.27 (1), p.67-77

2007

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A founder mutation in FLNC is likely a major cause of idiopathic dilated cardiomyopathy in Ashkenazi Jews

International journal of cardiology, 2021-01, Vol.323, p.124-124

2021

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Heterologous cross-seeding mimics cross-species prion conversion in a yeast model

BMC biology, 2009-05, Vol.7 (1), p.26-26, Article 26

2009

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Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]

Science (American Association for the Advancement of Science), 1995-05, Vol.268 (5212), p.880-884

1995

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Prions in yeast

The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion

Respiration Enhances TDP-43 Toxicity, but TDP-43 Retains Some Toxicity in the Absence of Respiration

Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis

Calcium-responsive transactivator (CREST) toxicity is rescued by loss of PBP1/ATXN2 function in a novel yeast proteinopathy model and in transgenic flies

Exploring the Basis of [PIN+] Variant Differences in [PSI+] Induction

TDP-43 Toxicity in Yeast Is Associated with a Reduction in Autophagy, and Deletions of TIP41 and PBP1 Counteract These Effects

Long non-coding RNA NEAT1_1 ameliorates TDP-43 toxicity in in vivo models of TDP-43 proteinopathy

A Genetic Tool to Track Protein Aggregates and Control Prion Inheritance

Heterologous aggregates promote de novo prion appearance via more than one mechanism

Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets

Prion Induction by the Short-Lived, Stress-Induced Protein Lsb2 Is Regulated by Ubiquitination and Association with the Actin Cytoskeleton

Comment on Billant et al. p53, A Victim of the Prion Fashion. Cancers 2021, 13 , 269

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

Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability

Localization of HET-S to the Cell Periphery, Not to [Het-s] Aggregates, Is Associated with [Het-s]–HET-S Toxicity

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

Interactions among Prions and Prion "Strains" in Yeast

Overexpression of a conserved HSP40 chaperone reduces toxicity of several neurodegenerative disease proteins

Protein folding: sticky N17 speeds huntingtin pile-up

Visualization of Aggregation of the Rnq1 Prion Domain and Cross-seeding Interactions with Sup35NM

A Non-Q/N-Rich Prion Domain of a Foreign Prion, [Het-s], Can Propagate as a Prion in Yeast

A founder mutation in FLNC is likely a major cause of idiopathic dilated cardiomyopathy in Ashkenazi Jews

Heterologous cross-seeding mimics cross-species prion conversion in a yeast model

Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]

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