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Disruption of the nascent polypeptide-associated complex leads to reduced polyglutamine aggregation and toxicity

PloS one, 2024-08, Vol.19 (8), p.e0303008

2024

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Client processing is altered by novel myopathy-causing mutations in the HSP40 J domain

PloS one, 2020-06, Vol.15 (6), p.e0234207-e0234207

2020

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Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones

Human molecular genetics, 2014-01, Vol.23 (1), p.157-170

2014

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Prion strains and amyloid polymorphism influence phenotypic variation

PLoS pathogens, 2014-09, Vol.10 (9), p.e1004328-e1004328

2014

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Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae

Scientific reports, 2017-07, Vol.7 (1), p.5853-11, Article 5853

2017

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Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions

PLoS genetics, 2014-05, Vol.10 (5), p.e1004337-e1004337

2014

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

Nature, 2004-09, Vol.431 (7005), p.184-187

2004

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Disease-associated mutations within the yeast DNAJB6 homolog Sis1 slow conformer-specific substrate processing and can be corrected by the modulation of nucleotide exchange factors

Nature communications, 2022-08, Vol.13 (1), p.4570-14, Article 4570

2022

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Prion-Associated Toxicity is Rescued by Elimination of Cotranslational Chaperones

PLoS genetics, 2016-11, Vol.12 (11), p.e1006431

2016

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Myopathy-causing Mutations in an HSP40 Chaperone Disrupt Processing of Specific Client Conformers

The Journal of biological chemistry, 2014-07, Vol.289 (30), p.21120-21130

2014

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Myofibrillar disruption and RNA-binding protein aggregation in a mouse model of limb-girdle muscular dystrophy 1D

Human molecular genetics, 2015-12, Vol.24 (23), p.6588-6602

2015

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Inhibition of DNAJ-HSP70 interaction improves strength in muscular dystrophy

The Journal of clinical investigation, 2020-08, Vol.130 (8), p.4470-4485

2020

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The Spontaneous Appearance Rate of the Yeast Prion [PSI+] and Its Implications for the Evolution of the Evolvability Properties of the [PSI+] System

Genetics (Austin), 2010-02, Vol.184 (2), p.393-400

2010

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A yeast prion provides a mechanism for genetic variation and phenotypic diversity

Nature (London), 2000-09, Vol.407 (6803), p.477-483

2000

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The Sua5 Protein Is Essential for Normal Translational Regulation in Yeast

Molecular and Cellular Biology, 2010-01, Vol.30 (1), p.354-363

2010

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Spontaneous variants of the [RNQ+] prion in yeast demonstrate the extensive conformational diversity possible with prion proteins

PloS one, 2013-10, Vol.8 (10), p.e79582-e79582

2013

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Remodeling of yeast genome expression in response to environmental changes

Molecular biology of the cell, 2001-02, Vol.12 (2), p.323-337

2001

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Rapid generation of hypomorphic mutations

Nature communications, 2017-01, Vol.8 (1), p.14112-14112, Article 14112

2017

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Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates

PLoS genetics, 2009-02, Vol.5 (2), p.e1000382

2009

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DNAJB6 isoform specific knockdown: Therapeutic potential for limb girdle muscular dystrophy D1

Molecular therapy. Nucleic acids, 2023-06, Vol.32, p.937-948

2023

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Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation

PloS one, 2014-01, Vol.9 (1), p.e87521

2014

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Heterologous Prion Interactions Are Altered by Mutations in the Prion Protein Rnq1p

Journal of molecular biology, 2009-05, Vol.388 (3), p.583-596

2009

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Wild yeast harbour a variety of distinct amyloid structures with strong prion‐inducing capabilities

Molecular microbiology, 2014-04, Vol.92 (1), p.183-193

2014

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Extracellular environment modulates the formation and propagation of particular amyloid structures

Molecular microbiology, 2014-05, Vol.92 (4), p.698-715

2014

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Structural variants of yeast prions show conformer‐specific requirements for chaperone activity

Molecular microbiology, 2014-09, Vol.93 (6), p.1156-1171

2014

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Disruption of the nascent polypeptide-associated complex leads to reduced polyglutamine aggregation and toxicity

Client processing is altered by novel myopathy-causing mutations in the HSP40 J domain

Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones

Prion strains and amyloid polymorphism influence phenotypic variation

Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae

Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions

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

Disease-associated mutations within the yeast DNAJB6 homolog Sis1 slow conformer-specific substrate processing and can be corrected by the modulation of nucleotide exchange factors

Prion-Associated Toxicity is Rescued by Elimination of Cotranslational Chaperones

Myopathy-causing Mutations in an HSP40 Chaperone Disrupt Processing of Specific Client Conformers

Myofibrillar disruption and RNA-binding protein aggregation in a mouse model of limb-girdle muscular dystrophy 1D

Inhibition of DNAJ-HSP70 interaction improves strength in muscular dystrophy

The Spontaneous Appearance Rate of the Yeast Prion [PSI+] and Its Implications for the Evolution of the Evolvability Properties of the [PSI+] System

A yeast prion provides a mechanism for genetic variation and phenotypic diversity

The Sua5 Protein Is Essential for Normal Translational Regulation in Yeast

Spontaneous variants of the [RNQ+] prion in yeast demonstrate the extensive conformational diversity possible with prion proteins

Remodeling of yeast genome expression in response to environmental changes

Rapid generation of hypomorphic mutations

Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates

DNAJB6 isoform specific knockdown: Therapeutic potential for limb girdle muscular dystrophy D1

Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation

Heterologous Prion Interactions Are Altered by Mutations in the Prion Protein Rnq1p

Wild yeast harbour a variety of distinct amyloid structures with strong prion‐inducing capabilities

Extracellular environment modulates the formation and propagation of particular amyloid structures

Structural variants of yeast prions show conformer‐specific requirements for chaperone activity

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