Detalhe da pesquisa
1.
Prion-Associated Toxicity is Rescued by Elimination of Cotranslational Chaperones.
PLoS Genet
; 12(11): e1006431, 2016 Nov.
Artigo
em Inglês
| MEDLINE | ID: mdl-27828954
2.
A toxic imbalance of Hsp70s in Saccharomyces cerevisiae is caused by competition for cofactors.
Mol Microbiol
; 105(6): 860-868, 2017 Sep.
Artigo
em Inglês
| MEDLINE | ID: mdl-28665048
3.
Myofibrillar disruption and RNA-binding protein aggregation in a mouse model of limb-girdle muscular dystrophy 1D.
Hum Mol Genet
; 24(23): 6588-602, 2015 Dec 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-26362252
4.
Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions.
PLoS Genet
; 10(5): e1004337, 2014 May.
Artigo
em Inglês
| MEDLINE | ID: mdl-24811344
5.
Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones.
Hum Mol Genet
; 23(1): 157-70, 2014 Jan 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-23962724
6.
Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers.
J Biol Chem
; 289(30): 21120-30, 2014 Jul 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-24920671
7.
Structural variants of yeast prions show conformer-specific requirements for chaperone activity.
Mol Microbiol
; 93(6): 1156-71, 2014 Sep.
Artigo
em Inglês
| MEDLINE | ID: mdl-25060529
8.
Extracellular environment modulates the formation and propagation of particular amyloid structures.
Mol Microbiol
; 92(4): 698-715, 2014 May.
Artigo
em Inglês
| MEDLINE | ID: mdl-24628771
9.
Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities.
Mol Microbiol
; 92(1): 183-93, 2014 Apr.
Artigo
em Inglês
| MEDLINE | ID: mdl-24673812
10.
DNAJB6 isoform specific knockdown: Therapeutic potential for limb girdle muscular dystrophy D1.
Mol Ther Nucleic Acids
; 32: 937-948, 2023 Jun 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-37346979
11.
Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates.
PLoS Genet
; 5(2): e1000382, 2009 Feb.
Artigo
em Inglês
| MEDLINE | ID: mdl-19214209
12.
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.
Nat Commun
; 13(1): 4570, 2022 08 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-35931773
13.
Analysis of the [RNQ+] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagation.
J Biol Chem
; 285(27): 20748-55, 2010 Jul 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-20442412
14.
Prion strains and amyloid polymorphism influence phenotypic variation.
PLoS Pathog
; 10(9): e1004328, 2014 Sep.
Artigo
em Inglês
| MEDLINE | ID: mdl-25188330
15.
New insights into prion structure and toxicity.
Neuron
; 50(3): 353-7, 2006 May 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-16675391
16.
Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability.
Mol Cell Biol
; 27(15): 5445-55, 2007 Aug.
Artigo
em Inglês
| MEDLINE | ID: mdl-17548473
17.
Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits.
Nature
; 431(7005): 184-7, 2004 Sep 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-15311209
18.
Client processing is altered by novel myopathy-causing mutations in the HSP40 J domain.
PLoS One
; 15(6): e0234207, 2020.
Artigo
em Inglês
| MEDLINE | ID: mdl-32497100
19.
Inhibition of DNAJ-HSP70 interaction improves strength in muscular dystrophy.
J Clin Invest
; 130(8): 4470-4485, 2020 08 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-32427588
20.
The battle of the fold: chaperones take on prions.
Trends Genet
; 22(2): 110-7, 2006 Feb.
Artigo
em Inglês
| MEDLINE | ID: mdl-16378656