Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.
about
Asparaginase treatment side-effects may be due to genes with homopolymeric Asn codons (Review-Hypothesis)Determinants of Amyloid Formation for the Yeast Termination Factor Nab3Protein misfolding specifies recruitment to cytoplasmic inclusion bodiesSequestration of cellular interacting partners by protein aggregates: implication in a loss-of-function pathology.Protein aggregation as a mechanism of adaptive cellular responses.Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome.Live-cell multiphoton fluorescence correlation spectroscopy with an improved large Stokes shift fluorescent protein.Aggregation of Polyglutamine-expanded Ataxin 7 Protein Specifically Sequesters Ubiquitin-specific Protease 22 and Deteriorates Its Deubiquitinating Function in the Spt-Ada-Gcn5-Acetyltransferase (SAGA) Complex.Regulated Formation of an Amyloid-like Translational Repressor Governs GametogenesisThe Social Amoeba Dictyostelium discoideum Is Highly Resistant to Polyglutamine AggregationATXN2 trinucleotide repeat length correlates with risk of ALS.Vaccinia-Related Kinase 2 Controls the Stability of the Eukaryotic Chaperonin TRiC/CCT by Inhibiting the Deubiquitinating Enzyme USP25Prion-Like Characteristics of Polyglutamine-Containing Proteins.Candida albicans Is Resistant to Polyglutamine Aggregation and ToxicityReal-Time Monitoring of Alzheimer's-Related Amyloid Aggregation via Probe Enhancement-Fluorescence Correlation Spectroscopy.Spatial sequestration and detoxification of Huntingtin by the ribosome quality control complex.A protein polymerization cascade mediates toxicity of non-pathological human huntingtin in yeast.Differential effects of soluble and aggregating polyQ proteins on cytotoxicity and type-1 myosin-dependent endocytosis in yeast.The dual role of a yeast metacaspase: What doesn't kill you makes you stronger.The heat shock response in neurons and astroglia and its role in neurodegenerative diseases.Wild type huntingtin toxicity in yeast: Implications for the role of amyloid cross-seeding in polyQ diseases.Adaptation to Stressors by Systemic Protein Amyloidogenesis.Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths.A Genetic Tool to Track Protein Aggregates and Control Prion Inheritance.Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers.Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species.Natural Genetic Variation in Yeast Reveals That NEDD4 Is a Conserved Modifier of Mutant Polyglutamine Aggregation
P2860
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P2860
Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.
description
2014 nî lūn-bûn
@nan
2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.
@ast
Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.
@en
Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.
@nl
type
label
Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.
@ast
Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.
@en
Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.
@nl
prefLabel
Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.
@ast
Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.
@en
Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.
@nl
P2093
P2860
P50
P356
P1476
Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1
@en
P2093
Jagesh V Shah
Kent E S Matlack
Sohini Chakrabortee
Susan Lindquist
William R Hesse
Yinghua Guan
P2860
P304
12085-12090
P356
10.1073/PNAS.1412504111
P407
P577
2014-08-04T00:00:00Z