Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation.
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Huntingtin interacting proteins are genetic modifiers of neurodegenerationClioquinol down-regulates mutant huntingtin expression in vitro and mitigates pathology in a Huntington's disease mouse model.Improved activities of CREB binding protein, heterogeneous nuclear ribonucleoproteins and proteasome following downregulation of noncoding hsromega transcripts help suppress poly(Q) pathogenesis in fly modelsMisfolded proteins partition between two distinct quality control compartmentsThe cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome systemEndoplasmic Reticulum Stress and Associated ROSINS-gene mutations: from genetics and beta cell biology to clinical diseaseHuntington's disease: underlying molecular mechanisms and emerging conceptsDisease-Associated Polyglutamine Stretches in Monomeric Huntingtin Adopt a Compact StructureSmall molecule probes to quantify the functional fraction of a specific protein in a cell with minimal folding equilibrium shiftsConformational analysis of misfolded protein aggregation by FRET and live-cell imaging techniquesModulating self-assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases: strategies and mechanismsProteomic screening for amyloid proteinsCharacterization of oligomers of heterogeneous size as precursors of amyloid fibril nucleation of an SH3 domain: an experimental kinetics study.Length polymorphism and head shape association among genes with polyglutamine repeats in the stalk-eyed fly, Teleopsis dalmanni.Super-resolution fluorescence of huntingtin reveals growth of globular species into short fibers and coexistence of distinct aggregatesQuantitative relationships between huntingtin levels, polyglutamine length, inclusion body formation, and neuronal death provide novel insight into huntington's disease molecular pathogenesis.Formation and toxicity of soluble polyglutamine oligomers in living cells.The University of Washington Health Sciences Library BioCommons: an evolving Northwest biomedical research information support infrastructure.Proteome analysis of soluble nuclear proteins reveals that HMGB1/2 suppress genotoxic stress in polyglutamine diseases.The Princeton Protein Orthology Database (P-POD): a comparative genomics analysis tool for biologistsHAP1 can sequester a subset of TBP in cytoplasmic inclusions via specific interaction with the conserved TBP(CORE).PolyQ-expanded ataxin-3 interacts with full-length ataxin-3 in a polyQ length-dependent manner.Prions, amyloids, and RNA: Pieces of a puzzle.To fold or not to fold: modulation and consequences of Hsp90 inhibition.Modeling Huntington disease in yeast: perspectives and future directions.Potent inhibition of huntingtin aggregation and cytotoxicity by a disulfide bond-free single-domain intracellular antibody.Polyglutamine-rich suppressors of huntingtin toxicity act upstream of Hsp70 and Sti1 in spatial quality control of amyloid-like proteins.Distinct cellular toxicity of two mutant huntingtin mRNA variants due to translation regulation.Nonallele-specific silencing of mutant and wild-type huntingtin demonstrates therapeutic efficacy in Huntington's disease mice.Inefficient translocation of preproinsulin contributes to pancreatic β cell failure and late-onset diabetes.Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansioncAMP-response element-binding protein and heat-shock protein 70 additively suppress polyglutamine-mediated toxicity in DrosophilaThe polyubiquitin Ubc gene modulates histone H2A monoubiquitylation in the R6/2 mouse model of Huntington's disease.Valosin-containing protein (VCP) in novel feedback machinery between abnormal protein accumulation and transcriptional suppressionInteraction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.Protein folding in the cytoplasm and the heat shock response.Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptidesPromoters are differentially sensitive to N-terminal mutant huntingtin-mediated transcriptional repression.Hsp70 and Hsp40 functionally interact with soluble mutant huntingtin oligomers in a classic ATP-dependent reaction cycle
P2860
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P2860
Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Cellular toxicity of polygluta ...... scription factor deactivation.
@en
type
label
Cellular toxicity of polygluta ...... scription factor deactivation.
@en
prefLabel
Cellular toxicity of polygluta ...... scription factor deactivation.
@en
P2093
P1433
P1476
Cellular toxicity of polygluta ...... scription factor deactivation.
@en
P2093
Christian Behrends
Gregor Schaffar
Hideki Sakahira
Katja Siegers
Nadine Strippel
Nikolay Tzvetkov
Peter Breuer
Raina Boteva
P304
P356
10.1016/J.MOLCEL.2004.06.029
P577
2004-07-01T00:00:00Z