Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells.
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Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseasesAmyloid-like fibril formation by polyQ proteins: a critical balance between the polyQ length and the constraints imposed by the host proteinFormation and toxicity of soluble polyglutamine oligomers in living cells.The interplay between PolyQ and protein context delays aggregation by forming a reservoir of protofibrils.Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerizationMonomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansionTracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool.Protein quality control during erythropoiesis and hemoglobin synthesispolyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reactionHuntingtin fragments and SOD1 mutants form soluble oligomers in the cellSimultaneous measurement of amyloid fibril formation by dynamic light scattering and fluorescence reveals complex aggregation kinetics.Variables and strategies in development of therapeutic post-transcriptional gene silencing agentsExpression of the type VI intermediate filament proteins CP49 and filensin in the mouse lens epitheliumA century-old debate on protein aggregation and neurodegeneration enters the clinic.Studying polyglutamine aggregation in Caenorhabditis elegans using an analytical ultracentrifuge equipped with fluorescence detection.Do amyloid oligomers act as traps for misfolded proteins? A hypothesisAmyloid oligomers: dynamics and toxicity in the cytosol and nucleus.Prions Ex Vivo: What Cell Culture Models Tell Us about Infectious Proteins.Huntington's Disease: Mechanisms of Pathogenesis and Therapeutic Strategies.Sedimentation Velocity Analysis with Fluorescence Detection of Mutant Huntingtin Exon 1 Aggregation in Drosophila melanogaster and Caenorhabditis elegans.
P2860
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P2860
Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Formation of morphologically s ...... e proteins in mammalian cells.
@ast
Formation of morphologically s ...... e proteins in mammalian cells.
@en
type
label
Formation of morphologically s ...... e proteins in mammalian cells.
@ast
Formation of morphologically s ...... e proteins in mammalian cells.
@en
prefLabel
Formation of morphologically s ...... e proteins in mammalian cells.
@ast
Formation of morphologically s ...... e proteins in mammalian cells.
@en
P2093
P2860
P356
P1476
Formation of morphologically s ...... e proteins in mammalian cells.
@en
P2093
Atsuo Tamura
Emiko Goyama
Hideyuki Mukai
Neil F Bence
Ron R Kopito
Shuhei Tanaka
Takayuki Isagawa
Yoshitaka Ono
P2860
P304
10887-10892
P356
10.1073/PNAS.0409283102
P407
P577
2005-07-22T00:00:00Z