Huntingtin Fragments and SOD1 Mutants Form Soluble Oligomers in the Cell
Published 2012 View Full Article
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Title
Huntingtin Fragments and SOD1 Mutants Form Soluble Oligomers in the Cell
Authors
Keywords
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Journal
PLoS One
Volume 7, Issue 6, Pages e40329
Publisher
Public Library of Science (PLoS)
Online
2012-06-30
DOI
10.1371/journal.pone.0040329
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Note: Only part of the references are listed.- A Two-Step Path to Inclusion Formation of Huntingtin Peptides Revealed by Number and Brightness Analysis
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- Hsp70 and Hsp40 Functionally Interact with Soluble Mutant Huntingtin Oligomers in a Classic ATP-dependent Reaction Cycle
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- Quantitative Relationships between Huntingtin Levels, Polyglutamine Length, Inclusion Body Formation, and Neuronal Death Provide Novel Insight into Huntington's Disease Molecular Pathogenesis
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- (2009) L. Wang et al. HUMAN MOLECULAR GENETICS
- Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
- (2009) Pei-Hsien Ren et al. NATURE CELL BIOLOGY
- Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism
- (2009) Ashwani K Thakur et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS
- (2009) C. M. Karch et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS
- (2009) J. Wang et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants
- (2009) L. Banci et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- SOD1 and Amyotrophic Lateral Sclerosis: Mutations and Oligomerization
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