Conserved Acidic Amino Acid Residues in a Second RNA Recognition Motif Regulate Assembly and Function of TDP-43
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Title
Conserved Acidic Amino Acid Residues in a Second RNA Recognition Motif Regulate Assembly and Function of TDP-43
Authors
Keywords
Recombinant proteins, Enzyme-linked immunoassays, Immunoprecipitation, Oligomers, Dimers (Chemical physics), RNA splicing, Spinal cord, Superoxide dismutase
Journal
PLoS One
Volume 7, Issue 12, Pages e52776
Publisher
Public Library of Science (PLoS)
Online
2012-12-27
DOI
10.1371/journal.pone.0052776
References
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- (2011) Yoshiaki Furukawa et al. JOURNAL OF BIOLOGICAL CHEMISTRY
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- (2011) Han-Xiang Deng et al. NATURE
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- (2009) Takashi Nonaka et al. HUMAN MOLECULAR GENETICS
- Axonal ligation induces transient redistribution of TDP-43 in brainstem motor neurons
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- Structural insights into TDP-43 in nucleic-acid binding and domain interactions
- (2009) P.-H. Kuo et al. NUCLEIC ACIDS RESEARCH
- Enrichment of C-Terminal Fragments in TAR DNA-Binding Protein-43 Cytoplasmic Inclusions in Brain but not in Spinal Cord of Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
- (2008) Lionel M. Igaz et al. AMERICAN JOURNAL OF PATHOLOGY
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- A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity
- (2008) B. S. Johnson et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis
- (2008) J. Sreedharan et al. SCIENCE
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