Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently. [electronic resource]
Producer: 20020702Description: 19831-8 p. digitalISSN:- 0021-9258
- Adenosine Triphosphatases -- metabolism
- Amino Acid Sequence
- Animals
- Base Sequence
- Blotting, Northern
- Brain -- metabolism
- Cattle
- Cell Survival
- Cloning, Molecular
- DNA, Complementary -- metabolism
- Escherichia coli Proteins
- HSP40 Heat-Shock Proteins
- HSP70 Heat-Shock Proteins -- metabolism
- Humans
- Huntingtin Protein
- Immunohistochemistry
- Models, Genetic
- Molecular Chaperones -- biosynthesis
- Molecular Sequence Data
- Nerve Tissue Proteins -- metabolism
- Neurons -- metabolism
- Nuclear Proteins -- metabolism
- Peptides -- metabolism
- Protein Binding
- Time Factors
- Tissue Distribution
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
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