Characterization of a Brain-enriched Chaperone, MRJ, That Inhibits Huntingtin Aggregation and Toxicity Independently
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference66 articles.
1. Molecular chaperones in cellular protein folding
2. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.
3. Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum.
4. DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70
5. Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons
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1. Two novel DnaJ chaperone proteins CG5001 and P58IPK regulate the pathogenicity of Huntington’s disease related aggregates;Scientific Reports;2024-09-06
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