Protein folding: Sticky N17 speeds huntingtin pile-up
Copyright policy )Protein folding: Sticky N17 speeds huntingtin pile-up
Aggregation of huntingtin protein with an expanded polyglutamine region is enhanced by its 17-residue N-terminal domain, which binds to itself and to the polyglutamine region. This enhancement is inhibited when the N-terminal domain binds to the chaperonin TRiC.
- University of Illinois at Chicago United States
- University of Chicago United States
Huntingtin Protein, Protein Folding, Chaperonins, Models, Genetic, DNA Mutational Analysis, Nuclear Proteins, Nerve Tissue Proteins, Exons, Ligands, Protein Structure, Tertiary, Benzophenones, Humans, Peptides, Chaperonin Containing TCP-1, Gene Deletion, Protein Binding
Huntingtin Protein, Protein Folding, Chaperonins, Models, Genetic, DNA Mutational Analysis, Nuclear Proteins, Nerve Tissue Proteins, Exons, Ligands, Protein Structure, Tertiary, Benzophenones, Humans, Peptides, Chaperonin Containing TCP-1, Gene Deletion, Protein Binding
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