Pub. Date : 2018 Feb
PMID : 29334808
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Identification of a novel site of interaction between ataxin-3 and the amyloid aggregation inhibitor polyglutamine binding peptide 1. | polyglutamine | ataxin 3 | Homo sapiens |
2 | Ataxin-3 consists of a globular N-terminal Josephin domain, which can aggregate into curvilinear protofibrils, and an unstructured, dynamically disordered C-terminal domain containing three ubiquitin interacting motifs separated by a polyglutamine stretch. | polyglutamine | ataxin 3 | Homo sapiens |
3 | Upon expansion of the polyglutamine region above 50 residues, ataxin-3 undergoes a second stage of aggregation in which long, straight amyloid fibrils form. | polyglutamine | ataxin 3 | Homo sapiens |
4 | A peptide inhibitor of polyglutamine aggregation, known as polyQ binding peptide 1, has been shown previously to prevent the maturation of ataxin-3 fibrils. | polyglutamine | ataxin 3 | Homo sapiens |
5 | Using nanoelectrospray ionisation-mass spectrometry, we demonstrate that polyQ binding peptide 1 binds to monomeric ataxin-3. | polyglutamine | ataxin 3 | Homo sapiens |
6 | By investigating the ability of polyQ binding peptide 1 to bind to truncated ataxin-3 constructs lacking one or more domains, we localise the site of this interaction to a 39-residue sequence immediately C-terminal to the Josephin domain. | polyglutamine | ataxin 3 | Homo sapiens |