| http://purl.uniprot.org/citations/35643629 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/35643629 | http://www.w3.org/2000/01/rdf-schema#comment | "Misfolding of TATA-box binding protein-associated factor 15 (TAF15) may cause neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS). Some mutations of prion-like domain (PrLD) have been detected in patients with sporadic ALS, suggesting the importance of TAF15-PrLD in ALS pathogenesis. Herein, combining experiments and molecular dynamics (MD) simulations, we investigated the influences of several TAF15-PrLD mutations on the amyloid fibril formation of TAF15-PrLD-extracted peptide segments, and identified an essential β-amyloid-forming segment from TAF15-PrLD. A pathogenic mutation T2 E71G resulted in significantly enhanced aggregation of the TAF15-PrLD segment T2 (Y56GQSQSGYSQSYGGYENQ73). In addition, the peptide T2 with a strong β-amyloid-forming tendency was able to induce the liquid to solid phase transition of TAF15-PrLD protein. Further study identified the SGYS motif as a critical segment that promoted the formation of amyloid fibrils, which maintained a stable β-sheet structure through intermolecular hydrogen bonds and π-π stacking interaction. This work provides a clue to elucidate the molecular pathogenic mechanism of TAF15-associated neurodegenerative diseases, and will direct drug development targeting TAF15."xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bpj.2022.05.038"xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://purl.uniprot.org/core/author | "Chen J."xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://purl.uniprot.org/core/author | "Chen L."xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://purl.uniprot.org/core/author | "Chen C."xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://purl.uniprot.org/core/author | "Wang D."xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://purl.uniprot.org/core/author | "Yuan X."xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://purl.uniprot.org/core/author | "Guo Q."xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://purl.uniprot.org/core/author | "Wei P."xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://purl.uniprot.org/core/author | "Luo S.Z."xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://purl.uniprot.org/core/date | "2022"xsd:gYear |
| http://purl.uniprot.org/citations/35643629 | http://purl.uniprot.org/core/name | "Biophys J"xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://purl.uniprot.org/core/pages | "2613-2623"xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://purl.uniprot.org/core/title | "The SGYS motif of TAF15 prion-like domain is critical to amyloid fibril formation."xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://purl.uniprot.org/core/volume | "121"xsd:string |
| http://purl.uniprot.org/citations/35643629 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/35643629 |
| http://purl.uniprot.org/citations/35643629 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/35643629 |
| http://purl.uniprot.org/uniprot/#_B4E312-mappedCitation-35643629 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/35643629 |
| http://purl.uniprot.org/uniprot/#_Q92804-mappedCitation-35643629 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/35643629 |
| http://purl.uniprot.org/uniprot/Q92804 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/35643629 |
| http://purl.uniprot.org/uniprot/B4E312 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/35643629 |